東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

The networking of chaperones by co-c...

Edkins, Adrienne Lesley.

FindBook

Google Book

Amazon

博客來

The networking of chaperones by co-chaperones

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	The networking of chaperones by co-chaperones/ edited by Adrienne L. Edkins, Gregory L. Blatch.
其他作者:	Edkins, Adrienne Lesley.
出版者:	Cham :Springer International Publishing : : 2023.,
面頁冊數:	xv, 429 p. :ill., digital ;24 cm.
內容註:	Chapter 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.
Contained By:	Springer Nature eBook
標題:	Molecular chaperones. -
電子資源:	https://doi.org/10.1007/978-3-031-14740-1
ISBN:	9783031147401

The networking of chaperones by co-chaperones
The networking of chaperones by co-chaperones[electronic resource] /edited by Adrienne L. Edkins, Gregory L. Blatch. - Third edition. - Cham :Springer International Publishing :2023. - xv, 429 p. :ill., digital ;24 cm. - Subcellular biochemistry,v. 1012542-8810 ;. - Subcellular biochemistry ;v. 101..

Chapter 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.

Co-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.

ISBN: 9783031147401

Standard No.: 10.1007/978-3-031-14740-1doiSubjects--Topical Terms:

816775
Molecular chaperones.

LC Class. No.: QP552.M64 / N47 2023

Dewey Class. No.: 572.633

The networking of chaperones by co-chaperones
LDR:03382nmm a2200349 a 4500 001 2313968
003 DE-He213
005 20221215110108.0
006 m d
007 cr nn 008mamaa
008 230902s2023 sz s 0 eng d
020 $a 9783031147401 $q (electronic bk.)
020 $a 9783031147395 $q (paper)
024 7 $a 10.1007/978-3-031-14740-1 $2 doi
035 $a 978-3-031-14740-1
040 $a GP $c GP
041 0 $a eng
050 4 $a QP552.M64 $b N47 2023
072 7 $a PSF $2 bicssc
072 7 $a SCI049000 $2 bisacsh
072 7 $a PSF $2 thema
082 0 4 $a 572.633 $2 23
090 $a QP552.M64 $b N476 2023
245 0 4 $a The networking of chaperones by co-chaperones $h [electronic resource] / $c edited by Adrienne L. Edkins, Gregory L. Blatch.
250 $a Third edition.
260 $a Cham : $b Springer International Publishing : $b Imprint: Springer, $c 2023.
300 $a xv, 429 p. : $b ill., digital ; $c 24 cm.
490 1 $a Subcellular biochemistry, $x 2542-8810 ; $v v. 101
505 0 $a Chapter 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 $a Co-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.
650 0 $a Molecular chaperones. $3 816775
650 1 4 $a Protein Folding. $3 916838
650 2 4 $a Protein Biochemistry. $3 3603770
650 2 4 $a Post-translational Modifications. $3 3603792
650 2 4 $a Cell Biology. $3 892383
650 2 4 $a Structural Biology. $3 3538470
700 1 $a Edkins, Adrienne Lesley. $3 2133226
700 1 $a Blatch, Gregory L. $3 2054938
710 2 $a SpringerLink (Online service) $3 836513
773 0 $t Springer Nature eBook
830 0 $a Subcellular biochemistry ; $v v. 101. $3 3625083
856 4 0 $u https://doi.org/10.1007/978-3-031-14740-1
950 $a Biomedical and Life Sciences (SpringerNature-11642)