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Volumn 291, Issue 22, 2016, Pages 11657-11675

Receptor activity-modifying proteins 2 and 3 generate adrenomedullin receptor subtypes with distinct molecular properties

Author keywords

[No Author keywords available]

Indexed keywords

BINS; CARDIOVASCULAR SYSTEM; CHEMICAL ACTIVATION; CONFORMATIONS; PEPTIDES;

EID: 84971290136     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.688218     Document Type: Article
Times cited : (38)

References (79)
  • 1
    • 84885919203 scopus 로고    scopus 로고
    • Adrenomedullin in cardiovascular disease: A useful biomarker, its pathological roles and therapeutic application
    • Nishikimi, T., Kuwahara, K., Nakagawa, Y., Kangawa, K., and Nakao, K. (2013) Adrenomedullin in cardiovascular disease: a useful biomarker, its pathological roles and therapeutic application. Curr. Protein Pept. Sci. 14, 256-267
    • (2013) Curr. Protein Pept. Sci. , vol.14 , pp. 256-267
    • Nishikimi, T.1    Kuwahara, K.2    Nakagawa, Y.3    Kangawa, K.4    Nakao, K.5
  • 2
    • 84895835128 scopus 로고    scopus 로고
    • Adrenomedullin and intermedin gene transcription is increased in leukocytes of patients with chronic heart failure at different stages of the disease
    • Manuela, C., Laura, S., Benedetta, S., Raffaele, C., Alessandro, V., Chiara, C., Tommaso, P., Daniela, G., and Silvia, D. R. (2014) Adrenomedullin and intermedin gene transcription is increased in leukocytes of patients with chronic heart failure at different stages of the disease. Peptides 55, 13-16
    • (2014) Peptides , vol.55 , pp. 13-16
    • Manuela, C.1    Laura, S.2    Benedetta, S.3    Raffaele, C.4    Alessandro, V.5    Chiara, C.6    Tommaso, P.7    Daniela, G.8    Silvia, D.R.9
  • 3
    • 84879181792 scopus 로고    scopus 로고
    • Acute myocardial infarction: Clinical features and outcomes in young adults in Singapore
    • Wong, C. P., Loh, S. Y., Loh, K. K., Ong, P. J., Foo, D., and Ho, H. H. (2012) Acute myocardial infarction: clinical features and outcomes in young adults in Singapore. World J. Cardiol. 4, 206-210
    • (2012) World J. Cardiol. , vol.4 , pp. 206-210
    • Wong, C.P.1    Loh, S.Y.2    Loh, K.K.3    Ong, P.J.4    Foo, D.5    Ho, H.H.6
  • 4
    • 35848942395 scopus 로고    scopus 로고
    • Cardioprotective actions of peptide hormones in myocardial ischemia
    • Burley, D. S., Hamid, S. A., and Baxter, G. F. (2007) Cardioprotective actions of peptide hormones in myocardial ischemia. Heart Fail. Rev. 12, 279-291
    • (2007) Heart Fail. Rev. , vol.12 , pp. 279-291
    • Burley, D.S.1    Hamid, S.A.2    Baxter, G.F.3
  • 6
    • 0032765216 scopus 로고    scopus 로고
    • Bioactivity and interactions of adrenomedullin and brain natriuretic peptide in patients with heart failure
    • Lainchbury, J. G., Nicholls, M. G., Espiner, E. A., Yandle, T. G., Lewis, L. K., and Richards, A. M. (1999) Bioactivity and interactions of adrenomedullin and brain natriuretic peptide in patients with heart failure. Hypertension 34, 70-75
    • (1999) Hypertension , vol.34 , pp. 70-75
    • Lainchbury, J.G.1    Nicholls, M.G.2    Espiner, E.A.3    Yandle, T.G.4    Lewis, L.K.5    Richards, A.M.6
  • 8
    • 21744447714 scopus 로고    scopus 로고
    • Biodistribution, plasma kinetics and quantification of single-pass pulmonary clearance of adrenomedullin
    • Dupuis, J., Caron, A., and Ruël, N. (2005) Biodistribution, plasma kinetics and quantification of single-pass pulmonary clearance of adrenomedullin. Clin. Sci. 109, 97-102
    • (2005) Clin. Sci. , vol.109 , pp. 97-102
    • Dupuis, J.1    Caron, A.2    Ruël, N.3
  • 9
    • 84936802765 scopus 로고    scopus 로고
    • Bench-to-bedside pharmacology of adrenomedullin
    • Kato, J., and Kitamura, K. (2015) Bench-to-bedside pharmacology of adrenomedullin. Eur. J. Pharmacol. 764, 140-148
