,

The Networking of Chaperones by Co-chaperones

Control of Cellular Protein Homeostasis

Specificaties
Gebonden, 276 blz. | Engels
Springer International Publishing | 2015e druk, 2015
ISBN13: 9783319117300
Rubricering
Springer International Publishing 2015e druk, 2015 9783319117300
Onderdeel van serie Subcellular Biochemistry
Verwachte levertijd ongeveer 9 werkdagen

Samenvatting

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.

Specificaties

ISBN13:9783319117300
Taal:Engels
Bindwijze:gebonden
Aantal pagina's:276
Uitgever:Springer International Publishing
Druk:2015

Inhoudsopgave

<p>Preface<br>List of Contributors<br>About the Editors<br>1<br>GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones<br>Andreas Bracher and Jacob Verghese<br><br>2<br>Functions of the Hsp90-Binding FKBP Immunophilins<br>Naihsuan Guy, Yenni A. Garcia, Jeffrey C. Sivils, Mario D. Galigniana, and Marc B. Cox<br><br>3<br>Hsp70/Hsp90 organising protein (Hop): beyond interactions with chaperones and prion proteins<br>Swati Baindur-Hudson, Adrienne L. Edkins, and Gregory L. Blatch<br><br>4<br> Specification of Hsp70 function by Type I and Type II Hsp40<br>Douglas M. Cyr and Carlos H. Ramos<br><br>5<br>Cdc37 as a Co-chaperone to Hsp90<br>Stuart K Calderwood<br><br>6<br>p23 and Aha1<br>Alexandra B Rehn and Johannes Buchner<br><br>7<br>UCS proteins: chaperones for myosin and co-chaperones for Hsp90<br>Weiming Ni and Odutayo O. Odunuga<br><br>8<br>Chaperonin - Co-chaperonin Interactions<br>Aileen Boshoff<br><br>9<br> Co-chaperones of the mammalian endoplasmic reticulum<br>Armin Melnyk, Heiko Rieger and Richard Zimmermann<br><br>10<br>The evolution and function of co-chaperones in mitochondriaNeta Regev-Rudzki, Kip Gabriel and Dejan Bursać<br><br>11<br>CHIP: a co-chaperone for degradation by the proteasome<br>Adrienne L. Edkins<br><br>12<br>The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease<br>Emma J. Duncan, Michael E. Cheetham, J. Paul Chapple, and Jacqueline van der Spuy<br><br>Index<br></p>

Rubrieken

    Personen

      Trefwoorden

        The Networking of Chaperones by Co-chaperones