Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 205,614,741 papers from all fields of science
Search
Sign In
Create Free Account
Molecular Chaperones
Known as:
Chaperone
, Chaperone, Molecular
, Molecular Chaperones [Chemical/Ingredient]
Expand
Cytoplasmic proteins of both prokaryotes and eukaryotes that bind to nascent or unfolded polypeptides and ensure correct folding or transport…
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
50 relations
Narrower (37)
BAG6 protein, Arabidopsis
BAG6 protein, human
CDC37L1 protein, human
CesT protein, E coli
Expand
Broader (1)
Carrier Proteins
HSP40 Heat-Shock Proteins
Heat Shock Protein Beta-8
Heat shock proteins
Heat-Shock Proteins 70
Expand
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Review
2011
Review
2011
Molecular chaperones in protein folding and proteostasis
F. Hartl
,
A. Bracher
,
M. Hayer‐Hartl
Nature
2011
Corpus ID: 4337671
Most proteins must fold into defined three-dimensional structures to gain functional activity. But in the cellular environment…
Expand
Review
2005
Review
2005
Modulation of neurodegeneration by molecular chaperones
P. Muchowski
,
Jennifer L. Wacker
Nature Reviews Neuroscience
2005
Corpus ID: 31103737
Many neurodegenerative disorders are characterized by conformational changes in proteins that result in misfolding, aggregation…
Expand
Review
2005
Review
2005
HSP90 and the chaperoning of cancer
L. Whitesell
,
S. Lindquist
Nature Reviews Cancer
2005
Corpus ID: 22098282
Standing watch over the proteome, molecular chaperones are an ancient and evolutionarily conserved class of proteins that guide…
Expand
Review
2004
Review
2004
Hsp70 chaperones: Cellular functions and molecular mechanism
M. Mayer
,
B. Bukau
Cellular and Molecular Life Sciences
2004
Corpus ID: 17373725
Abstract.Hsp70 proteins are central components of the cellular network of molecular chaperones and folding catalysts. They assist…
Expand
Review
2002
Review
2002
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
F. Hartl
,
M. Hayer‐Hartl
Science
2002
Corpus ID: 15037639
Efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent…
Expand
Review
1999
Review
1999
Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology.
M. Feder
,
G. Hofmann
Annual review of physiology
1999
Corpus ID: 16061054
Molecular chaperones, including the heat-shock proteins (Hsps), are a ubiquitous feature of cells in which these proteins cope…
Expand
Review
1998
Review
1998
Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators.
R. Morimoto
Genes & development
1998
Corpus ID: 1678147
Our cells and tissues are challenged constantly by exposure to extreme conditions that cause acute and chronic stress…
Expand
Review
1996
Review
1996
Molecular chaperones in cellular protein folding
F. Hartl
Nature
1996
Corpus ID: 4347271
The folding of many newly synthesized proteins in the cell depends on a set of conserved proteins known as molecular chaperones…
Expand
Review
1993
Review
1993
Molecular chaperone functions of heat-shock proteins.
J. Hendrick
,
F. Hartl
Annual review of biochemistry
1993
Corpus ID: 6371388
3. HSP70 PROTEINS: CHAPERONES WITH DIVERSE ROLES IN PROTEIN METABOLISM…
Expand
Highly Cited
1992
Highly Cited
1992
Alpha-crystallin can function as a molecular chaperone.
J. Horwitz
Proceedings of the National Academy of Sciences…
1992
Corpus ID: 38227297
The alpha-crystallins (alpha A and alpha B) are major lens structural proteins of the vertebrate eye that are related to the…
Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
,
Terms of Service
, and
Dataset License
ACCEPT & CONTINUE