메뉴 건너뛰기




Volumn 14, Issue 5, 2013, Pages 375-385

Ectodomain structures of the CGRP and AM receptors

Author keywords

Adrenomedullin; Antagonist; Calcitonin gene related peptide; Calcitonin receptor like receptor; Crystal structure; Migraine; Neovascularization; Receptor activity modifying protein

Indexed keywords

ADRENOMEDULLIN RECEPTOR; CALCITONIN GENE RELATED PEPTIDE RECEPTOR; CALCITONIN RECEPTOR LIKE RECEPTOR; CHEMOKINE RECEPTOR CXCR4; DOPAMINE RECEPTOR; DUAL SPECIFICITY PHOSPHATASE 2; GASTRIC INHIBITORY POLYPEPTIDE; GLUCAGON LIKE PEPTIDE 1; GLUCAGON RECEPTOR; HISTAMINE RECEPTOR; LIGAND; MUSCARINIC RECEPTOR; OLCEGEPANT; OPIATE RECEPTOR; RECEPTOR ACTIVITY MODIFYING PROTEIN; RECEPTOR ACTIVITY MODIFYING PROTEIN 1; RECEPTOR ACTIVITY MODIFYING PROTEIN 2; TELCAGEPANT;

EID: 84882724902     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/13892037113149990054     Document Type: Article
Times cited : (4)

References (74)
  • 1
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of G proteincoupled receptors and significance for drug discovery
    • Lagerstrom, M. C.; Schioth, H. B. Structural diversity of G proteincoupled receptors and significance for drug discovery. Nat. Rev. Drug Discov., 2008, 7(4), 339-357.
    • (2008) Nat. Rev. Drug Discov , vol.7 , Issue.4 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 2
    • 77953798683 scopus 로고    scopus 로고
    • G protein--mediated signaling: Same receptor, multiple effectors
    • Woehler A, Ponimaskin E. G. G protein--mediated signaling: same receptor, multiple effectors. Curr.Mol.Pharmacol.,2009, 2 (3):237-248.
    • (2009) Curr.Mol.Pharmacol , vol.2 , Issue.3 , pp. 237-248
    • Woehler, A.1    Ponimaskin, E.G.2
  • 3
    • 74949133915 scopus 로고    scopus 로고
    • G protein-coupled receptors: The inside story
    • Jalink K, Moolenaar W. H. G protein-coupled receptors: the inside story. Bioessays 2010, 32 (1),13-16.
    • (2010) Bioessays , vol.32 , Issue.1 , pp. 13-16
    • Jalink, K.1    Moolenaar, W.H.2
  • 4
    • 79952488185 scopus 로고    scopus 로고
    • Therapeutic potential of beta-arrestin-and G protein-biased agonists
    • Whalen E. J., Rajagopal S, Lefkowitz R. J. Therapeutic potential of beta-arrestin-and G protein-biased agonists. Trends Mol. Med.,2011, 17 (3):126-139.
    • (2011) Trends Mol. Med , vol.17 , Issue.3 , pp. 126-139
    • Whalen, E.J.1    Rajagopal, S.2    Lefkowitz, R.J.3
  • 5
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R, Lagerstrom M. C.;, Lundin L.G.; Schioth H. B. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 2003,63 (6),1256-1272.
    • (2003) Mol. Pharmacol , vol.63 , Issue.6 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 6
    • 22144448173 scopus 로고    scopus 로고
    • Expansion of the superfamily of G-protein-coupled receptors in chordates
    • Fredriksson R, Lagerstrom M.C.; Schioth, H. B. Expansion of the superfamily of G-protein-coupled receptors in chordates. Ann. N. Y.Acad. Sci., 2005,1040:89-94.
    • (2005) Ann. N. Y.Acad. Sci , vol.1040 , pp. 89-94
    • Fredriksson, R.1    Lagerstrom, M.C.2    Schioth, H.B.3
  • 7
    • 73549104285 scopus 로고    scopus 로고
    • The year in G protein-coupled receptor research
    • Millar, R.P.; Newton, C. L. The year in G protein-coupled receptor research. Mol. Endocrinol. 2010,24 (1):261-274.
