Wyniki wyszukiwania

1

Light and low-temperature induced transmembrane potential changes in mesophyll cells

100%

Krol E., Dziubinska H., Trebacz K., Zawadzki T., Stolarz M., Buda A., Krupa M.

Cellular and Molecular Biology Letters

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2002

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tom 07

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nr Suppl.

2

Interaction of class A G protein-coupled receptors with G proteins

88%

Slusarz R., Ciarkowski J.

Acta Biochimica Polonica

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2004

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tom 51

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nr 1

A model for interaction of class A G protein-coupled receptor with the G protein Ga subunit is proposed using the rhodopsin-transducin (RD/Gt) prototype. The model combines the resolved interactions/distances, essential in the active RD*/Gt system, with the structure of Gta C-terminal peptide bound to RD* while stabilizing it. Assuming the interactions involve conserved parts of the partners, the model specifies the conserved Helix 2 non-polar X- - -X, Helix 3 DRY and Helix 7/8 NP- -Y- - F RD* motifs interacting with the Gta C-terminal peptide, in compliance with the structure of the latter. A concomitant role of Gta and Gtγ C-termini in stabilizing RD* could possibly be resolved assuming a receptor dimer as requisite for G protein activation.

3

Targeting drug-efflux pumps - a pharmacoinformatic approach

75%

Pleban K., Kaiser D., Kopp S., Peer M., Chiba P., Ecker G. F.

Acta Biochimica Polonica

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2005

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tom 52

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nr 3

In line with our studies on propafenone-type inhibitors of P-glycoprotein (P-gp), we applied several methods to approach virtual screening tools for identification of new P-gp inhibitors on one hand and the molecular basis of ligand-protein interaction on the other hand. For virtual screening, a combination of autocorrelation vectors and selforganising artificial neural networks proved extremely valuable in identifying P-gp inhibitors with structurally new scaffolds. For a closer view on the binding region for propafenone-type ligands we applied a combination of pharmacophore-driven photoaffinity labeling and protein homology modeling. On LmrA, a bacterial homologue of P-gp, we were able to identify distinct regions on transmembrane helices 3, 5 and 6 which show significant changes in the labeling pattern during different steps of the catalytic cycle.

4

Syndecan signaling: when, where and why?

51%

Multhaupt H. A. B., Yoneda A., Whiteford J. R., Oh E.-S., Lee W., Couchman J. R.

Journal of Physiology and Pharmacology. Supplement

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2009

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tom 60

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nr 4

Ograniczanie wyników

2 Acta Biochimica Polonica

1 Cellular and Molecular Biology Letters

1 Journal of Physiology and Pharmacology. Supplement

1 Buda A.

1 Chiba P.

1 Ciarkowski J.

1 Couchman J. R.

1 Dziubinska H.

1 Ecker G. F.

1 Kaiser D.

1 Kopp S.

1 Krol E.

1 Krupa M.

1 Lee W.

1 Multhaupt H. A. B.

1 Oh E.-S.

1 Peer M.

1 Pleban K.

1 Slusarz R.

1 Stolarz M.

1 Trebacz K.

1 Whiteford J. R.

1 Yoneda A.

1 Zawadzki T.

1 2009

1 2005

1 2004

1 2002

Light and low-temperature induced transmembrane potential changes in mesophyll cells

Interaction of class A G protein-coupled receptors with G proteins

Targeting drug-efflux pumps - a pharmacoinformatic approach

Syndecan signaling: when, where and why?