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Journal Abstract Search

452 related items for PubMed ID: 16987818

  • 1. The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation.
    Ballar P, Shen Y, Yang H, Fang S.
    J Biol Chem; 2006 Nov 17; 281(46):35359-68. PubMed ID: 16987818
    [Abstract] [Full Text] [Related]

  • 2. AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation.
    Zhong X, Shen Y, Ballar P, Apostolou A, Agami R, Fang S.
    J Biol Chem; 2004 Oct 29; 279(44):45676-84. PubMed ID: 15331598
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  • 3. Identification of SVIP as an endogenous inhibitor of endoplasmic reticulum-associated degradation.
    Ballar P, Zhong Y, Nagahama M, Tagaya M, Shen Y, Fang S.
    J Biol Chem; 2007 Nov 23; 282(47):33908-14. PubMed ID: 17872946
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  • 4. Regulation of ER-associated degradation via p97/VCP-interacting motif.
    Ballar P, Fang S.
    Biochem Soc Trans; 2008 Oct 23; 36(Pt 5):818-22. PubMed ID: 18793143
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  • 5. Different p97/VCP complexes function in retrotranslocation step of mammalian ER-associated degradation (ERAD).
    Ballar P, Pabuccuoglu A, Kose FA.
    Int J Biochem Cell Biol; 2011 Apr 23; 43(4):613-21. PubMed ID: 21199683
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  • 6. Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase.
    Cao J, Wang J, Qi W, Miao HH, Wang J, Ge L, DeBose-Boyd RA, Tang JJ, Li BL, Song BL.
    Cell Metab; 2007 Aug 23; 6(2):115-28. PubMed ID: 17681147
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  • 9. Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP.
    Yang H, Liu C, Zhong Y, Luo S, Monteiro MJ, Fang S.
    PLoS One; 2010 Jan 26; 5(1):e8905. PubMed ID: 20126661
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  • 10. Structural and mechanistic insights into the arginine/lysine-rich peptide motifs that interact with P97/VCP.
    Liu S, Fu QS, Zhao J, Hu HY.
    Biochim Biophys Acta; 2013 Dec 26; 1834(12):2672-8. PubMed ID: 24100225
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  • 12. The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism.
    Bruderer RM, Brasseur C, Meyer HH.
    J Biol Chem; 2004 Nov 26; 279(48):49609-16. PubMed ID: 15371428
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  • 14. Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors.
    Alzayady KJ, Panning MM, Kelley GG, Wojcikiewicz RJ.
    J Biol Chem; 2005 Oct 14; 280(41):34530-7. PubMed ID: 16103111
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  • 15. BRSK2 is a valosin-containing protein (VCP)-interacting protein that affects VCP functioning in endoplasmic reticulum-associated degradation.
    Wang Y, Wan B, Zhou J, Li R, Yu L.
    Biotechnol Lett; 2013 Dec 14; 35(12):1983-9. PubMed ID: 23907667
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  • 17. ATPase activity of p97/valosin-containing protein is regulated by oxidative modification of the evolutionally conserved cysteine 522 residue in Walker A motif.
    Noguchi M, Takata T, Kimura Y, Manno A, Murakami K, Koike M, Ohizumi H, Hori S, Kakizuka A.
    J Biol Chem; 2005 Dec 16; 280(50):41332-41. PubMed ID: 16234241
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  • 19. Pro178 and Pro183 of selenoprotein S are essential residues for interaction with p97(VCP) during endoplasmic reticulum-associated degradation.
    Lee JH, Kwon JH, Jeon YH, Ko KY, Lee SR, Kim IY.
    J Biol Chem; 2014 May 16; 289(20):13758-68. PubMed ID: 24700463
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  • 20. Complex of Fas-associated factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD).
    Lee JJ, Park JK, Jeong J, Jeon H, Yoon JB, Kim EE, Lee KJ.
    J Biol Chem; 2013 Mar 08; 288(10):6998-7011. PubMed ID: 23293021
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