X-Ray Crystallography Laboratory

2019-2015

ORCID

ORCID iD iconorcid.org/0000-0002-5535-5760

ResearchID

2014

Pustelny, K., Zdzalik, M., Stach, N., Stec-Niemczyk, J., Cichon, P., Czarna, A., Popowicz, G., Mak, P., Drag, M., Salvesen, G.S., Wladyka, B., Potempa, J., Dubin, A., Dubin, G. (2014). Staphylococcal SplB Serine Protease Utilizes a Novel Molecular Mechanism of Activation. J. Biol. Chem. 289:15544-15553.

Pustelny, K., Stach, N., Wladyka, B., Dubin, A., Dubin, G. (2014). Evaluation of P1' substrate specificity of staphylococcal SplB protease. Acta Biochim. Pol. 61:149-52.

Zdzalik, M., Kalinska, M., Wysocka, M., Stec-Niemczyk, J., Cichon, P., Stach, N., Gruba, N., Stennicke, H.R., Jabaiah, A., Markiewicz, M., Kedracka-Krok, S., Wladyka, B., Daugherty, P.S., Lesner, A., Rolka, K., Dubin, A., Potempa, J., Dubin, G. (2014). Biochemical and structural characterization of SplD protease from Staphylococcus aureus. PLoS One. 8:e76812. doi: 10.1371/journal.pone.0076812.

Burchacka, E., Zdzalik, M., Stec-Niemczyk, J., Pustelny, K., Popowicz, G., Wladyka, B., Dubin, A., Potempa, J., Sienczyk, M., Dubin, G., Oleksyszyn, J. (2014). Development and binding characteristics of phosphonate inhibitors of SplA protease from Staphylococcus aureus. Prot. Sci. 23:179-189.

2013

Bukowski, M., Lyzen, R., Helbin, WM., Bonar, E., Szalewska-Palasz, A., Wegrzyn, G., Dubin, G.,Dubin, A., Wladyka. B. (2013). A regulatory role for Staphylococcus aureus toxin-antitoxin system pemIKSa. Nature Communications, 4:2012. doi:10.1038/ncomms3012

Jusko, M., Potempa, J., Kantyka, T., Bielecka, E., Miller, HK., Kalinska, M., Dubin, G., Garred, P., Shaw, LN., Blom, AM. (2013). Staphylococcal proteases aid in evasion of the human complement system. Jorunal of Innate Immunity, 6:31-46.

Zubko, M., Kusz, J., Prodan, A., Sturm, S., van Midden, HJP., Bennett, JC., Dubin, G., Zupanic, E., Bohm, H. (2013). Structural phase transition and related electronic properties in quasi one-dimensional (NbSe4)10/3I. Acta Crystallographica Section B. 69:229-237

Zak, K., Pecak, A., Rys, B., Wladyka, B., Domling, A., Weber, L., Holak, TA., Dubin, G. (2013). MDM2 and MdmX Inhibitors for the treatment of cancer: a patent review (2011-present). Expert Opinion On Therapeutic Patents – e-published ahead of print

Kolesinski, P., Golik, P., Grudnik, P., Piechota, J., Markiewicz, M., Tarnawski, M., Dubin, G., Szczepaniak, A. (2013). Insights into eukaryotic Rubisco assembly - crystal structures of RbcX chaperones from Arabidopsis thaliana. Biochim. Biophys. Acta. 1830:2899-2906

2012

Wladyka, B., Wielebska, K., Wloka, M., Bochenska, O., Dubin, G., Dubin, A., Mak, P. (2012). Isolation, biochemical characterization, and cloning of a bacteriocin from the poultry-associated Staphylococcus aureus strain CH-91. Appl Microbiol Biotechnol.

Kaminski, MM., Sauer, SW., Kaminski, M., Opp, S., Ruppert, T., Grigaravicius, P., Grudnik, P., Grone, HJ., Krammer, PH., Gülow, K. (2012). T cell activation is driven by an ADP-dependent glucokinase linking enhanced glycolysis with mitochondrial reactive oxygen species generation. Cell Rep. 29:1300-15.

Polakowska, K., Lis, M., Helbin, W.M., Dubin, G., Dubin, A., Niedziolka, J., Miedzobrodzki, J., Wladyka, B. (2012). The virulence of Staphylococcus aureus correlates with strain genotype in a chicken embryo model but not a nematode model. Microbes Infect. – e-published ahead of print.

