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Journal Abstract Search

240 related items for PubMed ID: 10675324

  • 1. Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system.
    Hill K, Cooper AA.
    EMBO J; 2000 Feb 15; 19(4):550-61. PubMed ID: 10675324
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  • 2. Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex.
    Graham LA, Hill KJ, Stevens TH.
    J Cell Biol; 1998 Jul 13; 142(1):39-49. PubMed ID: 9660861
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  • 3. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation.
    Plemper RK, Bordallo J, Deak PM, Taxis C, Hitt R, Wolf DH.
    J Cell Sci; 1999 Nov 13; 112 ( Pt 22)():4123-34. PubMed ID: 10547371
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  • 7. Vma22p is a novel endoplasmic reticulum-associated protein required for assembly of the yeast vacuolar H(+)-ATPase complex.
    Hill KJ, Stevens TH.
    J Biol Chem; 1995 Sep 22; 270(38):22329-36. PubMed ID: 7673216
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  • 9. Eps1, a novel PDI-related protein involved in ER quality control in yeast.
    Wang Q, Chang A.
    EMBO J; 1999 Nov 01; 18(21):5972-82. PubMed ID: 10545109
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  • 12. Endoplasmic reticulum degradation: reverse protein flow of no return.
    Sommer T, Wolf DH.
    FASEB J; 1997 Dec 01; 11(14):1227-33. PubMed ID: 9409541
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  • 13. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.
    Biederer T, Volkwein C, Sommer T.
    EMBO J; 1996 May 01; 15(9):2069-76. PubMed ID: 8641272
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  • 15. PKR1 encodes an assembly factor for the yeast V-type ATPase.
    Davis-Kaplan SR, Compton MA, Flannery AR, Ward DM, Kaplan J, Stevens TH, Graham LA.
    J Biol Chem; 2006 Oct 20; 281(42):32025-35. PubMed ID: 16926153
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  • 16. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p.
    Gardner RG, Swarbrick GM, Bays NW, Cronin SR, Wilhovsky S, Seelig L, Kim C, Hampton RY.
    J Cell Biol; 2000 Oct 02; 151(1):69-82. PubMed ID: 11018054
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