SEARCH

SEARCH BY CITATION

References

  • 1
    Kitamura K, Kangawa K, Kawamoto M, Ichiki Y, Nakamura S, Matsuo H, Eto T ( 1993) Adrenomedullin: a novel hypotensive peptide isolated from human pheochromocytoma. Biochem Biophys Res Commun 192: 553560.
  • 2
    Ichikawa-Shindo Y, Sakurai T, Kamiyoshi A, Kawate H, Iinuma N, Yoshizawa T, Koyama T, Fukuchi J, Iimuro S, Moriyama N, Kawakami H, Murata T, Kangawa K, Nagai R, Shindo T ( 2008) The GPCR modulator protein RAMP2 is essential for angiogenesis and vascular integrity. J Clin Invest 118: 2939.
  • 3
    Iinuma N, Sakurai T, Kamiyoshi A, Ichikawa-Shindo Y, Arai T, Yoshizawa T, Koyama T, Uetake R, Kawate H, Muto SI, Tagawa YI, Miyagawa S, Shindo T ( 2010) Adrenomedullin in sinusoidal endothelial cells play protective roles against cold injury of liver. Peptides 31: 865871.
  • 4
    Recober A, Kuburas A, Zhang Z, Wemmie JA, Anderson MG, Russo AF ( 2009) Role of calcitonin gene-related peptide in light-aversive behavior: implications for migraine. J Neurosci 29: 87988804.
  • 5
    Fritz-Six KL, Dunworth WP, Li M, Caron KM ( 2008). Adrenomedullin signaling is necessary for murine lymphatic vascular development. J Clin Invest 118: 4050.
  • 6
    Udawela M, Christopoulos G, Tilakaratne N, Christopoulos A, Albiston A, Sexton PM ( 2006) Distinct receptor activity-modifying protein domains differentially modulate interaction with calcitonin receptors. Mol Pharmacol 69: 19841989.
  • 7
    Christopoulos A ( 2002) Allosteric binding sites on cell-surface receptors: novel targets for drug discovery. Nat Rev Drug Discov 1: 198210.
  • 8
    McLatchie LM, Fraser NJ, Main MJ, Wise A, Brown J, Thompson N, Solari R, Lee MG, Foord SM ( 1998) RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 393: 333339.
  • 9
    Hoare SR ( 2005) Mechanisms of peptide and nonpeptide ligand binding to Class B G-protein-coupled receptors. Drug Discov Today 10: 417427.
  • 10
    Parthier C, Reedtz-Runge S, Rudolph R, Stubbs MT ( 2009) Passing the baton in class B GPCRs: peptide hormone activation via helix induction? Trends Biochem Sci 34: 303310.
  • 11
    Pioszak AA, Xu HE ( 2008) Molecular recognition of parathyroid hormone by its G protein-coupled receptor. Proc Natl Acad Sci USA 105: 50345039.
  • 12
    Runge S, Thogersen H, Madsen K, Lau J, Rudolph R ( 2008) Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain. J Biol Chem
  • 13
    Parthier C, Kleinschmidt M, Neumann P, Rudolph R, Manhart S, Schlenzig D, Fanghanel J, Rahfeld JU, Demuth HU, Stubbs MT ( 2007) Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor. Proc Natl Acad Sci USA 104: 1394213947.
  • 14
    Hay DL, Poyner DR, Sexton PM ( 2006) GPCR modulation by RAMPs. Pharmacol Ther 109: 173197.
  • 15
    Walker CS, Conner AC, Poyner DR, Hay DL ( 2010) Regulation of signal transduction by calcitonin gene-related peptide receptors. Trends Pharmacol Sci 31: 476483.
  • 16
    Kusano S, Kukimoto-Niino M, Akasaka R, Toyama M, Terada T, Shirouzu M, Shindo T, Yokoyama S ( 2008) Crystal structure of the human receptor activity-modifying protein 1 extracellular domain. Protein Sci 17: 19071914.
  • 17
    ter Haar E, Koth CM, Abdul-Manan N, Swenson L, Coll JT, Lippke JA, Lepre CA, Garcia-Guzman M, Moore JM ( 2010) Crystal structure of the ectodomain complex of the CGRP receptor, a class-B GPCR, reveals the site of drug antagonism. Structure 18: 10831093.
  • 18
    Gouet P, Courcelle E, Stuart DI, Metoz F ( 1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15: 305308.
  • 19
