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Human nasal primary cell cultures for peptide delivery studies
Many proteins and peptides possess biological activity that makes them highly specific and effective therapeutic agents. For the treatment of chronic diseases or disorders (e.g. diabetes, cancer, osteoporosis, etc), however, they cannot be orally administered due to a rapid hydrolysis of the peptide bonds by digestive proteases. This work was done to explore the nasal route as a promi... zur Produkt-Seite
4588892 {"price-changing":null,"image":"https:\/\/image.vergleiche.ch\/small\/aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTQ5NDExODgzX2pieWFkLXBuZw==!aHR0cHM6Ly9jNC1zdGF0aWMuZG9kYXguY29tL3YyLzE4MC0xODAtMTQ5NDExODgzX2pieWFkLXBuZw==","post_title":"Human nasal primary cell cultures for peptide delivery studies","deeplink":"https:\/\/www.awin1.com\/pclick.php?p=22944228465&a=401125&m=11816&pref1=9783659824913","labels":[],"brand_id":1,"post_content":"Many proteins and peptides possess biological activity that makes them highly specific and effective therapeutic agents. For the treatment of chronic diseases or disorders (e.g. diabetes, cancer, osteoporosis, etc), however, they cannot be orally administered due to a rapid hydrolysis of the peptide bonds by digestive proteases. This work was done to explore the nasal route as a promising alternative to parenteral injections for systemic delivery of proteins and peptides due to its high vascularity of the mucosa, large surface area, avoidance of first-pass metabolism, ease of drug administration and high systemic bioavailability. Four primary culture systems of human nasal epithelium (i.e. immersion, air-liquid interface, floating collagen and sequential monolayer-suspension) were compared for peptide absorption and metabolism studies. Although these cell culture models are not identical with the epithelial cells under in vivo situation, the results reported in this book highlight the biopharmaceutical relevance of collagen-based human nasal primary cell culture systems as models for mechanistic assessment of nasal drug delivery.","merchants_number":1,"ean":9783659824913,"category_id":103,"size":null,"min_price":48.64999999999999857891452847979962825775146484375,"low_price_merchant_id":1087639,"ID":4588892,"merchants":["dodax"],"brand":"undefined","slug":"human-nasal-primary-cell-cultures-for-peptide-delivery-studies","url":"\/unterhaltung\/produkt\/human-nasal-primary-cell-cultures-for-peptide-delivery-studies\/","low_price_merchant_name":null}
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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"}
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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"}
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Human nasal primary cell cultures for pept...
Many proteins and peptides possess biological activity that makes them highly specific and effective therapeutic agents. For the treatment of chron...
undefined
Peptide Self-Assembly
Part I: Fundamental Methods for Characterizing Peptide Self-Assembly 1. Methods for Structural Analysis of Aggregates Formed by Self-Assemblin...
undefined
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-Translat...