000 04179nam a22005535i 4500
001 978-3-031-14740-1
003 DE-He213
005 20240729135850.0
007 cr nn 008mamaa
008 221215s2023 sz | s |||| 0|eng d
020 _a9783031147401
_9978-3-031-14740-1
024 7 _a10.1007/978-3-031-14740-1
_2doi
072 7 _aPSF
_2bicssc
072 7 _aSCI017000
_2bisacsh
072 7 _aPSF
_2thema
245 1 4 _aThe Networking of Chaperones by Co-Chaperones
250 _a3rd ed. 2023.
264 1 _aCham :
_bSpringer International Publishing :
_bImprint: Springer,
_c2023.
300 _aXV, 429 p. 53 illus., 46 illus. in color.
_bonline resource.
336 _atext
_btxt
_2rdacontent
337 _acomputer
_bc
_2rdamedia
338 _aonline resource
_bcr
_2rdacarrier
347 _atext file
_bPDF
_2rda
490 1 _aSubcellular Biochemistry,
_x2542-8810 ;
_v101
505 0 _aChapter 1: GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones -- Chapter 2: Functions of the Hsp90-Binding FKBP Immunophilins -- Chapter 3: Hsp70/Hsp90 organising protein (Hop): coordinating much more than chaperones -- Chapter 4: Specification of Hsp70 function by Hsp40 Co-Chaperones -- Chapter 5: Cdc37 as a Co-chaperone to Hsp90 -- Chapter 6: p23 and Aha1 - Distinct functions promote client maturation -- Chapter 7: Beyond chaperoning: UCS proteins emerge as regulators of myosin-mediated cellular processes -- Chapter 8: Chaperonin - Co-Chaperonin Interactions -- Chapter 9: Co-chaperones of the human endoplasmic reticulum: an update -- Chapter 10: J Domain Proteins Orchestrate the Multifunctionality of Hsp70s in Mitochondria: Insights from Mechanistic and Evolutionary Analyses -- Chapter 11: Impact of co-chaperones and post-translational modifications towards Hsp90 drug sensitivity -- Chapter 12: CHIP: a co-chaperone for degradation by the proteasome and lysosome -- Chapter 13: HSP70-HSP90 chaperone networking in protein misfolding disease.
520 _aCo-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is the dynamic integration of the processes of protein folding, degradation and translocation to ensure that cellular function is finely tuned in space and time. This third edition of the book The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by co-chaperones, a diverse cohort of non-client proteins. Since the second edition was released, not only has knowledge deepened on how co-chaperones act as nodes to network and functionalise chaperones, but an understanding of their broader biological function has started to emerge. The third edition provides new and updated chapters highlighting recent developments and emerging themes on co-chaperones, such as their extracellular functions, their role in human disease and their status as putative drug targets. The book is a useful resourcefor both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology. .
650 0 _aProtein folding.
650 0 _aProteins .
_97571
650 0 _aPost-translational modification.
650 0 _aCytology.
650 0 _aBiomolecules.
650 0 _aPhysical biochemistry.
650 0 _aMacromolecules.
650 1 4 _aProtein Folding.
650 2 4 _aProtein Biochemistry.
650 2 4 _aPost-translational Modifications.
650 2 4 _aCell Biology.
650 2 4 _aStructural Biology.
700 1 _aEdkins, Adrienne L.
_eeditor.
_4edt
_4http://id.loc.gov/vocabulary/relators/edt
700 1 _aBlatch, Gregory L.
_eeditor.
_4edt
_4http://id.loc.gov/vocabulary/relators/edt
710 2 _aSpringerLink (Online service)
830 0 _aSubcellular Biochemistry,
_x2542-8810 ;
_v101
856 _u#gotoholdings
_yAccess resource
912 _aZDB-2-SBL
912 _aZDB-2-SXB
245 _h[E-Book]
999 _c103336
_d103336