The SSB1 heat shock cognate gene of the yeast Saccharomyces cerevisiae.Slater M.R., Craig E.A.Cited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]StrainATCC 204508 / S288cCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNucleic Acids Res. 17:4891-4891 (1989)Cited in1
S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP.Normington K., Kohno K., Kozutsumi Y., Gething M.J., Sambrook J.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 57:1223-1236 (1989)Cited in2
The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A.[...], Zaccaria P.View abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]StrainATCC 204508 / S288cCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 387:75-78 (1997)Cited in99+
The reference genome sequence of Saccharomyces cerevisiae: Then and now.Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K.[...], Cherry J.M.View abstractCited forGENOME REANNOTATIONStrainATCC 204508 / S288cCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCG3 (Bethesda) 4:389-398 (2014)Cited in99+
Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila.Ingolia T.D., Slater M.R., Craig E.A.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78 AND 180-403, INDUCTIONStrainATCC 204508 / S288cCategoriesSequences, ExpressionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Biol. 2:1388-1398 (1982)Cited in22Mapped to1
Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides.Norbeck J., Blomberg A.View abstractCited forPROTEIN SEQUENCE OF 39-49 AND 431-439StrainATCC 38531 / Y41CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCElectrophoresis 16:149-156 (1995)Cited in9
Protein identifications for a Saccharomyces cerevisiae protein database.Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.View abstractCited forPROTEIN SEQUENCE OF 145-159StrainATCC 204508 / S288cCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCElectrophoresis 15:1466-1486 (1994)Cited in27
Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae.Werner-Washburne M., Stone D.E., Craig E.A.View abstractCited forGENE FAMILYCategoriesNamesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Biol. 7:2568-2577 (1987)Cited in2Mapped to4
Yeast Hsp70 RNA levels vary in response to the physiological status of the cell.Werner-Washburne M., Becker J., Kosic-Smithers J., Craig E.A.View abstractCited forINDUCTIONCategoriesExpressionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 171:2680-2688 (1989)Cited in2
The translation machinery and 70 kd heat shock protein cooperate in protein synthesis.Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A.View abstractCited forFUNCTION, SUBCELLULAR LOCATIONCategoriesFunction, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 71:97-105 (1992)Cited in3
Detection and expression of the 70 kDa heat shock protein SSB1P at different temperatures in Saccharomyces cerevisiae.Iwahashi H., Wu Y., Tanguay R.M.View abstractCited forINDUCTIONCategoriesExpressionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. Biophys. Res. Commun. 213:484-489 (1995)Cited in1Mapped to1
Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins.Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S.[...], Payne W.E.View abstractCited forACETYLATION AT ALA-2CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCElectrophoresis 18:1347-1360 (1997)Cited in25
Functional specificity among Hsp70 molecular chaperones.James P., Pfund C., Craig E.A.View abstractCited forFUNCTIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCScience 275:387-389 (1997)Cited in1Mapped to1
The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.Pfund C., Lopez-Hoyo N., Ziegelhoffer T., Schilke B.A., Lopez-Buesa P., Walter W.A., Wiedmann M., Craig E.A.View abstractCited forFUNCTION, SUBUNITCategoriesFunction, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEMBO J. 17:3981-3989 (1998)Cited in2
The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains.Lopez-Buesa P., Pfund C., Craig E.A.View abstractCited forBIOPHYSICOCHEMICAL PROPERTIESCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 95:15253-15258 (1998)Cited in1Mapped to3
SSB, encoding a ribosome-associated chaperone, is coordinately regulated with ribosomal protein genes.Lopez N., Halladay J., Walter W., Craig E.A.View abstractCited forINDUCTIONCategoriesExpressionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Bacteriol. 181:3136-3143 (1999)Cited in2Mapped to6
A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport.Shulga N., James P., Craig E.A., Goldfarb D.S.View abstractCited forSUBCELLULAR LOCATIONCategoriesSubcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 274:16501-16507 (1999)Cited in1Mapped to1
Divergent functional properties of the ribosome-associated molecular chaperone Ssb compared with other Hsp70s.Pfund C., Huang P., Lopez-Hoyo N., Craig E.A.View abstractCited forFUNCTIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Biol. Cell 12:3773-3782 (2001)Cited in2Mapped to1
A functional chaperone triad on the yeast ribosome.Gautschi M., Mun A., Ross S., Rospert S.View abstractCited forFUNCTION, SUBUNITCategoriesFunction, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 99:4209-4214 (2002)Cited in3Mapped to1
Global analysis of protein expression in yeast.Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.View abstractCited forLEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]CategoriesExpressionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNature 425:737-741 (2003)Cited in99+
Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding.Yam A.Y., Albanese V., Lin H.T., Frydman J.View abstractCited forFUNCTION, INTERACTION WITH SSE1CategoriesFunction, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 280:41252-41261 (2005)Cited in2Mapped to3
The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb.Shaner L., Wegele H., Buchner J., Morano K.A.View abstractCited forFUNCTION, INTERACTION WITH SSE1CategoriesFunction, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 280:41262-41269 (2005)Cited in2Mapped to3
Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p.Dragovic Z., Shomura Y., Tzvetkov N., Hartl F.U., Bracher A.View abstractCited forINTERACTION WITH FES1CategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiol. Chem. 387:1593-1600 (2006)Cited in2Mapped to2
Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.View abstractCited forIDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]StrainADR376CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Proteome Res. 6:1190-1197 (2007)Cited in99+
Phosphorylation by casein kinase 2 regulates Nap1 localization and function.Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.View abstractCited forINTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRYCategoriesSequences, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Biol. 28:1313-1325 (2008)Cited in21Mapped to1