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214 related items for PubMed ID: 10913171

  • 1. Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role.
    Krimmer T, Rassow J, Kunau WH, Voos W, Pfanner N.
    Mol Cell Biol; 2000 Aug; 20(16):5879-87. PubMed ID: 10913171
    [Abstract] [Full Text] [Related]

  • 2. Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.
    Voos W, von Ahsen O, Müller H, Guiard B, Rassow J, Pfanner N.
    EMBO J; 1996 Jun 03; 15(11):2668-77. PubMed ID: 8654364
    [Abstract] [Full Text] [Related]

  • 3. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane.
    Bömer U, Meijer M, Maarse AC, Hönlinger A, Dekker PJ, Pfanner N, Rassow J.
    EMBO J; 1997 May 01; 16(9):2205-16. PubMed ID: 9171336
    [Abstract] [Full Text] [Related]

  • 4. Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44.
    Moro F, Okamoto K, Donzeau M, Neupert W, Brunner M.
    J Biol Chem; 2002 Mar 01; 277(9):6874-80. PubMed ID: 11733493
    [Abstract] [Full Text] [Related]

  • 5. The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.
    Merlin A, Voos W, Maarse AC, Meijer M, Pfanner N, Rassow J.
    J Cell Biol; 1999 May 31; 145(5):961-72. PubMed ID: 10352014
    [Abstract] [Full Text] [Related]

  • 6. Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane.
    D'Silva P, Liu Q, Walter W, Craig EA.
    Nat Struct Mol Biol; 2004 Nov 31; 11(11):1084-91. PubMed ID: 15489862
    [Abstract] [Full Text] [Related]

  • 7. Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins.
    Bömer U, Maarse AC, Martin F, Geissler A, Merlin A, Schönfisch B, Meijer M, Pfanner N, Rassow J.
    EMBO J; 1998 Aug 03; 17(15):4226-37. PubMed ID: 9687491
    [Abstract] [Full Text] [Related]

  • 8. The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria.
    Strub A, Röttgers K, Voos W.
    EMBO J; 2002 Jun 03; 21(11):2626-35. PubMed ID: 12032075
    [Abstract] [Full Text] [Related]

  • 9. Regulated cycling of mitochondrial Hsp70 at the protein import channel.
    Liu Q, D'Silva P, Walter W, Marszalek J, Craig EA.
    Science; 2003 Apr 04; 300(5616):139-41. PubMed ID: 12677068
    [Abstract] [Full Text] [Related]

  • 10. The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis.
    Horst M, Oppliger W, Feifel B, Schatz G, Glick BS.
    Protein Sci; 1996 Apr 04; 5(4):759-67. PubMed ID: 8845766
    [Abstract] [Full Text] [Related]

  • 11. A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria.
    Truscott KN, Voos W, Frazier AE, Lind M, Li Y, Geissler A, Dudek J, Müller H, Sickmann A, Meyer HE, Meisinger C, Guiard B, Rehling P, Pfanner N.
    J Cell Biol; 2003 Nov 24; 163(4):707-13. PubMed ID: 14638855
    [Abstract] [Full Text] [Related]

  • 12. Biogenesis of the yeast frataxin homolog Yfh1p. Tim44-dependent transfer to mtHsp70 facilitates folding of newly imported proteins in mitochondria.
    Geissler A, Krimmer T, Schönfisch B, Meijer M, Rassow J.
    Eur J Biochem; 2000 Jun 24; 267(11):3167-80. PubMed ID: 10824101
    [Abstract] [Full Text] [Related]

  • 13. The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import.
    Schneider HC, Westermann B, Neupert W, Brunner M.
    EMBO J; 1996 Nov 01; 15(21):5796-803. PubMed ID: 8918457
    [Abstract] [Full Text] [Related]

  • 14. Mitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase.
    Hutu DP, Guiard B, Chacinska A, Becker D, Pfanner N, Rehling P, van der Laan M.
    Mol Biol Cell; 2008 Jun 01; 19(6):2642-9. PubMed ID: 18400944
    [Abstract] [Full Text] [Related]

  • 15. Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering.
    Schiller D, Cheng YC, Liu Q, Walter W, Craig EA.
    Mol Cell Biol; 2008 Jul 01; 28(13):4424-33. PubMed ID: 18426906
    [Abstract] [Full Text] [Related]

  • 16. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44.
    Dekker PJ, Martin F, Maarse AC, Bömer U, Müller H, Guiard B, Meijer M, Rassow J, Pfanner N.
    EMBO J; 1997 Sep 01; 16(17):5408-19. PubMed ID: 9312000
    [Abstract] [Full Text] [Related]

  • 17. Coupling chemical energy by the hsp70/tim44 complex to drive protein translocation into mitochondria.
    Cyr DM.
    J Bioenerg Biomembr; 1997 Feb 01; 29(1):29-34. PubMed ID: 9067799
    [Abstract] [Full Text] [Related]

  • 18. Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins.
    Geissler A, Rassow J, Pfanner N, Voos W.
    Mol Cell Biol; 2001 Oct 01; 21(20):7097-104. PubMed ID: 11564892
    [Abstract] [Full Text] [Related]

  • 19. Pam16 has an essential role in the mitochondrial protein import motor.
    Frazier AE, Dudek J, Guiard B, Voos W, Li Y, Lind M, Meisinger C, Geissler A, Sickmann A, Meyer HE, Bilanchone V, Cumsky MG, Truscott KN, Pfanner N, Rehling P.
    Nat Struct Mol Biol; 2004 Mar 01; 11(3):226-33. PubMed ID: 14981507
    [Abstract] [Full Text] [Related]

  • 20. The import motor of the yeast mitochondrial TIM23 preprotein translocase contains two different J proteins, Tim14 and Mdj2.
    Mokranjac D, Sichting M, Popov-Celeketić D, Berg A, Hell K, Neupert W.
    J Biol Chem; 2005 Sep 09; 280(36):31608-14. PubMed ID: 16027163
    [Abstract] [Full Text] [Related]

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