Dubin, G., Koziel, J., Pyrc, K., Wladyka, B., Potempa. J. (2012). Bacterial proteases in disease - role in intracellular survival, evasion of coagulation/fibrinolysis innate defenses, toxicoses and viral infections. Curr. Pharm. Des. 19:1090-113

Burchacka, E. Walczak, M., Sienczyk, M., Dubin, G., Zdzalik, M., Potempa, J., Oleksyszyn, J. (2012). The development of first Staphylococcus aureus SplB protease inhibitors: Phosphonic analogues of glutamine. Bioorg. Med. Chem. Lett. 22: 5574-5578.

Zdzalik, M., Karim, A.Y., Wolski, K., Buda, P., Wojcik, K., Brueggemann, S., Wojciechowski, P., Eick, S., Calander, A.M., Jonsson, I.M., Kubica, M., Polakowska, K., Miedzobrodzki, J., Wladyka, B., Potempa, J., Dubin, G. (2012). Prevalence of genes encoding extracellular proteases in Staphylococcus aureus – important targets triggering immune response in vivo. FEMS Immunol. Med. Microbiol. 66:220-229

Bista, M., Smithson, D., Pecak, A., Salinas, G., Pustelny, K., Min, J., Pirog, A., Finch, K., Zdzalik, M., Waddell, B., Wladyka, B., Kedracka-Krok, S., Dyer, M.A., Dubin, G., Guy, R.K. (2012). On the mechanism of action of SJ-172550 in inhibiting the interaction of MDM4 and p53. PLoS One, 7:e37518.

Kalinska, M., Kantyka, T., Greenbaum, D.C., Larsen, K.S., Wladyka, B., Jabaiah, A., Bogyo, M., Daugherty, P.S., Wysocka, M., Jaros, M., Lesner, A., Rolka, K., Schaschke, N., Stennicke, H., Dubin, A., Potempa, J., Dubin, G. (2012). Substrate specificity of Staphylococcus aureus cysteine proteases – Staphopains A, B and C. Biochimie, 94:318-327.

2011

Wladyka, B., Kozik, A.J., Bukowski, M., Rojowska, A., Kantyka, T., Dubin, G., Dubin, A. (2011) Alpha-1-Antichymotrypsin inactivates staphylococcal cysteine protease in cross-class inhibition. Biochimie, 93: 948-953.

Wladyka, B., Dubin, G., Dubin, A. (2011). Activation mechanism of thiol protease precursor from broiler chicken specific Staphylococcus aureus strain CH-91. Vet. Microbiol. 147:195-199.

2010-2001

Zdzalik, M., Pustelny, K., Kedracka-Krok, S., Huben, K., Pecak, A., Wladyka, B., Jankowski, S., Dubin, A., Potempa, J., Dubin, G. (2010). Interaction of regulators Mdm2 and Mdmx with transcription factors p53, p63 and p73. Cell Cycle 9:4584-91.

Bukowski, M., Wladyka, B., Dubin, G. (2010). Exfoliative toxins of Staphylococcus Aureus. Toxins 2: 1148-1165.

Karim, A.Y., Kulczycka, M., Kantyka, T., Dubin, G., Jabaiah, A., Daugherty, P.S., Thogersen, I.B, Enghild, J.J., Nguyen, K.A., Potempa, J. (2010). A Novel Matrix Metalloprotease-like Enzyme (Karilysin) of the Periodontal Pathogen Tannerella forsythia ATCC 43037. Biol. Chem. 391: 105-117.

Kantyka, T., Latendorf, T., Wiedow, O., Bartels J., Gläser, R., Dubin, G., Schröder, J-M., Potempa, J., Meyer-Hoffert, U. (2009). Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage. Biol. Chem. 390: 1313-1320.

Czarna, A., Popowicz, G.M., Pecak, A., Wolf, S., Dubin, G., Holak, T.A. (2009). High affinity interaction of the p53 peptide-analogue with human Mdm2 and Mdmx. Cell Cycle. 8: 1176-1184.

Stec-Niemczyk, J., Pustelny, K., Kisielewska, M., Bista, M., Boulware, K.T., Stennicke, H.R., Thogersen, I.B., Daugherty, P.S., Enghild, J.J., Baczynski, K., Popowicz, G.M., Dubin, A., Potempa, J., Dubin, G. (2009). Structural and functional characterization of SplA, an exclusively specific protease of Staphylococcus aureus. Biochem. J. 419: 555-564.

