Year |
Citation |
Score |
2022 |
Spaulding Z, Thevarajan I, Schrag LG, Zubcevic L, Zolkiewska A, Zolkiewski M. Human mitochondrial AAA+ ATPase SKD3/CLPB assembles into nucleotide-stabilized dodecamers. Biochemical and Biophysical Research Communications. 602: 21-26. PMID 35247700 DOI: 10.1016/j.bbrc.2022.02.101 |
0.321 |
|
2020 |
Thevarajan I, Zolkiewski M, Zolkiewska A. Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space. The International Journal of Biochemistry & Cell Biology. 127: 105841. PMID 32866687 DOI: 10.1016/J.Biocel.2020.105841 |
0.381 |
|
2020 |
Velazhahan V, Glaza P, Herrera AI, Prakash O, Zolkiewski M, Geisbrecht BV, Schrick K. Dietary flavonoid fisetin binds human SUMO1 and blocks sumoylation of p53. Plos One. 15: e0234468. PMID 32530958 DOI: 10.1371/Journal.Pone.0234468 |
0.389 |
|
2018 |
Ranaweera CB, Glaza P, Yang T, Zolkiewski M. Interaction of substrate-mimicking peptides with the AAA+ ATPase ClpB from Escherichia coli. Archives of Biochemistry and Biophysics. PMID 30092228 DOI: 10.1016/J.Abb.2018.08.002 |
0.422 |
|
2018 |
Krajewska J, Arent Z, Zolkiewski M, Kędzierska-Mieszkowska S. Isolation and Identification of Putative Protein Substrates of the AAA+ Molecular Chaperone ClpB from the Pathogenic Spirochaete . International Journal of Molecular Sciences. 19. PMID 29670056 DOI: 10.3390/Ijms19041234 |
0.394 |
|
2017 |
Krajewska J, Modrak-Wójcik A, Arent ZJ, Więckowski D, Zolkiewski M, Bzowska A, Kędzierska-Mieszkowska S. Characterization of the molecular chaperone ClpB from the pathogenic spirochaete Leptospira interrogans. Plos One. 12: e0181118. PMID 28700685 DOI: 10.1371/Journal.Pone.0181118 |
0.506 |
|
2017 |
Kuczynska-Wisnik D, Cheng C, Ganta RR, Zolkiewski M. Protein aggregation in Ehrlichia chaffeensis during infection of mammalian cells. Fems Microbiology Letters. PMID 28333306 DOI: 10.1093/Femsle/Fnx059 |
0.381 |
|
2016 |
Zolkiewski M, Chesnokova LS, Witt SN. Reactivation of Aggregated Proteins by the ClpB/DnaK Bi-Chaperone System. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. 83: 28.10.1-28.10.18. PMID 26836408 DOI: 10.1002/0471140864.Ps2810S83 |
0.433 |
|
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 |
0.433 |
|
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 |
0.393 |
|
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 |
0.405 |
|
2014 |
Zblewska K, Krajewska J, Zolkiewski M, Kędzierska-Mieszkowska S. Role of the disaggregase ClpB in processing of proteins aggregated as inclusion bodies. Archives of Biochemistry and Biophysics. 555: 23-7. PMID 24943258 DOI: 10.1016/J.Abb.2014.05.012 |
0.436 |
|
2014 |
Wielgus-Kutrowska B, Modrak-Wójcik A, Dyzma A, Breer K, Zolkiewski M, Bzowska A. Purine nucleoside phosphorylase activity decline is linked to the decay of the trimeric form of the enzyme. Archives of Biochemistry and Biophysics. 549: 40-8. PMID 24686197 DOI: 10.1016/J.Abb.2014.03.009 |
0.415 |
|
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 |
0.364 |
|
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 |
0.514 |
|
2013 |
Zhang T, Kedzierska-Mieszkowska S, Liu H, Cheng C, Ganta RR, Zolkiewski M. Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis. Plos One. 8: e62454. PMID 23667479 DOI: 10.1371/Journal.Pone.0062454 |
0.383 |
|
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 |
0.389 |
|
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 |
0.384 |
|
