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Hemorrhagic Fever Viruses
Preface Table of Contents Contributing Authors Part I Surveillance, Diagnosis and Classification of hemorrhagic fever viruses 1. Global Spread of Hemorrhagic Fever Viruses: Predicting PandemicsJean Paul Gonzalez, Marc Souris, and Willy Valdivia-Granda 2. An Approach to the Identification and Phylogenetic Analysis of Emerging and Hemorrhagic Fever VirusesFrancisco J. Díaz, Lui... zur Produkt-Seite
4908656 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvODgvMWIvMjEvNjQ4OTQzMDEwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvODgvMWIvMjEvNjQ4OTQzMDEwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9oZW1vcnJoYWdpYy1mZXZlci12aXJ1c2VzLTI3MzU0NTQ1MS5qcGc=","post_title":"Hemorrhagic Fever Viruses","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493969807&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fmedizin-pharmazie%2F377943%2Fhemorrhagic-fever-viruses-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Preface Table of Contents Contributing Authors Part I Surveillance, Diagnosis and Classification of hemorrhagic fever viruses 1. Global Spread of Hemorrhagic Fever Viruses: Predicting PandemicsJean Paul Gonzalez, Marc Souris, and Willy Valdivia-Granda 2. An Approach to the Identification and Phylogenetic Analysis of Emerging and Hemorrhagic Fever VirusesFrancisco J. D\u00edaz, Luis Paternina, and Juan D. Rodas 3. Preliminary Classification of Novel Hemorrhagic Fever-Causing Viruses Using Sequence-Based Pairwise Sequence Comparison (PASC) AnalysisYim\u00edng B\u00e0o and Jens H. Kuhn 4. Epidemiological Surveillance of Viral Hemorrhagic Fevers with Emphasis on Clinical VirologyCarolina Montoya-Ruiz and Juan D. Rodas 5. Diagnostics for Lassa Fever: Detecting Host Antibody ResponsesMaria S. Salvato, Igor S. Lukashevich, Sandra Medina-Moreno, and Juan Carlos Zapata 6. Sampling Design and Mosquito Trapping for Surveillance of Arboviral ActivityLuis E. Paternina and Juan D. Rodas 7. Epidemiological Surveillance of Rodent-Borne Viruses (Roboviruses)Juan D. Rodas, Andr\u00e9s Londo\u00f1o, and Sergio Solari Part II Structural Studies and Reverse Genetics of Hemorrhagic Fever Viruses 8. Entry Studies of New World ArenavirusesMar\u00eda Guadalupe Mart\u00ednez, Mar\u00eda Bel\u00e9n Forlenza, N\u00e9lida A. Candurra, and Sandra M. Cordo 9. Studies of Lassa Virus Cell EntryAntonella Pasquato, Antonio Herrador Fernandez, and Stefan Kunz 10. A Cell-Cell Fusion Assay to Assess Arenavirus Envelope Glycoprotein Membrane-Fusion ActivityJoanne York and Jack H. Nunberg 11. Assays to Assess Arenaviral Glycoprotein FunctionJunjie Shao, Xiaoying Liu, Yuying Liang, and Hinh Ly 12. Expression and X-Ray Structural Determination of the Nucleoprotein of Lassa Fever VirusXiaoxuan Qi, Wenjian Wang, Haohao Dong, Yuying Liang, Changjiang Donga, and Hinh Ly 13. Assays to Demonstrate the Roles of Arenaviral Nucleoproteins (NP) in Viral RNA Synthesis and in Suppressing Type I InterferonQinfeng Huang, Junjie Shao, Yuying Liang, and Hinh Ly 14. Intracellular Detection of Viral Transcription and Replication using RNA FISHMichael E. Lindquist and Connie S. Schmlajohn 15. Hemorrhagic Fever Virus Budding StudiesRonald N. Harty Part III In Vivo Models of Hemorrhagic Fever Virus Infection 16. Murine Models for Viral Hemorrhagic FeverRosana Gonzalez-Quintial and Roberto Baccala 17. Testing Experimental Therapies in a Guinea Pig Model for Hemorrhagic FeverGary Wong, Yuhai Bi, Gary Kobinger, George F. Gao, and Xiangguo Qiu 18. A Primate Model for Viral Hemorrhagic FeverMaria S. Salvato, Igor S. Lukashevich, Yida Yang, Sandra Medina-Moreno, Mahmoud Djavani, Joseph Bryant, and Juan C. Zapata 19. A Primary Human Liver Cell Culture Model for Hemorrhagic Fever VirusesMahmoud Djavani Part IV Immune Assays and Vaccine Production for Hemorrhagic Fever Viruses 20. Protocol for the Production of a Vaccine Against Argentine Hemorrhagic FeverAna Mar\u00eda Ambrosio, Mauricio Andr\u00e9s Mariani, Andrea Soledad Maiza, Graciela Susana Gamboa, Sebasti\u00e1n Edgardo Fossa, and Alejando Javier Bottale 21. Detection of Virus-Antibody Immune Complexes in Secondary Dengue Virus InfectionMeng Ling Moi, Tomohiko Takasaki, and Ichiro Kurane 22. Future Approaches to DNA Vaccination Against Hemorrhagic Fever VirusesJohn J. Suschak and Connie S. Schmaljohn Part V Host Responses to Viral Hemorrhagic Fever 23. Identifying Restriction Factors for Hemorrhagic Fever Viruses: Dengue and Jun\u00ednFederico Giovannoni, Jose Rafael Pe\u00f1a C\u00e1rcamo, Mar\u00eda Laura Morell, Sandra Myriam Cordo, and Cybele Carina Garc\u00eda 24. Determining the Virus Life-Cycle Stage Blocked by an AntiviralClaudia S. Sep\u00falveda, Cybele C. Garc\u00eda, and Elsa B. Damonte 25. Retrovirus-Based Surrogate Systems for BSL-2 High-Throughput Screening of Antivirals Targeting BSL-3\/4 Hemorrhagic Fever-Causing VirusesSheli R. Radoshitzky, Veronica Soloveva, Dima Gharaibeh, Jens H. Kuhn, and Sina Bavari 26. Protocols to Assess Coagulation following In Vitro Infection with Hemorrhagic Fever VirusesMelissa L. Tursiella, Shannon L. Taylor, and Connie S. Schmaljohn","merchants_number":2,"ean":9781493969807,"category_id":103,"size":null,"min_price":157,"low_price_merchant_id":70255345,"ID":4908656,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"hemorrhagic-fever-viruses","url":"\/unterhaltung\/produkt\/hemorrhagic-fever-viruses\/","low_price_merchant_name":"eUniverse"}
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Many-body Approaches at Different Scales
Part I Condensed matter theory.- 1 Correlations in the superconducting properties of several material Classes.- 2 Viscous electron liquids in encapsulated grapheme.- 3 Computer simulations of the structure of nanoporous carbons and higher density phases of carbon.- 4 On Dirac points in the Harper model.- 5 Theory of Mott localization in silicone.- 6 Molecular ordering in covalent latt... zur Produkt-Seite
4093598 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9pLndlbHRiaWxkLmRlL3AvbWFueS1ib2R5LWFwcHJvYWNoZXMtYXQtZGlmZmVyZW50LXNjYWxlcy0yNzgxMjE2NDcuanBn!aHR0cHM6Ly9pLndlbHRiaWxkLmRlL3AvbWFueS1ib2R5LWFwcHJvYWNoZXMtYXQtZGlmZmVyZW50LXNjYWxlcy0yNzgxMjE2NDcuanBnfH58aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvMDUvZjYvOGQvNjY5MzU5NjcwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"Many-body Approaches at Different Scales","deeplink":"https:\/\/track.adtraction.com\/t\/t?a=1632201226&as=1592767275&t=2&tk=1&url=https:\/\/www.weltbild.ch\/artikel\/x\/_23815618-1","labels":[],"brand_id":1,"post_content":"Part I Condensed matter theory.- 1 Correlations in the superconducting properties of several material Classes.- 2 Viscous electron liquids in encapsulated grapheme.- 3 Computer simulations of the structure of nanoporous carbons and higher density phases of carbon.- 4 On Dirac points in the Harper model.- 5 Theory of Mott localization in silicone.- 6 Molecular ordering in covalent lattices.- 7 An ab initio evaluation of Mott properties.- 8 Wavefunctions for large electron numbers: the Exponential Wall problem.- 9 Electron tunneling excitation of a coupled two impurity system.- 10 Quantifying the effect of point and line defect densities on the melting temperature in the transition metals.- 11 Application of the plane-wave-based perturbation theory to the density modulation induced by a point charge in an electron gas.- 11.1 Introduction.- 12 An overview of concepts in liquid state physics.- 13 Structure of water in dilute ionic solutions.- 14 Atomic spectra calculations using a solvable model potential for fusion plasma engineering.- 15 Solar cell efficiency: the Shockley-Queisser limit revisited.- Part II Theoretical chemistry.- 16 Shannon entropy and correlation energy for electrons in atoms.- 17 On combinatoric identities for electron-pair wavefunctions.- 18 From molecules and clusters of atoms to solid state properties.- 19 Alchemical derivatives of atoms: a walk through the periodic table.- 20 Title to be announced.- 21 Orbital-free density functional theory: Pauli potential and density scaling.- 22 The role of the N-representability in one-particle functional theories.- 23 Title to be announced.- Part III Theoretical physics.- 24 Energy density functional theory in atomic and nuclear physics.- 25 Second order exchange energy of a d-dimensional electron fluid.- 26 Nonlocal quantum kinetic theory and the formation of correlations.- 27 Numerical evidence of Sinai-like diffusion of random-mass Dirac-Klein particles.- 28 Topological effects and critical phenomena in the three-dimensional (3D) Ising model.- 29 Do symmetry-breaking transitions in photosynthetic light harvesting complexes form a Kibble-Zurek Model (KZM) topological defect?.- 30 The universe as a quantum many-body system.- Author index.- Keyword index.","merchants_number":2,"ean":9783319723730,"category_id":103,"size":null,"min_price":118,"low_price_merchant_id":27291482,"ID":4093598,"merchants":["weltbild","euniverse"],"brand":"undefined","slug":"many-body-approaches-at-different-scales","url":"\/unterhaltung\/produkt\/many-body-approaches-at-different-scales\/","low_price_merchant_name":"Weltbild"}
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Enzyme Engineering
1. A Tripartite Fusion System for the Selection of Protein Variants with Increased Stability in vivoLinda Foit and James Bardwell 2. Determining Enzyme Kinetics via Isothermal Titration CalorimetryNeil A. Demarse, Marie C. Killian, Lee D. Hansen, and Colette F. Quinn 3. GFP Reporter Screens for the Engineering of Amino Acid Degrading Enzymes from Libraries Expressed in BacteriaOlga P... zur Produkt-Seite
4394669 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNGQvZjEvNDgvMzQ2OTcyNjAwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNGQvZjEvNDgvMzQ2OTcyNjAwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9lbnp5bWUtZW5naW5lZXJpbmctMjczNTE4NzMwLmpwZw==","post_title":"Enzyme Engineering","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781627032926&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F381326%2Fenzyme-engineering-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"1. A Tripartite Fusion System for the Selection of Protein Variants with Increased Stability in vivoLinda Foit and James Bardwell 2. Determining Enzyme Kinetics via Isothermal Titration CalorimetryNeil A. Demarse, Marie C. Killian, Lee D. Hansen, and Colette F. Quinn 3. GFP Reporter Screens for the Engineering of Amino Acid Degrading Enzymes from Libraries Expressed in BacteriaOlga Paley, Giulia Agnello, Jason Cantor, Tae Hyun Yoo, George Georgiou, and Everett Stone 4. Flow Cytometric Assays for Interrogating LAGLIDADG Homing Endonuclease DNA Binding and Cleavage PropertiesSarah K. Baxter, Abigail R. Lambert, Andrew M. Scharenberg, and Jordan Jarjour 5. TAL Effector Nuclease (TALEN) EngineeringTing Li and Bing Yang 6. In vitro Evolution of EnzymesMisha V. Golynskiy, John C. Haugner III, Aleardo Morelli, Dana Morrone, and Burckhard Seelig 7. Residue-Specific Incorporation of Unnatural Amino Acids into Proteins In vitro and In vivoAmrita Signh-Blom, Randall A. Hughes, and Andrew. D. Ellington 8. Reconstructing Evolutionary Adaptive Paths for Protein EngineeringMegan F. Cole, Vanessa E. Cox, Kelsey L. Gratton, and Eric A. Gaucher 9. Oligonucleotide Recombination Enabled Site-Specific Mutagenesis in BacteriaBryan M. Swingle 10. FX Cloning: A Versatile High-Throughput Cloning System for Characterization of Enzyme Variants Eric R. Geertsma 11. Use of Sulfolobus solfataricus PCNA Subunit Proteins to Direct the Assembly of Multimeric Enzyme ComplexesHidehiko Hirakawa and Teruyuki Nagamune 12. Gene Synthesis by Assembly of Deoxyuridine Containing Oligonucleotides Romualdas Vaisvila and Jurate Bitinaite 13. Protein Engineering: Single or Multiple Site-Directed MutagenesisPei-Chung Hsieh and Romualdas Vaisvila 14. Gene Assembly and Combinatorial Libraries in S. cerevisiae via Reiterative RecombinationNili Ostrov, Laura M. Wingler, and Virginia Cornish 15. Promiscuity-Based Enzyme Selection for Rational Directed Evolution ExperimentsSandeep Chakraborty, Renu Minda, Lipika Salaye, Abhaya M. dandekar, Swapan K. Bhattacharjee, and Basuthkar J. Rao 16. Rational Protein Sequence Diversification by Multi-Codon Scanning MutagenesisJia Liu and T. Ashton Cropp 17. Screening Libraries for Improved Solubility: Using E. coli Dihydrofolate Reductase as a ReporterJian-Wei Liu and David Ollis 18. In Vitro Directed Evolution of Enzymes Expressed by E. coli in Micro-Titre Plates Bradley J. Stevenson, Sylvia H.C. Yip, and David L. Ollis","merchants_number":2,"ean":9781627032926,"category_id":103,"size":null,"min_price":168,"low_price_merchant_id":70255345,"ID":4394669,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"enzyme-engineering","url":"\/unterhaltung\/produkt\/enzyme-engineering\/","low_price_merchant_name":"eUniverse"}
