An investigation into the origin of the biased agonism associated with the urotensin II receptor activation (926 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2015 Feb 19; 21(5): 392-399.
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Paper type: Journal Article, Abstract, Conference,
Impact factor: 1.951, 5-year impact factor: 1.707
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84923344165&partnerID=40&md5=31120d404da681a7ed9f8d483b7a88c2
Keywords: Biased Agonism, Conformation By Nmr, Docking Studies, Therapeutic Peptide, Urotensin Ii-Related Peptide, Urotensin-Ii, Dodecyl Sulfate Sodium, Protein, Unclassified Drug, Urotensin Ii Related Peptide, Urotensin Receptor, Article, Cell Proliferation, Controlled Study, Heart Contraction, Human, Molecular Docking, Nonhuman, Pathophysiology, Priority Journal, Protein Conformation, Protein Expression, Protein Structure, Proton Nuclear Magnetic Resonance, Smooth Muscle Fiber, Transcription Regulation,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy University of Naples 'Federico II' I-80131 Naples Italy
CIRPEB: Centro Interuniversitario di Ricerca sui Peptidi Bioattivi University of Naples 'Federico II', DFM-Scarl Institute of Biostructures and Bioimaging - CNR 80134 Naples Italy
References:
Not available.
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2015 Feb 19; 21(5): 392-399.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Abstract, Conference,
Impact factor: 1.951, 5-year impact factor: 1.707
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84923344165&partnerID=40&md5=31120d404da681a7ed9f8d483b7a88c2
Keywords: Biased Agonism, Conformation By Nmr, Docking Studies, Therapeutic Peptide, Urotensin Ii-Related Peptide, Urotensin-Ii, Dodecyl Sulfate Sodium, Protein, Unclassified Drug, Urotensin Ii Related Peptide, Urotensin Receptor, Article, Cell Proliferation, Controlled Study, Heart Contraction, Human, Molecular Docking, Nonhuman, Pathophysiology, Priority Journal, Protein Conformation, Protein Expression, Protein Structure, Proton Nuclear Magnetic Resonance, Smooth Muscle Fiber, Transcription Regulation,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy University of Naples 'Federico II' I-80131 Naples Italy
CIRPEB: Centro Interuniversitario di Ricerca sui Peptidi Bioattivi University of Naples 'Federico II', DFM-Scarl Institute of Biostructures and Bioimaging - CNR 80134 Naples Italy
References:
Not available.
An investigation into the origin of the biased agonism associated with the urotensin II receptor activation
The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U-II) and urotensin II-related peptide (URP). Extensive expression of the two ligands uncovers the diversified pathophysiological effects mediated by the urotensinergic system such as cardiovascular disorders, smooth muscle cell proliferation, renal disease, diabetes, and tumour growth. As newly reported, U-II and URP have distinct effects on transcriptional activity, cell proliferation, and myocardial contractile activities supporting the idea that U-II and URP interact with UTR in a distinct manner (biased agonism). To shed light on the origin of the divergent activities of the two endogenous ligands, we performed a conformational study on URP by solution NMR in sodium dodecyl sulfate micelle solution and compared the obtained NMR structure of URP with that of hU-II previously determined. Finally, we undertook docking studies between URP, hU-II, and an UT receptor model. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.
The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U-II) and urotensin II-related peptide (URP). Extensive expression of the two ligands uncovers the diversified pathophysiological effects mediated by the urotensinergic system such as cardiovascular disorders, smooth muscle cell proliferation, renal disease, diabetes, and tumour growth. As newly reported, U-II and URP have distinct effects on transcriptional activity, cell proliferation, and myocardial contractile activities supporting the idea that U-II and URP interact with UTR in a distinct manner (biased agonism). To shed light on the origin of the divergent activities of the two endogenous ligands, we performed a conformational study on URP by solution NMR in sodium dodecyl sulfate micelle solution and compared the obtained NMR structure of URP with that of hU-II previously determined. Finally, we undertook docking studies between URP, hU-II, and an UT receptor model. Copyright © 2015 European Peptide Society and John Wiley & Sons, Ltd.
An investigation into the origin of the biased agonism associated with the urotensin II receptor activation
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An investigation into the origin of the biased agonism associated with the urotensin II receptor activation
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Farina B, Sturlese M, Mascanzoni F, Caporale A, Monti A, Sorbo GD, Fattorusso R, Ruvo M, Doti N
* Binding mode of AIF(370–394) peptide to CypA: insights from NMR, label-free and molecular docking studies (2267 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2018; 475(14): 2377-2393.
Impact Factor: 4.897
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* Binding mode of AIF(370–394) peptide to CypA: insights from NMR, label-free and molecular docking studies (2267 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2018; 475(14): 2377-2393.
Impact Factor: 4.897
View Export to BibTeX Export to EndNote
1 Records (1 excluding Abstracts).
Total impact factor: 4.897 (4.897 excluding Abstracts).
Total 5 year impact factor: 4.693 (4.693 excluding Abstracts).
Total impact factor: 4.897 (4.897 excluding Abstracts).
Total 5 year impact factor: 4.693 (4.693 excluding Abstracts).
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