prof. UAM dr hab. Genowefa Ślósarek

@article{Szymanska2012,

title = {Light Scattering Studies of Hydration and Structural Transformations of Lysozyme},

author = {A Szymańska and Genowefa Ślósarek},

url = {http://przyrbwn.icm.edu.pl/APP/PDF/121/a121z3p24.pdf},

doi = {10.12693/APhysPolA.121.694},

issn = {0587-4246},

year  = {2012},

date = {2012-03-01},

journal = {Acta Physica Polonica A},

volume = {121},

number = {3},

pages = {694--698},

abstract = {We have applied the method of dynamic light scattering to analyse the lysozymeethanol interaction. For low ethanol concentration (below 4.3% (v/v)) no chemical denaturation process is observed. When the ethanol concentration grows above the triggering concentration the hydrodynamic radius of lysozyme increases, indicating the structural changes within the protein molecule. The observed structural modications are attributed to dehydration and preliminary tertiary structure modication of the protein molecule.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Szymanska2012a,

title = {Denaturation and aggregation of lysozyme in water-ethanol solution.},

author = {Agnieszka Szymańska and Tomasz Hornowski and Genowefa Ślósarek},

url = {http://www.ncbi.nlm.nih.gov/pubmed/22712059},

issn = {1734-154X},

year  = {2012},

date = {2012-01-01},

journal = {Acta Biochimica Polonica},

volume = {59},

number = {2},

pages = {317--21},

abstract = {We have applied rheological methods for the analysis of ethanol-lysozyme interaction during the process of denaturation and aggregation of the protein. At low concentration of ethanol a destruction of the hydration shell of lysozyme is observed. With the increase in the ethanol concentration a structural transformation takes place. It leads to the formation of a protein aggregate with an elongated structure. The rheological characteristics of lysozyme-water-ethanol solution changes from Newtonian to pseudoplastic.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek2012b,

title = {Współczesna rewolucja naukowa na pograniczu fizyki i biologii},

author = {Genowefa Ślósarek},

url = {http://cejsh.icm.edu.pl/cejsh/element/bwmeta1.element.cejsh-5e0cf13c-1391-4434-8b9a-88e146652db4},

issn = {0867-8296},

year  = {2012},

date = {2012-01-01},

journal = {Zagadnienia Filozoficzne w Nauce (Philosophical Problems in Science)},

number = {51},

pages = {96--115},

publisher = {Uniwersytet Papieski Jana Pawła II w Krakowie - Wydawnictwo Naukowe},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Zawadzki2010,

title = {A fluorescence correlation spectroscopy study of ligand interaction with cytokinin-specific binding protein from mung bean},

author = {Paweł Zawadzki and Genowefa Ślósarek and Jerzy Boryski and Przemysław Wojtaszek},

url = {http://www.ncbi.nlm.nih.gov/pubmed/19919180 https://www.degruyter.com/view/j/bchm.2010.391.issue-1/bc.2010.005/bc.2010.005.xml},

doi = {10.1515/bc.2010.005},

issn = {1437-4315},

year  = {2010},

date = {2010-01-01},

journal = {Biological Chemistry},

volume = {391},

number = {1},

pages = {43--53},

abstract = {Cytokinins are essential plant hormones that regulate numerous physiological processes. Recently, a protein was identified in mung bean (Vigna radiata) and characterized as a cytokinin-specific binding protein (VrCSBP). Fluorescence correlation spectroscopy was used to investigate the interaction between VrCSBP and its ligands. The synthetic cytokinin, N-phenyl-N'-(4-pyridyl) urea, was labeled with two fluorophores, 7-nitro-2,1,3-benzoxadiazole and rhodamine B. Protein-ligand binding was analyzed in an equilibrium saturation binding experiment and confirmed by the competition assay. Surprisingly, it was found that VrCSBP binds not only to cytokinins, but also to gibberellins. In addition, in the presence of natural cytokinins and gibberellins, two populations of VrCSBP that differ in their diffusion coefficients were detected. The diffusion coefficients of these two populations could be related to mono- and dimeric states, which suggests a new mode of operation in ligand binding by VrCSBP, in which dimerization induced by natural ligands enhances the ligand binding capacity of the protein.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Szymanska2008,

