Blatch / Edkins | The Networking of Chaperones by Co-chaperones | E-Book | sack.de
E-Book

E-Book, Englisch, Band 78, 276 Seiten, eBook

Reihe: Subcellular Biochemistry

Blatch / Edkins The Networking of Chaperones by Co-chaperones

Control of Cellular Protein Homeostasis
1. Auflage 2014
ISBN: 978-3-319-11731-7
Verlag: Springer International Publishing
Format: PDF
 Kopierschutz: 1 - PDF Watermark

Control of Cellular Protein Homeostasis

E-Book, Englisch, Band 78, 276 Seiten, eBook

Reihe: Subcellular Biochemistry

ISBN: 978-3-319-11731-7
Verlag: Springer International Publishing
Format: PDF
 Kopierschutz: 1 - PDF Watermark

Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a 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.
Blatch / Edkins The Networking of Chaperones by Co-chaperones jetzt bestellen!

Zielgruppe

Research

Autoren/Hrsg.

Blatch, Gregory Lloyd
Blatch, Gregory
Edkins, Adrienne Lesley

Weitere Infos & Material

Preface.- List of Contributors- About the Editors- GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones.- Functions of the Hsp90-Binding FKBP Immunophilins.- Hsp70/Hsp90 organising protein (Hop): beyond interactions with chaperones and prion proteins.- Specification of Hsp70 function by Type I and Type II Hsp40.- Cdc37 as a Co-chaperone to Hsp90.- p23 and Aha1- UCS proteins: chaperones for myosin and co-chaperones for Hsp90.- Chaperonin - Co-chaperonin Interactions.- Co-chaperones of the mammalian endoplasmic reticulum.- The evolution and function of co-chaperones in mitochondria.- CHIP: a co-chaperone for degradation by the proteasome.- The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease.- Index

Ihre Fragen, Wünsche oder Anmerkungen
Vorname*
Nachname*
Ihre E-Mail-Adresse*
Kundennr.
Ihre Nachricht*
Lediglich mit * gekennzeichnete Felder sind Pflichtfelder.
Wenn Sie die im Kontaktformular eingegebenen Daten durch Klick auf den nachfolgenden Button übersenden, erklären Sie sich damit einverstanden, dass wir Ihr Angaben für die Beantwortung Ihrer Anfrage verwenden. Selbstverständlich werden Ihre Daten vertraulich behandelt und nicht an Dritte weitergegeben. Sie können der Verwendung Ihrer Daten jederzeit widersprechen. Das Datenhandling bei Sack Fachmedien erklären wir Ihnen in unserer Datenschutzerklärung.