Small glutamine-rich protein/viral protein U–binding protein is a novel cochaperone that affects heat shock protein 70 activity
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Biochemistry
Reference36 articles.
1. Tyrosine kinase-dependent release of an adenovirus preterminal protein complex from the nuclear matrix
2. Adenovirus Preterminal Protein Binds to the CAD Enzyme at Active Sites of Viral DNA Replication on the Nuclear Matrix
3. Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions
4. BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release
5. Functional Interaction of Human Immunodeficiency Virus Type 1 Vpu and Gag with a Novel Member of the Tetratricopeptide Repeat Protein Family
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1. Hsp70/Hsp90 Organising Protein (Hop): Coordinating Much More than Chaperones;Subcellular Biochemistry;2022-12-16
2. Insights into the structure and function of the C-terminus of SGTs (small glutamine-rich TPR-containing proteins): A study of the Aedes aegypti homolog;Biochimie;2021-08
3. Vincristine ablation of Sirt2 induces cell apoptosis and mitophagy via Hsp70 acetylation in MDA-MB-231 cells;Biochemical Pharmacology;2019-04
4. SGTb regulates a surface localization of a guidance receptor BOC to promote neurite outgrowth;Cellular Signalling;2019-03
5. Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities;International Journal of Biological Macromolecules;2018-10
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