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CHF 50.30
Perforation Repair with Dental Pulp Stem Cells and DMP1
Perforations due to iatrogenic errors can compromise the tooth prognosis. There is still no ideal endodontic material in the market to be used in a perforation site. This study evaluates the ability of Dental Pulp Stem Cells (DPSCs) and Dentin Matrix Protein 1 (DMP1) impregnated within a collagen scaffold to induce dentin formation in a furcal perforation site. Under the conditions of... zur Produkt-Seite
4758044 {"price-changing":null,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTI4MDQ1NjI1X1huMzZKLXBuZw==!aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTI4MDQ1NjI1X1huMzZKLXBuZw==","post_title":"Perforation Repair with Dental Pulp Stem Cells and DMP1","deeplink":"https:\/\/www.awin1.com\/pclick.php?p=24465053567&a=401125&m=11816&pref1=9783639191790","labels":[],"brand_id":1,"post_content":"Perforations due to iatrogenic errors can compromise the tooth prognosis. There is still no ideal endodontic material in the market to be used in a perforation site. This study evaluates the ability of Dental Pulp Stem Cells (DPSCs) and Dentin Matrix Protein 1 (DMP1) impregnated within a collagen scaffold to induce dentin formation in a furcal perforation site. Under the conditions of this study, it may be concluded that DPSCs impregnated within a collagen scaffold can differentiate into odontoblast-like cells secreting a highly cellular, vascular, and mineralized matrix that can be the ground substance for dentin formation, in the presence of DMP1.","merchants_number":1,"ean":9783639191790,"category_id":103,"size":null,"min_price":50.2999999999999971578290569595992565155029296875,"low_price_merchant_id":1087639,"ID":4758044,"merchants":["dodax"],"brand":"undefined","slug":"perforation-repair-with-dental-pulp-stem-cells-and-dmp1","url":"\/unterhaltung\/produkt\/perforation-repair-with-dental-pulp-stem-cells-and-dmp1\/","low_price_merchant_name":null}


CHF 61.45
Development of a Collagen Gel Sandwich Hepatocyte Bioreactor
Understanding the hepatotoxicity of drugs is essential for progress in academic and industrial research. Studying hepatotoxicity in vitro is challenging because hepatocytes, the metabolically active cells of the liver, are very difficult to maintain in culture. It has been observed that culturing hepatocytes between two layers of collagen maintains in vivo-like morphology and also man... zur Produkt-Seite
5246573 {"price-changing":null,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTQ2NjA5MjUyX2JiMmdQLXBuZw==!aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTQ2NjA5MjUyX2JiMmdQLXBuZw==","post_title":"Development of a Collagen Gel Sandwich Hepatocyte Bioreactor","deeplink":"https:\/\/www.awin1.com\/pclick.php?p=27402553949&a=401125&m=11816&pref1=9783838350165","labels":[],"brand_id":1,"post_content":"Understanding the hepatotoxicity of drugs is essential for progress in academic and industrial research. Studying hepatotoxicity in vitro is challenging because hepatocytes, the metabolically active cells of the liver, are very difficult to maintain in culture. It has been observed that culturing hepatocytes between two layers of collagen maintains in vivo-like morphology and also many drug metabolizing enzymes for weeks. In spite of the research examining drug metabolism in collagen sandwiches, there is limited data regarding the applicability of this system to hepatotoxicity studies. We cultured primary rat hepatocytes in the collagen sandwich configuration and optimized this system for long-term hepatotoxicity studies. In addition, we also examined the conditioned medium from the hepatocytes to investigate the secreted protein profile, which could potentially be used to find toxicity biomarkers. Our proteomics analysis combined gel electrophoresis with Qstar LC-MS\/MS, and we were able to identify 493 proteins. In summary, we have shown that the collagen sandwich is a suitable system for hepatotoxicity studies as well as proteomics analysis.","merchants_number":1,"ean":9783838350165,"category_id":103,"size":null,"min_price":61.4500000000000028421709430404007434844970703125,"low_price_merchant_id":1087639,"ID":5246573,"merchants":["dodax"],"brand":"undefined","slug":"development-of-a-collagen-gel-sandwich-hepatocyte-bioreactor","url":"\/unterhaltung\/produkt\/development-of-a-collagen-gel-sandwich-hepatocyte-bioreactor\/","low_price_merchant_name":null}


