M. Mital, K. Szutkowski, K. Bossak-Ahmad, P. Skrobecki, S.C. Drew, J. Poznański, I. Zhukov, T. Frączyk, W. Bal; The palladium(II) complex of Aβ4-16 as suitable model for structural studies of biorelevant copper(II) complexes of N-truncated beta-amyloids. Int. J. Mol. Sci. 2020; 21: 9200. (T. Frączyk – corresponding author) [PubMed] [ResearchGate]

A. Mieczkowski, T. Frączyk, M. Psurski, P. Wińska, P. Siedlecki, M. Dziełak, D. Trzybiński, M. Wilczek, M. Bagiński, B. Bieszczad, K. Woźniak; Design and in vitro characterization of tricyclic benzodiazepine derivatives as potent and selective anti-leukemic agents. Chem. Biodiversity 2020; 17: e2000733. [PubMed] [ResearchGate]

K. Bossak-Ahmad, M.D. Wiśniewska, W. Bal, S.C. Drew, T. Frączyk; Ternary Cu(II) complex with GHK peptide and cis-urocanic acid as a potential physiologically functional copper chelate. Int. J. Mol. Sci. 2020; 21: 6190. (T. Frączyk – corresponding author) [PubMed] [ResearchGate]

N.E. Wezynfeld, T. Frączyk, A. Bonna, W. Bal; Peptide bond cleavage in the presence of Ni-containing particles. Metallomics 2020; 12: 649-653. [PubMed] [ResearchGate]

T. Frączyk, A. Bonna, E. Stefaniak, N.E. Wezynfeld, W. Bal; Peptide bond cleavage by Ni(II) ions within the nuclear localization signal sequence. Chem. Biodiversity 2020; 17: e1900652. (T. Frączyk – corresponding author) [PubMed] [ResearchGate]

K. Bossak-Ahmad, T. Frączyk, W. Bal, S.C. Drew; The sub-picomolar Cu2+ dissociation constant of human serum albumin. ChemBioChem 2020; 21: 331-334. [PubMed] [ResearchGate]


J. Sobich, M. Prokopowicz, P. Maj, P. Wilk, Z. Zieliński, T. Frączyk, W. Rode; Thymidylate synthase-catalyzed, tetrahydrofolate-dependent self-inactivation by 5-FdUMP. Arch. Biochem. Biophys. 2019; 674: 108106. [PubMed] [ResearchGate]


R. Kotuniak, T. Frączyk, P. Skrobecki, D. Płonka, W. Bal; Gly-His-Thr-Asp-amide, an insulin-activating peptide from the human pancreas is a strong Cu(II) but a weak Zn(II) chelator. Inorg. Chem. 2018; 57: 15507-15516. [PubMed] [ResearchGate]

M. Mital, W. Bal, T. Frączyk, S.C. Drew; Interplay between copper, neprilysin, and N-truncation of β-amyloid. Inorg. Chem. 2018; 57: 6193-6197. [PubMed] [ResearchGate]


A. Jarmuła, P. Wilk, P. Maj, J. Ludwiczak, A. Dowierciał, K. Banaszak, W. Rypniewski, J. Cieśla, M. Dąbrowska, T. Frączyk, A.K. Bronowska, J. Jakowiecki, S. Filipek, W. Rode; Crystal structures of nematode (parasitic T. spiralis and free living C. elegans), compared to mammalian, thymidylate synthases (TS). Molecular docking and molecular dynamics simulations in search for nematode-specific inhibitors of TS. J. Mol. Graph. Model. 2017; 77: 33-50. [PubMed] [ResearchGate]

A. Dowierciał, A. Jarmuła, P. Wilk, W. Rypniewski, M. Kowalska, T. Frączyk, J. Cieśla, W. Rode; Mouse thymidylate synthase does not show the inactive conformation, observed for the human enzyme. Struct. Chem. 2017; 28: 667-674. [ResearchGate]

A. Premchandar, A. Kupniewska, A. Bonna, G. Faure, T. Fraczyk, A. Roldan, B. Hoffmann, M. Faria da Cunha, H. Herrmann, G.L. Lukacs, A. Edelman, M. Dadlez; New insights into interactions between the nucleotide-binding domain of CFTR and keratin 8. Protein Sci. 2017; 26: 343-354. [PubMed] [ResearchGate]


A. Kezwoń, I. Góral, T. Frączyk, K. Wojciechowski; Effect of surfactants on surface activity and rheological properties of type I collagen at air/water interface. Colloids Surf. B Biointerfaces 2016; 148: 238-248. [PubMed] [ResearchGate]

