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Journal Abstract Search

307 related items for PubMed ID: 32397253

  • 1. Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron-Sulfur Cluster Biogenesis.
    Kleczewska M, Grabinska A, Jelen M, Stolarska M, Schilke B, Marszalek J, Craig EA, Dutkiewicz R.
    Int J Mol Sci; 2020 May 08; 21(9):. PubMed ID: 32397253
    [Abstract] [Full Text] [Related]

  • 2. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation.
    Vickery LE, Cupp-Vickery JR.
    Crit Rev Biochem Mol Biol; 2007 May 08; 42(2):95-111. PubMed ID: 17453917
    [Abstract] [Full Text] [Related]

  • 3. Evolution of mitochondrial chaperones utilized in Fe-S cluster biogenesis.
    Schilke B, Williams B, Knieszner H, Pukszta S, D'Silva P, Craig EA, Marszalek J.
    Curr Biol; 2006 Aug 22; 16(16):1660-5. PubMed ID: 16920629
    [Abstract] [Full Text] [Related]

  • 4. Compensation for a defective interaction of the hsp70 ssq1 with the mitochondrial Fe-S cluster scaffold isu.
    Knieszner H, Schilke B, Dutkiewicz R, D'Silva P, Cheng S, Ohlson M, Craig EA, Marszalek J.
    J Biol Chem; 2005 Aug 12; 280(32):28966-72. PubMed ID: 15958384
    [Abstract] [Full Text] [Related]

  • 5. Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart.
    Dutkiewicz R, Schilke B, Knieszner H, Walter W, Craig EA, Marszalek J.
    J Biol Chem; 2003 Aug 08; 278(32):29719-27. PubMed ID: 12756240
    [Abstract] [Full Text] [Related]

  • 6. Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function.
    Dutkiewicz R, Schilke B, Cheng S, Knieszner H, Craig EA, Marszalek J.
    J Biol Chem; 2004 Jul 09; 279(28):29167-74. PubMed ID: 15123690
    [Abstract] [Full Text] [Related]

  • 7. Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones.
    Bonomi F, Iametti S, Morleo A, Ta D, Vickery LE.
    Biochemistry; 2008 Dec 02; 47(48):12795-801. PubMed ID: 18986169
    [Abstract] [Full Text] [Related]

  • 8. The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation.
    Uzarska MA, Dutkiewicz R, Freibert SA, Lill R, Mühlenhoff U.
    Mol Biol Cell; 2013 Jun 02; 24(12):1830-41. PubMed ID: 23615440
    [Abstract] [Full Text] [Related]

  • 9. Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution.
    Ciesielski SJ, Schilke BA, Osipiuk J, Bigelow L, Mulligan R, Majewska J, Joachimiak A, Marszalek J, Craig EA, Dutkiewicz R.
    J Mol Biol; 2012 Mar 16; 417(1-2):1-12. PubMed ID: 22306468
    [Abstract] [Full Text] [Related]

  • 10. Iron-Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein-Protein Interaction.
    Delewski W, Paterkiewicz B, Manicki M, Schilke B, Tomiczek B, Ciesielski SJ, Nierzwicki L, Czub J, Dutkiewicz R, Craig EA, Marszalek J.
    Mol Biol Evol; 2016 Mar 16; 33(3):643-56. PubMed ID: 26545917
    [Abstract] [Full Text] [Related]

  • 11. Fe-S Cluster Hsp70 Chaperones: The ATPase Cycle and Protein Interactions.
    Dutkiewicz R, Nowak M, Craig EA, Marszalek J.
    Methods Enzymol; 2017 Mar 16; 595():161-184. PubMed ID: 28882200
    [Abstract] [Full Text] [Related]

  • 12. Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli.
    Hoff KG, Silberg JJ, Vickery LE.
    Proc Natl Acad Sci U S A; 2000 Jul 05; 97(14):7790-5. PubMed ID: 10869428
    [Abstract] [Full Text] [Related]

  • 13. Overlapping binding sites of the frataxin homologue assembly factor and the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster scaffold protein.
    Manicki M, Majewska J, Ciesielski S, Schilke B, Blenska A, Kominek J, Marszalek J, Craig EA, Dutkiewicz R.
    J Biol Chem; 2014 Oct 31; 289(44):30268-30278. PubMed ID: 25228696
    [Abstract] [Full Text] [Related]

  • 14. Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange.
    Bonomi F, Iametti S, Morleo A, Ta D, Vickery LE.
    Biochemistry; 2011 Nov 08; 50(44):9641-50. PubMed ID: 21977977
    [Abstract] [Full Text] [Related]

  • 15. Binding of the chaperone Jac1 protein and cysteine desulfurase Nfs1 to the iron-sulfur cluster scaffold Isu protein is mutually exclusive.
    Majewska J, Ciesielski SJ, Schilke B, Kominek J, Blenska A, Delewski W, Song JY, Marszalek J, Craig EA, Dutkiewicz R.
    J Biol Chem; 2013 Oct 04; 288(40):29134-42. PubMed ID: 23946486
    [Abstract] [Full Text] [Related]

  • 16. Chaperone function in Fe-S protein biogenesis: Three possible scenarios.
    Marszalek J, Craig EA, Pitek M, Dutkiewicz R.
    Biochim Biophys Acta Mol Cell Res; 2024 Jun 04; 1871(5):119717. PubMed ID: 38574821
    [Abstract] [Full Text] [Related]

  • 17. The functional interaction of mitochondrial Hsp70s with the escort protein Zim17 is critical for Fe/S biogenesis and substrate interaction at the inner membrane preprotein translocase.
    Lewrenz I, Rietzschel N, Guiard B, Lill R, van der Laan M, Voos W.
    J Biol Chem; 2013 Oct 25; 288(43):30931-43. PubMed ID: 24030826
    [Abstract] [Full Text] [Related]

  • 18. Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1.
    Sichting M, Mokranjac D, Azem A, Neupert W, Hell K.
    EMBO J; 2005 Mar 09; 24(5):1046-56. PubMed ID: 15719019
    [Abstract] [Full Text] [Related]

  • 19. Regulation of human Nfu activity in Fe-S cluster delivery-characterization of the interaction between Nfu and the HSPA9/Hsc20 chaperone complex.
    Wachnowsky C, Liu Y, Yoon T, Cowan JA.
    FEBS J; 2018 Jan 09; 285(2):391-410. PubMed ID: 29211945
    [Abstract] [Full Text] [Related]

  • 20. Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU.
    Silberg JJ, Tapley TL, Hoff KG, Vickery LE.
    J Biol Chem; 2004 Dec 24; 279(52):53924-31. PubMed ID: 15485839
    [Abstract] [Full Text] [Related]

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