2012 |
Guenther I, Zolkiewski M, Kędzierska-Mieszkowska S. Cooperation between two ClpB isoforms enhances the recovery of the recombinant β-galactosidase from inclusion bodies. Biochemical and Biophysical Research Communications. 426: 596-600. PMID 22982305 DOI: 10.1016/J.Bbrc.2012.08.135 |
0.521 |
|
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 |
0.587 |
|
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 |
0.391 |
|
2010 |
Gilmore JM, Bieber Urbauer RJ, Minakhin L, Akoyev V, Zolkiewski M, Severinov K, Urbauer JL. Determinants of affinity and activity of the anti-sigma factor AsiA. Biochemistry. 49: 6143-54. PMID 20545305 DOI: 10.1021/Bi1002635 |
0.416 |
|
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 |
0.768 |
|
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 |
0.543 |
|
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 |
0.516 |
|
2006 |
Zolkiewski M. A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases. Molecular Microbiology. 61: 1094-100. PMID 16879409 DOI: 10.1111/J.1365-2958.2006.05309.X |
0.429 |
|
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 |
0.544 |
|
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 |
0.532 |
|
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 |
0.785 |
|
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 |
0.771 |
|
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 |
0.76 |
|
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 |
0.764 |
|
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 |
0.394 |
|
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 DOI: 10.1021/Bi026161S |
0.765 |
|
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 DOI: 10.1016/S0022-2836(02)00591-0 |
0.577 |
|
2002 |
Tek V, Zolkiewski M. Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli. Protein Science : a Publication of the Protein Society. 11: 1192-8. PMID 11967375 DOI: 10.1110/Ps.4860102 |
0.571 |
|
2001 |
Zavodszky M, Chen CW, Huang JK, Zolkiewski M, Wen L, Krishnamoorthi R. Disulfide bond effects on protein stability: Designed variants of Cucurbita maxima trypsin inhibitor-V Protein Science. 10: 149-160. PMID 11266603 DOI: 10.1110/Ps.26801 |
0.341 |
|
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 |
0.781 |
|
2000 |
Gong X, Peng T, Yakhnin A, Zolkiewski M, Quinn J, Yeaman SJ, Roche TE. Specificity determinants for the pyruvate dehydrogenase component reaction mapped with mutated and prosthetic group modified lipoyl domains. The Journal of Biological Chemistry. 275: 13645-53. PMID 10788482 DOI: 10.1074/Jbc.275.18.13645 |
0.415 |
|
2000 |
Zheng L, Krishnamoorthi R, Zolkiewski M, Wang X. Distinct Ca2+ binding properties of novel C2 domains of plant phospholipase Dα and β Journal of Biological Chemistry. 275: 19700-19706. PMID 10777500 DOI: 10.1074/Jbc.M001945200 |
0.374 |
|
1999 |
Zolkiewski M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. The Journal of Biological Chemistry. 274: 28083-6. PMID 10497158 DOI: 10.1074/Jbc.274.40.28083 |
0.5 |
|
1999 |
Zolkiewski M, Kessel M, Ginsburg A, Maurizi MR. Nucleotide-dependent oligomerization of ClpB from Escherichia coli. Protein Science : a Publication of the Protein Society. 8: 1899-903. PMID 10493591 DOI: 10.1110/Ps.8.9.1899 |
0.43 |
|
1994 |
Ginsburg A, Zolkiewski M. Temperature and guanidine induced unfolding of dodecameric glutamine synthetase from E. coli Pure and Applied Chemistry. 66: 469-472. DOI: 10.1351/Pac199466030469 |