title = {The SAXS and Rheological Studies of HEWL Amyloid Formation},

author = {A Szymańska and Genowefa Ślósarek and T Hornowski and M Kozak},

url = {http://przyrbwn.icm.edu.pl/APP/PDF/114/a114z216.pdf},

doi = {10.12693/APhysPolA.114.447},

issn = {0587-4246},

year  = {2008},

date = {2008-08-01},

journal = {Acta Physica Polonica A},

volume = {114},

number = {2},

pages = {447--454},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek2008,

title = {Odkrycie struktury komórkowej tkanki nerwowej},

author = {Genowefa Ślósarek},

year  = {2008},

date = {2008-01-01},

journal = {Kosmos. Problemy Nauk Biologicznych},

volume = {57},

number = {1-2},

pages = {103--107},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek2006,

title = {Structure of N 6 -furfurylaminopurine (kinetin) dihydrogenphosphate},

author = {Genowefa Ślósarek and M Kozak and J Gierszewski and A Pietraszko},

url = {http://scripts.iucr.org/cgi-bin/paper?S010876810502673X},

doi = {10.1107/S010876810502673X},

issn = {0108-7681},

year  = {2006},

date = {2006-02-01},

journal = {Acta Crystallographica Section B Structural Science},

volume = {62},

number = {1},

pages = {102--108},

publisher = {International Union of Crystallography},

abstract = {The crystal structure of kinetin dihydrogenphosphate has been determined at 115 and 293 K. Kinetin dihydrogenphos­phate undergoes a polymorphic phase transition at 291.1 K. In both phases the crystal belongs to the triclinic system with the symmetry described by the space group P$backslash$bar 1. In the low-temperature phase, the unit cell is doubled along the a axis. There is a dynamic equilibrium between different tautomeric forms of the adenine residue, determined by the distribution of H atoms within the network of hydrogen bonds.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Krzaczkowska2004,

title = {Solubility of Adenine and Kinetin in Water–Ethanol Solutions},

author = {J Krzaczkowska and J Gierszewski and Genowefa Ślósarek},

url = {http://link.springer.com/10.1023/B:JOSL.0000036309.37357.70},

doi = {10.1023/B:JOSL.0000036309.37357.70},

issn = {0095-9782},

year  = {2004},

date = {2004-04-01},

journal = {Journal of Solution Chemistry},

volume = {33},

number = {4},

pages = {395--406},

publisher = {Kluwer Academic Publishers-Plenum Publishers},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Kaszynska2002,

title = {Dynamic Light Scattering and NMR Studies of Napin},

author = {Katarzyna Kaszyńska and Ewa Banachowicz and Genowefa Ślósarek and Adrian Morawiec and Iwona Gawrońska and Jan Barciszewski},

url = {http://link.springer.com/10.1023/A:1021877526536},

doi = {10.1023/A:1021877526536},

issn = {00959782},

year  = {2002},

date = {2002-01-01},

journal = {Journal of Solution Chemistry},

volume = {31},

number = {12},

pages = {987--993},

publisher = {Kluwer Academic Publishers-Plenum Publishers},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Hoderna-Natkaniec2001,

title = {Spectroscopy of Kinetin},

author = {Krystyna Hołderna-Natkaniec and W Kasperkowiak and I Natkaniec and Genowefa Ślósarek},

year  = {2001},

date = {2001-01-01},

journal = {Molecular Physics Reports},

volume = {34},

number = {2},

pages = {61--64},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Popenda2001,

title = {1H NMR Relaxation and Spectroscopy of Kinetin},

author = {ł Popenda and R Utrecht and Genowefa Ślósarek and Krystyna Hołderna-Natkaniec and J Wąsicki},

year  = {2001},

date = {2001-01-01},

journal = {Molecular Physics Reports},

volume = {33},

pages = {114--117},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek2001,

title = {NMR of peptides},

author = {Genowefa Ślósarek},

year  = {2001},

date = {2001-01-01},

journal = {Molecular Physics Reports},

volume = {34},

number = {2},

pages = {48--54},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Mucha1999,

title = {Conformation of Systemin, a Polypeptide Activator of Proteinase Inhibitor Synthesis in Plants},

author = {Piotr Mucha and Agnieszka Szyk and Piotr Rekowski and Gotfryd Kupryszewski and Genowefa Ślósarek and Jan Barciszewski},

url = {http://cccc.uochb.cas.cz/64/3/0553/},

doi = {10.1135/cccc19990553},

issn = {0010-0765},

year  = {1999},

date = {1999-01-01},

journal = {Collection of Czechoslovak Chemical Communications},

volume = {64},

number = {3},

pages = {553--558},

publisher = {Institute of Organic Chemistry and Biochemistry AS CR, v.v.i.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek1998,