CHF 32.40
Chiral Imprinting in Nanomaterials for Enantioselective Separations
Controlling enantioselective separations of chiral compounds is one of the important challenges in chemistry. The enantioselectivity of chiral chemicals usually requires the use of chiral media such as chiral catalysts for synthesis and chiral stationary phases for chromatographic separations. This study has been devoted to the preparation, characterization and applications of chiral ... zur Produkt-Seite
4634651 {"price-changing":null,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTQ5Mzk4MjgwX3hSWUxKLXBuZw==!aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTQ5Mzk4MjgwX3hSWUxKLXBuZw==","post_title":"Chiral Imprinting in Nanomaterials for Enantioselective Separations","deeplink":"https:\/\/www.awin1.com\/pclick.php?p=22944224591&a=401125&m=11816&pref1=9783659766800","labels":[],"brand_id":1,"post_content":"Controlling enantioselective separations of chiral compounds is one of the important challenges in chemistry. The enantioselectivity of chiral chemicals usually requires the use of chiral media such as chiral catalysts for synthesis and chiral stationary phases for chromatographic separations. This study has been devoted to the preparation, characterization and applications of chiral nanosurfaces in enantioselective chemical processes. The first part of the book focuses on the development of chiral mesoporous silica based on the imprinting approach using chiral organic templates such as fatty acid micelles and collagen protein. The second part focuses on the preparation and investigation of templated chiral alumina nanosurfaces using atomic layer deposition (ALD) process on chiral self-assembled monolayers (SAMs) surfaces.","merchants_number":1,"ean":9783659766800,"category_id":103,"size":null,"min_price":32.39999999999999857891452847979962825775146484375,"low_price_merchant_id":1087639,"ID":4634651,"merchants":["dodax"],"brand":"undefined","slug":"chiral-imprinting-in-nanomaterials-for-enantioselective-separations","url":"\/unterhaltung\/produkt\/chiral-imprinting-in-nanomaterials-for-enantioselective-separations\/","low_price_merchant_name":null}


CHF 51.15
Biomineralisation
Biomineralisation is the process by which living organisms produce minerals, often to harden or stiffen existing tissues. It is an extremely widespread phenomenon, all six taxonomic kingdoms contain members that are able to form minerals, and over 60 different minerals have been identified in organisms. Examples include silicates in algae and diatoms, carbonates in invertebrates, and ... zur Produkt-Seite
5158736 {"price-changing":null,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTI4MDc3MTAyXzVEUDhWLXBuZw==!aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTI4MDc3MTAyXzVEUDhWLXBuZw==","post_title":"Biomineralisation","deeplink":"https:\/\/www.awin1.com\/pclick.php?p=27481556859&a=401125&m=11816&pref1=9786130672003","labels":[],"brand_id":1,"post_content":"Biomineralisation is the process by which living organisms produce minerals, often to harden or stiffen existing tissues. It is an extremely widespread phenomenon, all six taxonomic kingdoms contain members that are able to form minerals, and over 60 different minerals have been identified in organisms. Examples include silicates in algae and diatoms, carbonates in invertebrates, and calcium phosphates and carbonates in vertebrates. These minerals often form structural features such as sea shells and the bone in mammals and birds. Organisms have been producing mineralised skeletons for the past 550 million years. Other examples include copper, iron and gold deposits involving bacteria. Biologically-formed minerals often have special uses such as magnetic sensors in magnetotactic bacteria (Fe3O4), gravity sensing devices (CaCO3, CaSO4, BaSO4) and iron storage and mobilization (Fe2O3 H2O in the protein ferritin). In terms of taxonomic distribution, the most common biominerals are the phosphate and carbonate salts of calcium that are used in conjunction with organic polymers such as collagen and chitin to give structural support to bones and shells.","merchants_number":1,"ean":9786130672003,"category_id":103,"size":null,"min_price":51.14999999999999857891452847979962825775146484375,"low_price_merchant_id":1087639,"ID":5158736,"merchants":["dodax"],"brand":"undefined","slug":"biomineralisation","url":"\/unterhaltung\/produkt\/biomineralisation\/","low_price_merchant_name":null}



