The Hsp70 chaperone network
R Rosenzweig, NB Nillegoda, MP Mayer… - … reviews molecular cell …, 2019 - nature.com
The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a
large variety of cellular protein folding and remodelling processes. They function virtually at …
large variety of cellular protein folding and remodelling processes. They function virtually at …
In vivo aspects of protein folding and quality control
BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …
Molecular dissection of amyloid disaggregation by human HSP70
AS Wentink, NB Nillegoda, J Feufel, G Ubartaitė… - Nature, 2020 - nature.com
The deposition of highly ordered fibrillar-type aggregates into inclusion bodies is a hallmark
of neurodegenerative diseases such as Parkinson's disease. The high stability of such …
of neurodegenerative diseases such as Parkinson's disease. The high stability of such …
Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones
MP Mayer, LM Gierasch - Journal of Biological Chemistry, 2019 - ASBMB
Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …
Molecular mechanism of J-domain-triggered ATP hydrolysis by Hsp70 chaperones
R Kityk, J Kopp, MP Mayer - Molecular cell, 2018 - cell.com
Efficient targeting of Hsp70 chaperones to substrate proteins depends on J-domain
cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and …
cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and …
A J-protein co-chaperone recruits BiP to monomerize IRE1 and repress the unfolded protein response
N Amin-Wetzel, RA Saunders, MJ Kamphuis, C Rato… - Cell, 2017 - cell.com
When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein
response (UPR) increases ER-protein-folding capacity to restore protein-folding …
response (UPR) increases ER-protein-folding capacity to restore protein-folding …
Recent advances in understanding catalysis of protein folding by molecular chaperones
Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …
How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions
EM Clerico, JM Tilitsky, W Meng… - Journal of molecular …, 2015 - Elsevier
Hsp70 molecular chaperones are implicated in a wide variety of cellular processes,
including protein biogenesis, protection of the proteome from stress, recovery of proteins …
including protein biogenesis, protection of the proteome from stress, recovery of proteins …
[HTML][HTML] Chaperones directly and efficiently disperse stress-triggered biomolecular condensates
Stresses such as heat shock trigger the formation of protein aggregates and the induction of
a disaggregation system composed of molecular chaperones. Recent work reveals that …
a disaggregation system composed of molecular chaperones. Recent work reveals that …
J-domain protein chaperone circuits in proteostasis and disease
The J-domain proteins (JDP) form the largest protein family among cellular chaperones. In
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …