KAR2/YJL034W Literature Guide Help

Other names published for KAR2: GRP78, BIP, Hsp70 family ATPase KAR2, YJL034W

KAR2 - Protein-protein Interactions (58)

Results: 1 - 30 of 58 records
   1  2 
ReferenceOther Genes Addressed
Izawa T, et al.  (2012) Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation. Mol Biol Cell 23(7):1283-93
Jin F, et al.  (2012) Loss of function of the cik1/kar3 motor complex results in chromosomes with syntelic attachment that are sensed by the tension checkpoint. PLoS Genet 8(2):e1002492
Ishiwata-Kimata Y, et al.  (2011) Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways. Mol Biol Cell 22(18):3520-32
Oikawa D and Kimata Y  (2011) Experimental Approaches for Elucidation of Stress-Sensing Mechanisms of the IRE1 Family Proteins. Methods Enzymol 490():195-216
Yan M, et al.  (2011) Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor. Biochem J 438(3):447-55
Andreasson C, et al.  (2010) The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. J Biol Chem 285(16):12445-53
Hale SJ, et al.  (2010) Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct. J Biol Chem 285(28):21600-6
Pincus D, et al.  (2010) BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response. PLoS Biol 8(7):e1000415
Puts CF, et al.  (2010) A P(4)-ATPase Protein Interaction Network Reveals a Link between Aminophospholipid Transport and Phosphoinositide Metabolism. J Proteome Res 9(2):833-42
Vembar SS, et al.  (2010) J domain co-chaperone specificity defines the role of BiP during protein translocation. J Biol Chem 285(29):22484-94
Wang S and Ng DT  (2010) Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality control. Mol Biol Cell 21(7):1153-65
Gong Y, et al.  (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5:275
Markov DA, et al.  (2009) Identification of proteins associated with the yeast mitochondrial RNA polymerase by tandem affinity purification. Yeast 26(8):423-40
de Keyzer J, et al.  (2009) Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo. J Biol Chem 284(46):31564-71
Goder V, et al.  (2008) The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48p. FEBS Lett 582(11):1575-80
Makio T, et al.  (2008) Identification and characterization of a Jem1p ortholog of Candida albicans: dissection of Jem1p functions in karyogamy and protein quality control in Saccharomyces cerevisiae. Genes Cells 13(10):1015-26
Takeuchi M, et al.  (2008) Saccharomyces cerevisiae Rot1 Is an Essential Molecular Chaperone in the Endoplasmic Reticulum. Mol Biol Cell 19(8):3514-25
Kimata Y, et al.  (2007) Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J Cell Biol 179(1):75-86
Ng W, et al.  (2007) Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J Cell Sci 120(Pt 4):682-91
Oikawa D, et al.  (2007) Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1. J Cell Sci 120(Pt 9):1681-8
Todd-Corlett A, et al.  (2007) Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein response in Saccharomyces cerevisiae. J Mol Biol 367(3):770-87
Denic V, et al.  (2006) A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126(2):349-59
Fujita M, et al.  (2006) Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins. Mol Biol Cell 17(2):834-50
Tagwerker C, et al.  (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol Cell Proteomics 5(4):737-48
Takeuchi M, et al.  (2006) Causal links between protein folding in the ER and events along the secretory pathway. Autophagy 2(4):323-4
Takeuchi M, et al.  (2006) Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding. J Biochem 139(3):597-605
Xia Y, et al.  (2006) Integrated prediction of the helical membrane protein interactome in yeast. J Mol Biol 357(1):339-49
Kimura T, et al.  (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41
Kimata Y, et al.  (2004) A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J Cell Biol 167(3):445-56
Steel GJ, et al.  (2004) Coordinated activation of Hsp70 chaperones. Science 303(5654):98-101
Results: 1 - 30 of 58 records
   1  2