CHF 178.00
Post-translational Modifications of Proteins
Contents Preface Contributors 1 Disulfide Bond Mapping by Cyanylation-Induced Cleavage and Mass Spectrometry Jiang Wu 2 Detection of Post-Translational Modifications by Fluorescent Staining of 2D gels Archana M. Jacob and Chris W. Turck 3 Identification of Protein Phosphorylation Sites by Advanced LC-ESI-MS/MS Methods Christoph Weise and Christof Lenz 4 Analysis of Tyrosine-O-Sulfati... zur Produkt-Seite
4394531 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvMGUvZmMvNzUvMjA3MzEzODEwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvMGUvZmMvNzUvMjA3MzEzODEwMDAwMUFfNjAweDYwMC5qcGc=","post_title":"Post-translational Modifications of Proteins","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781588297198&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F379866%2Fpost-translational-modifications-of-proteins-tools-for-functional-proteomics%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"Contents Preface Contributors 1 Disulfide Bond Mapping by Cyanylation-Induced Cleavage and Mass Spectrometry Jiang Wu 2 Detection of Post-Translational Modifications by Fluorescent Staining of 2D gels Archana M. Jacob and Chris W. Turck 3 Identification of Protein Phosphorylation Sites by Advanced LC-ESI-MS\/MS Methods Christoph Weise and Christof Lenz 4 Analysis of Tyrosine-O-Sulfation Jens R. Bundgaard, Jette W. Sen, Anders H. Johnsen, and Jens F. Rehfeld 5 a -Amidated Peptides: Approaches for Analysis Gregory P. Mueller and William J. Driscoll 6 Gamma-Glutamate and b -Hydroxyaspartate in Proteins Francis J. Castellino, Victoria A. Ploplis, and Li Zhang 7 Lysine Hydroxylation and Cross-linking of Collagen Mitsuo Yamauchi and Masashi Shiiba 8 Mass Spectrometric Determination of Protein Ubiquitination Carol E. Parker, Maria R. E. Warren, Viorel Mocanu, Susanna F. Greer, and Christoph H. Borchers 9 Analysis of Sumoylation Andrea Pichler 10 Detection and Analysis of Protein ISGylation Tomoharu Takeuchi and Hideyoshi Yokosawa 11 Analysis of Methylation, Acetylation and other Modifications in Bacterial Ribosomal Proteins Randy J. Arnold, William Running, and James P. Reilly 12 Analysis of S-Acylation of Proteins Michael Veit, Evgeni Ponimaskin, and Michael F.G. Schmidt 13 Metabolic Labeling and Structural Analysis of Glycosylphosphatidylinositols from Parasitic Protozoa Nahid Azzouz, Peter Gerold, and Ralph T. Schwarz 14 2D-Electrophoresis: Detection of Glycosylation and Influence on Spot Pattern Klemens L\u00f6ster and Christoph Kannicht 15 Carbohydrate Composition Analysis of Glycoproteins by HPLC Using Highly Fluorescent Anthranilic Acid (AA) Tag George N. Saddic, Shirish T. Dhume, and KalyanR. Anumula 16 Enzymatical Hydrolysis of N-glycans from Glycoproteins and Fluorescent Labelling by 2-Aminobenzamide (2-AB) Rolf Nuck 17 Separation of N-glycans by HPLC Martin Gohlke and V\u00e9ronique Blanchard 18 Enzymatic Sequence Analysis of N-glycans By Exoglycosidase Cleavage and Mass Spectrometry - Detection of Lewis X Structures Christoph Kannicht, Detlef Grunow, and Lothar Lucka 19 Immunochamical Methods for the Rapid Sceening of the O-Glycosidically Linked N-Acetylglucosamine Modification of Proteins Monika Rex-Mathes, J\u00fcrgen Koch, Sabine Werner, Lee S. Griffith, and Brigitte Schmitz 20 Analysis of O-Glycosylation Juan J. Calvete and Libia Sanz 21 Characterization of Site Specific N-Glycosylation Katalin F. Medzihradszky 22 Monitoring Glycosylation of Therapeutic Glycoproteins for Consistency by HPLC Using Highly Fluorescent Anthranilic Acid (AA) Tag Shirish T. Dhume, George N. Saddic, and Kalyan R. Anumula 23 Comparability and Monitoring Immunogenic N-linked Oligosaccharides from Recombinant Monoclonal Antibodies from two Different Cell Lines using HPLC with Fluorescence Detection and Mass Spectrometry Bruce R. Kilgore, Adam W. Lucka, Rekha Patel, Bruce A. Andrien, Jr., and Shirish T. Dhume 24 Mass Spectrometry and HPLC with Fluorescent Detection-Based Orthogonal Approaches to Characterize N-linked Oligosaccharides of Recombinant Monoclonal Antibodies Adam Lucka, Bruce R. Kilgore, Rekha Patel, Bruce A. Andrien, Jr., and Shirish T. Dhume 25 Web-based Computational Tools for the Prediction and Analysis of Posttranslational Modifications of Proteins Vladimir A. Ivanisenko, Dimitry A. Afinnikov, and Nikolay A. Kolchanov","merchants_number":1,"ean":9781588297198,"category_id":103,"size":null,"min_price":178,"low_price_merchant_id":70255345,"ID":4394531,"merchants":["euniverse"],"brand":"undefined","slug":"post-translational-modifications-of-proteins","url":"\/unterhaltung\/produkt\/post-translational-modifications-of-proteins\/","low_price_merchant_name":"eUniverse"}



