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J domain independent functions of J proteins

Published:2016-05-04 Issue:4 Volume:21 Page:563-570
ISSN:1355-8145
Container-title:Cell Stress and Chaperones
language:en
Short-container-title:Cell Stress and Chaperones

Author:

Ajit Tamadaddi Chetana,Sahi Chandan

Funder

Department of Biotechnology , Ministry of Science and Technology

IISER Bhopal (IN)

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s12192-016-0697-1.pdf

Reference57 articles.

1. Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92:351–366

2. Cao M et al (2014) DnaJA1/Hsp40 is co-opted by influenza A virus to enhance its viral RNA polymerase activity. J Virol 88:14078–14089. doi: 10.1128/JVI.02475-14

3. Caplan AJ, Douglas MG (1991) Characterization of YDJ1: a yeast homologue of the bacterial dnaJ protein. J Cell Biol 114:609–621

4. Caplan AJ, Cyr DM, Douglas MG (1992) YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71:1143–1155

5. Chai Y, Koppenhafer SL, Bonini NM, Paulson HL (1999) Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease. J Neurosci 19:10338–10347

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2. Plasmodium falciparum J‐dot localized J domain protein A8iJp modulates the chaperone activity of human HSPA8;FEBS Letters;2024-02-28

3. The essential chaperone DNAJC17 activates HSP70 to coordinate RNA splicing and G2-M progression;2023-10-26

4. Unveiling Metastable Ensembles of GRB2 and the Relevance of Interdomain Communication during Folding;Journal of Chemical Information and Modeling;2023-10-12

5. The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70;Nature Communications;2023-09-05

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