An investigation into the origin of the biased agonism associated with the urotensin II receptor activation (465 views)
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:
Pearson, D., Shively, J.E., Clark, B.R., Geschwind, I.I., Barkley, M., Nishioka, R.S., Bern, H.A., Urotensin II: A somatostain-like peptide in the caudal neurosecretory system of fishes (1980) Proc. Natl. Acad. Sci. U. S. A., 77, pp. 5021-502
Conlon, J.M., O'Harte, F., Smith, D.D., Tonon, M.C., Vaudry, H., Isolation and primary structure of urotensin II from the brain of a tetrapod, the frog Rana ridibunda (1992) Biochem. Biophys. Res. Commun., 188, pp. 578-583
Beauvillain, J.C., Conlon, J.M., Bern, H.A., Vaudry, H., Cloning of the cDNA encoding the urotensin II precursor in frog and human reveals intense expression of the urotensin II gene in motoneurons of the spinal cord (1998) Proc. Natl. Acad. Sci. U. S. A., 95, pp. 15803-15808
Coulouarn, Y., Jegou, S., Tostivint, H., Vaudry, H., Lihrmann, I., Cloning, sequence analysis and tissue distribution of the mouse and rat urotensin II precursors (1999) FEBS Lett., 457, pp. 28-32
Mori, M., Sugo, T., Abe, M., Shimomura, Y., Kurihara, M., Kitada, C., Kikuchi, K., Fujino, M., Urotensin II is the endogenous ligand of a G-protein coupled orphan receptor, SENR (GPR14) (1999) Biochem. Biophys. Res. Commun., 265, pp. 123-129
Elshourbagy, N.A., Douglas, S.A., Shabon, U., Harrison, S., Duddy, G., Sechler, J.L., Ao, Z., Aiyar, N.V., Molecular and pharmacological characterization of genes encoding urotensin II-related peptides and their cognate G-protein coupled receptors from the mouse and monkey (2002) Br. J. Pharmacol., 136, pp. 9-22
Ames, R.S., Sarau, H.M., Chambers, J.K., Willette, R.N., Aiyar, R.V., Romanic, A.M., Louden, C.S., Douglas, S.A., Human urotensin-II is a potent vasoconstrictor and agonist for the orphan receptor GPR14 (1999) Nature, 401, pp. 282-286
Sugo, T., Murakami, Y., Shimomura, Y., Harada, M., Abe, M., Ishibashi, Y., Kitada, C., Fujino, M., Identification of urotensin II-related peptide as the urotensin II immunoreactive molecule in the rat brain (2003) Biochem. Biophys. Res. Commun., 310, pp. 860-868
Chatenet, D., Dubessy, C., Leprince, J., Boularan, C., Carlier, L., Segalas-Milazzo, I., Guilhaudis, L., Vaudry, H., Structure-activity relationships and structural conformation of a novel urotensin II-related peptide (2004) Peptides, 25, pp. 1819-1830
Chartrel, N., Conlon, J.M., Collin, F., Braun, B., Waugh, D., Vallarino, M., Lahrichi, S.L., Vaudry, H., Urotensin II in the central nervous system of the frog Rana ridibunda: Immunohistochemical localization and biochemical characterization (1996) J. Comput. Neurol., 364, pp. 324-339
Coulouarn, Y., Fernex, C., Jegou, S., Henderson, C.E., Vaudry, H., Lihrmann, I., Specific expression of the urotensin II gene in sacral motoneurons of developing rat spinal cord (2001) Mech. Dev., 101, pp. 187-190
Pelletier, G., Lihrmann, I., Vaudry, H., Role of androgens in the regulation of urotensin II precursor mRNA expression in the rat brainstem and spinal cord (2002) Neuroscience, 115, pp. 525-532
Novellino, E., Grieco, P., Caraglia, M., Budillon, A., Franco, R., Addeo, S.R., (2008) Peptidic and Non Peptidic Ligands for Immunodetection of Urotensin-II Receptor, , PCT Int. Appl. 21 WO 2008095995
Vaudry, H., Do Rego, J.C., Le Mevel, J.C., Chatenet, D., Tostivint, H., Fournier, A., Urotensin II, from fish to human (2010) Ann. N.Y. Acad. Sci., 1200, pp. 53-66
