TCP1/YDR212W Literature Guide Help

Other names published for TCP1: CCT1, YDR212W

TCP1 - Function/Process (17)

ReferenceOther Genes Addressed
Pan X, et al.  (2010) Trivalent arsenic inhibits the functions of chaperonin complex. Genetics 186(2):725-34
Stirling PC, et al.  (2007) Functional interaction between phosducin-like protein 2 and cytosolic chaperonin is essential for cytoskeletal protein function and cell cycle progression. Mol Biol Cell 18(6):2336-45
Pappenberger G, et al.  (2006) Quantitative actin folding reactions using yeast CCT purified via an internal tag in the CCT3/gamma subunit. J Mol Biol 360(2):484-96
Tam S, et al.  (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62
Kabir MA, et al.  (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39
Camasses A, et al.  (2003) The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20. Mol Cell 12(1):87-100
Siegers K, et al.  (2003) TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J 22(19):5230-40
Somer L, et al.  (2002) The eukaryote chaperonin CCT is a cold shock protein in Saccharomyces cerevisiae. Cell Stress Chaperones 7(1):47-54
Plath K and Rapoport TA  (2000) Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum. J Cell Biol 151(1):167-78
Siegers K, et al.  (1999) Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system. EMBO J 18(1):75-84
Lin P and Sherman F  (1997) The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex. Proc Natl Acad Sci U S A 94(20):10780-5
Burns RG  (1995) Identification of two new members of the tubulin family. Cell Motil Cytoskeleton 31(4):255-8
Kim S, et al.  (1994) Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends Biochem Sci 19(12):543-8
Miklos D, et al.  (1994) Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta. Proc Natl Acad Sci U S A 91(7):2743-7
Ursic D, et al.  (1994) The essential yeast Tcp1 protein affects actin and microtubules. Mol Biol Cell 5(10):1065-80
Ursic D and Culbertson MR  (1992) Is yeast TCP1 a chaperonin? Nature 356(6368):392
Ursic D and Culbertson MR  (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40