KAR2/YJL034W Literature Guide Help

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

KAR2 - Mutants/Phenotypes (60)

Results: 1 - 30 of 60 records
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ReferenceOther Genes Addressed
Hsu CL, et al.  (2012) Endoplasmic reticulum stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways. Mol Biol Cell 23(4):630-41
Morrow MW, et al.  (2011) The Candida albicans Kar2 protein is essential and functions during the translocation of proteins into the endoplasmic reticulum. Curr Genet 57(1):25-37
Stuchell-Brereton MD, et al.  (2011) Functional interaction between dynein light chain and intermediate chain is required for mitotic spindle positioning. Mol Biol Cell 22(15):2690-701
Buck TM, et al.  (2010) The Endoplasmic Reticulum-associated Degradation of the Epithelial Sodium Channel Requires a Unique Complement of Molecular Chaperones. Mol Biol Cell 21(6):1047-58
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
Kanehara K, et al.  (2010) Modularity of the Hrd1 ERAD complex underlies its diverse client range. J Cell Biol 188(5):707-16
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
Melloy P, et al.  (2009) Distinct roles for key karyogamy proteins during yeast nuclear fusion. Mol Biol Cell 20(17):3773-82
Pineau L, et al.  (2009) Lipid-induced ER stress: synergistic effects of sterols and saturated fatty acids. Traffic 10(6):673-90
Tartakoff AM and Jaiswal P  (2009) Nuclear fusion and genome encounter during yeast zygote formation. Mol Biol Cell 20(12):2932-42
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
Breslow DK, et al.  (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8
Liu Y and Chang A  (2008) Heat shock response relieves ER stress. EMBO J 27(7):1049-59
Carla Fama M, et al.  (2007) The Saccharomyces cerevisiae YFR041C/ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum. Biochim Biophys Acta 1773(2):232-42
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
Apodaca J, et al.  (2006) Cellular tolerance of prion protein PrP in yeast involves proteolysis and the unfolded protein response. Biochem Biophys Res Commun 347(1):319-26
Heiligenstein S, et al.  (2006) Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD. EMBO J 25(20):4717-27
Takeuchi M, et al.  (2006) Causal links between protein folding in the ER and events along the secretory pathway. Autophagy 2(4):323-4
Raden D, et al.  (2005) Analysis of cellular response to protein overexpression. Syst Biol (Stevenage) 152(4):285-9
Uchimura S, et al.  (2005) Effects of N-glycosylation and inositol on the ER stress response in yeast Saccharomyces cerevisiae. Biosci Biotechnol Biochem 69(7):1274-80
Xu P, et al.  (2005) Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding. Metab Eng 7(4):269-79
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
Nakatsukasa K, et al.  (2004) Roles of O-mannosylation of aberrant proteins in reduction of the load for endoplasmic reticulum chaperones in yeast. J Biol Chem 279(48):49762-72
Smith JD, et al.  (2004) Protein disulfide isomerase, but not binding protein, overexpression enhances secretion of a non-disulfide-bonded protein in yeast. Biotechnol Bioeng 85(3):340-50
Kabani M, et al.  (2003) Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Mol Biol Cell 14(8):3437-48
Lee K, et al.  (2003) The unfolded protein response is required for haploid tolerance in yeast. J Biol Chem 278(14):11818-27
Palmer EA, et al.  (2003) Differential requirements of novel A1PiZ degradation deficient (ADD) genes in ER-associated protein degradation. J Cell Sci 116(Pt 11):2361-73
Taxis C, et al.  (2003) Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 278(38):35903-13
Yabal M, et al.  (2003) Translocation of the C terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocation. J Biol Chem 278(5):3489-96
Nishikawa SI, et al.  (2001) Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 153(5):1061-70
Results: 1 - 30 of 60 records
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