Cracking the Chaperone Code: Cellular Roles for Hsp70 Phosphorylation

Trends in Biochemical Sciences
Nitika, Andrew W Truman

Abstract

Heat shock protein 70 (Hsp70) is a molecular chaperone required for protein folding, cell viability, and cancer cell proliferation. Recent studies suggest that Hsp70 phosphorylation regulates important cellular processes, such as cell cycle progression, apoptosis, protein degradation, and resistance to anticancer therapeutics.

Citations

Nov 23, 2019·Biochemical Society Transactions·Cristina Daneri-BecerraMario D Galigniana
Jun 11, 2020·The Journal of Biological Chemistry· NitikaMatthias C Truttmann
Jun 13, 2020·The Journal of Biological Chemistry·Sarah J BackeMehdi Mollapour
Dec 7, 2018·Current Genetics·Laura E KnightonAndrew W Truman
Aug 28, 2019·International Journal of Molecular Sciences·Lorea VelascoArturo Muga
Oct 2, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Xiaoying HeJunying Miao
Apr 27, 2018·Cell Stress & Chaperones·Shawn J WallerAndrew W Truman
Nov 9, 2019·Scientific Reports·Linan XuAndrew W Truman
Sep 27, 2019·Frontiers in Molecular Biosciences·Jade E TakakuwaAndrew W Truman
Apr 26, 2019·Current Genetics·Sarah K LotzAndrew W Truman
Apr 2, 2020·Cancer Biology & Therapy·Sonam Mittal, Maitreyi S Rajala
Apr 25, 2020·The Science of the Total Environment·Silvia FranzellittiElena Fabbri
Jan 23, 2020·Biochimica Et Biophysica Acta. Proteins and Proteomics·Ziva WeissmanDaniel Kornitzer
Aug 25, 2021·International Journal of Biological Macromolecules·Vaha Akbary MoghaddamAsadollah Mohammadi

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