CCT4/YDL143W Literature Guide Help

Other names published for CCT4: TCP4, ANC2, YDL143W

CCT4 - Additional Literature (21)

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
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
Haarer B, et al.  (2011) Novel Interactions between Actin and the Proteasome Revealed by Complex Haploinsufficiency. PLoS Genet 7(9):e1002288
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
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8
Guerrero C, et al.  (2008) Characterization of the proteasome interaction network using a QTAX-based tag-team strategy and protein interaction network analysis. Proc Natl Acad Sci U S A 105(36):13333-8
Kabir MA and Sherman F  (2008) Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae. FEMS Yeast Res 8(8):1236-44
Altmann K and Westermann B  (2005) Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol Biol Cell 16(11):5410-7
Millson SH, et al.  (2005) A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p). Eukaryot Cell 4(5):849-60
Aloy P, et al.  (2004) Structure-based assembly of protein complexes in yeast. Science 303(5666):2026-9
Zhang Z and Kishino H  (2004) Genomic background predicts the fate of duplicated genes: evidence from the yeast genome. Genetics 166(4):1995-9
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
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