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1

The lectin-binding pattern of nucleolin and its interaction with endogenous galectin-3

100%
Hoja-Lukowicz D., Kedracka-Krok S., Duda W., Litynska A.
Cellular and Molecular Biology Letters
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2014
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tom 19
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nr 3
Unlike nuclear nucleolin, surface-expressed and cytoplasmic nucleolin exhibit Tn antigen. Here, we show localization-dependent differences in the glycosylation and proteolysis patterns of nucleolin. Our results provide evidence for different paths of nucleolin proteolysis in the nucleus, in the cytoplasm, and on the cell surface. We found that full-length nucleolin and some proteolytic fragments coexist within live cells and are not solely the result of the preparation procedure. Extranuclear nucleolin undergoes N- and O-glycosylation, and unlike cytoplasmic nucleolin, membrane-associated nucleolin is not fucosylated. Here, we show for the first time that nucleolin and endogenous galectin-3 exist in the same complexes in the nucleolus, the cytoplasm, and on the cell surface of melanoma cells. Assessments of the interaction of nucleolin with galectin-3 revealed nucleolar co-localization in interphase, suggesting that galectin-3 may be involved in DNA organization and ribosome biogenesis.
2

Quantitative analysis of the ternary complex of RNA polymerase, cyclic AMP receptor protein and DNA by fluorescence anisotropy measurements

100%
Bonarek P., Kedracka-Krok S., Kepys B., Wasylewski Z.
Acta Biochimica Polonica
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2008
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tom 55
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nr 3
537-547
The in vitro formation of transcription complexes with Escherichia coli RNA polymerase was monitored using fluorescence anisotropy measurements of labeled fragments of DNA. The multicomponent system consisted of holo or core RNA polymerase (RNAP) and lac or galpromoter fragments of DNA (in different configurations), in the presence or absence of CRP activator protein (wt or mutants) with its ligand, cAMP. Values of the apparent binding constants characterizing the system were obtained, as a result of all processes taking place in the system. The interaction of the promoters with core RNAP in the absence of CRP protein was characterized by apparent binding constants of 0.67 and 1.9×106M–1 for lac166 and gal178, respectively, and could be regarded as nonspecific. The presence of wt CRP enhanced the strength of the interaction of core RNAP with the promoter, and even in the case of galpromoter it made this interaction specific (apparent binding constant 2.93×107M–1). Holo RNAP bound the promoters significantly more strongly than core RNAP did (apparent binding constants 1.46 and 40.14×106M–1 for lac166 and gal178, respectively), and the presence of CRP also enhanced the strength of these interactions. The mutation in activator region 1 of CRP did not cause any significant disturbances in the holo RNAP–lacpromoter interaction, but mutation in activator region 2 of the activator protein substantially weakened the RNAP–galpromoter interaction.
3
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Changes in cell physiology at the stage of dehydration in a cryopreservation protocol

100%
Domzalska L., Kedracka-Krok S., Mikula A., Rybczynski J. J.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2015
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tom 96
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nr 1
4

Kinetic and thermodynamic characterization of the interactions between the components of human plasma kinin-forming system and isolated and purified cell wall proteins of Candida albicans

76%
Seweryn K., Karkowska-Kuleta J., Wolak N., Bochenska O., Kedracka-Krok S., Kozik A., Rapala-Kozik S.
Acta Biochimica Polonica
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2015
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tom 62
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nr 4
5

Characterization of the interactions between human high-molecular-mass kininogen and cell wall proteins of pathogenic yeasts Candida tropicalis

64%
Karkowska-Kuleta J., Zajac D., Bras G., Bochenska O., Seweryn K., Kedracka-Krok S., Jankowska U., Rapala-Kozik M., Kozik A.
Acta Biochimica Polonica
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2016
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tom 63
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nr 3
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