FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W5959882> ?p ?o ?g. }

• W5959882 endingPage "562" @default.
• W5959882 startingPage "555" @default.
• W5959882 abstract "Research Article1 March 1991free access Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. W. Heinemeyer W. Heinemeyer Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author J. A. Kleinschmidt J. A. Kleinschmidt Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author J. Saidowsky J. Saidowsky Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author C. Escher C. Escher Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author D. H. Wolf D. H. Wolf Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author W. Heinemeyer W. Heinemeyer Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author J. A. Kleinschmidt J. A. Kleinschmidt Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author J. Saidowsky J. Saidowsky Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author C. Escher C. Escher Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author D. H. Wolf D. H. Wolf Institut für Biochemie, Universität Stuttgart, FRG. Search for more papers by this author Author Information W. Heinemeyer1, J. A. Kleinschmidt1, J. Saidowsky1, C. Escher1 and D. H. Wolf1 1Institut für Biochemie, Universität Stuttgart, FRG. The EMBO Journal (1991)10:555-562https://doi.org/10.1002/j.1460-2075.1991.tb07982.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Proteinase yscE is the yeast equivalent of the proteasome, a multicatalytic-multifunctional proteinase found in higher eukaryotic cells. We have isolated three mutants affecting the proteolytic activity of proteinase yscE. The mutants show a specific reduction in the activity of the complex against peptide substrates with hydrophobic amino acids at the cleavage site and define two complementation groups, PRE1 and PRE2. The PRE1 gene was cloned and shown to be essential. The deduced amino acid sequence encoded by the PRE1 gene reveals weak, but significant similarities to proteasome subunits of other organisms. Two-dimensional gel electrophoresis identified the yeast proteasome to be composed of 14 different subunits. Comparison of these 14 subunits with the translation product obtained from PRE1 mRNA synthesized in vitro demonstrated that PRE1 encodes the 22.6 kd subunit (numbered 11) of the yeast proteasome. Diploids homozygous for pre1–1 are defective in sporulation. Strains carrying the pre1–1 mutation show enhanced sensitivity to stresses such as incorporation of the amino acid analogue canavanine into proteins or a combination of poor growth medium and elevated temperature. Under these stress conditions pre1–1 mutant cells exhibit decreased protein degradation and accumulate ubiquitin-protein conjugates. Previous ArticleNext Article Volume 10Issue 31 March 1991In this issue RelatedDetailsLoading ..." @default.
• W5959882 created "2016-06-24" @default.
• W5959882 creator A5015274886 @default.
• W5959882 creator A5030687294 @default.
• W5959882 creator A5041584392 @default.
• W5959882 creator A5058065410 @default.
• W5959882 creator A5084814331 @default.
• W5959882 date "1991-03-01" @default.
• W5959882 modified "2023-10-17" @default.
• W5959882 title "Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival." @default.
• W5959882 cites W1493156205 @default.
• W5959882 cites W1498359524 @default.
• W5959882 cites W1510475344 @default.
• W5959882 cites W1512725344 @default.
• W5959882 cites W1518640128 @default.
• W5959882 cites W1519470329 @default.
• W5959882 cites W1529813906 @default.
• W5959882 cites W1535473877 @default.
• W5959882 cites W1536742797 @default.
• W5959882 cites W1537782690 @default.
• W5959882 cites W1546177497 @default.
• W5959882 cites W1551502631 @default.
• W5959882 cites W1551702901 @default.
• W5959882 cites W1606423922 @default.
• W5959882 cites W1838616807 @default.
• W5959882 cites W1972078441 @default.
• W5959882 cites W1973782344 @default.
• W5959882 cites W1975436203 @default.
• W5959882 cites W1976783944 @default.
• W5959882 cites W1977647593 @default.
• W5959882 cites W1978138686 @default.
• W5959882 cites W1984553096 @default.
• W5959882 cites W1989990175 @default.
• W5959882 cites W1990011328 @default.
• W5959882 cites W1991915276 @default.
• W5959882 cites W1995596496 @default.
• W5959882 cites W2001362559 @default.
• W5959882 cites W2004180892 @default.
• W5959882 cites W2004183686 @default.
• W5959882 cites W2008689421 @default.
• W5959882 cites W2009441693 @default.
• W5959882 cites W2018289835 @default.
• W5959882 cites W2018847585 @default.
• W5959882 cites W2023687151 @default.
• W5959882 cites W2025013837 @default.
• W5959882 cites W2030373829 @default.
• W5959882 cites W2030645841 @default.
• W5959882 cites W2050051607 @default.
• W5959882 cites W2073946289 @default.
• W5959882 cites W2075433094 @default.
• W5959882 cites W2076559362 @default.
• W5959882 cites W2085847856 @default.
• W5959882 cites W2095230275 @default.
• W5959882 cites W2098671505 @default.
• W5959882 cites W2100837269 @default.
• W5959882 cites W2101108802 @default.
• W5959882 cites W2134409607 @default.
• W5959882 cites W2138270253 @default.
• W5959882 cites W2145352278 @default.
• W5959882 cites W2166738891 @default.
• W5959882 cites W2169996826 @default.
• W5959882 cites W2413715038 @default.
• W5959882 cites W2915256003 @default.
• W5959882 cites W54201039 @default.
• W5959882 doi "https://doi.org/10.1002/j.1460-2075.1991.tb07982.x" @default.
• W5959882 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/452684" @default.
• W5959882 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2001673" @default.
• W5959882 hasPublicationYear "1991" @default.
• W5959882 type Work @default.
• W5959882 sameAs 5959882 @default.
• W5959882 citedByCount "406" @default.
• W5959882 countsByYear W59598822012 @default.
• W5959882 countsByYear W59598822013 @default.
• W5959882 countsByYear W59598822014 @default.
• W5959882 countsByYear W59598822015 @default.
• W5959882 countsByYear W59598822016 @default.
• W5959882 countsByYear W59598822017 @default.
• W5959882 countsByYear W59598822018 @default.
• W5959882 countsByYear W59598822019 @default.
• W5959882 countsByYear W59598822020 @default.
• W5959882 countsByYear W59598822021 @default.
• W5959882 countsByYear W59598822023 @default.
• W5959882 crossrefType "journal-article" @default.
• W5959882 hasAuthorship W5959882A5015274886 @default.
• W5959882 hasAuthorship W5959882A5030687294 @default.
• W5959882 hasAuthorship W5959882A5041584392 @default.
• W5959882 hasAuthorship W5959882A5058065410 @default.
• W5959882 hasAuthorship W5959882A5084814331 @default.
• W5959882 hasBestOaLocation W59598822 @default.
• W5959882 hasConcept C138885662 @default.
• W5959882 hasConcept C15708023 @default.
• W5959882 hasConcept C161191863 @default.
• W5959882 hasConcept C27740335 @default.
• W5959882 hasConcept C2781287369 @default.
• W5959882 hasConcept C41008148 @default.
• W5959882 hasConcept C55493867 @default.
• W5959882 hasConcept C86803240 @default.
• W5959882 hasConceptScore W5959882C138885662 @default.

• next