    • (2010) Mol. Endocrinol , vol.24 , Issue.1 , pp. 261-274
    • Millar, R.P.1    Newton, C.L.2
  • 8
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M.; Rasmussen, S. G.; Kobilka, B. K. The structure and function of G-protein-coupled receptors. Nature, 2009, 459 (7245), 356-363.
    • (2009) Nature , vol.459 , Issue.7245 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 9
    • 84855799592 scopus 로고    scopus 로고
    • Diversity and modularity of G protein-coupled receptor structures
    • Katritch, V.; Cherezov, V.; Stevens, R. C. Diversity and modularity of G protein-coupled receptor structures. Trends Pharmacol. Sci. 2012,33 (1):17-27.
    • (2012) Trends Pharmacol. Sci , vol.33 , Issue.1 , pp. 17-27
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 21
    • 67149136711 scopus 로고    scopus 로고
    • Passing the baton in class B GPCRs: Peptide hormone activation via helix induction?
    • Parthier, C.; Reedtz-Runge, S.; Rudolph, R.; Stubbs M. T. Passing the baton in class B GPCRs: peptide hormone activation via helix induction? Trends Biochem. Sci., 2009,34 (6),303-310.
    • (2009) Trends Biochem. Sci , vol.34 , Issue.6 , pp. 303-310
    • Parthier, C.1    Reedtz-Runge, S.2    Rudolph, R.3    Stubbs, M.T.4
  • 22
    • 67349176115 scopus 로고    scopus 로고
    • Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes
    • Ahren, B. Islet G protein-coupled receptors as potential targets for treatment of type 2 diabetes. Nat. Rev. Drug Discov., 2009,8 (5),369-385.
    • (2009) Nat. Rev. Drug Discov , vol.8 , Issue.5 , pp. 369-385
    • Ahren, B.1
  • 23
    • 84865525059 scopus 로고    scopus 로고
    • The structure of secretin family GPCR peptide ligands: Implications for receptor pharmacology and drug development
    • Watkins, H. A.; Au, M.; Hay, D. L. The structure of secretin family GPCR peptide ligands: implications for receptor pharmacology and drug development. Drug Discov. Today, 2012,17 (17-18),1006-1014.
    • (2012) Drug Discov. Today , vol.17 , Issue.17-18 , pp. 1006-1014
    • Watkins, H.A.1    Au, M.2    Hay, D.L.3
  • 26
    • 42449160533 scopus 로고    scopus 로고
    • Molecular recognition of parathyroid hormone by its G protein-coupled receptor
    • Pioszak, A. A.; Xu, H. E. Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc. Natl. Acad. Sci. U. S. A., 2008,105 (13):5034-5039.
    • (2008) Proc. Natl. Acad. Sci. U. S. A , vol.105 , Issue.13 , pp. 5034-5039
    • Pioszak, A.A.1    Xu, H.E.2
  • 27
    • 57749102733 scopus 로고    scopus 로고
    • Molecular recognition of corticotropin-releasing factor by its G-proteincoupled receptor CRFR1
    • Pioszak, A. A.; Parker, N. R.; Suino-Powell, K.; Xu, H. E. Molecular recognition of corticotropin-releasing factor by its G-proteincoupled receptor CRFR1. J. Biol. Chem., 2008,283 (47),32900-32912.
    • (2008) J. Biol. Chem , vol.283 , Issue.47 , pp. 32900-32912
    • Pioszak, A.A.1    Parker, N.R.2    Suino-Powell, K.3    Xu, H.E.4
  • 28
    • 78650036810 scopus 로고    scopus 로고
    • Structural basis for hormone recognition by the Human CRFR2{alpha} G protein-coupled receptor
    • Pal, K.; Swaminathan, K.; Xu, H. E.; Pioszak, A. A. Structural basis for hormone recognition by the Human CRFR2{alpha} G protein-coupled receptor. J. Biol. Chem., 2010,285 (51):40351-40361.
    • (2010) J. Biol. Chem , vol.285 , Issue.51 , pp. 40351-40361
    • Pal, K.1    Swaminathan, K.2    Xu, H.E.3    Pioszak, A.A.4
  • 29
    • 45549086826 scopus 로고    scopus 로고
    • Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain
    • Runge, S.; Thogersen, H.; Madsen, K.; Lau, J.; Rudolph, R. Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain. J. Biol. Chem., 2008.