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The Story of the Lost Child
Longlisted for the 2016 MAN BOOKER INTERNATIONAL PRIZENamed TIME Magazine's #1 Book in it's "10 Best Fiction Books of 2015" listNamed one of the "10 Best Fiction Books of 2015" by The New York Times Book ReviewNamed one of the "10 Best Fiction Books of 2015" by People MagazineFeatured in the Wall Street Journal's list of "15 Books to Read This Fall"Included as one of "30 blockbuster n... zur Produkt-Seite
4394525 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvZGYvNDYvNTcvNTMyMzA1MTMwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvZGYvNDYvNTcvNTMyMzA1MTMwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"The Story of the Lost Child","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781609452865&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fbelletristik-unterhaltung%2Fromane-erzaehlungen-anthologien%2F521670%2Fthe-story-of-the-lost-child-a-novel-neapolitan-novels-4%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Longlisted for the 2016 MAN BOOKER INTERNATIONAL PRIZENamed TIME Magazine's #1 Book in it's \"10 Best Fiction Books of 2015\" listNamed one of the \"10 Best Fiction Books of 2015\" by The New York Times Book ReviewNamed one of the \"10 Best Fiction Books of 2015\" by People MagazineFeatured in the Wall Street Journal's list of \"15 Books to Read This Fall\"Included as one of \"30 blockbuster novels to look out for this fall\" by Entertainment WeeklyListed as one of Publisher Weekly's \"Most Anticipated Books of Fall 2015\"Included in the Kirkus list of \"21 Must-read Fall books\"Featured as one of the New York Times Book Review's \"100 Notable Books of 2015\"Praise for The Story of the Lost Child\"Dazzling...stunning...an extraordinary epic.\"-Michiko Kakutani, The New York Times\"It's spectacular, but you will only realize how spectacular The Story of the Lost Child is if you do not cheat. You must read the three earlier (also superb) Neapolitan Novels or the perfect devastation wrought by the conclusion of this last novel will be lost on you.\"-Maureen Corrigan, NPR Fresh Air\"It is the exploration of the women's mental underworld that makes the book so singular an achievement in feminist literature, indeed, in all literature.\"-Joan Acocella, The New Yorker\"This is Ferrante at the height of her brilliance.\"-Elissa Schappell, Vanity Fair\"Ms. Ferrante has in fact, for more than 20 years, written about female identity with a heft and sharpness unmatched by anyone since Doris Lessing.\"-The Wall Street Journal\"What words do you save? Here's your chance to bring them out, like the silver for the wedding of the first-born: genius, tour de force, masterpiece. They apply to the work of Elena Ferrante, whose newly translated novel \"The Story of the Lost Child\" is the fourth and final one of her magnificent Neapolitan quartet, a sequence which now seems to me, at least within all that I've read, to be the greatest achievement in fiction of the post-war era.\"-Charles Finch, The Chicago Tribune\"We are dealing with masterpieces here, old-fashioned classics, filled with passion and pathos. [...] The sheer power of her books is a challenge to the chilly, dour craftsmanship of too many 21st century literary novels.\"-Joe Klein, TIME Magazine\"The saga is both comfortingly traditional and radically fresh, it gives readers not just what they want, but something more than they didn't know they craved...through this fusion of high and low art, Ms. Ferrante emerges as a 21st-century Dickens.\"-The Economist\"Ferrante's accomplishment in these novels is to extract an enduring masterpiece from dissolving margins, from the commingling of self and other, creator and created, new and old, real and whatever the opposite of real may be. [...] Ferrante's voice is very much her own, but it's force is communal. Perhaps her quartet should be seen as one of the first great works of post-authorial literature.\"-Judith Shulevitz, The Atlantic\"Ferrante [. . .] adumbrates the mysterious beauty and brutality of personal experience.\"-Rachel Cusk, The New York Times Book Review\"[. . .] with her new novel, \"The Story of the Lost Child,\" Ferrante has written what I'd call a \"city book,\" a knowing and complex tale that encompasses an entire metropolis. The breadth of vision makes this final installment feel like the essential volume.\"-John Domini, The Washington Post\"This stunning conclusion further solidifies the Neapolitan novels as Ferrante's masterpiece.\" -Publishers Weekly (starred review)\"Ferrante has created a mythic portrait of a female friendship in the chthonian world of postwar Naples.\"-Kirkus Reviews (starred review)\"Word of mouth launched this series, glowing reviews helped, and, eventually, a publishing phenomenon was born. The series' conclusion is a genuine literary event.\"-Booklist (starred review)Praise for The Neapolitan Novels\"Ferrante's Naples Quart","merchants_number":1,"ean":9781609452865,"category_id":103,"size":null,"min_price":23.25,"low_price_merchant_id":70255345,"ID":4394525,"merchants":["euniverse"],"brand":"undefined","slug":"the-story-of-the-lost-child","url":"\/unterhaltung\/produkt\/the-story-of-the-lost-child\/","low_price_merchant_name":"eUniverse"}
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Computer-Assisted Microscopy
1 Introduction.- The importance of images.- Why measure images?.- Computer methods: an overview.- Implementation.- Acquisition and processing of images.- Measurements within images.- More than two dimensions.- 2 Acquiring Images.- Image sources.- Multi-spectral images.- Image sensors.- Digitization.- Specifications.- References.- 3 Image Processing.- Point operations.- Time sequences.... zur Produkt-Seite
4798781 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvZDgvYTAvODkvNDI5NDAxNzYwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvZDgvYTAvODkvNDI5NDAxNzYwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"Computer-Assisted Microscopy","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781461278689&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F365419%2Fcomputer-assisted-microscopy-the-measurement-and-analysis-of-images%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"1 Introduction.- The importance of images.- Why measure images?.- Computer methods: an overview.- Implementation.- Acquisition and processing of images.- Measurements within images.- More than two dimensions.- 2 Acquiring Images.- Image sources.- Multi-spectral images.- Image sensors.- Digitization.- Specifications.- References.- 3 Image Processing.- Point operations.- Time sequences.- Correcting image defects - averaging to reduce noise.- Reducing noise in a single image.- Frequency space.- Color images.- Shading correction.- Fitting backgrounds.- Rubber sheeting.- Image sharpening.- Focussing images.- References.- 4 Segmentation of Edges and Lines.- Defining a feature and its boundary.- Roberts' cross edge operator.- The Sobel and Kirsch operators.- Other edge-finding methods.- Other segmentation methods.- The Hough transform.- Touching features.- Manual outlining.- References.- 5 Discrimination and Thresholding.- Brightness thresholds.- Thresholding after processing.- Selecting threshold settings.- The need for automatic thresholding.- Automatic methods.- Histogram minimum method.- Minimum area sensitivity method 1ll.- Minimum perimeter sensitivity method.- Reproducibility testing.- Fixed percentage setting.- Color images.- Encoding binary images.- Contiguity.- References.- 6 Binary Image Editing.- Manual editing.- Combining images.- Neighbor operations.- Skeletonization.- Measurement using binary image editing.- Covariance.- Watershed segmentation.- Mosaic amalgamation and fractal dimensions.- Contiguity and filling interior holes.- References.- 7 Image Measurements.- Reference areas.- Boundary curvature.- Feature measurements.- Perimeter points.- Length and breadth.- Radius of curvature.- Image processing approaches.- Counting neighbor patterns.- Shape.- Corners as a measure of shape.- Harmonic analysis.- Position.- Neighbor relationships.- Edge effects.- Brightness.- References.- 8 Stereological Interpretation of Measurement Data.- Global measurements.- Global parameters.- Mean free path.- Problems in 3-D interpretation.- Feature specific measurements.- Distribution histograms of size.- Interpreting distributions.- Nonparametric tests.- Cumulative plots.- Plotting shape and position data.- Other plots.- References.- 9 Object Recognition.- Locating features.- Parametric object description.- Distinguishing populations.- Decision points.- Other identification methods.- An example.- Comparing multiple populations.- An example of contextual learning.- Other applications.- Artificial intelligence.- References.- 10 Surface Image Measurements.- Depth cues.- Image contrast.- Shape from texture.- The scanning electron microscope.- Line width measurement.- Roughness and fractal dimensions.- Other surface measurement methods.- References.- 11 Stereoscopy.- Principles from human vision.- Measurement of elevation from parallax.- Presentation of the data.- Automatic fusion.- Stereoscopy in transparent volumes.- References.- 12 Serial Sections.- Obtaining serial section images.- Optical sectioning.- Presentation of 3-D image information.- Aligning slices.- Displays of outline images.- Surface modelling.- Measurements on surface-modelled objects.- Voxel displays.- Measurements on voxel images.- Network analysis.- Connectivity.- References.- 13 Tomography.- Reconstruction.- Instrumentation.- 3-D Imaging.- References.- 14 Lessons from Human Vision.- The language of structure.- Illusion.- Conclusion.- References.- For further reading.","merchants_number":1,"ean":9781461278689,"category_id":103,"size":null,"min_price":132.5,"low_price_merchant_id":70255345,"ID":4798781,"merchants":["euniverse"],"brand":"undefined","slug":"computer-assisted-microscopy","url":"\/unterhaltung\/produkt\/computer-assisted-microscopy\/","low_price_merchant_name":"eUniverse"}