CHF 177.00
The Complement System
1. OverviewMihaela Gadjeva 2. Evaluation of Complement Function by ELISAAnja Roos and Jorgen Wieslander3. Classical Complement Pathway Component C1q - Purification of Human C1q, Isolation of C1q Collagen-like and Globular Head Fragments and Production of Recombinant C1q - Derivatives. Functional Characterization. Mihaela Kojouharova 4. Classical Complement Pathway Components C1r and ... zur Produkt-Seite
4418333 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9pLndlbHRiaWxkLmRlL3AvdGhlLWNvbXBsZW1lbnQtc3lzdGVtLTA4MTY0MzA4NC5qcGc=!aHR0cHM6Ly9pLndlbHRiaWxkLmRlL3AvdGhlLWNvbXBsZW1lbnQtc3lzdGVtLTA4MTY0MzA4NC5qcGd8fnxodHRwczovL29zMS5tZWluZWNsb3VkLmlvL2IxMDE1OC9tZWRpYS9pbWFnZS85ZS83Yy9kOC80MTcyNTYyMTAwMDAxQV82MDB4NjAwLmpwZw==","post_title":"The Complement System","deeplink":"https:\/\/track.adtraction.com\/t\/t?a=1632201226&as=1592767275&t=2&tk=1&url=https:\/\/www.weltbild.ch\/artikel\/x\/_18312762-1","labels":[],"brand_id":1,"post_content":"1. OverviewMihaela Gadjeva 2. Evaluation of Complement Function by ELISAAnja Roos and Jorgen Wieslander3. Classical Complement Pathway Component C1q - Purification of Human C1q, Isolation of C1q Collagen-like and Globular Head Fragments and Production of Recombinant C1q - Derivatives. Functional Characterization. Mihaela Kojouharova 4. Classical Complement Pathway Components C1r and C1s - Purification from Human Serum and in Recombinant Form and Functional CharacterizationV\u00e9ronique Rossi, Isabelle Bally, Monique Lacroix, G\u00e9rard J Arlaud, and Nicole M Thielens 5. Expression and Purification Methods for the Production of Recombinant Human Complement Component C2 Angela W. Norton, Paolo G.V. Martini, Lynette C. Cook, Scott Alderucci, Dianna M. Lundberg, Susan M. Fish, Charles Bedard3, John Gill, Arthur O. Tzianabos, and Michael F. Concino 6. Purification and Characterisation of human and Mouse Complement C3Marieta M Ruseva and Meike Heurich 7. Purification of Human Complement Protein C5Lars Sottrup-Jensen and Gregers Rom Andersen 8. Quantification of Complement C5b-9 Binding to Cells by Flow CytometryOren Moskovich and Zvi Fishelson 9. Challenges and Opportunities in Fractionation of Recombinant Human Mannan-binding LectinThomas Vorup-Jensen 10. Genotyping of FCN and MBL2 Polymorphisms using PyrosequencingLea Munthe-Fog, Hans Ole Madsen, and Peter Garred 11. Assay for Estimation of the Functional Activity of the Mannan Binding Lectin Pathway of the Complement SystemTroels R. Kjaer and Steffen Thiel 12. Purification, Measurement of Concentration, and Functional Complement Assay of Human Ficolins Misao Matsushita, David Kilpatrick, Hiroshi Shiraki, Yu Liu, Koichiro Tateishi, Mitsushi Tsujimura, Yuichi Endo, Teizo Fujita 13. Purification and Functional Analysis of Human ProperdinJoseph O`Flynn, Maria C. Faber Krol, Mohamed R. Daha, Cees van Kooten 14. Purification and Functional Characterization of C4b-binding Protein (C4BP)Frida C. Mohlin and Anna M. Blom 15. Purification and Functional Characterization of Factor ISara C. Nilsson and Anna M. Blom 16. C1 inhibitor - Quantification and PurificationLilian Varga and J\u00f3zsef Dob\u00f3 17. Purification, Quantification and Functional Analysis of Complement Factor H Bing-Bin Yu, Beryl E. Moffatt, Marina Fedorova, Ali Ryan, Claire G.S. Villiers, James N. Arnold, Eugenie Du, Astrid Swinkels, Man Chung Li, Robert B. Sim 18. Factor H-related ProteinsMih\u00e1ly J\u00f3zsiand Seppo Meri 19. Functional Evaluation of Factor H genetic and Acquired Abnormalities, Application for Atypical Hemolytic Uremic Syndrome (aHUS)Lubka T. Roumenina, Roxane Roquigny, Caroline Blanc, Nelly Poulain, Stephanie Ngo, Marie-Agnes Dragon-Durey, and Veronique Fremeaux-Bacchi 20. Anti-Factor H Auto Antibodies AssayMarie-Agn\u00e8s Dragon-Durey, Caroline Blanc, Lubka Roumenina, Nelly Poulain Poulain, St\u00e9phanie Ngo, Pauline Bordereau, V\u00e9ronique Fr\u00e9meaux-Bacchi 21. Purification of Native Surfactant Protein SP-A from Pooled Amniotic Fluid and Bronchoalveolar Lavage