Chatenet, D., Nguyen, T.T., Létourneau, M., Fournier, A., Update on the urotensinergic system: New trends in receptor localization, activation, and drug design (2013) Front. Endocrinol., 3, pp. 1-13
Maryanoff, E.B., Kinney, A.W., Urotensin-II receptor modulators as potential drugs (2010) J. Med. Chem., 53, pp. 2695-2708
Chatenet, D., Létourneau, M., Nguyen, Q.T., Doan, N.D., Dupuis, J., Fournier, A., Discovery of new antagonists aimed at discriminating UII and URP-mediated biological activities: Insight into UII and URP receptor activation (2013) Br. J. Pharmacol., 168, pp. 807-821
Patel, C.B., Noor, N., Rockman, H.A., Functional selectivity in adrenergic and angiotensin signaling systems (2010) Mol. Pharmacol., 78, pp. 983-992
Misika, A., Hruby, V.J., Optimization of disulfide bond formation (1994) Pol. J. Chem., 68, pp. 893-899
Hwang, T.L., Shaka, A.J., Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients (1995) J. Magn. Res., 112, pp. 275-279
Piantini, U., Sorensen, O.W., Ernst, R.R., Multiple quantum filters for elucidating NMR coupling network (1982) J. Am. Chem. Soc., 104, pp. 6800-6801
Marion, D., Wüthrich, K., Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins (1983) Biochem. Biophys. Res. Commun., 113, pp. 967-974
Braunschweiler, L., Ernst, R.R., Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy (1983) J. Magn. Reson., 53, pp. 521-528
Jenner, J., Meyer, B.H., Bachman, P., Ernst, R.R., Investigation of exchange processes by two-dimensional NMR spectroscopy (1979) J. Chem. Phys., 71, pp. 4546-4553
States, D.J., Haberkorn, R.A., Ruben, D.J., A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants (1982) J. Magn. Reson., 48, pp. 286-292
Bartels, C., Xia, T., Billeter, M., Güntert, P., Wüthrich, K., The program XEASY for computer-supported NMR spectral analysis of biological macromolecules (1995) J. Biomol. NMR, 6, pp. 1-10
Güntert, P., Mumenthaler, C., Wüthrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) J. Mol. Biol., 273, pp. 283-298
Maple, J., Dinur, U., Hagler, A.T., Derivation of force fields for molecular mechanics and dynamics from ab initio energy surface (1988) Proc. Natl. Acad. Sci. U. S. A., 85, pp. 5350-5353
Carotenuto, A., Grieco, P., Campiglia, P., Novellino, E., Rovero, P., Unraveling the active conformation of urotensin II (2004) J. Med. Chem., 47, pp. 1652-1661
Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., Ferrin, T.E., UCSF Chimera - A visualization system for exploratory research and analysis (2004) J. Comput. Chem., 25, pp. 1605-1612
Zhang, Y., I-TASSER server for protein 3D structure prediction (2008) BMC Bioinf, 9, p. 40
Kelley, L.A., Sternberg, M.J., Protein structure prediction on the Web: A case study using the Phyre server (2009) Nat. Protoc., 4, pp. 363-371
Roy, A., Kucukural, A., Zhang, Y., I-TASSER: A unified platform for automated protein structure and function prediction (2010) Nat. Protoc., 5, pp. 725-738
De Vries, S.J., Van Dijk, M., Bonvin, A., The HADDOCK web server for data-driven biomolecular docking (2010) Nat. Protoc., 5, pp. 883-897
Wassenaar, T.A., Van Dijk, M., Loureiro-Ferreira, N., Van Der Schot, G., De Vries, S.J., Schmitz, C., Van Der Zwan, J., Bonvin, A., WeNMR: Structural biology on the grid (2012) J. Grid. Comp., 10, pp. 743-767
Kinney, W.A., Almond, H.R., Qi, J., Smith, C.E., Santulli, R.J., De Garavilla, L., Andrade-Gordon, P., Maryanoff, B.E., Structure-function analysis of urotensin II and its use in the construction of a ligand-receptor working model (2002) Angew. Chem. Int. Ed., 41, pp. 2940-2944