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Reverse Chemical Genetics
Part I: The Importance of Fully-Characterized Genomic Resources and Informatics for Reverse Chemical Genetics 1. ORFeome Cloning Osamu Ohara 2. Systematic Cloning of an ORFeome Using the Gateway System Akihisa Matsuyama and Minoru Yoshida 3. High-Throughput Construction of ORF Clones for Production of the Recombinant Proteins Hisashi Yamakawa 4. Computational Overview of GPCR Gene... zur Produkt-Seite
4418804 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9pLndlbHRiaWxkLmRlL3AvcmV2ZXJzZS1jaGVtaWNhbC1nZW5ldGljcy0yNzM1OTU4NTQuanBn!aHR0cHM6Ly9pLndlbHRiaWxkLmRlL3AvcmV2ZXJzZS1jaGVtaWNhbC1nZW5ldGljcy0yNzM1OTU4NTQuanBnfH58aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYzUvMTkvMDQvMzYwMDc3MzgwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"Reverse Chemical Genetics","deeplink":"https:\/\/track.adtraction.com\/t\/t?a=1632201226&as=1592767275&t=2&tk=1&url=https:\/\/www.weltbild.ch\/artikel\/x\/_16118244-1","labels":[],"brand_id":1,"post_content":"Part I: The Importance of Fully-Characterized Genomic Resources and Informatics for Reverse Chemical Genetics 1. ORFeome Cloning Osamu Ohara 2. Systematic Cloning of an ORFeome Using the Gateway System Akihisa Matsuyama and Minoru Yoshida 3. High-Throughput Construction of ORF Clones for Production of the Recombinant Proteins Hisashi Yamakawa 4. Computational Overview of GPCR Gene Universe to Support Reverse Chemical Genomics Study Makiko Suwa and Yukiteru Ono 5. High-Performance Gene Expression Module Analysis Tool and Its Application to Chemical Toxicity Data Wataru Fujibuchi, Hyeryung Kim, Yoshifumi Okada, Takeaki Taniguchi, and Hideko Sone 6. Human Protein Reference Database and Human Proteinpedia as Discovery Tools for Systems Biology T.S. Keshava Prasad, Kumaran Kandasamy, and Akhilesh Pandey Part II: Modification of cDNA Resources Utilized for Reverse Chemical Genetics 7. High-Throughput Production of the Recombinant Proteins Expressed in Escherichia coli Utilizing cDNA Resources Kiyo Shimada and Hisashi Koga 8. An Insect Cell-Free System for Recombinant Protein Expression Using cDNA Resources Takashi Suzuki, Toru Ezure, Masaaki Ito, Masamitsu Shikata, and Eiji Ando 9. Recombinant Protein Production by a Kaiko-Baculovirus System Hidekazu Nagaya 10. Pulse-Chase Experiment for the Analysis of Protein Stability in Cultured Mammalian Cells by Covalent Fluorescent Labeling of Fusion Proteins Kei Yamaguchi, Shinichi Inoue, Osamu Ohara, and Takahiro Nagase Part III: The Refinement of Established Methods by Recent Innovations 11. Application of 2D-DIGE in Cancer Proteomics toward Personalized Medicine Tadashi Kondo and Setsuo Hirohashi 12. Fully Automated Two-Dimensional Electrophoresis System for High-Throughput Protein AnalysisAtsunori Hiratsuka and Kenji Yokoyama 13. Large-Scale Whole Mount In Situ Hybridization of Mouse Embryos Hirohito Shimizu, Kenta Uchibe, and Hiroshi Asahara 14. Identification of the Specific Binding Proteins of Bioactive Small Compound Using Affinity Resins Akito Tanaka Part IV: Potential Applicable Techniques for Reverse Chemical Genetics 15. Protein Microarrays: Effective Tools for the Study of Inflammatory Diseases Xiaobo Yu, Nicole Schneiderhan-Marra, Hsin-Yun Hsu, Jutta Bachmann, and Thomas O. Joos 16. Preparation of Highly Sensitive Protein Array Using Reactive Polymer Toshifumi Shiroya, Hiroyuki Tanaka, Minako Hanasaki, and Hisao Takeuchi 17. High-Throughput SPR Biosensor Motoki Kyo, Kimihiko Ohtsuka, Eiji Okamoto, and Kazuki Inamori 18. Drug Discovery through Functional Screening in the Drosophila Heart Takeshi Akasaka and Karen Ocorr 19. Permeable Cell Assay: A Method for High-Throughput Measurement of Cellular ATP Synthetic Activity Kiyotaka Y. Hara 20. Novel Methodology for Immobilization of Biomolecules on the Surface of a Photo-Responsible Polymer Containing Azobenzene Moiety Osamu Watanabe","merchants_number":2,"ean":9781607612315,"category_id":103,"size":null,"min_price":118,"low_price_merchant_id":27291482,"ID":4418804,"merchants":["weltbild","euniverse"],"brand":"undefined","slug":"reverse-chemical-genetics","url":"\/unterhaltung\/produkt\/reverse-chemical-genetics\/","low_price_merchant_name":"Weltbild"}
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Cholesterol Homeostasis
1. An Overview of Cholesterol Homeostasis Ingrid C. Gelissenand Andrew J. Brown 2. Hybrid In Silico/In Vitro Approaches for the Identification of Functional Cholesterol Binding Domains in Membrane Proteins Coralie Di Scala and Jacques Fantini 3. Structural Stringency of Cholesterol for Membrane Protein Function utilizing Stereoisomers as Novel Tools: A Review Md. Jafurulla and A... zur Produkt-Seite
4908926 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvMjIvN2YvNGYvNjA5ODQ2NzUwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvMjIvN2YvNGYvNjA5ODQ2NzUwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"Cholesterol Homeostasis","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493968732&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F377908%2Fcholesterol-homeostasis-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"1. An Overview of Cholesterol Homeostasis Ingrid C. Gelissenand Andrew J. Brown 2. Hybrid In Silico\/In Vitro Approaches for the Identification of Functional Cholesterol Binding Domains in Membrane Proteins Coralie Di Scala and Jacques Fantini 3. Structural Stringency of Cholesterol for Membrane Protein Function utilizing Stereoisomers as Novel Tools: A Review Md. Jafurulla and Amitabha Chattopadhyay 4. Manipulating Cholesterol Status within Cells Winnie Luu, Ingrid C. Gelissen, and Andrew J. Brown5. Assaying Low-Density-Lipoprotein (LDL) Uptake into Cells Anke Loregger, Jessica Kristine Nelson, and Noam Zelcer 6. The use of L-sIDOL Transgenic Mice as a Murine Model to Study Hypercholesterolaemia and Atherosclerosis Eser J. Zerenturk and Anna C. Calkin 7. CRISPR\/Cas9-mediated Generation of Niemann-Pick C1 Knockout Cell Line Ximing Du, Ivan Lukmantara, Hongyuan Yang 8. Quantitative Measurement of Cholesterol in Cell Population Using Flow Cytometry and Fluorescent Perfringolysin O* Jian Li, Peter L. Lee, and Suzanne R. Pfeffe 9. Transport Assays for Sterol-binding Proteins: Stopped-flow Fluorescence Methods for Investigating Intracellular Cholesterol Transport Mechanisms of NPC2 Protein Leslie A McCauliff1 and Judith Storch 10. Synthesis and Live-cell Imaging of Fluorescent Sterols for Analysis of Intracellular Cholesterol Transport Maciej Modzel, Frederik W. Lund, and Daniel W\u00fcstner 11. Measurement of Cholesterol Transfer from Lysosome to Peroxisomes Using an In Vitro Reconstitution Assay Jie Luo, Ya-Cheng Liao, Jian Xiao, and Bao-Liang Song 12. Measurement of Mitochondrial Cholesterol Import using a Mitochondria-targeted CYP11A1 Fusion Construct Barry Edward Kennedy, Mark Charman, and Barbara Karten 13. Identifying Sterol Response Elements within Promoters of Genes Laura J. Sharpe and Andrew J. Brown 14. Membrane Extraction of HMG CoA Reductase as Determined by Susceptibility of Lumenal Epitope to In Vitro Protease Digestion Lindsey L. Morris and Russell A. DeBose-Boyd 15. Determining the Topology of Membrane-bound Proteins using PEGylation Vicky Howeand Andrew J Brown 16. Measuring Activity of Cholesterol Synthesis Enzymes Using Gas Chromatography\/Mass Spectrometry Anika V. Prabhu, Winnie Luu, and Andrew J. Brown 17. Sterol Analysis by Quantitative Mass Spectrometry Andrew M. Jenner and Simon H.J. Brown 18. Measurement of Rates of Cholesterol and Fatty Acid Synthesis in vivo using Tritiated Water Adam M. Lopez, Jen-Chieh Chuang and Stephen D. Turley 19. Methods for Monitoring ABCA1-dependent Sterol Release Yoshio Yamauchi, Shinji Yokoyama, and Ta-Yuan Chang 20. ABC-transporter Mediated Sterol Export from Cells using Radio-Labeled Sterols Alryel Yang and Ingrid C. Gelissen21. Measurement of Macrophage-specific In Vivo Reverse Cholesterol Transport in Mice M. Kockx, W. Jessup and L. Kritharides","merchants_number":1,"ean":9781493968732,"category_id":103,"size":null,"min_price":153,"low_price_merchant_id":70255345,"ID":4908926,"merchants":["euniverse"],"brand":"undefined","slug":"cholesterol-homeostasis","url":"\/unterhaltung\/produkt\/cholesterol-homeostasis\/","low_price_merchant_name":"eUniverse"}
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The Mitotic Exit Network
Part I: Analysis of Cell Cycle Progression and Mitotic Exit 1. Regulation of Mitotic Exit in Saccharomyces cerevisiae Bàrbara Baro, Ethel Queralt, and Fernando Monje-Casas 2. Methods of Synchronization of Yeast Cells for the Analysis of Cell Cycle Progression M. Angeles Juanes 3. Analysis of Cell Cycle Progression in Saccharomyces cerevisiae Using the Budding Ind... zur Produkt-Seite
4908854 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvY2MvY2UvNGYvNTgzNzk4NDIwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvY2MvY2UvNGYvNTgzNzk4NDIwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"The Mitotic Exit Network","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493965007&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F377796%2Fthe-mitotic-exit-network-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Part I: Analysis of Cell Cycle Progression and Mitotic Exit\u00a01. Regulation of Mitotic Exit in Saccharomyces cerevisiae\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 B\u00e0rbara Baro, Ethel Queralt, and Fernando Monje-Casas\u00a02. Methods of Synchronization of Yeast Cells for the Analysis of Cell Cycle Progression\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 M. Angeles Juanes\u00a03. Analysis of Cell Cycle Progression in Saccharomyces cerevisiae\u00a0Using the Budding Index and Tubulin Staining\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Marta Mu\u00f1oz-Barrera and Fernando Monje-Casas\u00a04. Determination of Cell Cycle Stage and Mitotic Exit Through the Quantification of the Protein Levels of Known Mitotic Regulators\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Cristina Cepeda-Garc\u00eda\u00a05. Cdc14 Localization as a Marker for Mitotic Exit: In Vivo Quantitative Analysis of Cdc14 Release\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Gabriel Neurohr and Manuel Mendoza\u00a0Part II: Biochemistry of the MEN\u00a06. In Vitro Analysis of Tem1 GTPase Activity and Regulation by the Bfa1\/Bub2 GAP\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Marco Geymonat, Adonis Spanos, and Katrin Rittinger\u00a07. Analysis\u00a0of Protein-Protein Interactions Between MEN Components\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Rami Rahal\u00a08. A New Methodology for the Quantification of In Vivo Cdc14 Phosphatase Activity\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Ethel Queralt and Jos\u00e9-Antonio Rodriguez-Rodriguez\u00a09. Analysis of SUMOylation in the RENT Complex by Fusion to a SUMO-Specific Protease Domain\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Neus Colomina, Cl\u00e0udia Guasch, and Jordi Torres-Rosell\u00a010. A Substrate Trapping Method for Identification of Direct Cdc14 Phosphatase Targets\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Brendan L. Powers, Hana Hall, Harry Charbonneau, and Mark C. Hall\u00a0Part III: Analysis of the Localization of MEN Components\u00a011. Localizing MEN Components by Indirect Immunofluorescence Analysis