Department of Biochemistry & Molecular Biophysics
141 Chalmers Hall
Manhattan, KS 66506
785-532-6121
785-532-7278 fax
biochem@k-state.edu



Biotechnology Core Facility
206 Burt Hall
785-532-5956
785-532-6297 fax



Biomolecular NMR Facility
37 Chalmers Hall
785-532-2345

Michal Zolkiewski, Ph.D., Associate Professor
Chair Graduate Biochemistry Group

Complete Publications List

1980s | 1990s | 2000s | 2010s

1980s

Antosiewicz, J., Hoiland, H., Zolkiewski, M. and Shugar, D.: "Quasichemical Interpretation of the Ultrasonic Velocity in Ternary Aqueous Systems", J. Solution Chem., 16, 285-294, 1987.

Zolkiewski, M.: "Kirkwood-Buff Integrals and Density Fluctuations in Aqueous Solution of Caffeine", J. Solution Chem., 16, 1025-1034, 1987.

Zolkiewski, M., Krestov, G.A., V'yugin, A.I. and Zielenkiewicz, W.: "Enthalpies of Solution of 1,3-dimethyluracil and 1,3-diethylthymine in Water - N,N-dimethylformamide Mixtures", Bull. Pol. Acad. Sci. Chem., 37, 433-438, 1989.


1990s

Zolkiewski, M. and Zielenkiewicz, W.: "Enthalpies of Solvation of Alkylated Uracils in Water, Nonaqueous and Mixed Solvents", J. Solution Chem., 20, 517-530, 1991.

Kulinski, T., Bratek-Wiewiorowska, M.D., Wiewiorowski, M., Zielenkiewicz, A., Zolkiewski, M. and Zielenkiewicz, W.: "Comparative Calorimetric Studies on the Dynamic Conformation of Plant 5S rRNA: Structural Interpretation of the Thermal Unfolding Patterns for Lupin Seeds and Wheat Germ", Nucl. Acids Res., 19, 2449-2455, 1991.

Zielenkiewicz, A., Zolkiewski, M., Zielenkiewicz, W. and Wiewiorowski, M.: "The Conformational Changes of 5S rRNA of Plant Origin in Presence of Anions PO4-3, NO3-, ClO4-, Cl-, of tetra-Protonated Spermine and Magnesium Salts by Adiabatic Scanning Differential Calorimetry", Thermochim. Acta, 182, 165-174, 1991.

Wiewiorowski, M., Zielenkiewicz, A., Zielenkiewicz, W. and Zolkiewski, M.: "The Conformational Changes of 5S rRNA of Plant Origin in Presence of Sperminium and Spermidinium Cations by Adiabatic Scanning Differential Calorimetry", Thermochim. Acta, 182, 153-164, 1991.

Wiewiorowski, M., Zielenkiewicz, A., Zielenkiewicz, W. and Zolkiewski, M.: "The Conformational Changes of 5S rRNA of Plant Origin in Presence of Magnesium Cations by Adiabatic Scanning Differential Calorimetry", Thermochim. Acta, 182, 143-152, 1991.

Ginsburg, A. and Zolkiewski, M.: "Differential Scanning Calorimetry Study of Reversible, Partial Unfolding Transitions in Dodecameric Glutamine Synthetase from Escherichia coli", Biochemistry, 30, 9421-9429, 1991.

Zolkiewski, M. and Ginsburg, A.: "Thermodynamic Effects of Active-Site Ligands on the Reversible, Partial Unfolding of Dodecameric Glutamine Synthetase from Escherichia coli: Calorimetric Studies", Biochemistry, 31, 11991-12000, 1992.

Ginsburg, A. and Zolkiewski, M.: "Temperature and Guanidine Induced Unfolding of Dodecameric Glutamine Synthetase from E. coli", Pure Appl. Chem., 66, 469-472, 1994.