Stewart, J.M., Young, J.D., (1984) Solid Phase Peptide Synthesis, , Pierce Chemical: Rockford, IL
Grieco, P., Carotenuto, A., Campiglia, P., Gomez-Monterrey, I., Auriemma, L., Sala, M., Marcozzi, C., Novellino, E., New insight into the binding mode of peptide ligands at urotensin-II receptor: Structure-activity relationships study on P5U and urantide (2009) J. Med. Chem., 52, pp. 3927-3940
Carotenuto, A., Auriemma, L., Merlino, F., Yousif, A.M., Marasco, D., Limatola, A., Campiglia, P., Grieco, P., Lead optimization of P5U and urantide: Discovery of novel potent ligands at the urotensin-II receptor (2014) J. Med. Chem., 57, pp. 5965-5974
Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, , John Wiley & Sons, Inc: New York
Wishart, D.S., Sykes, B.D., Richards, F.M., The chemical shift index: A fast method for the assignment of protein secondary structure through NMR spectroscopy (1992) Biochemistry, 31, pp. 1647-1651
Fenalti, G., Giguere, P.M., Katritch, V., Huang, X.P., Thompson, A.A., Cherezov, V., Roth, B.L., Stevens, R.C., Molecular control of δ-opioid receptor signalling (2014) Nature, 506, pp. 191-196
Manglik, A., Kruse, A.C., Kobilka, T.S., Thian, F.S., Mathiesen, J.M., Sunahara, R.K., Pardo, L., Granier, S., Crystal structure of the μ-opioid receptor bound to a morphinan antagonist (2012) Nature, 485, pp. 321-326
Egloff, P., Hillenbrand, M., Klenk, C., Batyuk, A., Heine, P., Balada, S., Schlinkmann, K.M., Plueckthun, A., Structure of signaling-competent neurotensin receptor 1 obtained by directed evolution in Escherichia coli (2014) Proc. Natl. Acad. Sci. U. S. A., 111, pp. E655-E662
Laskowski, R.A., Mac Arthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: A program to check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Venkatakrishnan, A.J., Deupi, X., Lebon, G., Tate, C.G., Schertler, G.F., Babu, M.M., Molecular signatures of G-protein-coupled receptors (2013) Nature, 494, pp. 185-194
Moroder, L., Romano, R., Guba, W., Mierke, D.F., Kessler, H., Delporte, C., Winand, J., Christophe, J., New evidence for a membrane bound pathway in hormone receptor binding (1993) Biochemistry, 32, pp. 13551-13559
Grieco, P., Giusti, L., Carotenuto, A., Campiglia, P., Calderone, V., Lama, T., Gomez-Monterrey, I., Novellino, E., Morphiceptin analogues containing a dipeptide mimetic structure: An investigation on the bioactive topology at the μ-receptor (2005) J. Med. Chem., 48, pp. 3153-3163
D'Addona, D., Carotenuto, A., Novellino, E., Piccand, V., Reubi, J.C., Di Cianni, A., Gori, F., Ginanneschi, M., Novel sst5-selective somatostatin dicarba-analogues: Synthesis and conformation-affinity relationships (2008) J. Med. Chem., 51, pp. 512-520
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Grieco, P., Brancaccio, D., Novellino, E., Hruby, V.J., Carotenuto, A., Conformational study on cyclic melanocortin ligands and new insight into their binding mode at the MC4 receptor (2011) Eur. J. Med. Chem., 46, pp. 3721-3733
Mollica, A., Carotenuto, A., Novellino, E., Limatola, A., Costante, R., Pinnen, F., Stefanucci, A., Hruby, V.J., Novel cyclic biphalin analogue with improved antinociceptive properties (2014) ACS Med. Chem. Lett., 5, pp. 1032-1036
Brancaccio, D., Limatola, A., Campiglia, P., Gomez-Monterrey, I., Novellino, E., Grieco, P., Carotenuto, A., Urantide conformation and interaction with the urotensin-II receptor (2014) Arch. Pharm., 347, pp. 185-192