of Budding Yeast\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Francesca Senic-Matuglia and Rosella Visintin\u00a012. Analysis of the Localization of MEN Components by Live Cell Imaging Microscopy\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Zhiang Guo and Marisa Segal\u00a013. Evaluation of the Dynamicity of Mitotic Exit Network and Spindle Position Checkpoint Components on Spindle Pole Bodies by Fluorescence Recovery After Photobleaching (FRAP)\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Ayse Koca Caydasi and Gislene Pereira\u00a014. Asymmetric Localization of Components and Regulators of the Mitotic Exit Network at Spindle Pole Bodies\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Ilaria Scarfone and Simonetta Piatti\u00a015. Evaluation of the Nucleolar Localization of the RENT Complex to Ribosomal DNA by Chromatin Immunoprecipitation Assays\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Julie Huang, Nahid Iglesias, and Danesh Moazed\u00a0Part IV: Control of Cellular Processes by the MEN\u00a016. Analysis of the Functionality of the Mitotic Checkpoints\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Roberta Fraschini\u00a017. Cdc14 and Chromosome Condensation: Evaluation of the Recruitment of Condensin to Genomic Regions\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Facundo Ramos, Joanne Leonard, Andr\u00e9s Clemente-Blanco, and Luis Arag\u00f3n\u00a018. Studying the Role of the Mitotic Exit Network in Cytokinesis\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Magdalena Foltman and Alberto Sanchez-Diaz\u00a0Part V: Final Remarks: The MEN as a Model for Higher Eukaryotes\u00a019. Hippo Signaling in Mitosis: An Updated View in Light of the MEN Pathway\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Alexander Hergovich","merchants_number":1,"ean":9781493965007,"category_id":103,"size":null,"min_price":153,"low_price_merchant_id":70255345,"ID":4908854,"merchants":["euniverse"],"brand":"undefined","slug":"the-mitotic-exit-network","url":"\/unterhaltung\/produkt\/the-mitotic-exit-network\/","low_price_merchant_name":"eUniverse"}
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Current Views of Fatty Acid Oxidation and Ketogenesis
Preface & Dedication, P.A. Quant, S. Eaton. Historical overview. Cambridge, colleagues, carnitine and ketogenesis ......., P.K. Tubbs. Carnitine and carnitine acyltransferases. 1. Biogenesis of the rat liver mitochondrial carnitine palmitoyltransferase I, I. Cohen, et al. 2. Subcellular distribution of mitochondrial carnitine palmitoyltransferase I in rat liver: Evidence for a d... zur Produkt-Seite
4917854 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvMjUvZGYvMzUvMjMzMTEyMjAwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvMjUvZGYvMzUvMjMzMTEyMjAwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"Current Views of Fatty Acid Oxidation and Ketogenesis","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9780306462009&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F356478%2Fcurrent-views-of-fatty-acid-oxidation-and-ketogenesis-from-organelles-to-point-mutations%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Preface & Dedication, P.A. Quant, S. Eaton. Historical overview. Cambridge, colleagues, carnitine and ketogenesis ......., P.K. Tubbs. Carnitine and carnitine acyltransferases. 1. Biogenesis of the rat liver mitochondrial carnitine palmitoyltransferase I, I. Cohen, et al. 2. Subcellular distribution of mitochondrial carnitine palmitoyltransferase I in rat liver: Evidence for a distinctive N-terminal structure of the microsomal but not the peroxisomal enzyme, V.A. Zammit,et al. 3. Topology of hepatic mitochondrial carnitine palmitoyltransferase I, K. Kashfi, G.A. Cook. 4. Possible involvement of cytoskeletal components in the control of hepatic carnitine palmitoyltransferase I activity, G. Velasco, et al. 5. Regulation of beta-oxidation and CPT I activity by 3-thia fatty acids in cultured rat hepatocytes, J. Sleboda, J. Bremer. 6. Carnitine acyltransferases and associated transport systems in the endoplasmic reticulum, N.M. Broadway, et al. 7. Reciprocal enzymatic interference of carnitine palmitoyl transferase I and glycerol-3-phosphate acyltransferase in purified liver mitochondria, F. Beauseigneur, et al. 8. Control of human muscle carnitine palmitoyltransferase I gene transcription by peroxisome proliferator-activated receptor , C. Mascar\u00f3, et al. 9. Kinetic investigation of carnitine palmitoyltransferases in homogenates of human skeletal muscle using L-aminocarnitine and malonyl-CoA, K. Hertel, et al. 10. Processing of carnitine octanoyltransferase pre-mRNAs by cis- and trans-splicing, C. Caudevilla, et al. 11. Selective modulation of carnitine long-chain acyltransferase activities: kinetics, inhibitors andactive sites of COT and CPT II, R.R. Ramsay, R.D. Gandour. 12. Confocal laser scanning microscopy of human skin fibroblasts showing transient expression of a green fluorescent carnitine palmitoyltransferase 1 fusion protein, F.R. van der Leij, et al. 13. Carnitine biosynthesis: purification of gamma-butyrobetaine from rat liver, F. Vaz, et al. Mitochondrial fatty acid oxidation and ketogenesis. 14. Hypolipidemic 3-thia fatty acids: Fatty acid oxidation and ketogenesis in rat liver under proliferation of mitochondria and peroxisomes, R.K. Berge, et al. 15. Molecular mechanisms of fatty acid &bgr,-oxidation enzyme catalysis, S.-Y. Yang, X.-Y. He. 16. Control of mitochondrial &bgr,-oxidation at the level of [NAD+]\/[NADH] and CoA acylation, S. Eaton, et al. 17. Production and export of acyl-carnitine esters by neonatal rat hepatocytes, S. Eaton, et al. 18. Tissue specific differences in intramitochondrial control of &bgr,-oxidation, S. Eaton, K. Bartlett. 19. Endotoxin-induced changes in very-low-density lipoprotein and myocardial utilisation of triacylglycerol from abnormal VLDL in the rat, D.G. Hole, et al. 20. Effect of valproic acid on the expression of acyl-CoA dehydrogenases in various tissues, M. Nagao, et al. 21. Formation of a human `electron transferring flavoprotein': medium chain acyl CoA dehydrogenase complex - preliminary evidence from crosslinking studies, A. Parker, P.C. Engel. 22. Cloning and regulation of peroxisome proliferator-induced acyl-CoA thioestereases from mouse liver, M. Hunt, et al. 23. Metabolic effects of 3-thia fatty acids in cancer cells, K.J. Tronstad,","merchants_number":1,"ean":9780306462009,"category_id":103,"size":null,"min_price":239,"low_price_merchant_id":70255345,"ID":4917854,"merchants":["euniverse"],"brand":"undefined","slug":"current-views-of-fatty-acid-oxidation-and-ketogenesis","url":"\/unterhaltung\/produkt\/current-views-of-fatty-acid-oxidation-and-ketogenesis\/","low_price_merchant_name":"eUniverse"}
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Exploring the World with the Laser
From quantum transitions to electronic motions (Mandy Singh, MPI Quantum Optics, Garching, Germany).- Nonadiabatic molecular alignment of linear molecules probed by photoelectron ionization yields (Hans Schüssler, Texas A&M Univ, USA).- Ultracold metastable helium: Ramsey fringes and atom interferometry (Wim Vassen, Vrije Universiteit, Amsterdam, Netherlands).- Monolayer graphene as d... zur Produkt-Seite
4838933 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvN2IvNGEvNzMvNjUwODE1NTUwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvN2IvNGEvNzMvNjUwODE1NTUwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9leHBsb3JpbmctdGhlLXdvcmxkLXdpdGgtdGhlLWxhc2VyLTI3NTA5MTU4MS5qcGc=","post_title":"Exploring the World with the Laser","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9783319643458&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fphysik-astronomie%2F462858%2Fexploring-the-world-with-the-laser-dedicated-to-theodor-haensch-on-his-75th-birthday%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"From quantum transitions to electronic motions (Mandy Singh, MPI Quantum Optics, Garching, Germany).- Nonadiabatic molecular alignment of linear molecules probed by photoelectron ionization yields (Hans Sch\u00fcssler, Texas A&M Univ, USA).- Ultracold metastable helium: Ramsey fringes and atom interferometry (Wim Vassen, Vrije Universiteit, Amsterdam, Netherlands).- Monolayer graphene as dissipative membrane in an optical resonator (Michael K\u00f6hl, Univ Cambridge , UK \/ Univ Bonn, Germany).- Cavity ring-up spectroscopy for dissipative and dispersive sensing in a whispering gallery mode resonator (S\u00edle Nic Chormaic, Okinawa Univ, Japan).- Quantum electrodynamics, high-resolution spectroscopy, and fundamental constants (Savely G. Karshenboim, Mendeleev Institute for Metrology, Russia).- Yb fiber amplifier at 972.5 nm with frequency quadrupling to 243.1 nm (Cory Rasor, Colorado Univ, USA).- Absorption spectroscopy of xenon and ethylene-noble gas mixtures at high pressure: Towards Bose-Einstein condensation of vacuum ultraviolet photons (Christian Wahl, Univ Bonn, Germany).- Ranging with frequency-shifted feedback lasers: from $\\mu$m-range accuracy to MHz-range measurement rate (Leonid Yatsenko, Nat. Acad. Sc. Ukraine \/ Kiew Univ, Ukraine).- Laser phase spectroscopy in closed-loop multilevel schemes (Ennio Arimondo, Univ Pisa, Italy).- Sensitivity and resolution in frequency comb spectroscopy of buffer gas cooled polyatomic molecules (Bryan Changala, Nat. Inst. of Standards (NIST) \/ Colorado Univ, USA).- Precision measurements and test of molecular theory in highly-excited vibrational states of H_2 _(v=11) (Edcel Salumbides, Vrije Universiteit, Amsterdam, Netherlands).- Quantum regime of a free-electron laser: relativistic approach (Peter Kling, Helmholtz-Center, Dresden, Germany).- Coherence in laser-driven electrons at and in solid matter (Peter Hommelhoff, Univ Erlangen, Germany).- Unexpectedly large difference of the electron density at the nucleus in the 4p 2P1\/2,3\/2 fine-structure doublet of Ca+ (Piet O. Schmidt, Inst. Experiment. Quantum Metrology, PTB, Braunschweig, Germany).- A 10^15 watt laser for DT Fusion Experiments at Livermore (John F. Holzrichter, Lawrence Livermore Nat Lab \/ Stanford Univ, USA).- Extraction of enhanced, ultrashort laser pulses from a passive 10-MHz stack-and-dump cavity (Sven Breitkopf, Univ Jena, Germany).- Adjacency Graphs and Long-Range Interactions of Atoms in Quasi-Degenerate States: Applied Graph Theory (Ulrich Jentschura, Missouri Univ, USA).- External Cavity Diode Laser Setup with Two Interference Filters (Patrick Baus. Univ Darmstadt, Germany).- Phase-stable, multi-\u00b5J femtosecond pulses from a repetition-rate tuneable Ti:Sa-oscillator-seeded Yb-fiber amplifier (Tobias Saule, Munich Univ (LMU), Germany).- High-precision spectroscopy of the HD+ molecule at the 1-p.p.b. level (Jeroen Koelemeij, Vrije Universiteit, Amsterdam, Netherlands).- Bose-Einstein condensates in an optical cavity with sub-recoil bandwidth (Andreas Hemmerich, Univ Hamburg, Germany).- Ultrafast optomechanical pulse picking (Nikolai Lilienfein, Munich Univ (LMU), Germany).- Parity-nonconserving interaction induced light shifts in the 7S_{1\/2} - 6D_{3\/2} transition of the ultracold Fr-210 atoms to probe new physics beyond the standard model (Takatoshi Aoki, Univ Tokio, Japan).- High-accuracy deep-UV Ramsey-comb spectroscopy in krypton (Robert Karl Altmann, Vrije Universiteit, Amsterdam, Netherlands).- Optical Autler-Townes spectroscopy in a heteronuclear mixture of laser-cooled atoms (Axel G\u00f6rlitz, Univ D\u00fcsseldorf, Germany).- A compact echelle spectrograph for characterization of astro-combs (Rafael Andreas Probst, MPI Quantum Optics, Garching, Germany).- Measuring and imaging nanomechanical motion with laser light (Albert Schliesser, Copenhagen Univ, Denmark).- Shifting the phase of a coherent beam with a Yb-174 ion: influence of the scattering cross section (Markus Sondermann, MPI Science of Light, Erlangen).- Orientational dependence of optically detected magnetic resonance signals in laser-driven atomic magnetometers (Simone Colombo, Univ Fribourg, Switzerland).- T^3-interferometer for atoms (Maxim Efremov, Inst. Quantum Physics, Ulm Univ, Germany).- Playing tricks to ions (Dietrich Leibfried, Nat. Inst. of Standards (NIST) \/ Colorado Univ, USA).- Frequency-comb based collinear laser spectroscopy of Be for nuclear structure investigations and many-body QED tests (Wilfried N\u00f6rtersh\u00e4user, Univ Darmstadt, Germany).- Index.","merchants_number":2,"ean":9783319643458,"category_id":103,"size":null,"min_price":157,"low_price_merchant_id":70255345,"ID":4838933,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"exploring-the-world-with-the-laser","url":"\/unterhaltung\/produkt\/exploring-the-world-with-the-laser\/","low_price_merchant_name":"eUniverse"}
