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000745205 019__ $$a891386943
000745205 020__ $$a9781493911301$$qelectronic book
000745205 020__ $$a1493911309$$qelectronic book
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000745205 0247_ $$a10.1007/978-1-4939-1130-1$$2doi
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000745205 035__ $$aSP(OCoLC)890794344$$z(OCoLC)891386943
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000745205 049__ $$aISEA
000745205 050_4 $$aQP552.M64
000745205 08204 $$a572/.6$$223
000745205 24504 $$aThe molecular chaperones interaction networks in protein folding and degradation$$h[electronic resource] /$$cWalid A. Houry, editor.
000745205 264_1 $$aNew York, NY :$$bSpringer,$$c[2014]
000745205 264_4 $$c©2014
000745205 300__ $$a1 online resource (xv, 485 pages) :$$billustrations.
000745205 336__ $$atext$$btxt$$2rdacontent
000745205 337__ $$acomputer$$bc$$2rdamedia
000745205 338__ $$aonline resource$$bcr$$2rdacarrier
000745205 4901_ $$aInteractomics and systems biology
000745205 500__ $$aIncludes index.
000745205 504__ $$aIncludes bibliographical references at the end of each chapters and index.
000745205 5050_ $$aPart I: Global View of the Chaperone Network -- Analysis of Chaperone Network Throughput -- Part II: Chaperones at the Ribosome -- Functions of Ribosome-associated Chaperones and Their Interaction Network -- Part III: The Hsp 70 and Hsp40 Chaperone Networks -- Yeast Hsp70 and J-protein Chaperones: Function and Interaction Network -- The Chaperone Networks: An Hsp70 Perspective -- Part IV: The Hsp90 Chaperone Network -- The Interaction Network of the Hsp90 Molecular Chaperone -- A Global View of the Proteome Perturbations by Hsp90 Inhibitors -- Designing Drugs Against Hsp90 for Cancer Therapy -- The Candida albicans Hsp90 Chaperone Network is Environmentally Flexible and Evolutionarily Divergent -- Part V: The p23 Chaperone Network -- Emergence and Characterization of the p23 Molecular Chaperone -- Part VI: Chaperones in the ER: Function and Interaction Network -- Chaperones of the ERAD Pathway -- Chaperones and Proteases of Mitochondria: From Protein Folding and Degradation to Mitophagy -- Part VII: The Ubiquitin-Proteasome System Network -- The Biogenesis of the Eukaryotic Proteasome -- Systems-wide Analysis of Protein Ubiquitylation: We Finally Have the Tiger by the Tail -- Part VIII: The Chaperone and Protease Networks in Model Bacteria and Parasites -- The Interaction Networks of E. coli Chaperones -- Chaperone-Proteases of Mycobacteria -- The Interaction Networks of Hsp70 and Hsp90 in the Plasmodium and Leishmania Parasites -- Index.
000745205 506__ $$aAccess limited to authorized users.
000745205 520__ $$aMolecular chaperones are a fundamental group of proteins that have been identified only relatively recently. They are key components of a protein quality machinery in the cell which insures that the folding process of any newly-synthesized polypeptide chain results in the formation of a properly folded protein and that the folded protein is maintained in an active conformation throughout its functional lifetime. Molecular chaperones have been shown to play essential roles in cell viability under both normal and stress conditions. Chaperones can also assist in the unfolding and degradation of misfolded proteins and in disaggregating preformed protein aggregates. Chaperones are also involved in other cellular functions including protein translocation across membranes, vesicle fusion events, and protein secretion. In recent years, tremendous advances have been made in our understanding of the biology, biochemistry, and biophysics of function of molecular chaperones. In addition, recent technical developments in the fields of proteomics and genomics allowed us to obtain a global view of chaperone interaction networks. Finally, there is now a growing interest in the role of molecular chaperones in diseases. This book will provide a comprehensive analysis of the structure and function of the diverse systems of molecular chaperones and their role in cell stress responses and in diseases from a global network perspective.
000745205 588__ $$aOnline resource; title from PDF title page (SpringerLink, viewed September 18, 2014).
000745205 650_0 $$aMolecular chaperones.
000745205 650_0 $$aProtein folding.
000745205 7001_ $$aHoury, Walid A.,$$eeditor.
000745205 77608 $$iPrint version:$$z9781493911295
000745205 830_0 $$aInteractomics and systems biology.
000745205 85280 $$bebk$$hSpringerLink
000745205 85640 $$3SpringerLink$$uhttps://univsouthin.idm.oclc.org/login?url=http://link.springer.com/10.1007/978-1-4939-1130-1$$zOnline Access$$91397441.1
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000745205 980__ $$aEBOOK
000745205 980__ $$aBIB
000745205 982__ $$aEbook
000745205 983__ $$aOnline
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