Chaperones (eBook, PDF)
Methods and Protocols
Redaktion: Calderwood, Stuart K.; Prince, Thomas L.
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Chaperones (eBook, PDF)
Methods and Protocols
Redaktion: Calderwood, Stuart K.; Prince, Thomas L.
- Format: PDF
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Includes cutting-edge methods and protocols Provides step-by-step detail essential for reproducible results Contains key notes and implementation advice from the experts
- Geräte: PC
- ohne Kopierschutz
- eBook Hilfe
- Größe: 10.55MB
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Includes cutting-edge methods and protocols
Provides step-by-step detail essential for reproducible results
Contains key notes and implementation advice from the experts
Dieser Download kann aus rechtlichen Gründen nur mit Rechnungsadresse in A, B, BG, CY, CZ, D, DK, EW, E, FIN, F, GR, HR, H, IRL, I, LT, L, LR, M, NL, PL, P, R, S, SLO, SK ausgeliefert werden.
Produktdetails
- Produktdetails
- Verlag: Springer US
- Seitenzahl: 445
- Erscheinungstermin: 24. November 2017
- Englisch
- ISBN-13: 9781493974771
- Artikelnr.: 64692266
- Verlag: Springer US
- Seitenzahl: 445
- Erscheinungstermin: 24. November 2017
- Englisch
- ISBN-13: 9781493974771
- Artikelnr.: 64692266
- Herstellerkennzeichnung Die Herstellerinformationen sind derzeit nicht verfügbar.
Targeted Deletion of Hsf1, 2 and 4 Genes in Mice.- Role of Heat Shock Factors in Stress-induced Transcription.- Monitoring of the Heat Shock Response with a Real-time Luciferase Reporter.- Quantitative Profiling of Chaperone/client Interactions with LUMIER Assay.- Measurement of chaperone-mediated effects on Polyglutamine Protein Aggregation by the Filter Trap Assay.- Fluorescent-linked Enzyme Chemoproteomic Strategy (FLECS) for Identifying HSP70 Inhibitors.- A High-throughput Screen for Inhibitors of the Hsp90-Chaperone Machine.- Primary Colorectal Cells Culture as a Translation Research Model.- Cell Death and Survival Assays.- Detecting the Potential Pharmacological Synergy of Drug Combination by Viability Assays In Vitro0pt;">.- nt-size: 12.0ptProteomic Profiling of Hsp90 Inhibitors.- Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and its Interaction with Specific Client Polypeptides.- Nucleotide Exchange Factors for Hsp70 Chaperones.- Determination of Hsp90Activity through Activation of Glucocorticoid Receptors in Yeast.- Bacterial Hsp90 ATPase Assays.- Detecting Post-translational Modifications of Hsp90.- Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90).- background-image: initial; background-position: initial; background-size: initial; background-repeat: initial; background-attachment: initial; background-origin: initial; background-clip: initial; font-size: 12pt; font-family: "Times New Roman", serif; color: rgb(33, 33, 33);">A Workflow Guide to RNA-seq Analysis of Chaperone Function and Beyond.- Computational Modeling of the Hsp90 Interactions with Cochaperones and Small Molecule Inhibitors.- Computational Analysis of the Chaperone Interaction Networks.- Immunohistochemistry of Human Hsp60 in Health and Disease: From Autoimmunity to Cancer.- Immunohistochemical and Flow Cytometric Analysis of Intracellular and Membrane-bound Hsp70, as a Putative Biomarker of Glioblastoma Multiforme, using the cmHsp70.1 MonoclonalDetection and Analysis of Extracellular Hsp90 (eHsp90).- Molecular Chaperone Receptors.- Creation of Recombinant Chaperone Vaccine using Large Heat Shock Protein for Antigen-targeted Cancer Immunotherapy.- A Novel Heat Shock Protein 70-based Vaccine Prepared from DC-Tumor Fusion Cells.- Hsp70: A Cancer Target Inside and Outside the Cell.- Evidence for Hsp90 Cochaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.- Clinical Evaluation and Biomarker Profiling of Hsp90 Inhibitors.n>ttom:.0001pt;line-height: normal;mso-layout-grid-align:none;text-autospace:none">
Targeted Deletion of Hsf1, 2 and 4 Genes in Mice.- Role of Heat Shock Factors in Stress-induced Transcription.- Monitoring of the Heat Shock Response with a Real-time Luciferase Reporter.- Quantitative Profiling of Chaperone/client Interactions with LUMIER Assay.- Measurement of chaperone-mediated effects on Polyglutamine Protein Aggregation by the Filter Trap Assay.- Fluorescent-linked Enzyme Chemoproteomic Strategy (FLECS) for Identifying HSP70 Inhibitors.- A High-throughput Screen for Inhibitors of the Hsp90-Chaperone Machine.- Primary Colorectal Cells Culture as a Translation Research Model.- Cell Death and Survival Assays.- Detecting the Potential Pharmacological Synergy of Drug Combination by Viability Assays In Vitro0pt;">.- nt-size: 12.0ptProteomic Profiling of Hsp90 Inhibitors.- Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and its Interaction with Specific Client Polypeptides.- Nucleotide Exchange Factors for Hsp70 Chaperones.- Determination of Hsp90Activity through Activation of Glucocorticoid Receptors in Yeast.- Bacterial Hsp90 ATPase Assays.- Detecting Post-translational Modifications of Hsp90.- Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90).- background-image: initial; background-position: initial; background-size: initial; background-repeat: initial; background-attachment: initial; background-origin: initial; background-clip: initial; font-size: 12pt; font-family: "Times New Roman", serif; color: rgb(33, 33, 33);">A Workflow Guide to RNA-seq Analysis of Chaperone Function and Beyond.- Computational Modeling of the Hsp90 Interactions with Cochaperones and Small Molecule Inhibitors.- Computational Analysis of the Chaperone Interaction Networks.- Immunohistochemistry of Human Hsp60 in Health and Disease: From Autoimmunity to Cancer.- Immunohistochemical and Flow Cytometric Analysis of Intracellular and Membrane-bound Hsp70, as a Putative Biomarker of Glioblastoma Multiforme, using the cmHsp70.1 MonoclonalDetection and Analysis of Extracellular Hsp90 (eHsp90).- Molecular Chaperone Receptors.- Creation of Recombinant Chaperone Vaccine using Large Heat Shock Protein for Antigen-targeted Cancer Immunotherapy.- A Novel Heat Shock Protein 70-based Vaccine Prepared from DC-Tumor Fusion Cells.- Hsp70: A Cancer Target Inside and Outside the Cell.- Evidence for Hsp90 Cochaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.- Clinical Evaluation and Biomarker Profiling of Hsp90 Inhibitors.n>ttom:.0001pt;line-height: normal;mso-layout-grid-align:none;text-autospace:none">