title = {Własności sprężyste aktyny F},

author = {Genowefa Ślósarek},

year  = {1998},

date = {1998-01-01},

journal = {Current Topics in Biophysics},

volume = {22C},

pages = {13--25},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek1998a,

title = {Analiza strukturalna białek o dużej masie cząsteczkowej},

author = {Genowefa Ślósarek},

year  = {1998},

date = {1998-01-01},

journal = {Current Topics in Biophysics},

volume = {22A},

pages = {40--43},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek1996,

title = {Struktura i funkcja systeminy - peptydu o własnościach hormonu roślinnego},

author = {Genowefa Ślósarek and Jan Barciszewski},

year  = {1996},

date = {1996-01-01},

journal = {Postępy Biologii Komórki},

volume = {23},

number = {3},

pages = {477--489},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek1996a,

title = {Spektroskopia magnetycznego rezonansu jądrowego w badaniach strukturalnych nad aktyną},

author = {Genowefa Ślósarek},

year  = {1996},

date = {1996-01-01},

journal = {Wiadomości Chemiczne},

volume = {50},

pages = {125--141},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek1995a,

title = {Mechanism of the Activation of Proteinase Inhibitor Synthesis by Systemin Involves $beta$-Sheet Structure, a Specific DNA-Binding Protein Domain},

author = {Genowefa Ślósarek and Hans Robert Kalbitzer and Piotr Mucha and Piotr Rekowski and Gotfryd Kupryszewski and Malgorzata Giel-Pietraszuk and Maciej Szymański and Jan Barciszewski},

url = {https://www.sciencedirect.com/science/article/pii/S104784778571026X http://linkinghub.elsevier.com/retrieve/pii/S104784778571026X},

doi = {10.1006/jsbi.1995.1026},

issn = {10478477},

year  = {1995},

date = {1995-07-01},

journal = {Journal of Structural Biology},

volume = {115},

number = {1},

pages = {30--36},

publisher = {Academic Press},

abstract = {We analyzed a tertiary structure of systemin, the first identified polypeptide plant hormone, using two-dimensional NMR spectroscopy. From these data and molecular dynamics calculations we concluded that the peptide can adopt a Z-like-$beta$-sheet structure, which has previously been found in many specific DNA-binding proteins. Using DNA-cellulose affinity chromatography, we showed that systemin binds strongly to DNA. We suggest that the specific systemin-DNA interaction, particularly in a promoter region of the proteinase inhibitors, could effect gone expression and thus explain the biological activity of systemin.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek1995b,

title = {1H NMR spectra of G- and F-actin},

author = {Genowefa Ślósarek},

year  = {1995},

date = {1995-01-01},

journal = {Current Topics in Biophysics},

volume = {19},

number = {1},

pages = {13--19},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{Slosarek1994,

title = {Mobile segments in rabbit skeletal muscle F-actin detected by 1H nuclear magnetic resonance spectroscopy.},

author = {Genowefa Ślósarek and D Heintz and H R Kalbitzer},

url = {http://www.ncbi.nlm.nih.gov/pubmed/8082804},

issn = {0014-5793},

year  = {1994},

date = {1994-09-01},

journal = {FEBS letters},

volume = {351},

number = {3},

pages = {405--10},

abstract = {Polymerization of actin by increasing the ionic strength leads to a quenching of almost all 1H NMR signals. Surprisingly, distinct signals with relatively small line widths can still be observed in actin filaments (F-actin) indicating the existence of mobile, NMR visible residues in the macromolecular structure. The intensity of the F-actin spectrum is much reduced if one replaces Mg2+ with Ca2+, and a moderate reduction of the signal intensity can also be obtained by increasing the ionic strength. These results can be explained in a two-state model of the actin promoters with a M- (mobile) state and a I- (immobile) state in equilibrium. In the M-state a number of residues in the actin promoter are mobile and give rise to observable NMR signals. This equilibrium is shifted towards the I-state specifically by replacing Mg2+ with Ca(2+)-ions and unspecifically by addition of monovalent ions such as K+. The binding of phalloidin to its high-affinity site in the filaments does not influence the equilibrium between M- and I-state. Phalloidin itself is completely immobilized in F-actin, its exchange with the solvent being slow on the NMR time scale.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}