Chaperonin CCT, alpha Subunit

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

Topic mentions per year

Topic mentions per year

1989-2016
0119892016

Papers overview

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2016
2016
Cytoplasmic dynein is a macromolecular motor complex with diverse functions in eukaryotic cells. Dynein plays essential roles in… (More)
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2009
2009
Two heptamer rings of chaperonin GroEL undergo opening-closing conformational transition in the reaction cycle with the aid of… (More)
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2008
2008
Saccharomyces cerevisiae yeast cells containing the chaperonin CCT (chaperonin-containing t-complex polypeptide 1 (TCP-1)) with… (More)
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1994
1994
beta-Tubulin synthesized in vitro in rabbit reticulocyte lysate is found associated with 900 kDa complexes (C900) containing T… (More)
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1994
1994
Chaperonins GroEL and GroES form two types of hetero-oligomers in vitro that can mediate the folding of proteins. Chemical cross… (More)
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1993
1993
The translation of a heat shock protein (HSP), TGroEL, of thermophilic bacterium PS3 increased within 10 minutes when the culture… (More)
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1992
1992
We have isolated clones of a processed pseudogene of mouse t complex polypeptide 1 (Tcp-1) and determined the nucleotide sequence… (More)
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1989
1989
The t complex polypeptide 1 (TCP-1) is a protein of unknown function expressed in large amounts during spermatogenesis. Rat… (More)
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