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B. Kierdaszuk

Department of Biophysics

Institute of Experimental Physics

University of Warsaw

93 Zwirki i Wigury Street

Poland

[email]@asp.biogeo.uw.edu.pl

Name/email consistency: low

 
 
 
 
 
 
 

Affiliations

  • Department of Biophysics, Institute of Experimental Physics, University of Warsaw, 93 Zwirki i Wigury Street, Poland. 2000
  • University of Warsaw, Department of Biophysics, Poland. 1997 - 1999

References

  1. Formycin A and its N-methyl analogues, specific inhibitors of E. coli purine nucleoside phosphorylase (PNP): induced tautomeric shifts on binding to enzyme, and enzyme-->ligand fluorescence resonance energy transfer. Kierdaszuk, B., Modrak-Wójcik, A., Wierzchowski, J., Shugar, D. Biochim. Biophys. Acta (2000) [Pubmed]
  2. Substrate/inhibitor properties of human deoxycytidine kinase (dCK) and thymidine kinases (TK1 and TK2) towards the sugar moiety of nucleosides, including O'-alkyl analogues. Kierdaszuk, B., Krawiec, K., Kazimierczuk, Z., Jacobsson, U., Johansson, N.G., Munch-Petersen, B., Eriksson, S., Shugar, D. Nucleosides. Nucleotides (1999) [Pubmed]
  3. Substrate/inhibitor specificities of human deoxycytidine kinase (dCK) and thymidine kinases (TK1 and TK2). Kierdaszuk, B., Krawiec, K., Kazimierczuk, Z., Jacobsson, U., Johansson, N.G., Munch-Petersen, B., Eriksson, S., Shugar, D. Adv. Exp. Med. Biol. (1998) [Pubmed]
  4. Binding of phosphate and sulfate anions by purine nucleoside phosphorylase from E. coli: ligand-dependent quenching of enzyme intrinsic fluorescence. Kierdaszuk, B., Modrak-Wójcik, A., Shugar, D. Biophys. Chem. (1997) [Pubmed]
 
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