    Thompson JD, Higgins DG, Gibson TJ ( 1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22: 46734680.
  • 20
    Flahaut M, Rossier BC, Firsov D ( 2002) Respective roles of calcitonin receptor-like receptor (CRLR) and receptor activity-modifying proteins (RAMP) in cell surface expression of CRLR/RAMP heterodimeric receptors. J Biol Chem 277: 1473114737.
  • 21
    Kamitani S, Sakata T ( 2001) Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling. Biochim Biophys Acta 1539: 131139.
  • 22
    Kuwasako K, Kitamura K, Uemura T, Nagoshi Y, Kato J, Eto T ( 2003) The function of extracellular cysteines in the human adrenomedullin receptor. Hypertens Res 26: S25S31.
  • 23
    Kuwasako K, Kitamura K, Ito K, Uemura T, Yanagita Y, Kato J, Sakata T, Eto T ( 2001) The seven amino acids of human RAMP2 (86) and RAMP3 (59) are critical for agonist binding to human adrenomedullin receptors. J Biol Chem 276: 4945949465.
  • 24
    Kuwasako K, Kitamura K, Nagata S, Kato J ( 2008) Functions of the extracellular histidine residues of receptor activity-modifying proteins vary within adrenomedullin receptors. Biochem Biophys Res Commun 377: 109113.
  • 25
    Chin JW, Cropp TA, Anderson JC, Mukherji M, Zhang Z, Schultz PG ( 2003) An expanded eukaryotic genetic code. Science 301: 964967.
  • 26
    Hino N, Okazaki Y, Kobayashi T, Hayashi A, Sakamoto K, Yokoyama S ( 2005). Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid. Nat Methods 2: 201206.
  • 27
    Dorman G, Prestwich GD ( 1994) Benzophenone photophores in biochemistry. Biochemistry 33: 56615673.
  • 28
    Sun C, Song D, Davis-Taber RA, Barrett LW, Scott VE, Richardson PL, Pereda-Lopez A, Uchic ME, Solomon LR, Lake MR, Walter KA, Hajduk PJ, Olejniczak ET ( 2007) Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS. Proc Natl Acad Sci USA 104: 78757880.
  • 29
    Pioszak AA, Parker NR, Suino-Powell K, Xu HE ( 2008) Molecular recognition of corticotropin-releasing factor by its G-protein-coupled receptor CRFR1. J Biol Chem 283: 3290032912.
  • 30
    Kigawa T, Yabuki T, Matsuda N, Matsuda T, Nakajima R, Tanaka A, Yokoyama S ( 2004) Preparation of Escherichia coli cell extract for highly productive cell-free protein expression. J Struct Funct Genomics 5: 6368.
  • 31
    Kigawa T, Matsuda T, Yabuki T, Yokoyama S, Bacterial cell-free system for highly efficient protein synthesis. In: Spirin AS and Swartz JR, Eds. ( 2007) Cell-free protein synthesis. Wiley-VCH, pp 8397.
  • 32
    Otwinowski Z, Minor W ( 1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307326.
  • 33
    Terwilliger TC, Berendzen J ( 1999) Automated MAD and MIR structure solution. Acta Cryst D55: 849861.
  • 34
    Terwilliger TC ( 2002) Automated structure solution, density modification and model building. Acta Cryst D58: 19371940.
  • 35
    Jones TA, Zou JY, Cowan SW, Kjeldgaard M ( 1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A47: 110119.
  • 36
    Emsley P, Cowtan K ( 2004) Coot: model-building tools for molecular graphics. Acta Cryst D60: 21262132.
  • 37
    Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL ( 1998) Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Cryst D54: 905921.
  • 38
    Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse-Kunstleve RW, McCoy AJ, Moriarty NW, Oeffner R, Read RJ, Richardson DC, Richardson JS, Terwilliger TC, Zwart PH ( 2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Cryst D 66: 213221.
  • 39
    Laskowski RA, MacArthur MW, Moss DS, Thornton JM ( 1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283291.