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C.A., Motoshima, H., Fox, B.A., Le Trong, I., Miyano, M., Crystal structure of rhodopsin: A G protein-coupled receptor (2000) Science, 289, pp. 739-745
Holleran, B.J., Domazet, I., Beaulieu, M.E., Yan, L.P., Guillemette, G., Lavigne, P., Escher, E., Leduc, R., Identification of transmembrane domain 6 & 7 residues that contribute to the binding pocket of the urotensin II receptor (2009) Biochem. Pharmacol., 77, pp. 1374-1382
Sainsily, X., Cabana, J., Boulais, P.E., Holleran, B.J., Escher, E., Lavigne, P., Leduc, R., Identification of transmembrane domain 3, 4 & 5 residues that contribute to the formation of the ligand-binding pocket of the urotensin-II receptor (2013) Biochem. Pharmacol., 86, pp. 1584-1593
Boivin, S., Guilhaudis, L., Milazzo, I., Oulyadi, H., Davoust, D., Fournier, A., Characterization of urotensin-II receptor structural domains involved in the recognition of U-II, URP, and urantide (2006) Biochemistry, 45, pp. 5993-6002
Wu, B., Chien, E.Y., Mol, C.D., Fenalti, G., Liu, W., Katritch, V., Abagyan, R., Stevens, R.C., Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists (2010) Science, 330, pp. 1066-1071
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:
Pearson, D., Shively, J.E., Clark, B.R., Geschwind, I.I., Barkley, M., Nishioka, R.S., Bern, H.A., Urotensin II: A somatostain-like peptide in the caudal neurosecretory system of fishes (1980) Proc. Natl. Acad. Sci. U. S. A., 77, pp. 5021-502
Conlon, J.M., O'Harte, F., Smith, D.D., Tonon, M.C., Vaudry, H., Isolation and primary structure of urotensin II from the brain of a tetrapod, the frog Rana ridibunda (1992) Biochem. Biophys. Res. Commun., 188, pp. 578-583
Beauvillain, J.C., Conlon, J.M., Bern, H.A., Vaudry, H., Cloning of the cDNA encoding the urotensin II precursor in frog and human reveals intense expression of the urotensin II gene in motoneurons of the spinal cord (1998) Proc. Natl. Acad. Sci. U. S. A., 95, pp. 15803-15808
Coulouarn, Y., Jegou, S., Tostivint, H., Vaudry, H., Lihrmann, I., Cloning, sequence analysis and tissue distribution of the mouse and rat urotensin II precursors (1999) FEBS Lett., 457, pp. 28-32
Mori, M., Sugo, T., Abe, M., Shimomura, Y., Kurihara, M., Kitada, C., Kikuchi, K., Fujino, M., Urotensin II is the endogenous ligand of a G-protein coupled orphan receptor, SENR (GPR14) (1999) Biochem. Biophys. Res. Commun., 265, pp. 123-129
Elshourbagy, N.A., Douglas, S.A., Shabon, U., Harrison, S., Duddy, G., Sechler, J.L., Ao, Z., Aiyar, N.V., Molecular and pharmacological characterization of genes encoding urotensin II-related peptides and their cognate G-protein coupled receptors from the mouse and monkey (2002) Br. J. Pharmacol., 136, pp. 9-22
Ames, R.S., Sarau, H.M., Chambers, J.K., Willette, R.N., Aiyar, R.V., Romanic, A.M., Louden, C.S., Douglas, S.A., Human urotensin-II is a potent vasoconstrictor and agonist for the orphan receptor GPR14 (1999) Nature, 401, pp. 282-286
Sugo, T., Murakami, Y., Shimomura, Y., Harada, M., Abe, M., Ishibashi, Y., Kitada, C., Fujino, M., Identification of urotensin II-related peptide as the urotensin II immunoreactive molecule in the rat brain (2003) Biochem. Biophys. Res. Commun., 310, pp. 860-868
Chatenet, D., Dubessy, C., Leprince, J., Boularan, C., Carlier, L., Segalas-Milazzo, I., Guilhaudis, L., Vaudry, H., Structure-activity relationships and structural conformation of a novel urotensin II-related peptide (2004) Peptides, 25, pp. 1819-1830
