Function, evolution, and structure of J-domain proteins-Reference-Cited by-同舟云学术

Function, evolution, and structure of J-domain proteins

Published:2018-11-26 Issue:1 Volume:24 Page:7-15
ISSN:1355-8145
Container-title:Cell Stress and Chaperones
language:en
Short-container-title:Cell Stress and Chaperones

Author:

Kampinga Harm H.,Andreasson Claes,Barducci Alessandro,Cheetham Michael E.,Cyr Douglas,Emanuelsson Cecilia,Genevaux Pierre,Gestwicki Jason E.,Goloubinoff Pierre,Huerta-Cepas Jaime,Kirstein Janine,Liberek Krzysztof,Mayer Matthias P.,Nagata Kazuhiro,Nillegoda Nadinath B.,Pulido Pablo,Ramos Carlos,De los Rios Paolo,Rospert Sabine,Rosenzweig Rina,Sahi Chandan,Taipale Mikko,Tomiczek Bratłomiej,Ushioda Ryo,Young Jason C.,Zimmermann Richard,Zylicz Alicja,Zylicz Maciej,Craig Elizabeth A.,Marszalek Jaroslaw

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry

Link

https://link.springer.com/article/10.1007/s12192-018-0948-4/fulltext.html

Reference52 articles.

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2. Behnke J, Mann MJ, Scruggs FL, Feige MJ, Hendershot LM (2016) Members of the Hsp70 family recognize distinct types of sequences to execute ER quality control. Mol Cell 63(5):739–752

3. Bracher A, Verghese J (2015) The nucleotide exchange factors of Hsp70 molecular chaperones. Front Mol Biosci 2:10

4. Cheetham ME, Caplan AJ (1998) Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3(1):28–36

5. Chen KC, Qu S, Chowdhury S, Noxon IC, Schonhoft JD, Plate L, Powers ET, Kelly JW, Lander GC, Wiseman RL (2017) The endoplasmic reticulum HSP40 co-chaperone ERdj3/DNAJB11 assembles and functions as a tetramer. EMBO J 36(15):2296–2309

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