Faculty Opinions recommendation of Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response.

Author(s):  
Franz Schmid
2001 ◽  
Vol 305 (5) ◽  
pp. 1173-1183 ◽  
Author(s):  
Yvonne Groemping ◽  
Dagmar Klostermeier ◽  
Christian Herrmann ◽  
Thomas Veit ◽  
Ralf Seidel ◽  
...  

2018 ◽  
Vol 399 (10) ◽  
pp. 1215-1221 ◽  
Author(s):  
Unekwu M. Yakubu ◽  
Kevin A. Morano

Abstract Cellular protein homeostasis (proteostasis) is maintained by a broad network of proteins involved in synthesis, folding, triage, repair and degradation. Chief among these are molecular chaperones and their cofactors that act as powerful protein remodelers. The growing realization that many human pathologies are fundamentally diseases of protein misfolding (proteopathies) has generated interest in understanding how the proteostasis network impacts onset and progression of these diseases. In this minireview, we highlight recent progress in understanding the enigmatic Hsp110 class of heat shock protein that acts as both a potent nucleotide exchange factor to regulate activity of the foldase Hsp70, and as a passive chaperone capable of recognizing and binding cellular substrates on its own, and its integration into the proteostasis network.


2000 ◽  
Vol 276 (9) ◽  
pp. 6098-6104 ◽  
Author(s):  
John P. A. Grimshaw ◽  
Ilian Jelesarov ◽  
Hans-Joachim Schönfeld ◽  
Philipp Christen

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