    • (2008) J. Biol. Chem
    • Runge, S.1    Thogersen, H.2    Madsen, K.3    Lau, J.4    Rudolph, R.5
  • 31
    • 84855822647 scopus 로고    scopus 로고
    • The family B1 GPCR: Structural aspects and interaction with accessory proteins
    • Couvineau, A.; Laburthe, M. The family B1 GPCR: structural aspects and interaction with accessory proteins. Curr. Drug. Targets, 2012,13 (1),103-115.
    • (2012) Curr. Drug. Targets , vol.13 , Issue.1 , pp. 103-115
    • Couvineau, A.1    Laburthe, M.2
  • 32
    • 84859310855 scopus 로고    scopus 로고
    • Calcitonin and calcitonin receptor-like receptors: Common themes with family B GPCRs
    • Barwell, J.; Gingell, J. J.; Watkins, H. A.; Archbold, J. K.; Poyner, D. R.; Hay, D. L. Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs? Br. J. Pharmacol., 2012,166 (1),51-65.
    • (2012) Br. J. Pharmacol , vol.166 , Issue.1 , pp. 51-65
    • Barwell, J.1    Gingell, J.J.2    Watkins, H.A.3    Archbold, J.K.4    Poyner, D.R.5    Hay, D.L.6
  • 36
    • 0036379870 scopus 로고    scopus 로고
    • Receptors for calcitonin generelated peptide, adrenomedullin, and amylin: The contributions of novel receptor-activity-modifying proteins
    • Born, W.; Fischer, J. A.; Muff, R. Receptors for calcitonin generelated peptide, adrenomedullin, and amylin: the contributions of novel receptor-activity-modifying proteins. Receptors Channels, 2002,8 (3-4),201-209.
    • (2002) Receptors Channels , vol.8 , Issue.3-4 , pp. 201-209
    • Born, W.1    Fischer, J.A.2    Muff, R.3
  • 37
    • 0033039911 scopus 로고    scopus 로고
    • Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product
    • Christopoulos, G.; Perry, K. J.; Morfis, M.; Tilakaratne, N.; Gao, Y.; Fraser, N. J.; Main, M. J.; Foord, S. M.; Sexton, P. M. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Mol. Pharmacol., 1999,56 (1),235-242.
    • (1999) Mol. Pharmacol , vol.56 , Issue.1 , pp. 235-242
    • Christopoulos, G.1    Perry, K.J.2    Morfis, M.3    Tilakaratne, N.4    Gao, Y.5    Fraser, N.J.6    Main, M.J.7    Foord, S.M.8    Sexton, P.M.9
  • 38
    • 54349103237 scopus 로고    scopus 로고
    • Receptor activitymodifying proteins differentially modulate the G protein-coupling efficiency of amylin receptors
    • Morfis, M.; Tilakaratne, N.; Furness, S. G.; Christopoulos, G.; Werry, T. D.; Christopoulos, A.; Sexton, P. M. Receptor activitymodifying proteins differentially modulate the G protein-coupling efficiency of amylin receptors. Endocrinology, 2008,149 (11),5423-5431.
    • (2008) Endocrinology , vol.149 , Issue.11 , pp. 5423-5431
    • Morfis, M.1    Tilakaratne, N.2    Furness, S.G.3    Christopoulos, G.4    Werry, T.D.5    Christopoulos, A.6    Sexton, P.M.7
  • 39
    • 52949141814 scopus 로고    scopus 로고
    • Identification of N-terminal receptor activity modifying protein residues important for calcitonin gene-related peptide, adrenomedullin, and amylin receptor function
    • Qi, T.; Christopoulos, G.; Bailey, R. J.; Christopoulos A.; Sexton, P. M.; Hay, D. L. Identification of N-terminal receptor activity modifying protein residues important for calcitonin gene-related peptide, adrenomedullin, and amylin receptor function. Mol. Pharmacol., 2008,74 (4),1059-1071.
    • (2008) Mol. Pharmacol , vol.74 , Issue.4 , pp. 1059-1071
    • Qi, T.1    Christopoulos, G.2    Bailey, R.J.3    Christopoulos, A.4    Sexton, P.M.5    Hay, D.L.6
  • 41
    • 33750307507 scopus 로고    scopus 로고
    • RAMPs: The past, present and future
    • Parameswaran, N.; Spielman, W. S. RAMPs: The past, present and future. Trends Biochem.Sci., 2006,31 (11),631-638.
