An edition of Molecular chaperones
(2011)
Molecular chaperones
methods and protocols
by Stuart K. Calderwood and Thomas L. Prince
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Book Details
Table of Contents
Targeted deletion of Hsf1, 2, and 4 genes in mice
The role of heat shock factors in stress-induced transcription
Hsp90 and client protein maturation
The role of p23, hop, immunophilins, and other co-chaperones in regulating hsp90 function
Detecting HSP90 phosphorylation
Role of molecular chaperones in biogenesis of the protein kinome
Nucleotide exchange factors for hsp70 chaperones
Reconstitution of CHIP E3 ubiquitin ligase activity
Structure-functions of hspB1 (hsp27)
Combined lentiviral and rnai technologies for the delivery and permanent silencing of the hsp25 gene
Quantification of HSP27 and HSP70 molecular chaperone activities
Measuring hsp72 (HSPA1A) by indirect sandwich ELISA
Analysis of heat-shock protein localisation using flow cytometry
Quantitation of heat-shock proteins in clinical samples using mass spectrometry
Bioinformatic approach to identify chaperone pathway relationship from large-scale interaction networks
Hsp70: Anti-apoptotic and tumorigenic protein
Determination of cell survival or death
Immunohistochemistry of human hsp60 in health and disease: From autoimmunity to cancer
Preparation of a heat-shock protein 70-based vaccine from DC-tumor fusion cells
Isolation of heat shock protein complexes
Enhancing antigen cross-presentation and T-cell priming by complexing protein antigen to recombinant large heat-shock protein
Investigating receptors for extracellular heat shock proteins
Analysis of cellular migration using a two-chamber methodology.
Edition Notes
Includes bibliographical references and index.
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History
- Created February 1, 2012
- 12 revisions
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| August 27, 2024 | Edited by MARC Bot | import existing book |
| February 17, 2024 | Edited by ImportBot | import existing book |
| December 23, 2022 | Edited by ImportBot | import existing book |
| December 4, 2022 | Edited by ImportBot | import existing book |
| February 1, 2012 | Created by LC Bot | Imported from Library of Congress MARC record |