Redowicz, M.J., Martin, B., Zolkiewski, M., Ginsburg, A. and Korn, E.D.: "Effects of Phosphorylation and Nucleotides on the Conformation of Myosin II from Acanthamoeba castellanii", J. Biol. Chem., 269, 13558-13563, 1994.

Zolkiewski, M., Redowicz, M.J., Korn, E.D. and Ginsburg, A.: "Thermally Induced Unfolding of Acanthamoeba Myosin II and Skeletal Muscle Myosin: Nucleotide Effects", Arch. Biochem. Biophys., 318, 207-214, 1995.

Zolkiewski, M., Nosworthy, N.J. and Ginsburg, A.: "Urea Induced Dissociation and Unfolding of Dodecameric Glutamine Synthetase from Escherichia coli: Calorimetric and Spectral Studies", Protein Sci., 4, 1544-1552, 1995.

Zolkiewski, M., Redowicz, M.J., Korn, E.D. and Ginsburg, A.: "Thermal Unfolding of Acanthamoeba Myosin II and Skeletal Muscle Myosin", Biophys. Chem., 59, 365-371, 1996.

Zolkiewski, M., Redowicz, M.J., Korn, E.D., Hammer, J.A. III and Ginsburg, A.: “A Two-State Unfolding of a Long Dimeric Coiled-Coil: the Acanthamoeba Myosin II Rod”, Biochemistry, 36, 7876-7883, 1997.

Redowicz, M.J., Hammer, J.A., Bowers, B., Zolkiewski, M., Ginsburg, A., Korn, E.D. and Rau, D.C.: “Flexibility of Acanthamoeba Myosin Rod Minifilaments”, Biochemistry, 38, 7243-7252, 1999.

Zolkiewski, M., Kessel, M., Ginsburg, A. and Maurizi, M.R.: “Nucleotide-dependent oligomerization of ClpB from Escherichia coli, Protein Sci., 8, 1899-1903, 1999.

Zolkiewski, M.: “ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation: a novel multi-chaperone system from Escherichia coli, J. Biol. Chem., 274, 28083-28086, 1999.

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2000s

Gong, X., Peng, T., Yakhnin, A., Zolkiewski, M., Quinn, J., Yeamen, S.J. and Roche, T.E.: “Specificity Determinants for the Pyruvate Dehydrogenase Component Reaction Mapped with Mutated and Prostethic Group Modified Lipoyl Domains”, J. Biol. Chem., 275, 13645-13653, 2000.

Zheng, L., Krishnamoorthi, R., Zolkiewski, M. and Wang, X.: “Distinct Ca2+-Binding Properties of Novel C2 Domains of Plant Phospholipase D alpha and beta”, J. Biol. Chem., 275, 19700-19706, 2000.

Barnett, M.E., Zolkiewska, A. and Zolkiewski, M.: “Structure and Activity of ClpB from Escherichia coli: Role of the Amino- and Carboxy-terminal Domains”, J. Biol. Chem., 275, 37565-37571, 2000.

Zavodszky, M., Chen, C.W., Huang, J.K., Zolkiewski, M., Wen, L. and Krishnamoorthi, R.: “Disulfide Bond Effects on Protein Stability: Designed Variants of Cucurbita maxima Trypsin Inhibitor-V”, Protein Sci., 10, 149-160, 2001.

Urbauer, J.L., Adelman, K., Bieber Urbauer, R.J., Simeonov, M.F., Gilmore, J.M., Zolkiewski, M. and Brody, E.N.: "Conserved Regions 4.1 and 4.2 of σ70 Constitute the Recognition Sites for the Anti-σ Factor AsiA, and AsiA Is a Dimer Free in Solution", J. Biol. Chem., 276, 41128-41132, 2001.

Tek, V. and Zolkiewski, M.: "Stability and Interactions of the Amino-terminal Domain of ClpB from Escherichia coli", Protein Sci., 11, 1192-1198, 2002.