Najmunisa Karbani, Eswari Dodagatta-Marri, Asif S. Qaseem, Priyaa Madhukaran, Patrick Waters, Anthony G. Tsolaki, Taruna Madan, and Uday Kishore 22. Purification of Surfactant Protein D (SP- D) from Pooled Amniotic Fluid and Bronchoalveolar LavageEswari Dodagatta-Marri, Asif Qaseem,Najmunisa Karbani, Anthony George Tsolaki, Patrick Waters, Taruna Madan, and Uday Kishore 23. Functional Analysis of C5a Effector Responses In Vitro and In Vivo Christian M. Karsten, Yves Laumonnier,and J\u00f6rg K\u00f6hl 24. Detection of Complement Receptors 1 and 2 on Mouse Splenic B Cells using Flow CytometryLuke R Donius and John H Weis 25. Quantification of Complement Receptor 2 Calcium Signaling Enhancement Using Flow CytometryLuke R Donius and John H Weis 26. Purification of C1q Receptors and Functional AnalysisBerhane Ghebrehiwet and Ellinor I.B. Peerschke 27. Detection of Cell Membrane-bound CD46 using Flow CytometryMartin Kolev and Claudia Kemper 28. Detection of CD59 using Flow CytometryMartin Kolev 29. Functional Analysis of CD59 using Complement Dependent Cytotoxicity AssayMartin Kolev 30. Detection of Soluble CR3 (CD11b\/CD18) by Time-resolved Immunofluorometry Gitte Krogh Nielsenand Thomas Vorup-Jensen 31. Analysis of the Complement Activation in MiceNirmal K. Banda and Kazue Takahashi 32. Opsonophagocytic AssayMarkryan Dwyer and Mihaela Gadjeva","merchants_number":2,"ean":9781627037235,"category_id":103,"size":null,"min_price":177,"low_price_merchant_id":27291482,"ID":4418333,"merchants":["weltbild","euniverse"],"brand":"undefined","slug":"the-complement-system","url":"\/unterhaltung\/produkt\/the-complement-system\/","low_price_merchant_name":"Weltbild"}



CHF 178.00
Peptide Self-Assembly
Part I: Fundamental Methods for Characterizing Peptide Self-Assembly 1. Methods for Structural Analysis of Aggregates Formed by Self-Assembling PeptidesV. Castelletto and I. W. Hamley 2. Solid state NMR Structural Characterization of Self-assembled Peptides With Selective 13C and 15N Isotopic Labels Danting Huang, Benjamin C. Hudson, Yuan Gao, Evan K. Roberts, and Anant K. Par... zur Produkt-Seite
4419806 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNGUvYzEvNTgvNjgwNDM1MDMwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvNGUvYzEvNTgvNjgwNDM1MDMwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC9wZXB0aWRlLXNlbGYtYXNzZW1ibHktMzI3ODI4ODQ0LmpwZw==","post_title":"Peptide Self-Assembly","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781493978090&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fbiologie%2F378166%2Fpeptide-self-assembly-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"\u00a0Part I: Fundamental Methods for Characterizing Peptide Self-Assembly\u00a0\u00a01.\u00a0\u00a0\u00a0 Methods for Structural Analysis of Aggregates Formed by Self-Assembling PeptidesV. Castelletto and I. W. Hamley\u00a02.\u00a0\u00a0\u00a0 Solid state NMR Structural Characterization of Self-assembled Peptides With Selective 13C and 15N Isotopic Labels Danting Huang, Benjamin C. Hudson, Yuan Gao, Evan K. Roberts, and Anant K. Paravastu\u00a03.\u00a0\u00a0\u00a0 ATR-FTIR Analysis of Amyloid ProteinsJean-Marie Ruysschaert and Vincent Raussens\u00a04.\u00a0\u00a0\u00a0 Imaging Protein Fibers at the Nanoscale and In SituAngelo Bella, Michael Shaw, Emiliana De Santis, and Maxim G. Ryadnov\u00a05.\u00a0\u00a0\u00a0 Replica Exchange Molecular Dynamics: A Practical Application Protocol with Solutions to Common Problems and a Peptide Aggregation and Self-Assembly ExampleRuxi Qi, Guanghong Wei, Buyong Ma and Ruth Nussinov\u00a06.\u00a0\u00a0\u00a0 An Aggregate Weight-normalized thioflavin-T Measurement Scale For Characterizing Polymorphic Amyloids And Assembly IntermediatesRonald Wetzel, Saketh Chemuru, Pinaki Misra, Ravi Kodali, Smita Mukherjee, and Karunakar Kar\u00a07.\u00a0\u00a0\u00a0 Nanoparticle Tracking for Protein Aggregation Research\u00a0Xiaomeng Lu and Regina M. Murphy\u00a08.\u00a0\u00a0\u00a0 Peptide Self-assembly Measured using Fluorescence Correlation SpectroscopyJudith J. Mittag, Joachim O. R\u00e4dler,\u00a0 and \u00a0Jennifer J. McManus\u00a0Part II: \u00a0Methods for the Preparation of Functional Self-Assembled Peptide Biomaterials\u00a09.