0.428 |
|
1992 |
Zolkiewski M, Ginsburg A. Thermodynamic effects of active-site ligands on the reversible, partial unfolding of dodecameric glutamine synthetase from Escherichia coli: calorimetric studies. Biochemistry. 31: 11991-2000. PMID 1360813 |
0.313 |
|
1991 |
Ginsburg A, Zolkiewski M. Differential scanning calorimetry study of reversible, partial unfolding transitions in dodecameric glutamine synthetase from Escherichia coli. Biochemistry. 30: 9421-9. PMID 1680002 DOI: 10.1021/Bi00103A005 |
0.341 |
|
Low-probability matches (unlikely to be authored by this person) |
1995 |
Zolkiewski M, Nosworthy NJ, Ginsburg A. Urea-induced dissociation and unfolding of dodecameric glutamine synthetase from Escherichia coli: calorimetric and spectral studies. Protein Science : a Publication of the Protein Society. 4: 1544-52. PMID 8520480 DOI: 10.1002/pro.5560040812 |
0.295 |
|
2016 |
Wise R, Duhachek-Muggy S, Qi Y, Zolkiewski M, Zolkiewska A. Abstract A40: Protein disulfide isomerases in the endoplasmic reticulum promote anchorage-independent growth of breast cancer cells Cancer Research. 76. DOI: 10.1158/1538-7445.Tummet15-A40 |
0.29 |
|
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 |
0.29 |
|
1997 |
Zolkiewski M, Redowicz MJ, Korn ED, Hammer JA, Ginsburg A. Two-state thermal unfolding of a long dimeric coiled-coil: the Acanthamoeba myosin II rod. Biochemistry. 36: 7876-83. PMID 9201932 DOI: 10.1021/Bi962947C |
0.284 |
|
2020 |
Glaza P, Ranaweera CB, Shiva S, Roy A, Geisbrecht BV, Schoenen FJ, Zolkiewski M. Repurposing p97 inhibitors for chemical modulation of the bacterial ClpB/DnaK bi-chaperone system. The Journal of Biological Chemistry. PMID 33187983 DOI: 10.1074/jbc.RA120.015413 |
0.275 |
|
2006 |
Modrak-Wójcik A, Stepniak K, Akoev V, Zółkiewski M, Bzowska A. Molecular architecture of E. coli purine nucleoside phosphorylase studied by analytical ultracentrifugation and CD spectroscopy. Protein Science : a Publication of the Protein Society. 15: 1794-800. PMID 16751611 DOI: 10.1110/ps.062183206 |
0.274 |
|
1999 |
Redowicz MJ, Hammer JA, Bowers B, Zolkiewski M, Ginsburg A, Korn ED, Rau DC. Flexibility of Acanthamoeba myosin rod minifilaments. Biochemistry. 38: 7243-52. PMID 10353836 DOI: 10.1021/Bi982679D |
0.265 |
|
2020 |
Bawa S, Gameros S, Baumann K, Brooks DS, Kollhoff JA, Zolkiewski M, David Re Cecconi A, Panini N, Russo M, Piccirillo R, Johnson DK, Kashipathy MM, Battaile KP, Lovell S, Bouyain SEA, et al. Costameric Integrin and Sarcoglycan protein levels are altered in a model for Limb Girdle Muscular Dystrophy type 2H. Molecular Biology of the Cell. mbcE20070453. PMID 33296226 DOI: 10.1091/mbc.E20-07-0453 |
0.258 |
|
2016 |
Krajewska J, Arent Z, Więckowski D, Zolkiewski M, Kędzierska-Mieszkowska S. Immunoreactivity of the AAA+ chaperone ClpB from Leptospira interrogans with sera from Leptospira-infected animals. Bmc Microbiology. 16: 151. PMID 27421882 DOI: 10.1186/S12866-016-0774-8 |
0.227 |
|
2017 |
Pieroni M, Azzali E, Basilico N, Parapini S, Zolkiewski M, Beato C, Annunziato G, Bruno A, Vacondio F, Costantino G. Accepting the Invitation to Open Innovation in Malaria Drug Discovery: Synthesis, Biological Evaluation and Investigation on the Structure‒Activity Relationships of Benzo[b]thiophene-2-carboxamides as Antimalarial Agents. Journal of Medicinal Chemistry. PMID 28128956 DOI: 10.1021/Acs.Jmedchem.6B01685 |
