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chaperone activity
OBSOLETE. Assists in the correct non-covalent assembly of polypeptide-containing structures in vivo, but is not a component of these assembled…
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National Institutes of Health
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Related topics
Related topics
3 relations
protein complex location assembly
protein folding
unfolded protein binding
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2008
Highly Cited
2008
The effect of small molecules in modulating the chaperone activity of αB‐crystallin against ordered and disordered protein aggregation
H. Ecroyd
,
J. Carver
The FEBS Journal
2008
Corpus ID: 12263485
Protein aggregation can proceed via disordered or ordered mechanisms, with the latter being associated with amyloid fibril…
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2006
2006
Pharmacological Chaperone Activity of SR49059 to Functionally Recover Misfolded Mutations of the Vasopressin V1a Receptor*
S. Hawtin
Journal of Biological Chemistry
2006
Corpus ID: 24426722
Pharmacological chaperones represent a new class of ligand with the potential to facilitate the delivery of misfolded, but still…
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2006
2006
Single DNA molecule stretching measures the activity of chemicals that target the HIV-1 nucleocapsid protein.
M. Cruceanu
,
A. Stephen
,
P. Beuning
,
R. Gorelick
,
R. Fisher
,
Mark C. Williams
Analytical Biochemistry
2006
Corpus ID: 46665772
2006
2006
Carnosine inhibits modifications and decreased molecular chaperone activity of lens alpha-crystallin induced by ribose and fructose 6-phosphate.
Hong Yan
,
J. Harding
Molecular Vision
2006
Corpus ID: 7103962
PURPOSE Alpha-crystallin, a major structural protein in the lens, prevents heat- and oxidative stress-induced aggregation of…
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2005
2005
Human Fas-associated Factor 1 Interacts with Heat Shock Protein 70 and Negatively Regulates Chaperone Activity*
Hee‐Jung Kim
,
E. J. Song
,
Yun S. Lee
,
Eunhee Kim
,
Kong-Joo Lee
Journal of Biological Chemistry
2005
Corpus ID: 22586370
We examined the cell death-inducing property of human Fas-associated factor 1 (hFAF1) in the heat shock signaling pathway. By…
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2003
2003
Disulfide bonds convert small heat shock protein Hsp16.3 from a chaperone to a non-chaperone: implications for the evolution of cysteine in molecular chaperones.
Xinmiao Fu
,
Wen Li
,
Q. Mao
,
Z. Chang
Biochemical and Biophysical Research…
2003
Corpus ID: 46531293
Highly Cited
2000
Highly Cited
2000
Functional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activity
P. Fernando
,
J. Heikkila
Cell stress & chaperones (Print)
2000
Corpus ID: 24541202
Abstract Small heat shock proteins protect cells from stress presumably by acting as molecular chaperones. Here we report on the…
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Highly Cited
2000
Highly Cited
2000
Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins.
G. B. Reddy
,
K. Das
,
J. Petrash
,
W. Surewicz
Journal of Biological Chemistry
2000
Corpus ID: 37699301
The chaperone activity and biophysical properties of recombinant human alphaA- and alphaB-crystallins were studied by light…
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2000
2000
High-molecular-mass complexes formed in vivo contain smHSPs and HSP70 and display chaperone-like activity.
P. Smýkal
,
I. Hrdý
,
P. Pechan
European Journal of Biochemistry
2000
Corpus ID: 23594906
Stress can have profound effects on the cell. The elicitation of the stress response in the cell is often accompanied by the…
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1996
1996
Induction of glucose-regulated protein (glucose-regulated protein 78/B:P and glucose-regulated protein 94) and heat shock protein 70 transcripts in the immature rat brain following status epilepticus
E. Little
,
G. Tocco
,
M. Baudry
,
A. Lee
,
S. Schreiber
Neuroscience
1996
Corpus ID: 23559973
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