Liu, Z., Tek, V., Akoev, V. and Zolkiewski, M.: "Conserved Amino-acid Residues within the Amino-terminal Domain of ClpB are Essential for the Chaperone Activity", J. Mol. Biol., 321, 111-120, 2002.

Barnett, M.E. and Zolkiewski, M.: "Site-directed Mutagenesis of Conserved Charged Amino-acid Residues in ClpB from Escherichia coli", Biochemistry, 41, 11277-11283, 2002.

Kedzierska, S., Akoev, V., Barnett, M.E. and Zolkiewski, M.: “Structure and Function of the Middle Domain of ClpB from Escherichia coli, Biochemistry, 42, 14242-14248, 2003.

Liu, Z., Zolkiewska, A. and Zolkiewski, M.: "Characterization of human torsinA and its dystonia-associated mutant form", Biochem., 374(Pt 1), 117-122, 2003.

Akoev, V., Gogol, E.P., Barnett, M.E. and Zolkiewski, M.: "Nucleotide-Induced Switch in Oligomerization of the AAA+ ATPase ClpB", Protein Sci., 13, 567-574, 2004.

Chow, I.T., Barnett, M.E., Zolkiewski, M. and Baneyx. F.: "The N-terminal domain of Escherichia coli ClpB enhances chaperone function", FEBS Lett., 579, 4242-8, 2005.

Barnett, M.E., Nagy, M., Kedzierska, S. and Zolkiewski, M.: "The Amino-Terminal Domain of ClpB Supports Binding to Strongly Aggregated Proteins", J. Biol. Chem., 280, 34940-34945, 2005.

Kedzierska, S., Chesnokova, L.S., Witt, St.N., and Zolkiewski, M.: "Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli", Archives of Biochemistry and Biophysics, 444, 61-65, 2005.

Modrak-Wojcik, A., Stepniak, K., Akoev, V., Zolkiewski, M., and Bzowska, A.: "Molecular architecture of E. coli purine nucleoside phosphorylase studied by analytical ultracentrifugation and CD spectroscopy", Protein Science, 15, 1794-1800, 2006.

Zolkiewski, M.: “A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases”, Mol. Microbiol., 61, 1094-1100, 2006.

Nagy, M., Akoev, V. and Zolkiewski, M.: “Domain Stability in the AAA+ ATPase ClpB from Escherichia coli”, Arch. Biochem. Biophys., 453, 63-69, 2006.

Doyle, S.M., Shorter, J., Zolkiewski, M., Hoskins, J.R., Lindquist, S. and Wickner, S.: “Asymmetric deceleration of ClpB and Hsp104 ATPase activity unleashes protein-remodeling activity”, Nature Struct. Mol. Biol., 14, 114-122, 2007.

Zolkiewski, M.: "ClpB: a chaperone for protein disaggregation", in Houry, W. (ed.), Molecular Chaperones: Principles and Diseases, The Biomedical & Life Sciences Collection, Henry Stewart Talks Ltd, London, 2007.

Nagy, M., Wu, H.-C., Liu, Z., Kedzierska-Mieszkowska, S. and Zolkiewski, M.: “Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB”, Protein Sci., 18, 287-293, 2009.

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2010s

Nagy, M., Guenther, I., Akoyev, V., Barnett, M.E., Zavodszky, M.I., Kedzierska-Mieszkowska, S. and Zolkiewski, M.: “Synergistic cooperation between two ClpB isoforms in aggregate reactivation”, J. Mol. Biol., 396, 697-707, 2010.

Gilmore, J.M., Bieber Urbauer, R.J., Minakhin, L., Akoyev, V., Zolkiewski, M., Severinov, K. and Urbauer J.L.: "Determinants of affinity and activity of the anti-sigma factor AsiA",  Biochemistry, 49(29), 6143-54, 2010.