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Characterization of Nanoparticles Intended for Drug Delivery
Preface Table of Contents... Contributing Authors... Part I Introduction 1. Evaluating Nanomedicines: Obstacles and Advancements Magdalena Swierczewska, Rachael M. Crist, and Scott E. McNeil Part II Sterility and Endotoxin Testing 2. Detection of Bacterial Contamination in Nanoparticle Formulations by Agar Plate Test Timothy M. Potter, Barry W. Neun, Anna N. Ilinskaya, and Marina A.... zur Produkt-Seite
4909145 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYTcvYTAvYmIvNjQ4OTQ2MjMwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYTcvYTAvYmIvNjQ4OTQ2MjMwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9jaGFyYWN0ZXJpemF0aW9uLW9mLW5hbm9wYXJ0aWNsZXMtaW50ZW5kZWQtZm9yLWRydWctMjczNTQ3NzI4LmpwZw==","post_title":"Characterization of Nanoparticles Intended for Drug Delivery","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493973507&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fmedizin-pharmazie%2F378044%2Fcharacterization-of-nanoparticles-intended-for-drug-delivery-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Preface Table of Contents... Contributing Authors... Part I Introduction 1. Evaluating Nanomedicines: Obstacles and Advancements Magdalena Swierczewska, Rachael M. Crist, and Scott E. McNeil Part II Sterility and Endotoxin Testing 2. Detection of Bacterial Contamination in Nanoparticle Formulations by Agar Plate Test Timothy M. Potter, Barry W. Neun, Anna N. Ilinskaya, and Marina A. Dobrovolskaia 3. Considerations and Some Practical Solutions to Overcome Nanoparticle Interference with LAL Assays and to Avoid Endotoxin Contamination in Nanoformulations Barry W. Neun and Marina A. Dobrovolskaia Part III Physicochemical Characterization 4. Elemental Analysis in Biological Matrices Using ICP-MS Matthew N. Hansen and Jeffrey D. Clogston 5. PEG Quantitation Using Reversed Phase High Performance Liquid Chromatography and Charged Aerosol Detection Mackensie C. Smith and Jeffrey D. Clogston 6. Quantitation of Surface Coating on Nanoparticles Using Thermogravimetric Analysis Alpana A. Dongargaonkar and Jeffrey D. Clogston 7. Immunoelectron Microscopy for Visualization of Nanoparticles Sarah R. Anderson, David Parmiter, Ulrich Baxa, and Kunio Nagashima 8. Imaging of Liposomes by Transmission Electron Microscopy Ulrich Baxa Part IV Immunology 9. Updated Method for In Vitro Analysis of Nanoparticle Hemolytic Properties Barry W. Neun, Anna N. Ilinskaya, and Marina A. Dobrovolskaia 10. In Vitro Assessment of Nanoparticle Effects on Blood Coagulation Timothy M. Potter, Jamie C. Rodriguez, Barry W. Neun, Anna N. Ilinskaya, Edward Cedrone, and Marina A. Dobrovolskaia 11. In Vitro Analysis of Nanoparticle Effects on the Zymosan Uptake by Phagocytic Cells Timothy M. Potter, Sarah L. Skoczen, Jamie C. Rodriguez, Barry W. Neun, Anna N. Ilinskaya, Edward Cedrone, and Marina A. Dobrovolskaia 12. Assessing NLRP3 Inflammasome Activation by Nanoparticles Bhawna Sharma, Christopher B. McLeland, Timothy M. Potter, Stephan T. Stern, and Pavan P. Adiseshaiah 13. Analysis of Complement Activation by Nanoparticles Barry W. Neun, Anna A. Ilinskaya, and Marina A. Dobrovolskaia 14. Methods for Analysis of Nanoparticle Immunosuppressive Properties In Vitro and In Vivo Timothy M. Potter, Barry W. Neun, and Marina A. Dobrovolskaia 15. Analysis of Pro-Inflammatory Cytokine and Type II Interferon Induction by Nanoparticles Timothy M. Potter, Barry W. Neun, Jamie C. Rodriguez, Anna N. Ilinskaya, and Marina A. Dobrovolskaia 16. Analysis of Nanoparticle Adjuvant Properties In Vivo Barry W. Neun and Marina A. Dobrovolskaia 17. In Vitro and In Vivo Methods for Analysis of Nanoparticle Potential to Induce Delayed Type Hypersensitivity Reactions Timothy M. Potter, Barry W. Neun, and Marina A. Dobrovolskaia 18. Autophagy Monitoring Assay II: Imaging Autophagy Induction in LLC-PK1 Cells Using GFP-LC3 Protein Fusion Construct Pavan P. Adiseshaiah, Sarah L. Skoczen, Jamie C. Rodriguez, Timothy M. Potter, Krishna Kota, and Stephan T. Stern Part V Drug Release and In Vivo Efficacy 19. Improved Ultrafiltration Method to Measure Drug Release from Nanomedicines Utilizing a Stable Isotope Tracer Sarah L. Skoczen and Stephan T. Stern 20. Designing an In Vivo Efficacy Study of Nanomedicines for Preclinical Tumor Growth Inhibition Pavan P. Adiseshaiah and Stephan T. Stern","merchants_number":2,"ean":9781493973507,"category_id":103,"size":null,"min_price":157,"low_price_merchant_id":70255345,"ID":4909145,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"characterization-of-nanoparticles-intended-for-drug-delivery-1","url":"\/unterhaltung\/produkt\/characterization-of-nanoparticles-intended-for-drug-delivery-1\/","low_price_merchant_name":"eUniverse"}
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Primate Craniofacial Function and Biology
I. Historical perspective on Experimental Research in Biological Anthropology 1. Experimental Comparative Anatomy in Physical Anthropology: The Contributions of Dr. William Hylander to Studies of Skull Form and Function. Daniel Schmitt, Christine E. Wall, and Pierre Lemelin II. In Vivo Research Into Masticatory Function 2. A nonprimate model for the fused symphysis: in vivo studies ... zur Produkt-Seite
4841933 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNDMvMjIvNjUvMjI2Njg4MTgwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNDMvMjIvNjUvMjI2Njg4MTgwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"Primate Craniofacial Function and Biology","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9780387765846&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F418183%2Fprimate-craniofacial-function-and-biology%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"I. Historical perspective on Experimental Research in Biological Anthropology 1. Experimental Comparative Anatomy in Physical Anthropology: The Contributions of Dr. William Hylander to Studies of Skull Form and Function. Daniel Schmitt, Christine E. Wall, and Pierre Lemelin II. In Vivo Research Into Masticatory Function 2. A nonprimate model for the fused symphysis: in vivo studies in the pig. Susan W. Herring, Katherine L. Rafferty, Zi Jun Liu, and Zongyang Sun 3. Symphyseal fusion in selenodont artiodactyls: new insights from in vivo and comparative data. Susan H. Williams, Christine E. Wall, Christopher J. Vinyard, William L. Hylander 4. Does the primate face torque? Callum F. Ross 5. Motor control of masticatory movements in the Southern hairy-nosed wombat (Lasiorhinus latifrons). Alfred W. Crompton, Daniel E. Lieberman, Tomasz Owerkowicz, Russell V. Baudinette and Jayne Skinner 6. Specialization of the Superficial Anterior Temporalis in Baboons for Mastication of Hard Foods. Christine E. Wall, Christopher J. Vinyard, Susan H. Williams, Kirk R. Johnson, William L. Hylander III. Modeling Masticatory Apparatus Function 7. Effects of Dental Alveoli on the Biomechanical Behavior of the Mandibular Corpus. David J. Daegling, Jennifer L. Hotzman and Andrew J. Rapoff 8. Surface strain on bone and sutures in a monkey facial skeleton: an in vitro approach and its relevance to Finite Element Analysis. Qian Wang, Paul C. Dechow, Barth W. Wright, Callum F. Ross, David S. Strait, Brian G. Richmond, Mark A. Spencer and Craig D. Byron. 9. Craniofacial Strain Patterns During Premolar Loading: Implications for Human Evolution. David S. Strait, Barth Wright, Brian G. Richmond, Callum F. Ross, Paul C. Dechow, Mark A. Spencer, Qian Wang. IV. Jaw-Muscle Architecture 10. Scaling of reduced physiologic cross-sectional area in primate muscles of mastication. Fred Anapol, Nazima Shahnoor and Callum F. Ross 11. Scaling of the Chewing Muscles in Prosimians. Jonathan M.G. Perry and Christine E. Wall 12. The relationship between jaw-muscle architecture and feeding behavior in primates: Tree-gouging and nongouging gummivorous callitrichids as a natural experiment. Andrea B. Taylor and Christopher J. Vinyard V. Bone and Dental Morphology 13. Relationship between three dimensional microstructure and elastic properties of cortical bone in the human mandible and femur. Paul C. Dechow, Dong Hwa Chung, and Mitra Bolouri 14. Adaptive plasticity in the mammalian masticatory complex: You are what, and how, you eat. Matthew J. Ravosa, Ravinder Kunwar, Elisabeth K. Nicholson, Emily B. Klopp, Jessie Pinchoff, Stuart R. Stock, M. Sharon Stack, and Mark W. Hamrick 15. Mandibular corpus form and its functional significance: Evidence from marsupials. Aaron S. Hogue 16. Putting shape to work: Making functional interpretations of masticatory apparatus shapes in primates. Christopher J. Vinyard 17. Food physical properties and their relationship to morphology: The curious case of kily. Nayuta Yamashita 18. Convergence and frontation in Fayum anthropoid orbits. Elwyn L. Simons 19. What else is the tall mandibular ramus of the robust australopiths good for? Yoel Rak and William L. Hylander 20. Framing the question: Diet and evolution in early Homo. Susan C. Ant\u00f3n","merchants_number":1,"ean":9780387765846,"category_id":103,"size":null,"min_price":299,"low_price_merchant_id":70255345,"ID":4841933,"merchants":["euniverse"],"brand":"undefined","slug":"primate-craniofacial-function-and-biology","url":"\/unterhaltung\/produkt\/primate-craniofacial-function-and-biology\/","low_price_merchant_name":"eUniverse"}
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Bacterial Protein Secretion Systems
1. Identification of Protein Secretion Systems in Bacterial Genomes using MacSyFinder Sophie S Abby and Eduardo PC Rocha 2. Protein Sorting Prediction Henrik Nielsen 3. Cell FractionationMelissa Petiti, Laetitia Houot, and Denis Duché 4. Defining Lipoprotein Localisation by Fluorescence MicroscopyMaria Guillermina Casabona, Mylène Robert-Genthon, Didier Grunwald, and Ina Attrée 5... zur Produkt-Seite