    • (2006) Trends Biochem.Sci , vol.31 , Issue.11 , pp. 631-638
    • Parameswaran, N.1    Spielman, W.S.2
  • 43
    • 27844496106 scopus 로고    scopus 로고
    • Receptor-activitymodifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane
    • Bouschet, T.; Martin, S.; Henley, J. M. Receptor-activitymodifying proteins are required for forward trafficking of the calcium-sensing receptor to the plasma membrane. J. Cell Sci. 2005,118 (Pt 20),4709-4720.
    • (2005) J. Cell Sci , vol.118 , Issue.Pt 20 , pp. 4709-4720
    • Bouschet, T.1    Martin, S.2    Henley, J.M.3
  • 45
    • 80053374553 scopus 로고    scopus 로고
    • Structural insights into RAMP modification of secretin family G protein-coupled receptors: Implications for drug development
    • Archbold, J. K.; Flanagan, J. U.; Watkins, H. A.; Gingell, J. J.; Hay, D. L. Structural insights into RAMP modification of secretin family G protein-coupled receptors: implications for drug development. Trends Pharmacol. Sci., 2011,32 (10),591-600.
    • (2011) Trends Pharmacol. Sci , vol.32 , Issue.10 , pp. 591-600
    • Archbold, J.K.1    Flanagan, J.U.2    Watkins, H.A.3    Gingell, J.J.4    Hay, D.L.5
  • 48
    • 84856185720 scopus 로고    scopus 로고
    • Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding
    • Kusano, S.; Kukimoto-Niino, M.; Hino, N.; Ohsawa, N.; Okuda, K.; Sakamoto, K.; Shirouzu, M.; Shindo, T.; Yokoyama, S. Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding. Protein Sci.,2012,21 (2),199-210.
    • (2012) Protein Sci , vol.21 , Issue.2 , pp. 199-210
    • Kusano, S.1    Kukimoto-Niino, M.2    Hino, N.3    Ohsawa, N.4    Okuda, K.5    Sakamoto, K.6    Shirouzu, M.7    Shindo, T.8    Yokoyama, S.9
  • 50
    • 72749105799 scopus 로고    scopus 로고
    • Mapping interaction sites within the N-terminus of the calcitonin generelated peptide receptor; the role of residues 23-60 of the calcitonin receptor-like receptor
    • Barwell, J.; Miller, P. S.; Donnelly, D.; Poyner, D. R. Mapping interaction sites within the N-terminus of the calcitonin generelated peptide receptor; the role of residues 23-60 of the calcitonin receptor-like receptor. Peptides,2010, 31 (1),170-176.
    • (2010) Peptides , vol.31 , Issue.1 , pp. 170-176
    • Barwell, J.1    Miller, P.S.2    Donnelly, D.3    Poyner, D.R.4
  • 51
    • 0038265460 scopus 로고    scopus 로고
    • Identification of the human receptor activity-modifying protein 1 domains responsible for agonist binding specificity
    • Kuwasako, K.; Kitamura, K.; Nagoshi, Y.; Cao, Y. N.; Eto, T. Identification of the human receptor activity-modifying protein 1 domains responsible for agonist binding specificity. J. Biol. Chem., 2003,278 (25),22623-22630.
    • (2003) J. Biol. Chem , vol.278 , Issue.25 , pp. 22623-22630
    • Kuwasako, K.1    Kitamura, K.2    Nagoshi, Y.3    Cao, Y.N.4    Eto, T.5
  • 52
    • 33745700337 scopus 로고    scopus 로고
    • Characterization of the structure of RAMP1 by mutagenesis and molecular modeling
    • Simms, J.; Hay, D. L.; Wheatley, M.; Poyner, D. R. Characterization of the structure of RAMP1 by mutagenesis and molecular modeling. Biophys. J., 2006,91 (2),662-669.
    • (2006) Biophys. J , vol.91 , Issue.2 , pp. 662-669
    • Simms, J.1    Hay, D.L.2    Wheatley, M.3    Poyner, D.R.4
  • 54
    • 0037299207 scopus 로고    scopus 로고
    • The function of extracellular cysteines in the human adrenomedullin receptor
    • Kuwasako, K.; Kitamura, K.; Uemura, T.; Nagoshi, Y.; Kato, J.; Eto, T. The function of extracellular cysteines in the human adrenomedullin receptor. Hypertens. Res., 2003,26,Suppl,S25-S31.
