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1

Był sobie mogilnik

100%
Stolarski R.
Bociek. Biuletyn Lubuskiego Klubu Przyrodników
|
2000
|
nr 2[62]
2

Thermodynamics of specific protein-RNA interactions

100%
Stolarski R.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 2
Description of the recognition specificity between proteins and nucleic acids at the level of molecular interactions is one of the most challenging tasks in biophysics. It is key to understanding the course and control of gene expression and to the application of the thus acquired knowledge in chemotherapy. This review presents experimental results of thermodynamic studies and a discussion of the role of thermodynamics in formation and stability of functional protein-RNA complexes, with a special attention to the interactions involving mRNA 5 ' cap and cap-binding proteins in the initiation of protein biosynthesis in the eukaryotic cell. A theoretical framework for analysis of the thermodynamic parameters of protein-nucleic acid association is also briefly sur­veyed. Overshadowed by more spectacular achievements in structural studies, the thermodynamic investigations are of equal importance for full comprehension of biopolymers' activity in a quantitative way. In this regard, thermodynamics gives a di­rect insight into the energetic and entropic characteristics of complex macro- molecular systems in their natural environment, aqueous solution, and thus comple­ments the structural view derived from X-ray crystallography and multidimensional NMR. Further development of the thermodynamic approach toward interpretation of recognition and binding specificity in terms of molecular biophysics requires more profound contribution from statistical mechanics.
3

Hydroxylamine and methoxyamine mutagenesis: Tautomeric equilibrium of the promutagenic, N6-methoxyadenosine in solvents of different polarities

51%
Kierdaszuk B., Stolarski R., Shugar D.
Acta Biochimica Polonica
|
1984
|
tom 31
|
nr 1
4

Acyclonucleosides: Acyclobenzimidazole nucleoside and nucleotide analogues and conformations of the acyclic chains by menas of NMR spectroscopy

51%
Kazmierczuk Z., Stolarski R., Shugar D.
Acta Biochimica Polonica
|
1984
|
tom 31
|
nr 1
5

Papiery termograficzne - technologia wytwarzania

51%
Rogaczewski Z., Drzewinska E., Korczynski A., Stolarski R.
Przegląd Papierniczy
|
1996
|
tom 52
|
nr 11
593-596
6

Papiery termograficzne - rodzaje i wlasciwosci

51%
Rogaczewski Z., Drzewinska E., Korczynski A., Stolarski R.
Przegląd Papierniczy
|
1996
|
tom 52
|
nr 10
531-534
7

Cyclic phosphates of some antiviral acyclonucleosides: relationship between conformation and substrate-inhibitor properties in some enzyme systems

51%
Ciesla J. M., Stolarski R., Shugar D.
Acta Biochimica Polonica
|
1993
|
tom 40
|
nr 2
Solution conformations, and substrate/inhibitor properties towards several phosphodiesterases and other nucleolytic enzymes, have been investigated for the cyclic phosphates of various acyclonucleosides, some with known antiviral activity, including 9-[(l,3-dihydroxy-2-propoxy)methyl]guanine (DHPG) and its carbocyclic congener, 9-(3,4-dihydroxybutyl)guanine (DHBG), 9-[4-hydroxy-2-(hydroxymethyl)- butyl]-guanine (2HM-HBG), and 9-(2,3-dihydroxypropyl)guanine (HPG). Conformations of the cyclic phosphate rings were derived from analysis of the 1H-1H and 1H-31P vicinal coupling constants in the n.m.r. spectra, subsequently optimalized by minimalization of the internal energy. The resulting structures were examined with respect to their ability to recognize various specific phosphodiesterases and nucleases, and some structural parameters were delineated for acyclonucleotide interactions. Qualitative data are presented for inhibitory properties of the acyclonucleoside cyclic phosphates, and, in those instances where they were substrates, kinetic constants were evaluated. An unusual finding was the apparent ability of nuclease P1 to hydrolyse a five-membered cyclic phosphate ring of an acyclonucleoside.
8

Sosna zwyczajna [Pinus sylvestris L.] z sukcesji na centralnym zwalowisku odpadow gornictwa wegla kamiennego

45%
Stolarska M., Stolarski R., Harabin Z., Krzaklewski W., Pietrzykowski M.
Roczniki Gleboznawcze
|
2006
|
tom 57
|
nr 1-2
183-191
9

5’cap-binding site mutations in eIF4E abolish positive effect of the cap on the eIF4E–4E-BP1 interaction

45%
Modrak-Wojcik A., Zuberek J., Stelmachowska A., Zdanowski K., Stolarski R.
Current Topics in Biophysics. Supplement
|
2016
|
tom 39
|
nr A: Posters
10

Fluorescence approach to investigate interaction of a dansyl-labeled 5’ mRNA cap analog with proteins

39%
Darzynkiewicz Z. M., Ubych K., Niewieczerzal S., Ferenc-Mrozek A., Luchowski R., Jemielity J., Stolarski R.
Current Topics in Biophysics. Supplement
|
2016
|
tom 39
|
nr A: Plenary lectures
11

New mRNA 5’-cap analogues as useful tools in translation studies in eukaryota

33%
Darzynkiewicz E., Jemielity J., Stepinski J., Zuberek J., Niedzwiecka A., Lewdorowicz M., Haber D., Stolarski R., Rhoads R.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
12

Interaction of three Caenorhabditis elegans isoforms of translation initiation factor eIF4E with mono- and trimethylated mRNA 5' cap analogues

33%
Stachelska A., Wieczorek Z., Ruszczynska K., Stolarski R., Pietrzak M., Lamphear B. J., Rhoads R. E., Darzynkiewicz E., Jankowska-Anyszka M.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 3
Translation initiation factor eIF4E binds the m G7 cap of eukaryotic mRNAs and me­diates recruitment of mRNA to the ribosome during cap-dependent translation initia­tion. This event is the rate-limiting step of translation and a major target for translational control. In the nematode Caenorhabditis elegans, about 70% of genes express mRNAs with an unusual cap structure containing m3 2,2,7 G, which is poorly rec­ognized by mammalian eIF4E. C. elegans expresses five isoforms of eIF4E (IFE-1, IFE-2, etc.). Three of these (IFE-3, IFE-4 and IFE-5) were investigated by means of spectroscopy and structural modelling based on mouse eIF4E bound to m7GDP. Intrinsic fluorescence quenching of Trp residues in the IFEs by iodide ions indicated structural differences between the apo and m7G cap bound proteins. Fluorescence quenching by selected cap analogues showed that only IFE-5 forms specific complexes with both m7G- and m3 2,2,7 G-containing caps (Kas 2 x 106M–1 to 7 x 106M–1) whereas IFE-3 and IFE-4 discriminated strongly in favor of m7G-containing caps. These spectroscopic results quantitatively confirm earlier qualitative data derived from affinity chromatography. The dependence of Kas on pH indicated optimal cap binding of IFE-3, IFE-4 and IFE-5 at pH 7.2, lower by 0.4 pH units than that of eIF4E from human erythrocytes. These results provide insight into the molecular mechanism of recognition of structurally different caps by the highly homologous IFEs.
13

Dinucleotide 5' mRNA cap analogues with modified triphosphate bridge: useful tools to study decapping and translation

27%
Kowalska J., Kalek M., Jemielity J., Zuberek J., Lewdorowicz M., Bojarski E., Darzynkiewicz Z., Stepinski J., Stolarski R., Rhoads R. E., Davis R. E.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
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