Other names published for KAR2: GRP78, BIP, Hsp70 family ATPase KAR2, YJL034W
KAR2 LITERATURE TOPICS
- Curated Literature
- Additional Literature
- All Curated References
- Primary Literature
- Reviews
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
KAR2 - Primary Literature (80)
| Reference | Other Genes Addressed |
|---|---|
| Brownridge P, et al. (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91 | |
| Ishiwata-Kimata Y, et al. (2013) BiP-bound and nonclustered mode of Ire1 evokes a weak but sustained unfolded protein response. Genes Cells 18(4):288-301 | |
| Sukhai MA, et al. (2013) Lysosomal disruption preferentially targets acute myeloid leukemia cells and progenitors. J Clin Invest 123(1):315-28 | |
| 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 | |
| Lajoie P, et al. (2012) Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells. Mol Biol Cell 23(5):955-64 | |
| 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 | |
| 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 | |
| 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 | |
| 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 | |
| Aguilera-Romero A, et al. (2008) The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus. J Cell Biol 180(4):713-20 | |
| Liu Y and Chang A (2008) Heat shock response relieves ER stress. EMBO J 27(7):1049-59 | |
| Parikh BA, et al. (2008) Ricin Inhibits Activation of the Unfolded Protein Response by Preventing Splicing of the HAC1 mRNA. J Biol Chem 283(10):6145-53 | |
| Schuldiner M, et al. (2008) The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell 134(4):634-45 | |
| Takeuchi M, et al. (2008) Saccharomyces cerevisiae Rot1 Is an Essential Molecular Chaperone in the Endoplasmic Reticulum. Mol Biol Cell 19(8):3514-25 | |
| Zhang H, et al. (2008) The effect of calnexin deletion on the expression level of binding protein (BiP) under heat stress conditions in Saccharomyces cerevisiae. Cell Mol Biol Lett 13(4):621-31 | |
| 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 | |
| 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 | |
| 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 | |
| Seppa L and Makarow M (2005) Regulation and recovery of functions of Saccharomyces cerevisiae chaperone BiP/Kar2p after thermal insult. Eukaryot Cell 4(12):2008-16 | |
| 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 | |
| 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 | |
| Kimata Y, et al. (2003) Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol Biol Cell 14(6):2559-69 | |
| Norgaard P, et al. (2003) Gene regulation in response to protein disulphide isomerase deficiency. Yeast 20(7):645-52 | |
| 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 |