4419596 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNjcvYTMvMzUvNjUwNzkyNjMwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNjcvYTMvMzUvNjUwNzkyNjMwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9iYWN0ZXJpYWwtcHJvdGVpbi1zZWNyZXRpb24tc3lzdGVtcy0yNzM1NDU3MTcuanBn","post_title":"Bacterial Protein Secretion Systems","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493970315&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F377956%2Fbacterial-protein-secretion-systems-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"1. Identification of Protein Secretion Systems in Bacterial Genomes using MacSyFinder Sophie S Abby and Eduardo PC Rocha\u00a02. Protein Sorting Prediction\u00a0 Henrik Nielsen\u00a0 \u00a03. Cell FractionationMelissa Petiti, Laetitia Houot, and Denis Duch\u00e9 \u00a04. Defining Lipoprotein Localisation by Fluorescence MicroscopyMaria Guillermina Casabona, Myl\u00e8ne Robert-Genthon, Didier Grunwald, and Ina Attr\u00e9e \u00a05. Components Sub-cellular Localization: Identification of Lipoproteins using Globomycin and Radioactive PalmitateNienke Buddelmeijer \u00a06. Defining Membrane Protein Localization by Isopycnic Density GradientsRhys A. Dunstan, Iain D. Hay, and Trevor Lithgow\u00a07. Components Sub-cellular Localisation: Cell Surface ExposureAnna Konovalova\u00a08. Probing Inner Membrane Protein Topology by ProteolysisMaxence S. Vincent and Eric Cascales\u00a09. Mapping of Membrane Protein Topology by Substituted Cysteine Accessibility Method (SCAMTM)Mikhail Bogdanov\u00a010. Defining Membrane Protein Topology using pho-lac Reporter FusionsGouzel Karimova and Daniel Ladant\u00a011. In vivo and in vitro Protein-peptidoglycan InteractionsGang Li and S. Peter Howard\u00a012. Measure of Peptidoglycan Hydrolase ActivityYoann G. Santin and Eric Cascales\u00a013. Protein-protein Interaction: Bacterial Two-Hybrid Gouzel Karimova, Emilie Gauliard, Marilyne Davi, Scot P. Ouellette, and Daniel Ladant\u00a014. Protein-protein Interactions: Yeast two-hybridJer-Sheng Linand Erh-Min Lai\u00a015. Protein-protein Interactions: Cytology Two-hybridKrishnamohan Atmakuri\u00a016. Fusion Reporter Approaches to Monitor Transmembrane Helix Interactions in Bacterial MembranesLaureen Logger, Abdelrahim Zoued, and Eric Cascales17. Protein-protein Interactions: Co-immunoprecipitationJer-Sheng Linand Erh-Min Lai\u00a018. Protein-protein Interaction: Tandem Affinity Purification in BacteriaJulie P.M. Viala and Emmanuelle Bouveret\u00a019. Site-directed and Time-resolved Photocrosslinking in Cells Metabolically Labeled With Radioisotopes Raffaele Ieva\u00a020. Protein-protein Interactions: Pull-down Assays Arthur Louche, Suzana P. Salcedo, and Sarah Bigot\u00a021. Protein-protein interactions: Surface Plasmon ResonanceBadreddine Douzi\u00a022. Assessing Energy-dependent Protein Conformational Changes in the TonB SystemRay A. Larsen\u00a023. Defining Assembly Pathways by Fluorescence MicroscopyAbdelrahim Zouedand Andreas Diepold\u00a024. Large Complexes: Cloning Strategy, Production, and PurificationEric Durand and Roland Lloubes \u00a025. Shearing and Enrichment of Extracellular Type IV PiliAlba Katiria, Gonzalez Rivera, and Katrina T. Forest\u00a026. Blue Native PAGE Analysis of Bacterial Secretion ComplexesSusann Zilkenat, Tobias Dietsche, Julia V. Monjar\u00e1s Feria, Claudia E. Torres-Vargas, Mehari Tesfazgi Mebrhatu, and Samuel Wagner\u00a027. In situ Imaging of Bacterial Secretion Systems by Electron Cryo-tomographyGregor L. Weiss, Jo\u00e3o M. Medeiros, and Martin Pilhofer\u00a028. Structural Analysis of Protein Complexes by Cryo Electron MicroscopyTiago R. D. Costa, Athanasios Ignatiou, and Elena V. Orlova \u00a029. Bacterial Filamentous Appendages Investigated by Solid-state NMR SpectroscopyBirgit Habenstein and Antoine Loquet\u00a030. Identification\u00a0of Effectors:\u00a0 Precipitation of Supernatant MaterialNicolas Flaugnatti and Laure Journet\u00a031. Energy Requirements for Protein Secretion via the Flagellar type-III Secretion SystemMarc Erhardt\u00a032. Screening for Secretion of the Type VI Secretion Protein Hcp by Enzyme-Linked Immunosorbent Assay and Colony BlotBrent S. Weber, Pek Man Ly, and Mario F. Feldman33. Effector Translocation: Cya\u00a0Reporter AssaySuma Chakravarthy, Bethany Huot, and Brian H. Kvitko\u00a034. Monitoring Effector Translocation with the TEM-1 Beta-lactamase Reporter SystemJulie Allombert, Anne Vianney, and Xavier Charpentier\u00a035. Effector Translocation Assay: Differential SolubilizationIrina S. Franco, Sara V. Pais, Nuno Charro, and Lu\u00eds Jaime Mota\u00a036. Quantitative Determination of Anti-bacterial Activity during Bacterial Co-cultureJuliana Alcoforado Diniz, Birte Hollmann, and Sarah Coulthurst","merchants_number":2,"ean":9781493970315,"category_id":103,"size":null,"min_price":211,"low_price_merchant_id":70255345,"ID":4419596,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"bacterial-protein-secretion-systems","url":"\/unterhaltung\/produkt\/bacterial-protein-secretion-systems\/","low_price_merchant_name":"eUniverse"}
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Fundamentals of Plasma Physics
CONTENTS 1. General Properties of Plasmas 1.1 Definition of a Plasma 1.2 Plasma as the Fourth State of Matter 1.3 Plasma Production 1.4 Particle Interactions and Collective Effects 1.5 Some Basic Plasma Phenomena 2. Criteria for the De.nition of a Plasma 2.1 Macroscopic Neutrality 2.2 Debye Shielding 2.3 The Plasma Frequency 3. The Occurrence of Plasmas in Nature 3.1 The Sun ... zur Produkt-Seite
4912187 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNDgvNTcvYTkvMTI5OTM2NTAwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNDgvNTcvYTkvMTI5OTM2NTAwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"Fundamentals of Plasma Physics","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9780387209753&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fphysik-astronomie%2F196911%2Ffundamentals-of-plasma-physics%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"CONTENTS 1. General Properties of Plasmas 1.1 Definition of a Plasma 1.2 Plasma as the Fourth State of Matter 1.3 Plasma Production 1.4 Particle Interactions and Collective Effects 1.5 Some Basic Plasma Phenomena 2. Criteria for the De.nition of a Plasma 2.1 Macroscopic Neutrality 2.2 Debye Shielding 2.3 The Plasma Frequency 3. The Occurrence of Plasmas in Nature 3.1 The Sun and its Atmosphere 3.2 The Solar Wind 3.3 The Magnetosphere and the Van Allen Radiation Belts 3.4 The Ionosphere 3.5 Plasmas Beyond the Solar System 4. Applications of Plasma Physics 4.1 Controlled Thermonuclear Fusion 4.2 The Magnetohydrodynamic Generator 4.3 Plasma Propulsion 4.4 Other Plasma Devices 5. Theoretical Description of Plasma Phenomena 5.1 General Considerations on a Self-Consistent Formulation 5.2 Theoretical Approaches Problems 1. Introduction 2. Energy Conservation 3. Uniform Electrostatic Field 4. Uniform Magnetostatic Field 4.1 Formal Solution of the Equation of Motion 4.2 Solution in Cartesian Coordinates 4.3 Magnetic Moment 4.4 Magnetization Current 5. Uniform Electrostatic and Magnetostatic Fields 5.1 Formal Solution of the Equation of Motion 5.2 Solution in Cartesian Coordinates 6. Drift Due to an External Force Problems 1. Introduction 2. Spatial Variation of the Magnetic Field 2.1 Divergence Terms 2.2 Gradient and Curvature Terms 2.3 Shear Terms 3. Equation of Motion in the First Order Approximation 4. Average Force Over One Gyration Period 4.1 Parallel Force 4.2 Perpendicular Force 4.3 Total Average Force 5. Gradient Drift 6. Parallel Acceleration of the Guiding Center 6.1 Invariance of the Orbital Magnetic Moment and of the Magnetic Flux 6.2 Magnetic Mirror Effect 6.3 The Longitudinal Adiabatic Invariant 7. Curvature Drift 8. Combined Gradient-Curvature Drift Problems 1. Introduction 2. Slowly Time-Varying Electric Field 2.1 Equation of Motion and Polarization Drift 2.2 Plasma Dielectric Constant 3. Electric Field with Arbitrary Time Variation 3.1 Solution of the Equation of Motion 3.2 Physical Interpretation 3.3 Mobility Dyad 3.4 Plasma Conductivity Dyad 3.5 Cyclotron Resonance 4. Time-Varying Magnetic Field and Space-Varying Electric Field 4.1 Equation of Motion and Adiabatic Invariants 4.2 Magnetic Heating of a Plasma 5. Summary of Guiding Center Drifts and Current Densities 5.1 Guiding Center Drifts 5.2 Current Densities Problems 1. Introduction 2. Phase Space 2.1 Single-Particle Phase Space 2.2 Many-Particle Phase Space 2.3 Volume Elements 3. Distribution Function 4. Number Density and Average Velocity 5. The Boltzmann Equation 5.1 Colisionless Boltzmann Equation 5.2 Jacobian of the Transformation in Phase Space 5.3 E.ects of Particle Interactions 6. Relaxation Model for the Collision Term 7. The Vlasov Equation Problems 1. Average Value of a Physical Quantity 2. Average Velocity and Peculiar Velocity 3. Flux 4. Particle Current Density 5. Momentum Flow Dyad or Tensor 6. Pressure Dyad or Tensor 6.1 Concept of Pressure 6.2 Force per Unit Area 6.3 Force per Unit Volume 6.4 Scalar Pressure and Absolute Temperature 7. Heat Flow Vector 8. Heat Flow Triad 9. Total Energy Flux Triad 10. Higher Moments of the Distribution Function Problems 1. The Equilibrium State Distribution Function 1.1 The General Principle of Detailed Balance and Binary Collisions 1.2 Summation Invariants 1.3 Maxwell-Boltzmann Distribution Function 1.4 Determination of the Constant Coe.cients 1.5 Local Maxwell-Boltzmann Distribution Function 2. The Most Probable Distribution 3. M","merchants_number":1,"ean":9780387209753,"category_id":103,"size":null,"min_price":111,"low_price_merchant_id":70255345,"ID":4912187,"merchants":["euniverse"],"brand":"undefined","slug":"fundamentals-of-plasma-physics","url":"\/unterhaltung\/produkt\/fundamentals-of-plasma-physics\/","low_price_merchant_name":"eUniverse"}
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Glycosylation Engineering of Biopharmaceuticals
Part I: Glyco-Engineering of Therapeutic Proteins 1. Engineering of Therapeutic and Diagnostic O-Glycans on Recombinant Mucin-Type Immunoglobulin Fusion Proteins Expressed in CHO Cells Linda Lindberg, Jining Liu, and Jan Holgersson 2. Engineering a Human-Like Glycosylation to Produce Therapeutic Glycoproteins Based on 6-Linked Sialylation in CHO Cells Nassimal El... zur Produkt-Seite