Zolkiewski, M. and Wu, H.-C.: “Emerging Area: TorsinA, a Novel ATP-Dependent Factor Linked to Dystonia” in Witt, S. N. (ed.), Protein Chaperones and Protection from Neurodegenerative Diseases, Wiley, 2011.

Zolkiewski M., Zhang, T. and Nagy, M.: "Aggregate reactivation mediated by the Hsp100 chaperones" Arch Biochem Biophys., 520, 1-6, 2012.

Zhang, T., Ploetz, E.A., Nagy, M., Doyle, S.M., Wickner, S., Smith, P.E. and Zolkiewski, M.: "Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency", Proteins, 80, 2758-68, 2012.

Guenther, I., Zolkiewski, M. and Kędzierska-Mieszkowska, S.: "Cooperation between two ClpB isoforms enhances the recovery of the recombinant β-galactosidase from inclusion bodies", Biochem Biophys REs Commun., 426, 596-600, 2012.

An, C., Hiromasa, Y., Zhang, X., Lovell, S., Zolkiewski, M., Tomich, J.M. and Michel. K.: "Biochemical characterization of Anopheles gambiae SRPN6, a malaria parasite invasion marker in mosquitoes", PLoS One, 7(11):e48689, 201

Park, S., Li, X., Kim, H.M., Singh, C.R., Tian, G., Hoyt, M.A., Lovell, S., Battaile, K.P., Zolkiewski, M., Coffino, P., Roelofs, J., Cheng, Y. and Finley, D.: "Reconfiguration of the proteasome during chaperone-mediated assembly", Nature, 497, 512-6, 2013.

Zhang, T., Kedzierska-Mieszkowska, S., Liu, H., Cheng, C., Ganta, R.R. and Zolkiewski, M.: "Aggregate-reactivation activity of the molecular chaperone ClpB from Ehrlichia chaffeensis", PLoS One, 8(5):e62454, 2013.

Ngansop, F., Li, H., Zolkiewska, A. and Zolkiewski, M.: "Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum", Biochem Biophys Res Commun., 469, 191-5, 2013.

Zacchi, L.F., Wu, H.C., Bell, S.L., Millen, L., Paton, A.W., Paton, J.C., Thomas, P.J., Zolkiewski, M. and Brodsky, J.L.: "The BiP Molecular Chaperone Plays Multiple Roles during the Biogenesis of TorsinA, an AAA+ ATPase Associated with the Neurological Disease Early-onset Torsion Dystonia", J Biol Chem., 289, 12727-47, 2014.

Wielgus-Kutrowska, B., Modrak-Wójcik, A., Dyzma, A., Breer, K., Zolkiewski, M. and Bzowska, A.: "Purine nucleoside phosphorylase activity decline is linked to the decay of the trimeric form of the enzyme", Arch Biochem Biophys., 549, 40-8, 2014. 

Zacchi, L. F., Wu, H.-C., Bell, S. L., Millen, L., Paton, A. W., Paton, J. C., Thomas, P. J., Zolkiewski, M., and Brodsky, J. L.: (2014) “The BiP molecular chaperone plays multiple roles during the biogenesis of TorsinA, a AAA+ ATPase associated with the neurological disease Early-Onset Torsion Dystonia”, J. Biol. Chem., 289:12727-12747.

Zblewska, K., Krajewska, J., Zolkiewski, M.,  and kedzierska-Mieszkowska, s.; (2014) "Role of the disaggregase ClpB in processing of proteins aggregated as inclusion bodies", Arch. Biochem. Biophys. 555/556C:23/27

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., and Geisbrecht, BV. (2014) “The Extracellular Adherence Protein from Staphylococcus aureus Inhibits the Classical and Lectin Pathways of Complement by Blocking Formation of the C3 Proconvertase.” J Immunol Nov 7. Pii:1401600. [Epub ahead of print] This paper was selected to be highlighted in the “In This Issue” section of the journal. 

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