Michal Zolkiewski - Publications

Kansas State University, Manhattan, KS, United States 

23 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2016 Wise R, Duhachek-Muggy S, Qi Y, Zolkiewski M, Zolkiewska A. Protein disulfide isomerases in the endoplasmic reticulum promote anchorage-independent growth of breast cancer cells. Breast Cancer Research and Treatment. PMID 27161215 DOI: 10.1007/s10549-016-3820-1  0.56
2015 Zhang X, Meekins DA, An C, Zolkiewski M, Battaile KP, Kanost MR, Lovell S, Michel K. Structural and inhibitory effects of hinge loop mutagenesis in serpin-2 from the malaria vector Anopheles gambiae. The Journal of Biological Chemistry. 290: 2946-56. PMID 25525260 DOI: 10.1074/jbc.M114.625665  0.56
2014 Li H, Wu HC, Liu Z, Zacchi LF, Brodsky JL, Zolkiewski M. Intracellular complexes of the early-onset torsion dystonia-associated AAA+ ATPase TorsinA. Springerplus. 3: 743. PMID 25674472 DOI: 10.1186/2193-1801-3-743  0.56
2014 Woehl JL, Stapels DA, Garcia BL, Ramyar KX, Keightley A, Ruyken M, Syriga M, Sfyroera G, Weber AB, Zolkiewski M, Ricklin D, Lambris JD, Rooijakkers SH, Geisbrecht BV. The extracellular adherence protein from Staphylococcus aureus inhibits the classical and lectin pathways of complement by blocking formation of the C3 proconvertase. Journal of Immunology (Baltimore, Md. : 1950). 193: 6161-71. PMID 25381436 DOI: 10.4049/jimmunol.1401600  0.56
2014 Zacchi LF, Wu HC, Bell SL, Millen L, Paton AW, Paton JC, Thomas PJ, Zolkiewski M, Brodsky JL. The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia. The Journal of Biological Chemistry. 289: 12727-47. PMID 24627482 DOI: 10.1074/jbc.M113.529123  0.56
2013 Ngansop F, Li H, Zolkiewska A, Zolkiewski M. Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum. Biochemical and Biophysical Research Communications. 439: 191-5. PMID 23994135 DOI: 10.1016/j.bbrc.2013.08.064  0.56
2013 Park S, Li X, Kim HM, Singh CR, Tian G, Hoyt MA, Lovell S, Battaile KP, Zolkiewski M, Coffino P, Roelofs J, Cheng Y, Finley D. Reconfiguration of the proteasome during chaperone-mediated assembly. Nature. 497: 512-6. PMID 23644457 DOI: 10.1038/nature12123  0.56
2012 An C, Hiromasa Y, Zhang X, Lovell S, Zolkiewski M, Tomich JM, Michel K. Biochemical characterization of Anopheles gambiae SRPN6, a malaria parasite invasion marker in mosquitoes. Plos One. 7: e48689. PMID 23152794 DOI: 10.1371/journal.pone.0048689  0.56
2012 Zhang T, Ploetz EA, Nagy M, Doyle SM, Wickner S, Smith PE, Zolkiewski M. Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency Proteins: Structure, Function and Bioinformatics. 80: 2758-2768. PMID 22890624 DOI: 10.1002/prot.24159  0.56
2012 Zolkiewski M, Zhang T, Nagy M. Aggregate reactivation mediated by the Hsp100 chaperones. Archives of Biochemistry and Biophysics. 520: 1-6. PMID 22306514 DOI: 10.1016/j.abb.2012.01.012  0.44
2010 Nagy M, Guenther I, Akoyev V, Barnett ME, Zavodszky MI, Kedzierska-Mieszkowska S, Zolkiewski M. Synergistic cooperation between two ClpB isoforms in aggregate reactivation. Journal of Molecular Biology. 396: 697-707. PMID 19961856 DOI: 10.1016/j.jmb.2009.11.059  0.56
2009 Nagy M, Wu HC, Liu Z, Kedzierska-Mieszkowska S, Zolkiewski M. Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB. Protein Science : a Publication of the Protein Society. 18: 287-93. PMID 19177562 DOI: 10.1002/pro.36  0.44
2007 Doyle SM, Shorter J, Zolkiewski M, Hoskins JR, Lindquist S, Wickner S. Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity Nature Structural and Molecular Biology. 14: 114-122. PMID 17259993 DOI: 10.1038/nsmb1198  0.56
2006 Nagy M, Akoev V, Zolkiewski M. Domain stability in the AAA+ ATPase ClpB from Escherichia coli. Archives of Biochemistry and Biophysics. 453: 63-9. PMID 16615934 DOI: 10.1016/j.abb.2006.03.004  0.56
2005 Kedzierska S, Chesnokova LS, Witt SN, Zolkiewski M. Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli. Archives of Biochemistry and Biophysics. 444: 61-5. PMID 16289019 DOI: 10.1016/j.abb.2005.10.005  0.56
2005 Barnett ME, Nagy M, Kedzierska S, Zolkiewski M. The amino-terminal domain of ClpB supports binding to strongly aggregated proteins. The Journal of Biological Chemistry. 280: 34940-5. PMID 16076845 DOI: 10.1074/jbc.M505653200  1
2005 Chow IT, Barnett ME, Zolkiewski M, Baneyx F. The N-terminal domain of Escherichia coli ClpB enhances chaperone function. Febs Letters. 579: 4242-8. PMID 16051221 DOI: 10.1016/j.febslet.2005.06.055  0.56
2004 Akoev V, Gogol EP, Barnett ME, Zolkiewski M. Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB. Protein Science : a Publication of the Protein Society. 13: 567-74. PMID 14978298 DOI: 10.1110/ps.03422604  0.56
2003 Kedzierska S, Akoev V, Barnett ME, Zolkiewski M. Structure and function of the middle domain of ClpB from Escherichia coli. Biochemistry. 42: 14242-8. PMID 14640692 DOI: 10.1021/bi035573d  1
2003 Liu Z, Zolkiewska A, Zolkiewski M. Characterization of human torsinA and its dystonia-associated mutant form. The Biochemical Journal. 374: 117-22. PMID 12780349 DOI: 10.1042/BJ20030258  0.56
2002 Barnett ME, Zolkiewski M. Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli. Biochemistry. 41: 11277-83. PMID 12220194  1
2002 Liu Z, Tek V, Akoev V, Zolkiewski M. Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity. Journal of Molecular Biology. 321: 111-20. PMID 12139937  0.56
2000 Barnett ME, Zolkiewska A, Zolkiewski M. Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains. The Journal of Biological Chemistry. 275: 37565-71. PMID 10982797 DOI: 10.1074/jbc.M005211200  0.56
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