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chaperonin activity
Known as:
chaperonin
National Institutes of Health
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chaperonin
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Highly Cited
2005
Highly Cited
2005
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
R. Horst
,
E. Bertelsen
,
Jocelyne Fiaux
,
G. Wider
,
A. Horwich
,
K. Wüthrich
Proceedings of the National Academy of Sciences…
2005
Corpus ID: 8456569
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well…
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Highly Cited
2005
Highly Cited
2005
Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
D. Rivenzon-Segal
,
S. Wolf
,
Liat Shimon
,
K. Willison
,
A. Horovitz
Nature Structural &Molecular Biology
2005
Corpus ID: 23019459
The eukaryotic cytoplasmic chaperonin containing TCP-1 (CCT) is a hetero-oligomeric complex that assists the folding of actins…
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Highly Cited
1997
Highly Cited
1997
Cytoplasmic chaperonin containing TCP-1: structural and functional characterization.
R. Melki
,
G. Batelier
,
S. Soulié
,
R. Williams
Biochemistry
1997
Corpus ID: 12667474
Actin and tubulin polypeptide chains acquire their native conformation in the presence of the cytoplasmic chaperonin containing…
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Review
1996
Review
1996
Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates
Jonathan King
,
C. Haase‐Pettingell
,
A. Robinson
,
M. Speed
,
A. Mitraki
The FASEB Journal
1996
Corpus ID: 10666197
An unexpected aspect of the expression of cloned genes is the frequent failure of newly synthesized polypeptide chains to reach…
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Highly Cited
1994
Highly Cited
1994
The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state
A. Okazaki
,
T. Ikura
,
K. Nikaido
,
K. Kuwajima
Nature Structural Biology
1994
Corpus ID: 30932656
We investigate here the interaction between GroEL and two kinds of non-native α-lactalbumin. α-Lactalbumin is a Ca2+-binding…
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Highly Cited
1993
Highly Cited
1993
ATP induces large quaternary rearrangements in a cage-like chaperonin structure
H. Saibil
,
D. Zheng
,
+9 authors
R. Ellis
Current Biology
1993
Corpus ID: 24443463
Highly Cited
1993
Highly Cited
1993
A polypeptide bound by the chaperonin groEL is localized within a central cavity.
K. Braig
,
M. Simon
,
Fred Furuya
,
J. F. Hainfeld
,
A. Horwich
Proceedings of the National Academy of Sciences…
1993
Corpus ID: 43864131
Chaperonins are oligomeric protein complexes that play an essential role in the cell, mediating ATP-dependent polypeptide chain…
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Highly Cited
1992
Highly Cited
1992
Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation
M. Sherman
,
A. Goldberg
Nature
1992
Corpus ID: 4339010
WHEN bacterial or enkaryotic cells are exposed to high temperatures or other harsh conditions, they respond by synthesis of a…
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Highly Cited
1992
Highly Cited
1992
DnaK-Mediated Alterations in Human Growth Hormone Protein Inclusion Bodies
P. Blum
,
M. Velligan
,
N. Lin
,
A. Matin
Bio/Technology
1992
Corpus ID: 2467334
Protein overproduction in microbes frequently results in protein misfolding and aggregation though the molecular basis for this…
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Highly Cited
1989
Highly Cited
1989
Molecular cloning of a Chinese hamster mitochondrial protein related to the "chaperonin" family of bacterial and plant proteins.
D. Picketts
,
C. Mayanil
,
R. Gupta
Journal of Biological Chemistry
1989
Corpus ID: 19561577
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