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155 related items for PubMed ID: 10383442

  • 21. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.
    Singh SK, Grimaud R, Hoskins JR, Wickner S, Maurizi MR.
    Proc Natl Acad Sci U S A; 2000 Aug 01; 97(16):8898-903. PubMed ID: 10922052
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  • 22. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities.
    Gottesman S, Clark WP, de Crecy-Lagard V, Maurizi MR.
    J Biol Chem; 1993 Oct 25; 268(30):22618-26. PubMed ID: 8226770
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  • 23. Site-directed mutagenesis of the Cys residues in ClpA, the ATPase component of protease Ti (ClpAP) in Escherichia coli.
    Seol JH, Kwon JA, Yoo SJ, Kim HS, Kang MS, Chung CH.
    Biol Chem; 1997 Oct 25; 378(10):1205-9. PubMed ID: 9372193
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  • 24. Requirement of ATP hydrolysis for assembly of ClpA/ClpP complex, the ATP-dependent protease Ti in Escherichia coli.
    Seol JH, Woo KM, Kang MS, Ha DB, Chung CH.
    Biochem Biophys Res Commun; 1995 Dec 05; 217(1):41-51. PubMed ID: 8526938
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  • 28. Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis.
    Thompson MW, Singh SK, Maurizi MR.
    J Biol Chem; 1994 Jul 08; 269(27):18209-15. PubMed ID: 8027082
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  • 29. Local and global mobility in the ClpA AAA+ chaperone detected by cryo-electron microscopy: functional connotations.
    Effantin G, Ishikawa T, De Donatis GM, Maurizi MR, Steven AC.
    Structure; 2010 May 12; 18(5):553-62. PubMed ID: 20462489
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  • 30. Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP.
    Hoskins JR, Wickner S.
    Proc Natl Acad Sci U S A; 2006 Jan 24; 103(4):909-14. PubMed ID: 16410355
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  • 32. Protease Ti (Clp), a multi-component ATP-dependent protease in Escherichia coli.
    Chung CH, Seol JH, Kang MS.
    Biol Chem; 1996 Sep 24; 377(9):549-54. PubMed ID: 9067252
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  • 34. The ClpP double ring tetradecameric protease exhibits plastic ring-ring interactions, and the N termini of its subunits form flexible loops that are essential for ClpXP and ClpAP complex formation.
    Gribun A, Kimber MS, Ching R, Sprangers R, Fiebig KM, Houry WA.
    J Biol Chem; 2005 Apr 22; 280(16):16185-96. PubMed ID: 15701650
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  • 37. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome.
    Kessel M, Maurizi MR, Kim B, Kocsis E, Trus BL, Singh SK, Steven AC.
    J Mol Biol; 1995 Jul 28; 250(5):587-94. PubMed ID: 7623377
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