TCP1/YDR212W Literature Guide Help

Other names published for TCP1: CCT1, YDR212W

TCP1 - Primary Literature (26)

ReferenceOther Genes Addressed
Brownridge P, et al.  (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91
Chiva R, et al.  (2012) Analysis of low temperature-induced genes (LTIG) in wine yeast during alcoholic fermentation. FEMS Yeast Res 12(7):831-43
Leitner A, et al.  (2012) The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure 20(5):814-25
Reissmann S, et al.  (2012) A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle. Cell Rep 2(4):866-77
Dekker C, et al.  (2011) The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.LID - 10.1038/emboj.2011.208 [doi] EMBO J ()
Amit M, et al.  (2010) Equivalent Mutations in the Eight Subunits of the Chaperonin CCT Produce Dramatically Different Cellular and Gene Expression Phenotypes. J Mol Biol 401(3):532-543
Pan X, et al.  (2010) Trivalent arsenic inhibits the functions of chaperonin complex. Genetics 186(2):725-34
Altschuler GM, et al.  (2009) A single amino acid residue is responsible for species-specific incompatibility between CCT and alpha-actin. FEBS Lett 583(4):782-6
Dekker C, et al.  (2008) The interaction network of the chaperonin CCT. EMBO J 27(13):1827-39
Albanese V, et al.  (2006) Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell 124(1):75-88
Behrends C, et al.  (2006) Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol Cell 23(6):887-97
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
Spiess C, et al.  (2006) Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell 24(1):25-37
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
Fares MA and Wolfe KH  (2003) Positive selection and subfunctionalization of duplicated CCT chaperonin subunits. Mol Biol Evol 20(10):1588-97
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
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  (1991) The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 11(5):2629-40