CCT8/YJL008C Literature Guide Help

Other names published for CCT8: YJL008C

CCT8 - 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
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
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
Picotti P, et al.  (2009) Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 138(4):795-806
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
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
Peng J, et al.  (2003) A proteomics approach to understanding protein ubiquitination. Nat Biotechnol 21(8):921-6
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
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
Escobar-Henriques M, et al.  (2001) Proteome analysis and morphological studies reveal multiple effects of the immunosuppressive drug mycophenolic acid specifically resulting from guanylic nucleotide depletion. J Biol Chem 276(49):46237-42
Jelinsky SA and Samson LD  (1999) Global response of Saccharomyces cerevisiae to an alkylating agent. Proc Natl Acad Sci U S A 96(4):1486-91
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