5462036 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvN2UvMTgvZDgvMzQ5NzM4NTcwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvN2UvMTgvZDgvMzQ5NzM4NTcwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9nbHljb3N5bGF0aW9uLWVuZ2luZWVyaW5nLW9mLWJpb3BoYXJtYWNldXRpY2Fscy0yNzM1MjI2NDkuanBn","post_title":"Glycosylation Engineering of Biopharmaceuticals","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781627033268&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fmedizin-pharmazie%2F381333%2Fglycosylation-engineering-of-biopharmaceuticals-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Part I: Glyco-Engineering of Therapeutic Proteins 1. Engineering of Therapeutic and Diagnostic O-Glycans on Recombinant Mucin-Type Immunoglobulin Fusion Proteins Expressed in CHO Cells Linda Lindberg, Jining Liu, and Jan Holgersson 2. Engineering a Human-Like Glycosylation to Produce Therapeutic Glycoproteins Based on 6-Linked Sialylation in CHO Cells Nassimal El Ma\u00ef, Sandrine Donadio-Andr\u00e9i, Chlo\u00e9 Iss, Val\u00e9rie Calabro, and Catherine Ronin 3. Glycoengineered Pichia-Based Expression of Monoclonal Antibodies Dongxing Zha 4. N-Glycosylation Humanization for Production of Therapeutic Recombinant Glycoproteins in Saccharomyces cerevisiae Christelle Arico, Christine Bonnet, and Christophe Javaud 5. Engineering the Baculovirus Genome to Produce Galactosylated Antibodies in Lepidopteran Cells Sylvie Juliant, Maryl\u00eane L\u00e9v\u00eaque, Pierre C\u00e9rutti, Annick Ozil, Sylvie Choblet, Marie-Luce Violet, Marie-Christine Slomianny, Anne Harduin-Lepers, and Martine C\u00e9rutti Part II: Glycoanalytics 6. Nano LC Chips MS\/MS for the Characterization of N-Glycopeptides Generated from Trypsin Digestion of a Monoclonal Antibody Elsa Wagner-Rousset, Christine Schaeffer-Reiss, Audrey Bednarczyk, Nathalie Corva\u00efa, Alain Van Dorsselaer, and Alain Beck 7. Cetuximab Fab and Fc N-Glycan Fast Characterization Using IdeS Digestion and Liquid Chromatography Coupled to Electrospray Ionization Mass Spectrometry Marie-Claire Janin-Bussat, Laure Tonini, C\u00e9line Huillet, Olivier Colas, Christine Klinguer-Hamour, Nathalie Corva\u00efa, and Alain Beck 8. Therapeutic Antibody Glycosylation Analysis: A Contract Research Organization Perspective in the Frame of Batch Release or Comparability Support Arnaud Delobel, Fabrice Cantais, Anicet Catrain, Erell Dereux, and G\u00e9ry Van Vyncht 9. Mass Spectrometric Analysis of O-Linked Oligosaccharides from Various Recombinant Expression Systems Diarmuid T. Kenny, Stefan Gaunit, Catherine A. Hayes, Anki Gustafsson, Magnus Sj\u00f6blom, Jan Holgersson, and Niclas G. Karlsson 10. Assessing Fc Glycan Heterogeneity of Therapeutic Recombinant Monoclonal Antibodies Using NP-HPLC T. Shantha Raju 11. Application of Capillary Electrophoresis in Glycoprotein Analysis Richard R. Rustandi, Carrie Anderson, and Melissa Hamm 12. Characterization of Glycoprotein Biopharmaceutical Products by Caliper LC90 CE-SDS Gel Technology Grace Chen, Sha Ha, and Richard R. Rustandi 13. Hydrophobic Interaction Chromatography to Analyze Glycoproteins Richard R. Rustandi 14. Lectin Glycoprofiling of Recombinant Therapeutic Interleukin-7 Ludovic Landemarre and Eric Duverger 15. Analysis of Monoclonal Antibodies by Sedimentation Velocity Analytical Ultracentrifugation W. Blaine Stine, Jr. Part III: Glycoprotein Complexes Characterization 16. Noncovalent Mass Spectrometry for the Characterization of Antibody\/Antigen Complexes C\u00e9dric Atmanene, Elsa Wagner-Rousset, Nathalie Corva\u00efa, Alain Van Dorsselaer, Alain Beck, and Sarah Sanglier-Cianferani 17. Conformational Analysis of Recombinant Monoclonal Antibodies with Hydrogen\/Deuterium Exchange Mass Spectrometry Damian Houde and John R. Engen 18. Epitope Mapping of Antibodies by Mass Spectroscopy: A Case Study Victor H. Obungu, Valentina Gelfanova, and Lihua Huang Part IV: PK\/PD Assays for Therapeutic Antibodies 19. Evaluation of Antibody-Dependent Cell Cytotoxicity Using Lactate Deshydrogenase (LDH) Measurement Matthieu Broussas, Lucile Broyer, and Liliane Goetsch 20. Evaluation of Complement Dependent Cytotoxicity Using ATP Measurement and C1q \/ C4b Binding Lucile Broyer, Liliane Goetsch, and Mattthieu Broussas 21. Capture of the Human IgG1 Antibodies by Protein A for the Kinetic Study of h-IgG \/ FcgR Interaction Using SPR-Based Biosensor Technology Thierry Champion and Alain Beck 22. Mass Spectrometry Protocol for the Absolute Quantification of a Monoclonal Antibody in Serum with Immunopurification Fran\u00e7ois Becher, Mathieu Dubois, Fran\u00e7ois Fenaille, and Eric Ezan","merchants_number":2,"ean":9781627033268,"category_id":103,"size":null,"min_price":178,"low_price_merchant_id":70255345,"ID":5462036,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"glycosylation-engineering-of-biopharmaceuticals","url":"\/unterhaltung\/produkt\/glycosylation-engineering-of-biopharmaceuticals\/","low_price_merchant_name":"eUniverse"}
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Chaperones
1. Targeted Deletion of Hsf1, 2 and 4 Genes in Mice Xiongjie Jin, Binnur Eroglu, Demetrius Moskophidis, and Nahid F. Mivechi 2. Role of Heat Shock Factors in Stress-induced Transcription Murshid, A., Prince T., Ben Lang, and Calderwood, S. K. 3. Monitoring of the Heat Shock Response with a Real-time Luciferase Reporter Toshiki Kijima, Takanori Eguchi, Len Neckers, and Thoma... zur Produkt-Seite
4102070 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYTIvOGQvNGMvNjU2NTY0MzcwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYTIvOGQvNGMvNjU2NTY0MzcwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9jaGFwZXJvbmVzLTI3MzU1MDIwMi5qcGc=","post_title":"Chaperones","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493974764&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F378081%2Fchaperones-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"1. Targeted Deletion of Hsf1, 2 and 4 Genes in Mice Xiongjie Jin, Binnur Eroglu, Demetrius Moskophidis, and Nahid F. Mivechi 2. Role of Heat Shock Factors in Stress-induced Transcription Murshid, A., Prince T., Ben Lang, and Calderwood, S. K. 3. Monitoring of the Heat Shock Response with a Real-time Luciferase Reporter Toshiki Kijima, Takanori Eguchi, Len Neckers, and Thomas L. Prince 4. Quantitative Profiling of Chaperone\/client Interactions with LUMIER Assay Mikko Taipale 5. Measurement of chaperone-mediated effects on Polyglutamine Protein Aggregation by the Filter Trap Assay Maria A.W.H. van Waarde-Verhagen and Harm H. Kampinga 6. Fluorescent-linked Enzyme Chemoproteomic Strategy (FLECS) for Identifying HSP70 Inhibitors Haystead, T.A.J. 7. A High-throughput Screen for Inhibitors of the Hsp90-Chaperone Machine Jason Davenport, Lakshmi Galam, and Robert L. Matts 8. Primary Colorectal Cells Culture as a Translation Research Model Sheah Lin Lee, Nina Claire Dempsey-Hibbert, Dale Vimalachandran, Terence David Wardle, Paul A Sutton, and John H. H. Williams 9. Cell Death and Survival Assays Alexander E. Kabakov and Vladimir L. Gabai 10. Detecting the Potential Pharmacological Synergy of Drug Combination by Viability Assays In Vitro Benjamin K. Gibbs and Carole Sourbier 11. Proteomic Profiling of Hsp90 Inhibitors Sudhakar Voruganti, Jake T. Kline, Maurie J. Balch, Janet Rogers, Robert L. Matts, and Steven D. Hartson 12. Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and its Interaction with Specific Client Polypeptides Andr\u00e9-Patrick Arrigo 13. Nucleotide Exchange Factors for Hsp70 Chaperones Heike Rampelt, Matthias P. Mayer, and Bernd Bukau 14. Determination of Hsp90 Activity through Activation of Glucocorticoid Receptors in Yeast Michael Reidy 15. Bacterial Hsp90 ATPase Assays Joel R. Hoskins, Sue Wickner, and Shannon M. Doyle 16. Detecting Post-translational Modifications of Hsp90 Rebecca A. Sager, Mark R. Woodford, Len Neckers, and Mehdi Mollapour 17. Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90) Aneliya Yoveva and Ritwick Sawarkar 18. A Workflow Guide to RNA-seq Analysis of Chaperone Function and Beyond Benjamin J. Lang, Kristina M. Holton, Jianlin Gong, and Stuart K. Calderwood 19. Computational Modeling of the Hsp90 Interactions with Cochaperones and Small Molecule Inhibitors Gennady M. Verkhivker 20. Computational Analysis of the Chaperone Interaction Networks Shwani Kumar, Kamran Rizzolo, Sandra Zilles, Mohan Babu, and Walid A. Houry 21. Immunohistochemistry of Human Hsp60 in Health and Disease: From Autoimmunity to Cancer Francesco Cappello, Everly Conway de Macario, Francesca Rappa, Giovanni Zummo, and Alberto J. L. Macario 22. Immunohistochemical and Flow Cytometric Analysis of Intracellular and Membrane-bound Hsp70, as a Putative Biomarker of Glioblastoma Multiforme, using the cmHsp70.1 Monoclonal Antibody Stefan Stangl, Gemma A. Foulds, Helena Fellinger, Geoffrey J. Pilkington, A. Graham Pockley,and Gabriele Multhoff 23. Detection and Analysis of Extracellular Hsp90 (eHsp90) Stephanie Cortes, Alexander Baker-Williams, Mehdi Mollapour, and Dimitra Bourboulia 24. Molecular Chaperone Receptors Ayesha Murshid, Jimmy Theriault,Jianlin Gong, and Stuart K. Calderwood 25. Creation of Recombinant Chaperone Vaccine using Large Heat Shock Protein for Antigen-targeted Cancer Immunotherapy Chunqing Guo, John R. Subjeck, and Xiang-Yang Wang 26. A Novel Heat Shock Protein 70-based Vaccine Prepared from DC-Tumor Fusion Cells Desheng Weng, Stuart K. Calderwood, and Jianlin Gong 27. Hsp70: A Cancer Target Inside and Outside the Cell Christophe Boudesco, Sebastien Cause, Ga\u00ebtan Jego, and Carmen Garrido 28. Evidence for Hsp90 Cochaperones in Regulating Hsp90 Function and Promoting Client Protein Folding Marc B. Cox and Jill L. Johnson 29. Clinical Evaluation and Biomarker Profiling of Hsp90 Inhibitors Akira Yuno, Min-Jung Lee, Sunmin Lee, Yusuke Tomita, David Rekhtman, Brittni Moore, and Jane B. Trepel","merchants_number":2,"ean":9781493974764,"category_id":103,"size":null,"min_price":178,"low_price_merchant_id":70255345,"ID":4102070,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"chaperones","url":"\/unterhaltung\/produkt\/chaperones\/","low_price_merchant_name":"eUniverse"}
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Antibody Engineering
Part I: In Silico Methods 1. Antibody Design and Humanization via In Silico Modeling Vinodh B. Kurella and Reddy Gali 2. Antibody Affinity Maturation by Computational Design Daisuke Kuroda and Kouhei Tsumoto 3. Use of IMGT® Databases and Tools for Antibody Engineering and Humanization Marie-Paule Lefranc, François Ehrenmann, Sofia Kossida, Véronique Gi... zur Produkt-Seite
4129445 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNDkvM2MvNjkvNjk2MTkxMDcwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNDkvM2MvNjkvNjk2MTkxMDcwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9hbnRpYm9keS1lbmdpbmVlcmluZy0yNzM1NjEzNDguanBn","post_title":"Antibody Engineering","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493986477&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fmedizin-pharmazie%2F378715%2Fantibody-engineering-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Part I: In Silico Methods\u00a01. Antibody Design and Humanization via In Silico Modeling\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Vinodh B. Kurella and Reddy Gali\u00a02. Antibody Affinity Maturation by Computational Design\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Daisuke Kuroda and Kouhei Tsumoto\u00a03. Use of IMGT\u00ae Databases and Tools for Antibody Engineering and Humanization\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Marie-Paule Lefranc, Fran\u00e7ois Ehrenmann, Sofia Kossida, V\u00e9ronique Giudicelli, and Patrice Duroux\u00a0Part II: Generation of Diversity\u00a04. Construction of Human Na\u00efve Antibody Gene Libraries\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Michela Pasello, Alessandra Mallano, Michela Flego, Silvia Zamboni, Anna Maria Giudice, and Katia Scotlandi\u00a05. Construction of Synthetic Antibody Libraries\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 D\u00e9borah Caucheteur, Gautier Robin, Vincent Parez, and Pierre Martineau\u00a06. Construction of Histidine-Enriched Shark IgNAR Variable Domain Antibody Libraries for the Isolation of pH-Sensitive vNAR Fragments\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Doreen K\u00f6nning, Steffen Hinz, Julius Grzeschik, Christian Schr\u00f6ter, Simon Krah, Stefan Zielonka, and Harald Kolmar\u00a07. Display Technologies for Generation of Ig Single Variable Domains\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Vladimir Bobkov, Bas van der Woning, and Hans de Haard\u00a08. A Streamlined Approach for the Construction of Large Yeast Surface Display Fab Antibody