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Wyszukujesz frazę "Kasztura, Monika" wg kryterium: Autor


Wyświetlanie 1-3 z 3
Tytuł:
Identification of a novel protein encoded by third conserved gene within RAG locus
Autorzy:
Kasztura, Monika
Miazek, Arkadiusz
Cebrat, Małgorzata
Kisielow, Paweł
Powiązania:
https://bibliotekanauki.pl/articles/1040654.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
RAG locus
lymphocytes
T cells
evolutionarily conserved proteins
Opis:
Recently, a third evolutionarily conserved gene, NWC, was discovered within the recombination activating gene (RAG) locus, known to contain the RAG1 and RAG2 genes. Here, we identify and characterize the murine endogenous NWC protein which has no homology to any known protein and is ubiquitously expressed. In the cell, the NWC protein which has been suggested to function as a transcriptional repressor, is found in the cytoplasm as well as in the nucleus.
Źródło:
Acta Biochimica Polonica; 2009, 56, 1; 177-181
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Degenerate specificity of PDZ domains from RhoA-specific nucleotide exchange factors PDZRhoGEF and LARG
Autorzy:
Smietana, Katarzyna
Kasztura, Monika
Paduch, Marcin
Derewenda, Urszula
Derewenda, Zygmunt
Otlewski, Jacek
Powiązania:
https://bibliotekanauki.pl/articles/1040739.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
binding specificity
LARG
PDZ domain
PDZRhoGEF
phage display
Opis:
PDZ domains are ubiquitous protein-protein interaction modules which bind short, usually carboxyterminal fragments of receptors, other integral or membrane-associated proteins, and occasionally cytosolic proteins. Their role in organizing multiprotein complexes at the cellular membrane is crucial for many signaling pathways, but the rules defining their binding specificity are still poorly understood and do not readily explain the observed diversity of their known binding partners. Two homologous RhoA-specific, multidomain nucleotide exchange factors PDZRhoGEF and LARG contain PDZ domains which show a particularly broad recognition profile, as suggested by the identification of five diverse biological targets. To investigate the molecular roots of this phenomenon, we constructed a phage display library of random carboxyterminal hexapeptides. Peptide variants corresponding to the sequences identified in library selection were synthesized and their affinities for both PDZ domains were measured and compared with those of peptides derived from sequences of natural partners. Based on the analysis of the binding sequences identified for PDZRhoGEF, we propose a sequence for an 'optimal' binding partner. Our results support the hypothesis that PDZ-peptide interactions may be best understood when one considers the sum of entropic and dynamic effects for each peptide as a whole entity, rather than preferences for specific residues at a given position.
Źródło:
Acta Biochimica Polonica; 2008, 55, 2; 269-280
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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