Chartrel, N., Conlon, J.M., Collin, F., Braun, B., Waugh, D., Vallarino, M., Lahrichi, S.L., Vaudry, H., Urotensin II in the central nervous system of the frog Rana ridibunda: Immunohistochemical localization and biochemical characterization (1996) J. Comput. Neurol., 364, pp. 324-339
Coulouarn, Y., Fernex, C., Jegou, S., Henderson, C.E., Vaudry, H., Lihrmann, I., Specific expression of the urotensin II gene in sacral motoneurons of developing rat spinal cord (2001) Mech. Dev., 101, pp. 187-190
Pelletier, G., Lihrmann, I., Vaudry, H., Role of androgens in the regulation of urotensin II precursor mRNA expression in the rat brainstem and spinal cord (2002) Neuroscience, 115, pp. 525-532
Novellino, E., Grieco, P., Caraglia, M., Budillon, A., Franco, R., Addeo, S.R., (2008) Peptidic and Non Peptidic Ligands for Immunodetection of Urotensin-II Receptor, , PCT Int. Appl. 21 WO 2008095995
Vaudry, H., Do Rego, J.C., Le Mevel, J.C., Chatenet, D., Tostivint, H., Fournier, A., Urotensin II, from fish to human (2010) Ann. N.Y. Acad. Sci., 1200, pp. 53-66
Chatenet, D., Nguyen, T.T., Létourneau, M., Fournier, A., Update on the urotensinergic system: New trends in receptor localization, activation, and drug design (2013) Front. Endocrinol., 3, pp. 1-13
Maryanoff, E.B., Kinney, A.W., Urotensin-II receptor modulators as potential drugs (2010) J. Med. Chem., 53, pp. 2695-2708
Chatenet, D., Létourneau, M., Nguyen, Q.T., Doan, N.D., Dupuis, J., Fournier, A., Discovery of new antagonists aimed at discriminating UII and URP-mediated biological activities: Insight into UII and URP receptor activation (2013) Br. J. Pharmacol., 168, pp. 807-821
Patel, C.B., Noor, N., Rockman, H.A., Functional selectivity in adrenergic and angiotensin signaling systems (2010) Mol. Pharmacol., 78, pp. 983-992
Misika, A., Hruby, V.J., Optimization of disulfide bond formation (1994) Pol. J. Chem., 68, pp. 893-899
Hwang, T.L., Shaka, A.J., Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients (1995) J. Magn. Res., 112, pp. 275-279
Piantini, U., Sorensen, O.W., Ernst, R.R., Multiple quantum filters for elucidating NMR coupling network (1982) J. Am. Chem. Soc., 104, pp. 6800-6801
Marion, D., Wüthrich, K., Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins (1983) Biochem. Biophys. Res. Commun., 113, pp. 967-974
Braunschweiler, L., Ernst, R.R., Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy (1983) J. Magn. Reson., 53, pp. 521-528
Jenner, J., Meyer, B.H., Bachman, P., Ernst, R.R., Investigation of exchange processes by two-dimensional NMR spectroscopy (1979) J. Chem. Phys., 71, pp. 4546-4553
States, D.J., Haberkorn, R.A., Ruben, D.J., A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants (1982) J. Magn. Reson., 48, pp. 286-292
Bartels, C., Xia, T., Billeter, M., Güntert, P., Wüthrich, K., The program XEASY for computer-supported NMR spectral analysis of biological macromolecules (1995) J. Biomol. NMR, 6, pp. 1-10
Güntert, P., Mumenthaler, C., Wüthrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA (1997) J. Mol. Biol., 273, pp. 283-298
Maple, J., Dinur, U., Hagler, A.T., Derivation of force fields for molecular mechanics and dynamics from ab initio energy surface (1988) Proc. Natl. Acad. Sci. U. S. A., 85, pp. 5350-5353
Carotenuto, A., Grieco, P., Campiglia, P., Novellino, E., Rovero, P., Unraveling the active conformation of urotensin II (2004) J. Med. Chem., 47, pp. 1652-1661
Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., Ferrin, T.E., UCSF Chimera - A visualization system for exploratory research and analysis (2004) J. Comput. Chem., 25, pp. 1605-1612
