CCT2/YIL142W Literature Guide Help

Other names published for CCT2: BIN3, TCP2, YIL142W

CCT2 - Additional Literature (23)

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
Dengjel J, et al.  (2012) Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol Cell Proteomics 11(3):M111.014035
Massoni A, et al.  (2012) Proteome analysis of a CTR9 deficient yeast strain suggests that Ctr9 has function(s) independent of the Paf1 complex. Biochim Biophys Acta 1824(5):759-68
Westman JO, et al.  (2012) Proteomic Analysis of the Increased Stress Tolerance of Saccharomyces cerevisiae Encapsulated in Liquid Core Alginate-Chitosan Capsules. PLoS One 7(11):e49335
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
He X, et al.  (2010) Prevalent positive epistasis in Escherichia coli and Saccharomyces cerevisiae metabolic networks. Nat Genet 42(3):272-6
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Gordon JL, et al.  (2009) Additions, losses, and rearrangements on the evolutionary route from a reconstructed ancestor to the modern Saccharomyces cerevisiae genome. PLoS Genet 5(5):e1000485
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
Kabir MA and Sherman F  (2008) Overexpressed ribosomal proteins suppress defective chaperonins in Saccharomyces cerevisiae. FEMS Yeast Res 8(8):1236-44
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
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
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