Dubin, G., Stec-Niemczyk, J., Kisielewska, M., Pustelny, K., Popowicz, G., Bista, M., Kantyka, K., Boulware, K.T., Stennicke, H.R., Czarna, A., Phopaisarn, M., Daugherty, P.S., Th?gersen, I.B., Enghild, J.J, Thornberry, N., Dubin, A., Potempa, J. (2008). Enzymatic activity of the Staphylococcus aureus SplB serine protease is induced by substrates containing the sequence Trp-Glu-Leu-Gln. J. Mol. Biol. 379: 343-356

Calander, A.M., Dubin, G., Potempa, J., Tarkowski, A. (2008). Staphylococcus aureus infection triggers production of neutralizing, V8 protease-specific antibodies. FEMS Immunol. Med. Mic. 52: 267-272

Beaufort, N., Wojciechowski, P., Sommerhoff, C.P., Szmyd, G., Dubin, G., Eick, S., Kellermann, J., Schmitt, M., Potempa, J., Magdolen, V. (2008). The human fibrinolytic system is a target for the staphylococcal metalloprotease aureolysin. Biochem. J. 410: 157-165.

Kulig, P., Zabel, B.A., Dubin, G., Allen, S.J., Ohyama, T., Potempa, J., Handel, T.M., Butcher, E.C., Cichy, J. (2007). Staphylococcus aureus-derived staphopain B, a potent cysteine protease activator of plasma chemerin. J. Immunol. 178: 3713-3720.

Dubin, G., Wladyka, B., Stec-Niemczyk, J., Chmiel, D., Zdzalik, M., Dubin, A., Potempa J. (2007) The staphostatin family of cysteine protease inhibitors in the genus Staphylococcus as an example of parallel evolution of protease and inhibitor specificity. Biol. Chem. 388: 227-235.

Hirsch, T., von Peter, S., Dubin, G., Mittler, D., Jacobsen, F., Lehnhardt, M., Eriksson, E., Steinau, H-U., Steinstraesser, L. (2006). Adenoviral Gene Delivery to Primary Human Cutaneous Cells and Burn Wounds. Mol. Med. 12: 199-207.

Popowicz, G., Dubin, G., Stec-Niemczyk, J., Czarny, A., Dubin, A., Potempa, J., Holak T.A. (2006). Functional and Structural Characterization of Spl proteases from Staphylococcus aureus. J. Mol. Biol. 358: 270-279.

Dubin, A., Mak, P., Dubin, G., Rzychon, M., Stec-Niemczyk, J., Wladyka, B., Maziarka, K., Chmiel, D. (2005). New generation of peptide antibiotics. Acta Biochim Pol. 52:633-638.

Dubin, G. (2005). Proteinaceous cysteine protease inhibitors. Cell. Mol. Life. Sci. 62:653-669.

Dubin, G., Stec-Niemczyk, J., Dylag, T., Silberring, J., Dubin, A., Potempa, J. (2004) Characterisation of a highly specific, endogenous inhibitor of cysteine protease from Staphylococcus epidermidis, a new member of the staphostatin family. Biol. Chem. 385:543-546.

Dubin, G., Popowicz, G., Krajewski, M., Potempa, J., Dubin, A., Holak, T.A., (2004). 1H, 15N and 13C NMR resonance assignments of staphostatin A, a specific Staphylococcus aureus cysteine proteinase inhibitor. J. Biomol. NMR 28:295-96.

Dubin, G., Krajewski, M., Popowicz, G., Stec-Niemczyk, J., Bochtler, M., Potempa, J., Dubin, A., Holak, T.A. (2003). A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus. Biochemistry. 42:13449-13456.

Dubin, G., (2003). Defense against own arms: staphylococcal cysteine proteases and their inhibitors. Acta Biochim. Pol. 50:715-724.

Dubin, G., (2002). Extracellular proteases of Staphylococcus spp. Biol. Chem. 383, 1075-1086.

Dubin, G., Chmiel, D., Mak, P., Rakwalska, M., Rzychon, M., Dubin, A. (2001). Molecular cloning and biochemical characterization of proteases form Staphylococcus epidermidis. Biol. Chem. 382, 1575-1582.

Granted patents:

PL394913. A protease having the activity of SplB protease.

PL394912. Variant fo SplA protease and the method of producing a mutant of SplA protease.

PL394914. SplB protease mutant and a method fo producing SplB protease mutant

PL394911. A protease having the activity of SplA protease.

PL382638. Polipeptide having affinity for the active site of SplB protease, protein, nucleotide sequence encoding the polipeptide or protein and their use. A method of producing SplB protease and its use.

Patent applications:

PL389523. Higlhy efficient promoter of protein expression in bacteria, gene construct, vector, transformant, expression system and secretion system for heterologous proteins and their use.

PL387416. Labeled peptides, methods of detection of substances modulating the mdm2-p53 and/or mdmx-p53 and kits for the detection of modulating substances.

PL382770. SplA protease and target peptides and their use.

 


 
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