0.226 |
|
2021 |
Kędzierska-Mieszkowska S, Zolkiewski M. Hsp100 Molecular Chaperone ClpB and Its Role in Virulence of Bacterial Pathogens. International Journal of Molecular Sciences. 22. PMID 34070174 DOI: 10.3390/ijms22105319 |
0.225 |
|
1995 |
Zolkiewski M, Redowicz MJ, Korn ED, Ginsburg A. Thermally induced unfolding of Acanthamoeba myosin II and skeletal muscle myosin: nucleotide effects. Archives of Biochemistry and Biophysics. 318: 207-14. PMID 7726563 DOI: 10.1006/Abbi.1995.1222 |
0.224 |
|
1987 |
Antosiewicz J, H�iland H, Zolkiewski M, Shugar D. Quasichemical interpretation of the ultrasonic velocity in ternary aqueous systems Journal of Solution Chemistry. 16: 285-294. DOI: 10.1007/Bf00646120 |
0.215 |
|
2021 |
Schrag LG, Liu X, Thevarajan I, Prakash O, Zolkiewski M, Chen J. Cancer-Associated Mutations Perturb the Disordered Ensemble and Interactions of the Intrinsically Disordered p53 Transactivation Domain. Journal of Molecular Biology. 167048. PMID 33984364 DOI: 10.1016/j.jmb.2021.167048 |
0.209 |
|
1996 |
Zolkiewski M, Redowicz MJ, Korn ED, Ginsburg A. Thermal unfolding of Acanthamoeba myosin II and skeletal muscle myosin. Biophysical Chemistry. 59: 365-71. PMID 8672724 DOI: 10.1016/0301-4622(95)00129-8 |
0.189 |
|
1991 |
Kuliński T, Bratek-Wiewiórowska MD, Wiewiórowski M, Zielenkiewicz A, Zółkiewski M, Zielenkiewicz W. Comparative calorimetric studies on the dynamic conformation of plant 5S rRNA: II. Structural interpretation of the thermal unfolding patterns for lupin seeds and wheat germ. Nucleic Acids Research. 19: 2449-55. PMID 2041782 DOI: 10.1093/nar/19.9.2449 |
0.184 |
|
2011 |
Zolkiewski M, Wu HC. Emerging Area: TorsinA, a Novel ATP-Dependent Factor Linked to Dystonia Protein Chaperones and Protection From Neurodegenerative Diseases. 359-383. DOI: 10.1002/9781118063903.ch11 |
0.155 |
|
2001 |
Urbauer JL, Adelman K, Urbauer RJ, Simeonov MF, Gilmore JM, Zolkiewski M, Brody EN. Conserved regions 4.1 and 4.2 of sigma(70) constitute the recognition sites for the anti-sigma factor AsiA, and AsiA is a dimer free in solution. The Journal of Biological Chemistry. 276: 41128-32. PMID 11518715 DOI: 10.1074/jbc.M106400200 |
0.146 |
|
1991 |
Zielenkiewicz A, Z̊ółkiewski M, Zielenkiewicz W, Wiewiórowski M. The conformational changes of 5SrRNA of plant origin in presence of anions PO4−3, NO−3, ClO−4, Cl−, of tetra-protonated spermine and magnesium salts by adiabatic scanning differential calorimetry Thermochimica Acta. 182: 165-174. DOI: 10.1016/0040-6031(91)87017-Q |
0.066 |
|
1991 |
Wiewiórowski M, Zielenkiewicz A, Zielenkiewicz W, żółkiewski M. The conformational changes of 5SrRNA of plant origin in presence of magnesium cations by adiabatic scanning differential calorimetry Thermochimica Acta. 182: 143-152. DOI: 10.1016/0040-6031(91)87015-O |
0.058 |
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2020 |
Michałowski A, Niedzielski P, Kozak L, Teska M, Jakubowski K, Żółkiewski M. Archaeometrical studies of prehistoric pottery using portable ED-XRF Measurement. 159: 107758. DOI: 10.1016/j.measurement.2020.107758 |
0.021 |
|
1987 |
Žółkiewski M. Kirkwood-Buff integrals and density fluctuations in aqueous solution of caffeine Journal of Solution Chemistry. 16: 1025-1034. DOI: 10.1007/BF00652586 |
0.019 |
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Hide low-probability matches. |