CCT3/YJL014W Literature Guide Help

Other names published for CCT3: BIN2, TCP3, YJL014W

CCT3 - Additional Literature (20)

ReferenceOther Genes Addressed
Knee KM, et al.  (2013) Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro. Cell Stress Chaperones 18(2):137-44
Bogumil D, et al.  (2012) Chaperones divide yeast proteins into classes of expression level and evolutionary rate. Genome Biol Evol 4(5):618-25
Hodgins-Davis A, et al.  (2012) Abundant gene-by-environment interactions in gene expression reaction norms to copper within Saccharomyces cerevisiae. Genome Biol Evol 4(11):1061-79
Jacobson T, et al.  (2012) Arsenite interferes with protein folding and triggers formation of protein aggregates in yeast. J Cell Sci 125(Pt 21):5073-83
Gong Y, et al.  (2011) Bioinformatic approach to identify chaperone pathway relationship from large-scale interaction networks. Methods Mol Biol 787():189-203
Helbig AO, et al.  (2011) The diversity of protein turnover and abundance under nitrogen-limited steady-state conditions in Saccharomyces cerevisiae. Mol Biosyst 7(12):3316-26
Stuart SF, et al.  (2011) A Two-step Mechanism for the Folding of Actin by the Yeast Cytosolic Chaperonin. J Biol Chem 286(1):178-84
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
McCormack EA, et al.  (2009) Yeast phosducin-like protein 2 acts as a stimulatory co-factor for the folding of actin by the chaperonin CCT via a ternary complex. J Mol Biol 391(1):192-206
Metzger MB and Michaelis S  (2009) Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins. Mol Biol Cell 20(3):1006-19
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8
Kabir MA and Sherman F  (2008) Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae. FEMS Yeast Res 8(8):1236-44
Mirzaei H and Regnier F  (2006) Enrichment of carbonylated peptides using Girard P reagent and strong cation exchange chromatography. Anal Chem 78(3):770-8
Tam S, et al.  (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-62
Aloy P, et al.  (2004) Structure-based assembly of protein complexes in yeast. Science 303(5666):2026-9
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
Zhang W, et al.  (2003) Microarray analyses of the metabolic responses of Saccharomyces cerevisiae to organic solvent dimethyl sulfoxide. J Ind Microbiol Biotechnol 30(1):57-69
Shevchenko A, et al.  (2002) Deciphering protein complexes and protein interaction networks by tandem affinity purification and mass spectrometry: analytical perspective. Mol Cell Proteomics 1(3):204-12
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
Walkley NA, et al.  (1996) Cloning, structure and mRNA expression of human Cctg, which encodes the chaperonin subunit CCT gamma. Biochem J 313 ( Pt 2)():381-9