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008			221215s2023 sz | o |||| 0|eng d
020			_a9783031147401
024	7		_a10.1007/978-3-031-14740-1 _2doi
040			_aES-MaUEC _bspa _cES-MaUEC _dES-MaUEC
050		4	_aQP551 _b2023 EB
245	0	4	_aThe Networking of Chaperones by Co-Chaperones _cedited by Adrienne L Edkins, Gregory L Blatch
250			_a3rd ed. 2023.
264		1	_aCham _bSpringer International Publishing _c2023
300			_a1 recurso en línea
336			_atexto _btxt _2rdacontent
337			_aelectrónico _bc _2rdamedia
338			_arecurso electrónico _bcr _2rdacarrier
490	0		_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 resource for 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.
988			_aSpringer_BiomedLife_2023
650		7	_2embne _9139861 _aProteínas
856	4	0	_uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1007/978-3-031-14740-1 _zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942			_2lcc _cLE
998			_b04/2024 _dz _ek _zSI