Zhang, Y., I-TASSER server for protein 3D structure prediction (2008) BMC Bioinf, 9, p. 40
Kelley, L.A., Sternberg, M.J., Protein structure prediction on the Web: A case study using the Phyre server (2009) Nat. Protoc., 4, pp. 363-371
Roy, A., Kucukural, A., Zhang, Y., I-TASSER: A unified platform for automated protein structure and function prediction (2010) Nat. Protoc., 5, pp. 725-738
De Vries, S.J., Van Dijk, M., Bonvin, A., The HADDOCK web server for data-driven biomolecular docking (2010) Nat. Protoc., 5, pp. 883-897
Wassenaar, T.A., Van Dijk, M., Loureiro-Ferreira, N., Van Der Schot, G., De Vries, S.J., Schmitz, C., Van Der Zwan, J., Bonvin, A., WeNMR: Structural biology on the grid (2012) J. Grid. Comp., 10, pp. 743-767
Kinney, W.A., Almond, H.R., Qi, J., Smith, C.E., Santulli, R.J., De Garavilla, L., Andrade-Gordon, P., Maryanoff, B.E., Structure-function analysis of urotensin II and its use in the construction of a ligand-receptor working model (2002) Angew. Chem. Int. Ed., 41, pp. 2940-2944
Stewart, J.M., Young, J.D., (1984) Solid Phase Peptide Synthesis, , Pierce Chemical: Rockford, IL
Grieco, P., Carotenuto, A., Campiglia, P., Gomez-Monterrey, I., Auriemma, L., Sala, M., Marcozzi, C., Novellino, E., New insight into the binding mode of peptide ligands at urotensin-II receptor: Structure-activity relationships study on P5U and urantide (2009) J. Med. Chem., 52, pp. 3927-3940
Carotenuto, A., Auriemma, L., Merlino, F., Yousif, A.M., Marasco, D., Limatola, A., Campiglia, P., Grieco, P., Lead optimization of P5U and urantide: Discovery of novel potent ligands at the urotensin-II receptor (2014) J. Med. Chem., 57, pp. 5965-5974
Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, , John Wiley & Sons, Inc: New York
Wishart, D.S., Sykes, B.D., Richards, F.M., The chemical shift index: A fast method for the assignment of protein secondary structure through NMR spectroscopy (1992) Biochemistry, 31, pp. 1647-1651
Fenalti, G., Giguere, P.M., Katritch, V., Huang, X.P., Thompson, A.A., Cherezov, V., Roth, B.L., Stevens, R.C., Molecular control of δ-opioid receptor signalling (2014) Nature, 506, pp. 191-196
Manglik, A., Kruse, A.C., Kobilka, T.S., Thian, F.S., Mathiesen, J.M., Sunahara, R.K., Pardo, L., Granier, S., Crystal structure of the μ-opioid receptor bound to a morphinan antagonist (2012) Nature, 485, pp. 321-326
Egloff, P., Hillenbrand, M., Klenk, C., Batyuk, A., Heine, P., Balada, S., Schlinkmann, K.M., Plueckthun, A., Structure of signaling-competent neurotensin receptor 1 obtained by directed evolution in Escherichia coli (2014) Proc. Natl. Acad. Sci. U. S. A., 111, pp. E655-E662
Laskowski, R.A., Mac Arthur, M.W., Moss, D.S., Thornton, J.M., PROCHECK: A program to check the stereochemical quality of protein structures (1993) J. Appl. Crystallogr., 26, pp. 283-291
Venkatakrishnan, A.J., Deupi, X., Lebon, G., Tate, C.G., Schertler, G.F., Babu, M.M., Molecular signatures of G-protein-coupled receptors (2013) Nature, 494, pp. 185-194
Moroder, L., Romano, R., Guba, W., Mierke, D.F., Kessler, H., Delporte, C., Winand, J., Christophe, J., New evidence for a membrane bound pathway in hormone receptor binding (1993) Biochemistry, 32, pp. 13551-13559
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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 (1067 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 (1067 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).
465 views. Last view on Monday 27 March 2023, 16:05:27
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