Libraries\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Simon Krah, Julius Grzeschik, Simon Rosowski, Ramona Gaa, Iris Willenbuecher, Deniz Demir, Lars Toleikis, Harald Kolmar, Stefan Becker, and Stefan Zielonka\u00a0Part III: Selections of Lead Candidate\u00a09. Phage Display and Selections on Purified Antigens\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Magali Colazet and Patrick Chames\u00a010. Selection of Antibodies to Transiently Expressed Membrane Proteins Using Phage Display\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Martina L. Jones, Stephen M. Mahler, and Sumukh Kumble\u00a011. Selection of Antibody Fragments against Structured DNA by Phage Display\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Mahdi Zeraati, Marcel E. Dinger, and Daniel Christ\u00a012. Selection of Antibody Fragments by Yeast Display\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Nathalie Scholler\u00a013. Rapid Selection of High Affinity Antibody scFv Fragments Using Ribosome Display\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Birgit Dreier and Andreas Pl\u00fcckthun\u00a014. In Vitro Selection of Single Domain Antibody (VHH) Using cDNA Display\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Naoto Nemoto, Shigefumi Kumachi, and Hidenao Arai\u00a015. Sequencing and Affinity Determination of Antigen-Specific B Lymphocytes from Peripheral Blood\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Peter Schofield, Rodrigo Vazquez-Lombardi, Mahmoud Abdelatti, Damien Nevoltris, Christopher C. Goodnow, Daniel Christ, and Joanne H. Reed\u00a0Part IV: Production of Recombinant Antibodies\u00a016. Expression of IgG Monoclonals with Engineered Immune Effector Functions\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Rodrigo Vazquez-Lombardi, Damien Nevoltris, Romain Rouet, and Daniel Christ\u00a017. An IRES-Mediated Tricistronic Vector for Efficient Generation of Stable, High Level Monoclonal Antibody Producing CHO DG44 Cell Lines\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Jessna H.M. Yeo, Mariati, and Yuansheng Yang\u00a018. Production, Purification, and Characterization of Antibody-TNF Superfamily Ligand Fusion Proteins\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Martin Siegemund, Nadine Beha, and Dafne M\u00fcller\u00a0Part V: Fc Engineering\u00a019. Chemoenzymatic Defucosylation of Therapeutic Antibodies for Enhanced Effector Functions Using Bacterial -Fucosidases\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Chao Li, Tiezheng Li, and Lai-Xi Wang\u00a020. Fc Glyco- and Fc Protein-Engineering: Design of Antibody Variants with Improved ADCC and CDC Activity\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Christian Kellner, Stefanie Derer, Katja Klausz, Sophia Rosskopf, Tim Wirt, Thies R\u00f6sner, Anna Otte, Elisa Cappuzzello, and Matthias Peipp\u00a021. Fc Engineering: Tailored Synthetic Human IgG1-Fc Repertoire for High Affinity Interaction with FcRn at pH 6.0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Abhishek Saxena, Bingxin Bai, Shin-Chen Hou, Lianlian Jiang, Tianlei Ying, Shane Miersch, Sachdev S. Sidhu, and Donghui Wu\u00a0Part VI: Characterization, Optimization, and Innovative Formats\u00a022. Measuring Antibody-Antigen Binding Kinetics Using Surface Plasmon Resonance\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Stephen Hearty, Paul Leonard, Hui Ma, and Richard O'Kennedy\u00a023. Parallel Evolution of Antibody Affinity and Thermal Stability for Optimal Biotherapeutic Development\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Edward Franklin, Orla Cunningham, and Brian Fennell\u00a024. The Use of Somatic Hypermutation for the Affinity Maturation of Therapeutic Antibodies\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Peter M. Bowers, William J. Boyle, and Robert Damoiseaux\u00a025. Selection and Use of Intracellular Antibodies\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Sandrine Moutel, Cl\u00e9ment Nizak, and Franck Perez\u00a026. Site-Specific Radioactive Labeling of Nanobodies\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Maxine Crauwels, Sam Massa, Charlotte Martin, Cecilia Betti, Steven Ballet, Nick Devoogdt, Catarina Xavier, and Serge Muyldermans","merchants_number":2,"ean":9781493986477,"category_id":103,"size":null,"min_price":211,"low_price_merchant_id":70255345,"ID":4129445,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"antibody-engineering","url":"\/unterhaltung\/produkt\/antibody-engineering\/","low_price_merchant_name":"eUniverse"}
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Extracellular Vesicles
1. Extracellular Vesicles: A Brief Overview and Its Role in Precision Medicine Mingyu Shang, John Ji, Chao Song, Bao Jun Gao, Jason Gang Jin, Winston Patrick Kuo, and Hongjun Kang 2. Red Blood Cells: A Source of Extracellular Vesicles Winston Patrick Kuo, John Tigges, Vasilis Toxavidis, and Ionita Ghiran Part I: Isolation of Extracellular Vesicles ... zur Produkt-Seite
4139549 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYmQvZjIvOTkvNjU1MDA1NzEwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvYmQvZjIvOTkvNjU1MDA1NzEwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9leHRyYWNlbGx1bGFyLXZlc2ljbGVzLTI3MzU0NjgzNi5qcGc=","post_title":"Extracellular Vesicles","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493972517&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F378015%2Fextracellular-vesicles-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"1. Extracellular Vesicles: A Brief Overview and Its Role in Precision Medicine Mingyu Shang, John Ji, Chao Song, Bao Jun Gao, Jason Gang Jin, Winston Patrick Kuo, and Hongjun Kang 2. Red Blood Cells: A Source of Extracellular Vesicles Winston Patrick Kuo, John Tigges, Vasilis Toxavidis, and Ionita Ghiran Part I: Isolation of Extracellular Vesicles 3. Isolation of Extracelullar Vesicles by Ultracentrifugation Fatemeh Momen-Heravi 4. Sequential Filtration: A Gentle Method for the Isolation of Functional Extracellular Vesicles Mitja L. Heinemann and Jody Vykoukal 5. Paper-Based Devices for Isolation of Extracellular Vesicles Yi-Hsing Hsiao and Chihchen Chen 6. Filter-Based Extracellular Vesicle mRNA Isolation and High-Throughput Gene Expression Analysis Cindy M. Yamamoto, Taku Murakami, and Shu-Wing Ng 7. Specific and Generic Isolation of Extracellular Vesicles with Magnetic Beads Ketil W. Pedersen, Bente Kierulf, and Axl Neurauter Part II: Purification of Extracellular Vesicles 8. Polymer-Based Purification of Extracellular Vesicles Peter N. Brown and Hang Yin 9. Size Exclusion Chromatography: A Simple and Reliable Method for Exosome Purification Richard Lobb and Andreas M\u00f6ller 10. Purification Protocols for Extracellular Vesicles Rebecca E. Lane, Darren Korbie, Matt Trau, and Michelle M. Hill Part III: Characterization of Extracellular Vesicles 11. Characterization of Extracellular Vesicles by Surface Plasmon Resonance Hyungsoon Im, Katherine Yang, Hakho Lee, and Cesar M. Castro 12. Extracellular Vesicle Isolation and Analysis by Western Blotting Emma J.K. Kowal, Dmitry Ter-Ovanesyan, Aviv Regev, and George M. Church 13. Analysis of Extracellular Vesicles Using Fluorescence Nanoparticle Tracking Analysis Pauline Carnell-Morris, Dionne Tannetta, Agnieszka Siupa, Patrick Hole, and Rebecca Dragovic 14. Characterization of Extracellular Vesicles by Flow Cytometry Virginia Camacho, Vasilis Toxavidis, and John C. Tigges 15. Characterization of Extracellular Vesicles by Size-Exclusion High-Performance Liquid Chromatography (HPLC) Tao Huang and Jiang He 16. Multi-Surface Antigen Staining of Larger Extracellular Vesicles Veronika Lukacs-Kornek, Henrike Julich, Sabine Katharina Urban, and Miroslaw Kornek 17. Microcapillary Chip-Based Extracellular Vesicle Profiling System Takanori Akagi and Takanori Ichiki Part IV: Imaging of Extracellular Vesicles 18. Detection and Characterization of Extracellular Vesicles by Transmission and Cryo-Transmission Electron Microscopy Petr Cizmar and Yuana Yuana 19. Imaging of Isolated Extracellular Vesicles Using Fluorescence Microscopy Dmitry Ter-Ovanesyan, Emma J.K. Kowal, Aviv Regev, George M. Church, and Emanuele Cocucci Part V: Tracking of Extracellular Vesicles 20. In Vivo Tracking of Extracellular Vesicles in Mice Using Fusion Protein Comprising Lactadherin and Gaussia Luciferase Yuki Takahashi, Makiya Nishikawa, and Yoshinobu Takakura 21. Tracking Extracellular Vesicles Delivery and RNA Translation Using Multiplexed Reporters Anthony Yan-Tang Wu and Charles Pin-Kuang Lai Part VI: Downstream Extracellular Vesicle Applications Genomics and Proteomics 22. Extraction and Analysis of Extracellular Vesicle-Associated miRNAs Following Antibody-Based Extracellular Vesicle Capture from Plasma Samples Davide Zocco and Natasa Zarovni 23. Extracellular Vesicle miRNA Detection Using Molecular Beacons Won Jong Rhee and Seunga Jeong 24. Rapid Isolation of Extracellular Vesicles from Blood Plasma with Size-Exclusion Chromatography Followed by Mass Spectrometry-Based Proteomic Profiling Simion Kreimer and Alexander R. Ivanov 25. An Adaptable Polyethylene Glycol-Based Workflow for Proteomic Analysis of Extracellar Vesicles Stephanie N. Hurwitz and David G. Meckes, Jr. Part VII: Isolation of Extracellular Vesicles from Biofluids 26. Isolation of Extracellular Vesicles from Ovarian Follicular Fluid: Evaluation of Ultracentrifugation and Commercial Kits Shlomit Kenigsberg, Clifford C. Librach, and Juliano C. da Silveira 27. Isolation of Extracellular Vesicles in Saliva Using Density Gradient Ultracentrifugation Kazuya Iwai, Satoshi Yamamoto, Mitsutaka Yoshida, and Kiyotaka Shiba 28. Isolation of Extracellular Vesicles from Breast Milk Xin Wang 29. An Integrated Double-Filtration Microfluidic Device for Detection of Extracellular Vesicles from Urine for Bladder Cancer Diagnosis Li-Guo Liang, Ye-Feng Sheng, Sherry Zhou, Fatih Inci, Lanjuan Li, Utkan Demirci, and ShuQi Wang Part VIII: Extracellular Vesicles Isolated from Cell Culture, Parasites, and Stem Cells 30. Electric Field-Induced Disruption and Releasing Viable Content from Extracellular Vesicles Chris Wang, Austin Wang, Fang Wei, David T.W. Wong, and Michael Tu 31. Production and Characterization of Extracellular Vesicles in Malaria Smart Mbagwu, Michael Walch, Luis Filgueira, and Pierre-Yves Mantel 32. Isolation of Extracellular Vesicles from Stem Cells Zixin Chen, Yongjun Li, Hong Yu, Yan Shen, Chengwei Ju, Genshan Ma, Yutao Liu, Il-man Kim, Neal L. Weintraub, and Yaoliang Tang Part IX: Extracellular Vesicles in Mouse Models 33. The Use of Peripheral Extracellular Vesicles for Identification of Molecular Biomarkers in a Solid Tumor Mouse Model Noem\u00ed Garc\u00eda-Romero, Gorjana Rackov, Cristobal Belda-Iniesta, and Angel Ayuso-Sacido Part X: Therapeutic Applications of Extracellular Vesicles 34. Therapeutic Applications of Extracellular Vesicles: Perspectives from Newborn Medicine Gareth R. Willis, Stella Kourembanas, and S. Alex Mitsialis 35. Therapeutic Use of Tumor Cell-Derived Extracellular Vesicles Jing Liu, Jingwei Ma, Ke Tang, and Bo Huang","merchants_number":2,"ean":9781493972517,"category_id":103,"size":null,"min_price":178,"low_price_merchant_id":70255345,"ID":4139549,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"extracellular-vesicles","url":"\/unterhaltung\/produkt\/extracellular-vesicles\/","low_price_merchant_name":"eUniverse"}
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