    • (2003) Hypertens. Res , vol.26 , Issue.SUPPL.
    • Kuwasako, K.1    Kitamura, K.2    Uemura, T.3    Nagoshi, Y.4    Kato, J.5    Eto, T.6
  • 55
    • 17144382079 scopus 로고    scopus 로고
    • The Nterminal extracellular domain 23-60 of the calcitonin receptor-like receptor in chimeras with the parathyroid hormone receptor mediates association with receptor activity-modifying protein 1
    • Ittner, L. M.; Koller, D.; Muff, R.; Fischer, J. A.; Born, W. The Nterminal extracellular domain 23-60 of the calcitonin receptor-like receptor in chimeras with the parathyroid hormone receptor mediates association with receptor activity-modifying protein 1. Biochemistry, 2005,44 (15),5749-5754.
    • (2005) Biochemistry , vol.44 , Issue.15 , pp. 5749-5754
    • Ittner, L.M.1    Koller, D.2    Muff, R.3    Fischer, J.A.4    Born, W.5
  • 56
    • 0037177801 scopus 로고    scopus 로고
    • Respective roles of calcitonin receptor-like receptor (CRLR) and receptor activitymodifying proteins (RAMP) in cell surface expression of CRLR/RAMP heterodimeric receptors
    • Flahaut, M.; Rossier, B. C.; Firsov, D. Respective roles of calcitonin receptor-like receptor (CRLR) and receptor activitymodifying proteins (RAMP) in cell surface expression of CRLR/RAMP heterodimeric receptors. J. Biol. Chem.,2002, 277 (17),14731-14737.
    • (2002) J. Biol. Chem , vol.277 , Issue.17 , pp. 14731-14737
    • Flahaut, M.1    Rossier, B.C.2    Firsov, D.3
  • 57
    • 0035962927 scopus 로고    scopus 로고
    • Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling
    • Kamitani, S.; Sakata, T. Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling. Biochim. Biophys. Acta., 2001,1539 (1-2),131-139.
    • (2001) Biochim. Biophys. Acta , vol.1539 , Issue.1-2 , pp. 131-139
    • Kamitani, S.1    Sakata, T.2
  • 58
    • 54449083954 scopus 로고    scopus 로고
    • Functions of the extracellular histidine residues of receptor activity-modifying proteins vary within adrenomedullin receptors
    • Kuwasako, K.; Kitamura, K.; Nagata, S.; Kato, J. Functions of the extracellular histidine residues of receptor activity-modifying proteins vary within adrenomedullin receptors. Biochem. Biophys. Res. Commun., 2008,377 (1),109-113.
    • (2008) Biochem. Biophys. Res. Commun , vol.377 , Issue.1 , pp. 109-113
    • Kuwasako, K.1    Kitamura, K.2    Nagata, S.3    Kato, J.4
  • 59
    • 0033970471 scopus 로고    scopus 로고
    • Pharmacological profile of BIBN4096BS, the first selective small molecule CGRP antagonist
    • Doods, H.; Hallermayer, G.; Wu, D.; Entzeroth, M.; Rudolf, K.; Engel, W.; Eberlein, W. Pharmacological profile of BIBN4096BS, the first selective small molecule CGRP antagonist. Br. J. Pharmacol., 2000,129 (3),420-423.
    • (2000) Br. J. Pharmacol , vol.129 , Issue.3 , pp. 420-423
    • Doods, H.1    Hallermayer, G.2    Wu, D.3    Entzeroth, M.4    Rudolf, K.5    Engel, W.6    Eberlein, W.7
  • 60
    • 35648995321 scopus 로고    scopus 로고
    • CGRP antagonists: Unravelling the role of CGRP in migraine
    • Doods, H.; Arndt, K.; Rudolf, K.; Just, S. CGRP antagonists: unravelling the role of CGRP in migraine. Trends Pharmacol. Sci., 2007, 28 (11),580-587.
