HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins
Human small heat shock proteins are molecular chaperones that regulate fundamental cellular processes in normal unstressed cells as well as in many cancer cells where they are over-expressed. These proteins are characterized by cell physiology dependent changes in their oligomerization and phosphory...
Main Authors: | André-Patrick Arrigo, Benjamin Gibert |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2014-02-01
|
Series: | Cancers |
Subjects: | |
Online Access: | http://www.mdpi.com/2072-6694/6/1/333 |
Similar Items
-
Phosphorylation of the Chaperone-Like HspB5 Rescues Trafficking and Function of F508del-CFTR
by: Fanny Degrugillier, et al.
Published: (2020-07-01) -
Quaternary Structure and Hetero-Oligomerization of Recombinant Human Small Heat Shock Protein HspB7 (cvHsp)
by: Lydia K. Muranova, et al.
Published: (2021-07-01) -
Small Hsps as Therapeutic Targets of Cystic Fibrosis Transmembrane Conductance Regulator Protein
by: Stéphanie Simon, et al.
Published: (2021-04-01) -
The Heterooligomerization of Human Small Heat Shock Proteins Is Controlled by Conserved Motif Located in the N-Terminal Domain
by: Vladislav M. Shatov, et al.
Published: (2020-06-01) -
Molecular Chaperones’ Potential against Defective Proteostasis of Amyotrophic Lateral Sclerosis
by: Sumit Kinger, et al.
Published: (2023-05-01)