\u00a0\u00a0\u00a0 A General Method to Prepare Peptide-based Supramolecular HydrogelsDan Yuan, Junfeng Shi, Ning Zhou, and Bing Xu\u00a0\u00a0\u00a0\u00a0\u00a0 10. Recursive Directional Ligation Approach for Cloning Recombinant Spider SilksNina Dinjaski, Wenwen Huang, and David L. Kaplan\u00a011. Synthesis of Mikto-Arm Star Peptide ConjugatesJin Mo Koo, Hao Su, Yi-An Lin, and Honggang Cui\u00a012. Synthesis and Evaluation of Self-Assembled Nanostructures of Peptide-pi chromophore conjugatesTejaswini S. Kale and John D. Tovar\u00a013. Programmable Fabrication of Multi-layer Collagen Nanosheets of Defined Composition Tao Jiang and Vincent P. Conticello\u00a014. Practical Considerations in the Design and use of Immunologically Active Fibrillar Peptide Assemblies Carolina Mora Solano,Yi Wen, Huifang Han, and Joel H. Collier\u00a015. Microwave-assisted Synthesis and Immunological Evaluation of Self-Assembling Peptide Vaccines C. Brent Chesson, Rojelio Elias Alverado, and Jai S. Rudra\u00a016. Preparation and Screening of Catalytic Amyloid AssembliesZsofia Lengyel, Caroline M. Rufo, and Ivan V. Korendovych\u00a017. Self-assembly of Filamentous Cell Penetrating Peptides for Gene Delivery Dawei Xu, Louis DeRidder, Brendan Elmore, and He Dong\u00a018. Biogelx: Cell Culture on Gels based on Aromatic Peptide AmphiphilesMhairi M. Harper, Michael L. Connolly, Laura Goldie, Eleanore J. Irvine, Joshua E. Shaw, Vineetha Jayawarna, Stephen M. Richardson, Matthew J. Dalby, David Lightbody, and Rein V. Ulijn\u00a0 \u00a0Part III: Methods Related to Preparing, Characterizing and Inhibiting Pathological Amyloid Peptide Self-Assembly\u00a019. Production and use of Recombinant Abeta for Aggregation StudiesTiernan T. O'Malley, Sara Linse, and Dominic M. Walsh\u00a020. Disaggregation of Ab42 for Structural and Biochemical Studies Hyewon Chung, Elliot Crooks, Martine Ziliox, and Steven O. Smith\u00a021. Preparation of Stable Amyloid-beta Oligomers Without Perturbative MethodsSamuel A. Kotler and Ayyalusamy Ramamoorthy\u00a022. Discriminating Strains of Self-Propagating Protein Aggregates Using a Conformational Stability AssayHeather H.C. Lau, Angus Lau,and Joel C. Watts\u00a023. Model Phospholipid Liposomes to Study the b-Amyloid-Peptide-Induced Membrane DisruptionWei Qiang and Katelynne E. Doherty \u00a0\u00a0\u00a0\u00a0\u00a0 24. Using Molecular Tweezers to Remodel Abnormal Protein Self-assembly and Inhibit the Toxicity of Amyloidogenic ProteinsRavinder Malik, Jing Di, Gayatri Nair, Aida Attar, Karen Taylor, Edmond Teng, Frank-Gerrit Kl\u00e4rner, Thomas Schrader, and Gal Bitan\u00a025. Incorporation of an azobenzene b-turn Peptidomimetic into Amyloid-b to Probe Potential Structural Motifs Leading to b-sheet self-assembly Todd M. Doran and Bradley L. Nilsson\u00a026. Solid State NMR Studies of Amyloid Materials: A Protocol to Define an Atomic Model of Abeta(1-42) in Amyloid Fibrils Yiling Xiao, Dan McElheny, Minako Hoshi, and Yoshitaka Ishii\u00a027. Experimental and Computational Protocols for Studies of Cross-seeding Amyloid AssembliesBaiping Ren, Rundong Hu, Mingzhen Zhang, Yonglan Liu, Lijian Xu, Binbo Jiang, Jie Ma, Buyong Ma, Ruth Nussinov, and Jie Zheng","merchants_number":2,"ean":9781493978090,"category_id":103,"size":null,"min_price":178,"low_price_merchant_id":70255345,"ID":4419806,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"peptide-self-assembly","url":"\/unterhaltung\/produkt\/peptide-self-assembly\/","low_price_merchant_name":"eUniverse"}



CHF 132.50
NanoBiotechnology Protocols
1. High Aspect Ratio Gold Nanorods: Their Synthesis and Application to Image Cell-Induced Strain Fields in Collagen FilmsDavin J. Chernak, Patrick N. Sisco, Edie C. Goldsmith, Sarah C. Baxter, and Catherine J. Murphy2. Imaging Intracellular Quantum Dots: Fluorescence Microscopy and Transmission Electron MicroscopyCraig J. Szymanski, Hong Yi, Joshua L. Liu, Elizabeth R. Wright, and Chr... zur Produkt-Seite
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CHF 178.00
Transplantation Immunology
PART I: Overview Chapters1. AlloreactivitySidonia B.G. Eckle, Jamie Rossjohn, and James McCluskey 2. Antibodies in Transplantation: The Effects of HLA and Non-HLA Antibody Binding and Mechanisms of InjuryNicole M. Valenzuela and Elaine F. Reed 3. Cell Mediated RejectionKathryn J Wood, Masaaki Zaitsu and Ryoichi Goto 4. Transplantation ToleranceColin Brinkman, Bryna Burrell, Joseph Sca... zur Produkt-Seite