    • (2007) Trends Pharmacol. Sci , vol.28 , Issue.11 , pp. 580-587
    • Doods, H.1    Arndt, K.2    Rudolf, K.3    Just, S.4
  • 61
    • 57649233374 scopus 로고    scopus 로고
    • Efficacy and tolerability of MK-0974 (telcagepant), a new oral antagonist of calcitonin gene-related peptide receptor, compared with zolmitriptan for acute migraine: A randomised, placebo-controlled, parallel-treatment trial
    • Ho, T. W.; Ferrari, M. D.; Dodick, D. W.; Galet, V.; Kost, J.; Fan, X.; Leibensperger, H.; Froman, S.; Assaid, C.; Lines, C.; Koppen, H.; Winner, P. K. Efficacy and tolerability of MK-0974 (telcagepant), a new oral antagonist of calcitonin gene-related peptide receptor, compared with zolmitriptan for acute migraine: a randomised, placebo-controlled, parallel-treatment trial. Lancet,2008, 372 (9656):2115-2123.
    • (2008) Lancet , vol.372 , Issue.9656 , pp. 2115-2123
    • Ho, T.W.1    Ferrari, M.D.2    Dodick, D.W.3    Galet, V.4    Kost, J.5    Fan, X.6    Leibensperger, H.7    Froman, S.8    Assaid, C.9    Lines, C.10    Koppen, H.11    Winner, P.K.12
  • 62
    • 72949116357 scopus 로고    scopus 로고
    • Non-peptidic antagonists of the CGRP receptor, BIBN4096BS and MK-0974, interact with the calcitonin receptor-like receptor via methionine-42 and RAMP1 via tryptophan-74
    • Miller, P. S.; Barwell, J.; Poyner, D. R.; Wigglesworth, M. J.; Garland, S. L.; Donnelly, D. Non-peptidic antagonists of the CGRP receptor, BIBN4096BS and MK-0974, interact with the calcitonin receptor-like receptor via methionine-42 and RAMP1 via tryptophan-74. Biochem,. Biophys. Res. Commun.,2010, 391 (1),437-442.
    • (2010) Biochem,. Biophys. Res. Commun , vol.391 , Issue.1 , pp. 437-442
    • Miller, P.S.1    Barwell, J.2    Poyner, D.R.3    Wigglesworth, M.J.4    Garland, S.L.5    Donnelly, D.6
  • 64
    • 77949873859 scopus 로고    scopus 로고
    • Mapping the CGRP receptor ligand binding domain: Tryptophan-84 of RAMP1 is critical for agonist and antagonist binding
    • Moore, E. L.; Gingell, J. J.; Kane, S. A.; Hay, D. L.; Salvatore, C. A. Mapping the CGRP receptor ligand binding domain: tryptophan-84 of RAMP1 is critical for agonist and antagonist binding. Biochem. Biophys. Res. Commun., 2010, 394 (1),141-145.
    • (2010) Biochem. Biophys. Res. Commun , vol.394 , Issue.1 , pp. 141-145
    • Moore, E.L.1    Gingell, J.J.2    Kane, S.A.3    Hay, D.L.4    Salvatore, C.A.5
  • 65
    • 16244383540 scopus 로고    scopus 로고
    • Mechanisms of peptide and nonpeptide ligand binding to Class B G-protein-coupled receptors
    • Hoare, S. R. Mechanisms of peptide and nonpeptide ligand binding to Class B G-protein-coupled receptors. Drug. Discov. Today, 2005, 10 (6),417-427.
    • (2005) Drug. Discov. Today , vol.10 , Issue.6 , pp. 417-427
    • Hoare, S.R.1
  • 66
    • 45749127879 scopus 로고    scopus 로고
    • Allosteric modulators of class B G-protein-coupled receptors
    • Hoare, S. R. Allosteric modulators of class B G-protein-coupled receptors. Curr. Neuropharmacol, 2007,5 (3),168-179.
    • (2007) Curr. Neuropharmacol , vol.5 , Issue.3 , pp. 168-179
    • Hoare, S.R.1
  • 68
    • 0026034171 scopus 로고
    • Human alpha-calcitonin generelated peptide-(8-37) as an antagonist of exogenous and endogenous calcitonin gene-related peptide
    • Maggi, C. A.; Chiba, T.; Giuliani, S. Human alpha-calcitonin generelated peptide-(8-37) as an antagonist of exogenous and endogenous calcitonin gene-related peptide. Eur. J. Pharmacol., 1991,192 (1),85-88.
