HLJ1/YMR161W Literature Guide Help

Other names published for HLJ1: YMR161W

HLJ1 Literature Curation Summary

Curated References for HLJ1: 28

Date of last curation: 2013-03-11

ReferenceOther Genes Addressed
Brownridge P, et al.  (2013) Quantitative analysis of chaperone network throughput in budding yeast. Proteomics 13(8):1276-91
Kakoi S, et al.  (2013) COPII machinery cooperates with ER-localized Hsp40 to sequester misfolded membrane proteins into ER-associated compartments. Mol Biol Cell 24(5):633-42
Alex D, et al.  (2012) Amino acid-derived 1,2-benzisothiazolinone derivatives as novel small-molecule antifungal inhibitors: identification of potential genetic targets. Antimicrob Agents Chemother 56(9):4630-9
Bogumil D, et al.  (2012) Chaperones divide yeast proteins into classes of expression level and evolutionary rate. Genome Biol Evol 4(5):618-25
Gillies AT, et al.  (2012) Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones. Mol Biosyst 8(11):2901-8
Thibault G and Ng DT  (2012) The endoplasmic reticulum-associated degradation pathways of budding yeast. Cold Spring Harb Perspect Biol 4(12)
Verghese J, et al.  (2012) Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System. Microbiol Mol Biol Rev 76(2):115-58
Furth N, et al.  (2011) Exposure of bipartite hydrophobic signal triggers nuclear quality control of Ndc10 at the endoplasmic reticulum/nuclear envelope. Mol Biol Cell 22(24):4726-39
Jung PP, et al.  (2011) Ploidy influences cellular responses to gross chromosomal rearrangements in Saccharomyces cerevisiae. BMC Genomics 12(1):331
Kolb AR, et al.  (2011) Saccharomyces cerivisiae as a model system for kidney disease: what can yeast tell us about renal function? Am J Physiol Renal Physiol 301(1):F1-11
Ushioda R and Nagata K  (2011) The Endoplasmic Reticulum-Associated Degradation and Disulfide Reductase ERdj5. Methods Enzymol 490():235-58
Goeckeler JL and Brodsky JL  (2010) Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation. Diabetes Obes Metab 12 Suppl 2():32-8
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
Vembar SS, et al.  (2009) The Mammalian Hsp40 ERdj3 Requires Its Hsp70 Interaction and Substrate-binding Properties to Complement Various Yeast Hsp40-dependent Functions. J Biol Chem 284(47):32462-71
Goeckeler JL, et al.  (2008) The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding. FEBS Lett 582(16):2393-6
Metzger MB, et al.  (2008) Degradation of a Cytosolic Protein Requires Endoplasmic Reticulum-associated Degradation Machinery. J Biol Chem 283(47):32302-16
Nakatsukasa K, et al.  (2008) Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 132(1):101-12
Han S, et al.  (2007) Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1. J Biol Chem 282(36):26140-9
Pagant S, et al.  (2007) Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Mol Biol Cell 18(9):3398-413
Qiu XB, et al.  (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63(22):2560-2570
Ahner A and Brodsky JL  (2004) Checkpoints in ER-associated degradation: excuse me, which way to the proteasome? Trends Cell Biol 14(9):474-8
Huyer G, et al.  (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 279(37):38369-78
Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71
Youker RT, et al.  (2004) Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol Biol Cell 15(11):4787-97
Beilharz T, et al.  (2003) Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J Biol Chem 278(10):8219-23
Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
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
Willingham S, et al.  (2003) Yeast genes that enhance the toxicity of a mutant huntingtin fragment or alpha-synuclein. Science 302(5651):1769-72