chaperonine-containing T-complex location

Known as: chaperonin-containing T-complex location, CCT particle, TriC 
A multisubunit ring-shaped complex that mediates protein folding in the cytosol without a cofactor. [GOC:sgd_curators, PMID:11580267]
National Institutes of Health

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Highly Cited
2012
Highly Cited
2012
The TRiC/CCT chaperonin is a 1-MDa hetero-oligomer of 16 subunits that assists the folding of proteins in eukaryotes. Low… (More)
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Highly Cited
2009
Highly Cited
2009
Aggregation of proteins containing polyglutamine (polyQ) expansions characterizes many neurodegenerative disorders, including… (More)
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Highly Cited
2009
Highly Cited
2009
Tricellulin is a tight junction protein localized in tricellular tight junctions (tTJs), the meeting points of three cells, but… (More)
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Highly Cited
2008
Highly Cited
2008
Folding within the crowded cellular milieu often requires assistance from molecular chaperones that prevent inappropriate… (More)
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Highly Cited
2006
Highly Cited
2006
Aberrant folding and fibrillar aggregation by polyglutamine (polyQ) expansion proteins are associated with cytotoxicity in… (More)
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Highly Cited
2006
Highly Cited
2006
Misfolding and aggregation of proteins containing expanded polyglutamine repeats underlie Huntington's disease and other… (More)
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Highly Cited
2003
Highly Cited
2003
The application of multiple en dm eiub er spec tral mixture ana lysis (MJ::SA1A) to map the ph ysical com pos ition of urban… (More)
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Highly Cited
2003
Highly Cited
2003
Chaperonins use ATPase cycling to promote conformational changes leading to protein folding. The prokaryotic chaperonin GroEL… (More)
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Highly Cited
1999
Highly Cited
1999
Molecular chaperones play a fundamental role in cellular protein folding. Using intact mammalian cells we examined the… (More)
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