    • (1991) Eur. J. Pharmacol , vol.192 , Issue.1 , pp. 85-88
    • Maggi, C.A.1    Chiba, T.2    Giuliani, S.3
  • 69
    • 78951482692 scopus 로고    scopus 로고
    • Converting the highly amyloidogenic human calcitonin into a powerful fibril inhibitor by three-dimensional structure homology with a non-amyloidogenic analogue
    • Andreotti, G.; Vitale, R. M.; Avidan-Shpalter, C.; Amodeo, P.; Gazit, E.; Motta, A. Converting the highly amyloidogenic human calcitonin into a powerful fibril inhibitor by three-dimensional structure homology with a non-amyloidogenic analogue. J. Biol. Chem., 2011,286 (4),2707-2718.
    • (2011) J. Biol. Chem , vol.286 , Issue.4 , pp. 2707-2718
    • Andreotti, G.1    Vitale, R.M.2    Avidan-Shpalter, C.3    Amodeo, P.4    Gazit, E.5    Motta, A.6
  • 70
    • 80055027760 scopus 로고    scopus 로고
    • Structure of micelle-bound adrenomedullin: A first step toward the analysis of its interactions with receptors and small molecules
    • Perez-Castells, J.; Martin-Santamaria, S.; Nieto, L.; Ramos, A.; Martinez, A.; Pascual-Teresa, B.; Jimenez-Barbero, J. Structure of micelle-bound adrenomedullin: a first step toward the analysis of its interactions with receptors and small molecules. Biopolymers, 2012,97 (1),45-53.
    • (2012) Biopolymers , vol.97 , Issue.1 , pp. 45-53
    • Perez-Castells, J.1    Martin-Santamaria, S.2    Nieto, L.3    Ramos, A.4    Martinez, A.5    Pascual-Teresa, B.6    Jimenez-Barbero, J.7
  • 71
    • 80051801366 scopus 로고    scopus 로고
    • Extracellular loops 1 and 3 and their associated transmembrane regions of the calcitonin receptor-like receptor are needed for CGRP receptor function
    • Barwell, J.; Conner, A.; Poyner, D. R. Extracellular loops 1 and 3 and their associated transmembrane regions of the calcitonin receptor-like receptor are needed for CGRP receptor function. Biochim. Biophys. Acta., 2011, 1813 (10),1906-1916.
    • (2011) Biochim. Biophys. Acta , vol.1813 , Issue.10 , pp. 1906-1916
    • Barwell, J.1    Conner, A.2    Poyner, D.R.3
  • 72
    • 84859334384 scopus 로고    scopus 로고
    • The role of the extracellular loops of the CGRP receptor, a family B GPCR
    • Barwell, J.; Woolley, M. J.; Wheatley, M.; Conner, A. C.; Poyner, D. R. The role of the extracellular loops of the CGRP receptor, a family B GPCR. Biochem. Soc. Trans., 2012,40 (2),433-437.
    • (2012) Biochem. Soc. Trans , vol.40 , Issue.2 , pp. 433-437
    • Barwell, J.1    Woolley, M.J.2    Wheatley, M.3    Conner, A.C.4    Poyner, D.R.5
  • 73
    • 84859723390 scopus 로고    scopus 로고
    • The third extracellular loop of the human calcitonin receptor-like receptor is crucial for the activation of adrenomedullin signalling
    • Kuwasako, K.; Hay, D. L.; Nagata, S.; Hikosaka, T.; Kitamura, K.; Kato, J. The third extracellular loop of the human calcitonin receptor-like receptor is crucial for the activation of adrenomedullin signalling. Br. J. Pharmacol., 2012,166 (1),137-150.
    • (2012) Br. J. Pharmacol , vol.166 , Issue.1 , pp. 137-150
    • Kuwasako, K.1    Hay, D.L.2    Nagata, S.3    Hikosaka, T.4    Kitamura, K.5    Kato, J.6
  • 74
    • 77949355583 scopus 로고    scopus 로고
    • Structure-function relationships of the Nterminus of receptor activity-modifying proteins
    • Qi, T.; Hay, D. L. Structure-function relationships of the Nterminus of receptor activity-modifying proteins. Br.J. Pharmacol., 2010,159 (5),1059-1068.
    • (2010) Br.J. Pharmacol , vol.159 , Issue.5 , pp. 1059-1068
    • Qi, T.1    Hay, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.