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The influence of modification at position 2 on the side-chain conformation in oxytocin analogs

100%
Śmiech B., Kaźmierkiewicz R., Lammek B.
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EN
The nonapeptide oxytocin (OT) is used in medicine to help begin and/or continue childbirth. Its analogs can be also used to control bleeding following fetus delivery. The main function of oxytocin is to stimulate contraction of uterus smooth muscle and the smooth muscle of mammary glands, thus regulating lactation. This paper describes theoretical simulations of the distribution of the torsional angles χ1 in the non-standard methylated phenylalanine residues of three oxytocin analogs: [(Phe)2o-Me]OT, [(Phe)2m-Me]OT, [(Phe)2p-Me]OT. The conformations of the oxytocin analogs were studied both in vacuum and in solution. We found some correlations between the biological activity of the considered peptides and the side-chain conformations of amino-acid residues 2 and 8.
2
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Elucidation of neurophysin/bioligand interactions horn rnolecular rnodeling

100%
Kaźmierkiewicz R., Czaplewski C., Ciarkowski J.
Acta Biochimica Polonica
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1997
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vol. 44
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issue 3
453-466
3
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Molecular modelling of the vasopressin V2 receptor/antagonist interactions

100%
Czaplewski C., Kaźmierkiewicz R., Ciarkowski J.
Acta Biochimica Polonica
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1998
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vol. 45
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issue 1
19-26
4
Content available remote

Design of a knowledge-based force field for off-lattice simulations of protein structure

88%
Liwo A., Ołdziej S., Kaźmierkiewicz R., Groth M., Czaplewski C.
Acta Biochimica Polonica
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1997
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vol. 44
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issue 3
527-547
5
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Molecular modelling study of the role of cholesterol in the stimulation of the oxytocin receptor.

88%
Politowska E., Kaźmierkiewicz R., Wiegand V., Fahrenholz F., Ciarkowski J.
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2001
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vol. 48
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issue 1
83-93
EN
Cholesterol, an integral component of membranes in Eucaryota, is a modifier of membrane properties. In vivo studies have demonstrated that cholesterol can also modulate activities of some G protein-coupled receptors (GPCRs), which are integral membrane proteins. This can result either from an effect of cholesterol on the membrane fluidity or from specific interactions of the membrane cholesterol with the receptor, as recently demonstrated for the cholecystokinin type β (CCKRβ) or the oxytocin receptor (OTR). Using molecular modelling, we studied conformational preferences of cholesterol and several of its analogues. Subsequently, we simulated the distributions of their preferred conformations around the surface of OTR, CCKRβ and a chimeric oxytocin/cholecystokinin receptor. Consequently, we suggest residues on the surface of OTR which are potentially significant in the OTR/cholesterol interaction.
6
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Signal transmission via G protein-coupled receptors in the light of rhodopsin structure determination.

88%
Ciarkowski J., Drabik P., Giełdoń A., Kaźmierkiewicz R., Ślusarz R.
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2001
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vol. 48
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issue 4
1203-1207
EN
G protein-coupled receptors (GPCRs) transducing diverse external signals to cells via activation of heterotrimeric GTP-binding (G) proteins, estimated to mediate actions of 60% of drugs, had been resistant to structure determination until summer 2000. The first atomic-resolution experimental structure of a GPCR, that of dark (inactive) rhodopsin, thus provides a trustworthy 3D prototype for antagonist-bound forms of this huge family of proteins. In this work, our former theoretical GPCR models are evaluated against the new experimental template. Subsequently, a working hypothesis regarding the signal transduction mechanism by GPCRs is presented.
7
Content available remote

Molecular docking-based test for affinities of two ligands toward vasopressin and oxytocin receptors.

88%
Ślusarz R., Kaźmierkiewicz R., Giełdoń A., Lammek B., Ciarkowski J.
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2001
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vol. 48
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issue 1
131-135
EN
Molecular docking simulations are now fast developing area of research. In this work we describe an effective procedure of preparation of the receptor-ligand complexes. The amino-acid residues involved in ligand binding were identified and described.
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