4927268 {"price-changing":0,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvZjAvODIvZDEvMzgyNjI4MTIwMDAwMUFfNjAweDYwMC5qcGc=!aHR0cHM6Ly9vczEubWVpbmVjbG91ZC5pby9iMTAxNTgvbWVkaWEvaW1hZ2UvZjAvODIvZDEvMzgyNjI4MTIwMDAwMUFfNjAweDYwMC5qcGd8fnxodHRwczovL2kud2VsdGJpbGQuZGUvcC90cmFuc3BsYW50YXRpb24taW1tdW5vbG9neS0yNzM1MTg4MTQuanBn","post_title":"Transplantation Immunology","deeplink":"https:\/\/cct.connects.ch\/tc.php?t=116298C1969900829T&subid=9781627034920&deepurl=https%3A%2F%2Feuniverse.ch%2Fbuecher%2Fmathematik-naturwissenschaft-technik%2Fmedizin-pharmazie%2F381367%2Ftransplantation-immunology-methods-and-protocols%3FsPartner%3Dtoppreise","labels":[],"brand_id":1,"post_content":"PART I: Overview Chapters1. AlloreactivitySidonia B.G. Eckle, Jamie Rossjohn, and James McCluskey 2. Antibodies in Transplantation: The Effects of HLA and Non-HLA Antibody Binding and Mechanisms of InjuryNicole M. Valenzuela and Elaine F. Reed 3. Cell Mediated RejectionKathryn J Wood, Masaaki Zaitsu and Ryoichi Goto 4. Transplantation ToleranceColin Brinkman, Bryna Burrell, Joseph Scalea, and Jonathan Bromberg 5. Composite Tissue TransplantationGerald Brandacher 6. Transplantation of the Sensitized Patient: Histocompatibility TestingRobert A. Montgomery, Mary S. Leffell, and Andrea A. Zachary 7. Thoracic Organ Transplantation: Laboratory MethodsJignesh K. Patel and Jon A. Kobashigawa PART II: Methods Chapters 8. HLA Typing by Sequence Specific PrimersMike Bunce, Biofortuna and Ben Passey, Biofortuna 9. Human Leukocyte Antigen (HLA) Typing By DNA SequencingAna Lazaro, Bin Tu, Ruyan Yang, Yi Xiao, Kanthi Kariyawasam, Jennifer Ng, Carolyn and Katovich Hurley 10. Next-Generation HLA Sequencing using the 454 GS FLX System Elizabeth A. Trachtenbergand Cherie L. Holcomb 11. Chimerism Testing by Quantitative PCR Using Indel MarkersKetevan Gendzekhadze, Laima Gaidulis, and David Senitzer 12. Gene-specific PCR Typing of Killer Cell Immunoglobulin-like Receptors (KIR)Raja Rajalingam and Elham Ashouri 13. Complement-dependent Cytotoxicity CrossmatchJeremy Ryan Pe\u00f1a, Donna Fitzpatrick, and Susan L. Saidman 14. Lymphocyte Crossmatching by Flow CytometryRobert A. Bray 15. Solid Phase Assay Measuring C4d Deposition to Determine Complement Fixation by HLA Specific AntibodiesJohn D Smith and Marlene L Rose 16. C1q Assay for the Detection of Complement Fixing Antibody to HLA AntigensGe Chen and Dolly B. Tyan 17. Tetramer Staining for the Detection of HLA-specific B cellsDonna P. Lucas, Mary S. Leffell, and Andrea A. Zachary 18. A Flow Cytometric Crossmatch Test Using Endothelial Precursor Cells Isolated from Peripheral BloodAnnette M. Jackson, Donna P. Lucas, Jessica L. Badders 19. The Detection of Antibodies to the Angiotensin II-Type 1 Receptor in TransplantationDuska Dragun 20. Detection of Antibodies to Self-antigens (K-alpha 1 Tubulin, Collagen I, II, IV and V Myosin and Vimentin) by Enzyme-Linked Immunosorbent Assay (ELISA)Nayan J. Sarma, Venkataswarup Tiriveedhi, and T. Mohanakumar 21. Cylex ImmuKnow Cell Function AssayAdriana Zeevi and John Lunz 22. Detection of Intracellular CytokinesNancy L. Reinsmoen and Chih-Hung Lai 23. Tolerogenic Dendritic Cells and Induction of T Suppresson Cells in Transplant RecipientsGeorge Vlad and Nicole Suciu-Foca 24. Discovery and Customized Validation of Antibody Targets by Protein Arrays and Indirect ELISATara K. Sigdel, and Minnie. M. Sarwal 25. RNA Purification and Expression Analysis using Microarrays and RNA Deep Sequencing Steven R. Head, Tony Mondala, Terri Gelbart, and Phillip Ordoukhanian","merchants_number":2,"ean":9781627034920,"category_id":103,"size":null,"min_price":178,"low_price_merchant_id":70255345,"ID":4927268,"merchants":["euniverse","weltbild"],"brand":"undefined","slug":"transplantation-immunology","url":"\/unterhaltung\/produkt\/transplantation-immunology\/","low_price_merchant_name":"eUniverse"}


CHF 93.50
Cell Migration
Preface...Table of Contents...Contributing Authors...1. Random Migration Assays of Mammalian Cells and Quantitative Analyses of Single Cell TrajectoriesIrene Dang and Alexis Gautreau2. Directional Collective Migration in Wound Healing AssaysNicolas Molinie and Alexis Gautreau3. An In Vitro System to Study the Mesenchymal-to-Amoeboid Transition Aleksandra S. Chikina and Antonina Y. Ale... zur Produkt-Seite
