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chaperonin
Known as:
Chaperonin Family
, Chaperonins
, Chaperonins [Chemical/Ingredient]
Â
A family of multisubunit protein complexes that form into large cylindrical structures which bind to and encapsulate non-native proteins. Chaperonins…Â
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National Institutes of Health
Topic mentions per year
Topic mentions per year
1988-2018
0
20
40
60
1988
2018
Related topics
Related topics
13 relations
In Blood
Molecular Chaperones
Process of secretion
administration & dosage
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Related mentions per year
Related mentions per year
1936-2018
1940
1960
1980
2000
2020
chaperonin
physiological aspects
agonists
chemical synthesis
Molecular Chaperones
standards characteristics
Papers overview
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Highly Cited
2005
Highly Cited
2005
Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli
Michael Kerner
,
Dean J. Naylor
,
+8 authors
F. Ulrich Hartl
Cell
2005
The E. coli chaperonin GroEL and its cofactor GroES promote protein folding by sequestering nonnative polypeptides in a cage-like…Â
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Highly Cited
2004
Highly Cited
2004
cpnDB: a chaperonin sequence database.
Janet E Hill
,
Susanne L. Penny
,
Kenneth G Crowell
,
Swee Han Goh
,
Sean M. Hemmingsen
Genome research
2004
Type I chaperonins are molecular chaperones present in virtually all bacteria, some archaea and the plastids and mitochondria of…Â
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Highly Cited
2002
Highly Cited
2002
A mitochondrial specific stress response in mammalian cells.
Quanming Zhao
,
Jianghui Wang
,
Ilya V Levichkin
,
Stan J. Stasinopoulos
,
Michael T. Ryan
,
Nicholas J. Hoogenraad
The EMBO journal
2002
Cells respond to a wide variety of stresses through the transcriptional activation of genes that harbour stress elements within…Â
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Highly Cited
2001
Highly Cited
2001
Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding
Achim Brinker
,
Günther W. Pfeifer
,
Michael Kerner
,
Dean J. Naylor
,
F. Ulrich Hartl
,
M Hayer-Hartl
Cell
2001
The GroEL/GroES chaperonin system mediates the folding of a range of newly synthesized polypeptides in the bacterial cytosol…Â
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Highly Cited
1999
Highly Cited
1999
Identification of in vivo substrates of the chaperonin GroEL.
Walid A. Houry
,
Dimitrij Frishman
,
Christoph Eckerskorn
,
Fritz Lottspeich
,
F Ulrich Hartl
Nature
1999
The chaperonin GroEL has an essential role in mediating protein folding in the cytosol of Escherichia coli. Here we show that…Â
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Highly Cited
1998
Highly Cited
1998
Prefoldin, a Chaperone that Delivers Unfolded Proteins to Cytosolic Chaperonin
Irina E Vainberg
,
Sally A. Lewis
,
+4 authors
Nicholas J. Cowan
Cell
1998
We describe the discovery of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded actin…Â
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Highly Cited
1997
Highly Cited
1997
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Z. Xu
,
Arthur L Horwich
,
Paul B. Sigler
Nature
1997
Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings…Â
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Highly Cited
1994
Highly Cited
1994
Residues in chaperonin GroEL required for polypeptide binding and release.
Wendy Fenton
,
Yafit Kashi
,
Krystyna J. Furtak
,
Arthur L Horwich
Nature
1994
Chaperonins are ring-shaped protein complexes that are essential in the cell, mediating ATP-dependent polypeptide folding in a…Â
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Highly Cited
1994
Highly Cited
1994
The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
Kerstin Braig
,
Zbyszek Otwinowski
,
+4 authors
Paul B. Sigler
Nature
1994
The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally…Â
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Highly Cited
1989
Highly Cited
1989
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP.
Pierre Goloubinoff
,
John T. Christeller
,
Anthony A. Gatenby
,
George H. Lorimer
Nature
1989
In vitro reconstitution of active ribulose bisphosphate carboxylase (Rubisco) from unfolded polypeptides is facilitated by the…Â
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