N.E. Wezynfeld, T. Frączyk, W. Bal; Metal assisted peptide bond hydrolysis: chemistry, biotechnology and toxicological implications. Coord. Chem. Rev. 2016; 327-328: 166-187. [ResearchGate]

T. Frączyk, I.A. Zawisza, W. Goch, E. Stefaniak, S.C. Drew, W. Bal; On the ability of CuAβ1-x peptides to form ternary complexes: Neurotransmitter glutamate is a competitor while not a ternary partner. J. Inorg. Biochem. 2016; 158: 5-10. [PubMed] [ResearchGate]

J. Ludwiczak, P. Maj, P. Wilk, T. Frączyk, T. Ruman, B. Kierdaszuk, A. Jarmuła, W. Rode; Phosphorylation of thymidylate synthase affects slow-binding inhibition by 5-fluoro-dUMP and N4-hydroxy-dCMP. Mol. BioSyst. 2016; 12: 1333-1341. [PubMed] [ResearchGate]

A. Kezwoń, I. Chromińska, T. Frączyk, K. Wojciechowski; Effect of enzymatic hydrolysis on surface activity and surface rheology of type I collagen. Colloids Surf. B Biointerfaces 2016; 137: 60-69. [PubMed] [ResearchGate]


T. Frączyk, T. Ruman, P. Wilk, P. Palmowski, A. Rogowska-Wrzesinska, J. Cieśla, Z. Zieliński, J. Nizioł, A. Jarmuła, P. Maj, B. Gołos, P. Wińska, S. Ostafil, E. Wałajtys-Rode, D. Shugar, W. Rode; Properties of Phosphorylated Thymidylate Synthase. Biochim Biophys Acta 2015; 1854: 1922-1934. [PubMed] [ResearchGate]

M. Mital, N.E. Wezynfeld, T. Frączyk, M.Z. Wiloch, U.E. Wawrzyniak, A. Bonna, C. Tumpach, K.J. Barnham, C.L. Haigh, W. Bal, S.C. Drew; A Functional Role for Aβ in Metal Homeostasis? N-Truncation and High-Affinity Copper Binding. Angew. Chem., Int. Ed. 2015; 54: 10460-10464. [PubMed] [ResearchGate]

K. Bossak, W. Goch, K. Piątek, T. Frączyk, J. Poznański, A. Bonna, C. Keil, A. Hartwig, W. Bal; Unusual Zn(II) Affinities of Zinc Fingers of Poly(ADP-ribose) Polymerase 1 (PARP-1) Nuclear Protein. Chem. Res. Toxicol. 2015; 28: 191-201. [PubMed] [ResearchGate]

N.E. Wezynfeld, A. Bonna, W. Bal, T. Frączyk; Ni(II) ions cleave and inactivate human alpha-1 antitrypsin hydrolytically, implicating nickel exposure as a contributing factor in pathologies related to antitrypsin deficiency. Metallomics 2015; 7: 596-604. (T. Frączyk – corresponding author) [PubMed] [ResearchGate]


N.E. Wezynfeld, K. Bossak, W. Goch, A. Bonna, W. Bal, T. Frączyk; Human Annexins A1, A2, and A8 as Potential Molecular Targets for Ni(II) Ions. Chem. Res. Toxicol. 2014; 27: 1996-2009. (T. Frączyk – corresponding author) [PubMed] [ResearchGate]

N.E. Wezynfeld, W. Goch, W. Bal, T. Frączyk; cis-Urocanic acid as a potential nickel(II) binding molecule in the human skin. Dalton Trans. 2014; 43: 3196-3201. (T. Frączyk – corresponding author) [PubMed] [ResearchGate]


J. Nagaj, K. Stokowa-Sołtys, E. Kurowska, T. Frączyk, M. Jeżowska-Bojczuk, W. Bal; Revised Coordination Model and Stability Constants of Cu(II) Complexes of Tris Buffer. Inorg. Chem. 2013; 52: 13927–13933. [PubMed] [ResearchGate]

A. Dowierciał, P. Wilk, W. Rypniewski, T. Frączyk, A. Jarmuła, K. Banaszak, M. Dąbrowska, J. Cieśla, W. Rode; Crystal structures of thymidylate synthase from nematodes, Trichinella spiralis and Caenorhabditis elegans, as a potential template for species-specific drug design. Pteridines 2013; 24: 87-91. [ResearchGate]


E. Dąbrowska-Maś, T. Frączyk, T. Ruman, K. Radziszewska, P. Wilk, J. Cieśla, Z. Zieliński, A. Jurkiewicz, B. Gołos, P. Wińska, E. Wałajtys-Rode, A. Leś, J. Nizioł, A. Jarmuła, P. Stefanowicz, Z. Szewczuk, W. Rode; Tyrosine nitration affects thymidylate synthase properties. Org. Biomol. Chem. 2012; 10: 323-331. (E. Dąbrowska-Maś and T. Frączyk contributed equally to the work) [PubMed] [ResearchGate]


