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Journal Abstract Search
372 related items for PubMed ID: 10777498
1. 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]
6. Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK. Landry SJ. Biochemistry; 2003 May 06; 42(17):4926-36. PubMed ID: 12718534 [Abstract] [Full Text] [Related]
7. 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 06; 9(12):3533-45. PubMed ID: 9843586 [Abstract] [Full Text] [Related]
11. A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomes. Dudek J, Volkmer J, Bies C, Guth S, Müller A, Lerner M, Feick P, Schäfer KH, Morgenstern E, Hennessy F, Blatch GL, Janoscheck K, Heim N, Scholtes P, Frien M, Nastainczyk W, Zimmermann R. EMBO J; 2002 Jun 17; 21(12):2958-67. PubMed ID: 12065409 [Abstract] [Full Text] [Related]
12. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Gässler CS, Buchberger A, Laufen T, Mayer MP, Schröder H, Valencia A, Bukau B. Proc Natl Acad Sci U S A; 1998 Dec 22; 95(26):15229-34. PubMed ID: 9860951 [Abstract] [Full Text] [Related]
14. Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. Suh WC, Burkholder WF, Lu CZ, Zhao X, Gottesman ME, Gross CA. Proc Natl Acad Sci U S A; 1998 Dec 22; 95(26):15223-8. PubMed ID: 9860950 [Abstract] [Full Text] [Related]
15. 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]
19. The chaperone proteins HSP70, HSP40/DnaJ and GRP78/BiP suppress misfolding and formation of β-sheet-containing aggregates by human amylin: a potential role for defective chaperone biology in Type 2 diabetes. Chien V, Aitken JF, Zhang S, Buchanan CM, Hickey A, Brittain T, Cooper GJ, Loomes KM. Biochem J; 2010 Nov 15; 432(1):113-21. PubMed ID: 20735358 [Abstract] [Full Text] [Related]