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Chaperonin CCT, alpha Subunit

Known as: t Complex Polypeptide 1, Chaperonin Containing TCP1, Subunit 1, t-Complex Protein 1 
 
National Institutes of Health

Papers overview

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2010
2010
The RNA polymerase of influenza A virus is a host range determinant and virulence factor. In particular, the PB2 subunit of the… Expand
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Highly Cited
2008
Highly Cited
2008
The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) has an important function in maintaining cellular homoeostasis by… Expand
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Highly Cited
2008
Highly Cited
2008
We have previously reported the association of a mutation (c.292G > A/p.V98I) in the human HSPD1 gene that encodes the… Expand
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Highly Cited
2008
Highly Cited
2008
All chaperonins mediate ATP-dependent polypeptide folding by confining substrates within a central chamber. Intriguingly, the… Expand
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Review
2002
Review
2002
Chaperonins are large oligomers made up of two superimposed rings, each enclosing a cavity used for the folding of other proteins… Expand
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Highly Cited
1998
Highly Cited
1998
Normal mode calculations on individual subunits and a multisubunit construct are used to analyze the structural transitions that… Expand
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1997
1997
Folding of newly synthesized proteins in vivo is believed to be facilitated by the cooperative interaction of a defined group of… Expand
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1997
1997
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in Escherichia coli. Recent studies… Expand
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Highly Cited
1994
Highly Cited
1994
CHAPERONINS are ring-shaped protein complexes that are essential in the cell, mediating ATP-dependent polypeptide folding in a… Expand
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Review
1994
Review
1994
CCT (also called the TCP-1 complex or TriC) is a chaperonin found in the eukaryotic cytosol, and has unique structural and… Expand
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