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478 related items for PubMed ID: 11836248

  • 1. Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress.
    Shen Y, Meunier L, Hendershot LM.
    J Biol Chem; 2002 May 03; 277(18):15947-56. PubMed ID: 11836248
    [Abstract] [Full Text] [Related]

  • 2. Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1.
    Chevalier M, Rhee H, Elguindi EC, Blond SY.
    J Biol Chem; 2000 Jun 30; 275(26):19620-7. PubMed ID: 10777498
    [Abstract] [Full Text] [Related]

  • 3. BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP.
    Chung KT, Shen Y, Hendershot LM.
    J Biol Chem; 2002 Dec 06; 277(49):47557-63. PubMed ID: 12356756
    [Abstract] [Full Text] [Related]

  • 4. JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs.
    Hosoda A, Kimata Y, Tsuru A, Kohno K.
    J Biol Chem; 2003 Jan 24; 278(4):2669-76. PubMed ID: 12446677
    [Abstract] [Full Text] [Related]

  • 5. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.
    McClellan AJ, Endres JB, Vogel JP, Palazzi D, Rose MD, Brodsky JL.
    Mol Biol Cell; 1998 Dec 24; 9(12):3533-45. PubMed ID: 9843586
    [Abstract] [Full Text] [Related]

  • 6. ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C.
    Dong M, Bridges JP, Apsley K, Xu Y, Weaver TE.
    Mol Biol Cell; 2008 Jun 24; 19(6):2620-30. PubMed ID: 18400946
    [Abstract] [Full Text] [Related]

  • 7. BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP.
    Awad W, Estrada I, Shen Y, Hendershot LM.
    Proc Natl Acad Sci U S A; 2008 Jan 29; 105(4):1164-9. PubMed ID: 18203820
    [Abstract] [Full Text] [Related]

  • 8. MDG1/ERdj4, an ER-resident DnaJ family member, suppresses cell death induced by ER stress.
    Kurisu J, Honma A, Miyajima H, Kondo S, Okumura M, Imaizumi K.
    Genes Cells; 2003 Feb 29; 8(2):189-202. PubMed ID: 12581160
    [Abstract] [Full Text] [Related]

  • 9. HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells.
    Yu M, Haslam RH, Haslam DB.
    J Biol Chem; 2000 Aug 11; 275(32):24984-92. PubMed ID: 10827079
    [Abstract] [Full Text] [Related]

  • 10. A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s.
    Schlenstedt G, Harris S, Risse B, Lill R, Silver PA.
    J Cell Biol; 1995 May 11; 129(4):979-88. PubMed ID: 7744969
    [Abstract] [Full Text] [Related]

  • 11. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein.
    Karzai AW, McMacken R.
    J Biol Chem; 1996 May 10; 271(19):11236-46. PubMed ID: 8626673
    [Abstract] [Full Text] [Related]

  • 12. Members of the Hsp70 Family Recognize Distinct Types of Sequences to Execute ER Quality Control.
    Behnke J, Mann MJ, Scruggs FL, Feige MJ, Hendershot LM.
    Mol Cell; 2016 Sep 01; 63(5):739-52. PubMed ID: 27546788
    [Abstract] [Full Text] [Related]

  • 13. ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress.
    Cunnea PM, Miranda-Vizuete A, Bertoli G, Simmen T, Damdimopoulos AE, Hermann S, Leinonen S, Huikko MP, Gustafsson JA, Sitia R, Spyrou G.
    J Biol Chem; 2003 Jan 10; 278(2):1059-66. PubMed ID: 12411443
    [Abstract] [Full Text] [Related]

  • 14. ERdj4 protein is a soluble endoplasmic reticulum (ER) DnaJ family protein that interacts with ER-associated degradation machinery.
    Lai CW, Otero JH, Hendershot LM, Snapp E.
    J Biol Chem; 2012 Mar 09; 287(11):7969-78. PubMed ID: 22267725
    [Abstract] [Full Text] [Related]

  • 15. The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends.
    Pobre KFR, Poet GJ, Hendershot LM.
    J Biol Chem; 2019 Feb 08; 294(6):2098-2108. PubMed ID: 30563838
    [Abstract] [Full Text] [Related]

  • 16. Deficiency of the BiP cochaperone ERdj4 causes constitutive endoplasmic reticulum stress and metabolic defects.
    Fritz JM, Dong M, Apsley KS, Martin EP, Na CL, Sitaraman S, Weaver TE.
    Mol Biol Cell; 2014 Feb 08; 25(4):431-40. PubMed ID: 24336520
    [Abstract] [Full Text] [Related]

  • 17. Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins.
    Morris JA, Dorner AJ, Edwards CA, Hendershot LM, Kaufman RJ.
    J Biol Chem; 1997 Feb 14; 272(7):4327-34. PubMed ID: 9020152
    [Abstract] [Full Text] [Related]

  • 18. ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates.
    Shen Y, Hendershot LM.
    Mol Biol Cell; 2005 Jan 14; 16(1):40-50. PubMed ID: 15525676
    [Abstract] [Full Text] [Related]

  • 19. ERdj3, a luminal ER DnaJ homologue, binds directly to unfolded proteins in the mammalian ER: identification of critical residues.
    Jin Y, Zhuang M, Hendershot LM.
    Biochemistry; 2009 Jan 13; 48(1):41-9. PubMed ID: 19090675
    [Abstract] [Full Text] [Related]

  • 20. Inactivation of the PKR protein kinase and stimulation of mRNA translation by the cellular co-chaperone P58(IPK) does not require J domain function.
    Yan W, Gale MJ, Tan SL, Katze MG.
    Biochemistry; 2002 Apr 16; 41(15):4938-45. PubMed ID: 11939789
    [Abstract] [Full Text] [Related]


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