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Journal Abstract Search

302 related items for PubMed ID: 21871892

  • 1. Yos9, a control protein for misfolded glycosylated and non-glycosylated proteins in ERAD.
    Benitez EM, Stolz A, Wolf DH.
    FEBS Lett; 2011 Oct 03; 585(19):3015-9. PubMed ID: 21871892
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  • 2. Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD.
    Szathmary R, Bielmann R, Nita-Lazar M, Burda P, Jakob CA.
    Mol Cell; 2005 Sep 16; 19(6):765-75. PubMed ID: 16168372
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  • 3. Mnl2, a novel component of the ER associated protein degradation pathway.
    Martinez Benitez E, Stolz A, Becher A, Wolf DH.
    Biochem Biophys Res Commun; 2011 Oct 28; 414(3):528-32. PubMed ID: 21971548
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  • 5. Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen.
    Bhamidipati A, Denic V, Quan EM, Weissman JS.
    Mol Cell; 2005 Sep 16; 19(6):741-51. PubMed ID: 16168370
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  • 7. Yos9p detects and targets misfolded glycoproteins for ER-associated degradation.
    Kim W, Spear ED, Ng DT.
    Mol Cell; 2005 Sep 16; 19(6):753-64. PubMed ID: 16168371
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  • 9. Fusion of an intact secretory protein permits a misfolded protein to exit from the endoplasmic reticulum in yeast.
    Suyama K, Hori M, Gomi K, Shintani T.
    Biosci Biotechnol Biochem; 2014 Sep 16; 78(1):49-59. PubMed ID: 25036483
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  • 10. A Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.
    Pfeiffer A, Stephanowitz H, Krause E, Volkwein C, Hirsch C, Jarosch E, Sommer T.
    J Biol Chem; 2016 Jun 03; 291(23):12195-207. PubMed ID: 27053108
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  • 12. A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins.
    Buschhorn BA, Kostova Z, Medicherla B, Wolf DH.
    FEBS Lett; 2004 Nov 19; 577(3):422-6. PubMed ID: 15556621
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  • 14. Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae.
    Chantret I, Kodali VP, Lahmouich C, Harvey DJ, Moore SEH.
    J Biol Chem; 2011 Dec 02; 286(48):41786-41800. PubMed ID: 21979948
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  • 15. Substrate ubiquitination retains misfolded membrane proteins in the endoplasmic reticulum for degradation.
    Sun Z, Guerriero CJ, Brodsky JL.
    Cell Rep; 2021 Sep 21; 36(12):109717. PubMed ID: 34551305
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  • 16. Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation.
    Spear ED, Ng DT.
    J Cell Biol; 2005 Apr 11; 169(1):73-82. PubMed ID: 15809311
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  • 17. Structural investigation of glycan recognition by the ERAD quality control lectin Yos9.
    Kniss A, Kazemi S, Löhr F, Berger M, Rogov VV, Güntert P, Sommer T, Jarosch E, Dötsch V.
    J Biomol NMR; 2018 Oct 11; 72(1-2):1-10. PubMed ID: 30066206
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  • 20. Sec61p is part of the endoplasmic reticulum-associated degradation machinery.
    Schäfer A, Wolf DH.
    EMBO J; 2009 Oct 07; 28(19):2874-84. PubMed ID: 19696741
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