J. Cieśla, T. Frączyk, W. Rode; Phosphorylation of basic amino acid residues in proteins: important but easily missed. Acta Biochim. Pol. 2011; 58: 137-148. [PubMed] [ResearchGate]


A. Jarmuła, T. Frączyk, P. Cieplak, W. Rode; Mechanism of influence of phosphorylation on serine 124 on a decrease of catalytic activity of human thymidylate synthase. Bioorg. Med. Chem. 2010; 18: 3361-3370. [PubMed] [ResearchGate]

T. Frączyk, K. Kubiński, M. Masłyk, J. Cieśla, U. Hellman, D. Shugar, W. Rode; Phosphorylation of thymidylate synthase from various sources by human protein kinase CK2 and its catalytic subunits. Bioorg. Chem. 2010; 38: 124-131. [PubMed] [ResearchGate]

K. Kowalewska, P. Stefanowicz, T. Ruman, T. Frączyk, W. Rode, Z. Szewczuk; Electron capture dissociation mass spectrometric analysis of lysine-phosphorylated peptides. Biosci. Rep. 2010; 30: 433-443. [PubMed] [ResearchGate]


T. Ruman, K. Długopolska, A. Jurkiewicz, D. Kramarz, T. Frączyk, A. Leś, W. Rode; The Synthesis, Reactivity and NMR Investigation on 15N-Thiophosphoramidates. Lett. Org. Chem. 2009; 6: 642-647. [ResearchGate]

T. Ruman, K. Długopolska, A. Jurkiewicz, D. Rut, T. Frączyk, J. Cieśla, A. Leś, Z. Szewczuk, W. Rode; Thiophosphorylation of free amino acids and enzyme protein by thiophosphoramidate ions. Bioorg. Chem. 2009; 38: 74-80. [PubMed] [ResearchGate]

A. Dowierciał, A. Jarmuła, W. Rypniewski, M. Sokołowska, T. Frączyk, J. Cieśla, W. Rode; Crystal Structures of Substrate-and Sulfate-Bound Mouse Thymidylate Synthase. Pteridines 2009; 20: 163-167. [ResearchGate]

T. Frączyk, T. Ruman, D. Rut, E. Dąbrowska-Maś, J. Cieśla, Z. Zieliński, K. Sieczka, J. Dębski, B. Gołos, P. Wińska, E. Wałajtys-Rode, D. Shugar, W. Rode; Histidine phosphorylation, or tyrosine nitration, affect thymidylate synthase properties. Pteridines 2009; 20: 137-142. [ResearchGate]


K. Winiarska, T. Frączyk, D. Malińska, J. Drożak, J. Bryła; Melatonin attenuates diabetes-induced oxidative stress in rabbits. J. Pineal Res. 2006; 40: 168-176. [PubMed] [ResearchGate]

J. Cieśla, T. Frączyk, Z. Zieliński, J. Sikora, W. Rode; Altered mouse leukemia L1210 thymidylate synthase, associated with cell resistance to 5-fluoro-dUrd, is not mutated but rather reflects posttranslational modification. Acta Biochim. Pol. 2006; 53: 189-198. [PubMed] [ResearchGate]


P. Wińska, B. Gołos, J. Cieśla, Z. Zieliński, T. Frączyk, E. Wałajtys-Rode, W. Rode; Developmental arrest in Caenorhabditis elegans dauer larvae causes high expression of enzymes involved in thymidylate biosynthesis, similar to that found in Trichinella muscle larvae. Parasitology 2005; 131: 247-254. [PubMed] [ResearchGate]


K. Winiarska, J. Drożak, M. Węgrzynowicz, T. Frączyk, J. Bryła; Diabetes-induced changes in glucose synthesis, intracellular glutathione status and hydroxyl free radical generation in rabbit kidney-cortex tubules. Mol. Cell. Biochem. 2004; 261: 91-98. [PubMed] [ResearchGate]

A. Kiersztan, K. Winiarska, J. Drożak, M. Przedlacka, M. Węgrzynowicz, T Frączyk, J. Bryła; Differential effects of vanadium, tungsten and molybdenum on inhibition of glucose formation in renal tubules and hepatocytes of control and diabetic rabbits: beneficial action of melatonin and N-acetylcysteine. Mol. Cell. Biochem. 2004; 261: 9-21. [PubMed] [ResearchGate]

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