TCP1/YDR212W Literature Guide Help

Other names published for TCP1: CCT1, YDR212W

TCP1 - Protein-protein Interactions (13)

ReferenceOther Genes Addressed
Leitner A, et al.  (2012) The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure 20(5):814-25
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 ()
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
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
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
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
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
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
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