4089587 {"price-changing":null,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTIxNzkxOTQ3X0RZUVd2YS1wbmc=!aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTIxNzkxOTQ3X0RZUVd2YS1wbmd8fnxodHRwczovL29zMS5tZWluZWNsb3VkLmlvL2IxMDE1OC9tZWRpYS9pbWFnZS8yNi9hZi83Mi82NzA1NDgzNTAwMDAxQV82MDB4NjAwLmpwZw==","post_title":"Cell Migration","deeplink":"https:\/\/www.awin1.com\/pclick.php?p=30619680763&a=401125&m=11816&pref1=9781493977000","labels":[],"brand_id":1,"post_content":"Preface...Table of Contents...Contributing Authors...1. Random Migration Assays of Mammalian Cells and Quantitative Analyses of Single Cell TrajectoriesIrene Dang and Alexis Gautreau2. Directional Collective Migration in Wound Healing AssaysNicolas Molinie and Alexis Gautreau3. An In Vitro System to Study the Mesenchymal-to-Amoeboid Transition Aleksandra S. Chikina and Antonina Y. Alexandrova4. An In Vitro System to Study the Epithelial-Mesenchymal Transition In Vitro Natalya A. Glushankova, Svetlana N. Rubtsova, and Irina Y. Zhitniak5. Detection of MigrasomesYang Chen, Ying Li, Liang Ma, and Li Yu6. 3D Endothelial Cell MigrationKathryn A. Jacobs and Julie Gavard7. Transmigration of Leukocytes across Epithelial MonolayersPenny E. Morton and Maddy Parsons8. Evaluation of Tumor Cell Invasiveness In Vivo: The Chick Chorioallantoic Membrane AssaySelma Maacha and Simon Saule9. Analysis of Invasion Dynamics of Matrix-Embedded Cells in a Multi-Sample FormatMarleen Van Troys, Paola Masuzzo, Lynn Huyck, Karima Bakkali, Davy Waterschoot, Lennart Martens, and Christophe Ampe10. Using Systems Microscopy to Understand the Emergence of Cell Migration from Cell OrganizationStaffan Str\u00f6mblad and John G. Lock11. Neuronal Precursor Migration in Ex Vivo Brain Slice CultureFu-Sheng Chou and Pei-Shan Wang12. In Vitro Models to Analyze the Migration of MGE-Derived InterneuronsClaire Leclech and Christine M\u00e9tin13. Cell Migration in Tissues: Explant Culture and Live ImagingRalitza Staneva, Jorge Barbazan, Anthony Simon, Danijela Matic Vignjevic, and Denis Krndija14. Intravital Imaging of Tumor Cell Motility in the Tumor Microenvironment ContextBattuya Bayarmagnai, Louisiane Perrin, Kamyar Esmaeilli Pourfarhangi, and Bojana Gligorijevic15. Using the Zebrafish Embryo to Dissect the Early Steps of Metastasis Cascade Gautier Follain, Na\u00ebl Osmani, C\u00e9dric Fuchs, Guillaume Allio, S\u00e9bastien Harlepp, and Jacky G. Goetz16. Analysis of In Vivo Cell Migration in Mosaic Zebrafish EmbryosArthur Boutillon, Florence A. Giger, and Nicolas B. David17. Analysis of Cell Shape and Cell Migration of Drosophila Macrophages In Vivo Marike R\u00fcder, Benedikt M. Nagel, and Sven Bogdan18. Migration of Q Cells in Caenorhabditis elegansYongping Chai, Zhiwen Zhu, and Guangshuo Ou\u00a019. Imaging the Molecular Machines that Power Cell MigrationAnika Steffen, Frieda Kage, and Klemens Rottner20. A Biologist-Friendly Method to Analyze Cross-Correlation between Protrusion Dynamics and Membrane Recruitment of Actin RegulatorsPerrine Paul-Gilloteaux, Fran\u00e7ois Waharte, Manish Kumar Singh, and Maria-Carla Parrini21. Using Single Protein Tracking to Study Cell MigrationThomas Orr\u00e9, Amine Mehidi, Sophie Massou, Olivier Rossier, and Gr\u00e9gory Giannone22. Optogenetics of Cell MigrationXenia Meshik, Patrick R. O'Neill, and N. Gautam23. Electrotaxis: Cell Directional Movement in Electric FieldsJolanta Sroka, Eliza Zimolag, Slawomir Lasota, Wlodzimierz Korohoda, and Zbigniew Madeja24. Analysis of Random Migration of Dictyostelium Amoeba in Confined or Unconfined EnvironmentsChristof Litschko, Julia Damiano-Guerico, Stefan Br\u00fchmann, and Jan Faix25. Neutrophil Chemotaxis in One Droplet of Blood using Microfluidic assaysXiao Wang and Daniel Irimia26. Leukocyte Migration and Deformation in Collagen Gels and Micro-Fabricated ConstrictionsPablo J. S\u00e1ez, Lucie Barbier, Rafaele Attia, Hawa-Racine Thiam, Matthieu Piel, and Pablo Vargas27. Microfluidic Devices for Examining the Physical Limits of Migration in Confined EnvironmentsMajid Malboubi, Asier Jayo, Maddy Parsons and Guillaume Charras28. Controlling Confinement and Topology to Study Collective Cell Behaviors Guillaume Duclos, Maxime Deforet, Hannah G. Yevick, Olivier Cochet-Escartin, Flora Ascione, Sarah Moitrier, Trinish Sarkar, Victor Yashunsky, Isabelle Bonnet, Axel Buguin, and Pascal Silberzan","merchants_number":2,"ean":9781493977000,"category_id":103,"size":null,"min_price":93.5,"low_price_merchant_id":1087639,"ID":4089587,"merchants":["dodax","euniverse"],"brand":"undefined","slug":"cell-migration","url":"\/unterhaltung\/produkt\/cell-migration\/","low_price_merchant_name":null}
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