    • (2015) Eur. J. Pharmacol. , vol.764 , pp. 140-148
    • Kato, J.1    Kitamura, K.2
  • 10
    • 0036266044 scopus 로고    scopus 로고
    • International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors
    • Poyner, D. R., Sexton, P. M., Marshall, I., Smith, D. M., Quirion, R., Born, W., Muff, R., Fischer, J. A., and Foord, S. M. (2002) International Union of Pharmacology. XXXII. The mammalian calcitonin gene-related peptides, adrenomedullin, amylin, and calcitonin receptors. Pharmacol. Rev. 54, 233-246
    • (2002) Pharmacol. Rev. , vol.54 , pp. 233-246
    • Poyner, D.R.1    Sexton, P.M.2    Marshall, I.3    Smith, D.M.4    Quirion, R.5    Born, W.6    Muff, R.7    Fischer, J.A.8    Foord, S.M.9
  • 11
    • 33645230587 scopus 로고    scopus 로고
    • Hydrops fetalis, cardiovascular defects, and embryonic lethality in mice lacking the calcitonin receptor-like receptor gene
    • Dackor, R. T., Fritz-Six, K., Dunworth, W. P., Gibbons, C. L., Smithies, O., and Caron, K. M. (2006) Hydrops fetalis, cardiovascular defects, and embryonic lethality in mice lacking the calcitonin receptor-like receptor gene. Mol. Cell. Biol. 26, 2511-2518
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2511-2518
    • Dackor, R.T.1    Fritz-Six, K.2    Dunworth, W.P.3    Gibbons, C.L.4    Smithies, O.5    Caron, K.M.6
  • 12
    • 34547107623 scopus 로고    scopus 로고
    • Receptor activity-modifying proteins 2 and 3 have distinct physiological functions from embryogenesis to old age
    • Dackor, R., Fritz-Six, K., Smithies, O., and Caron, K. (2007) Receptor activity-modifying proteins 2 and 3 have distinct physiological functions from embryogenesis to old age. J. Biol. Chem. 282, 18094-18099
    • (2007) J. Biol. Chem. , vol.282 , pp. 18094-18099
    • Dackor, R.1    Fritz-Six, K.2    Smithies, O.3    Caron, K.4
  • 13
    • 0035895276 scopus 로고    scopus 로고
    • Extreme hydrops fetalis and cardiovascular abnormalities in mice lacking a functional adrenomedullin gene
    • Caron, K. M., and Smithies, O. (2001) Extreme hydrops fetalis and cardiovascular abnormalities in mice lacking a functional adrenomedullin gene. Proc. Natl. Acad. Sci. U.S.A. 98, 615-619
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 615-619
    • Caron, K.M.1    Smithies, O.2
  • 15
    • 73349139226 scopus 로고    scopus 로고
    • Protection of angiotensin II-induced vascular hypertrophy in vascular smooth muscle-targeted receptor activity-modifying protein 2 transgenic mice
    • Liang, L., Tam, C. W., Pozsgai, G., Siow, R., Clark, N., Keeble, J., Husmann, K., Born, W., Fischer, J. A., Poston, R., Shah, A., and Brain, S. D. (2009) Protection of angiotensin II-induced vascular hypertrophy in vascular smooth muscle-targeted receptor activity-modifying protein 2 transgenic mice. Hypertension 54, 1254-1261
    • (2009) Hypertension , vol.54 , pp. 1254-1261
    • Liang, L.1    Tam, C.W.2    Pozsgai, G.3    Siow, R.4    Clark, N.5    Keeble, J.6    Husmann, K.7    Born, W.8    Fischer, J.A.9    Poston, R.10    Shah, A.11    Brain, S.D.12
  • 16
    • 84155186325 scopus 로고    scopus 로고
    • Loss of receptor activity-modifying protein 3 exacerbates cardiac hypertrophy and transition to heart failure in a sex-dependent manner
    • Barrick, C. J., Lenhart, P. M., Dackor, R. T., Nagle, E., and Caron, K. M. (2012) Loss of receptor activity-modifying protein 3 exacerbates cardiac hypertrophy and transition to heart failure in a sex-dependent manner. J. Mol. Cell Cardiol. 52, 165-174
    • (2012) J. Mol. Cell Cardiol. , vol.52 , pp. 165-174
    • Barrick, C.J.1    Lenhart, P.M.2    Dackor, R.T.3    Nagle, E.4    Caron, K.M.5
  • 18
    • 0037445796 scopus 로고    scopus 로고
    • Altered gene expression of adrenomedullin and its receptor system and molecular forms of tissue adrenomedullin in left ventricular hypertrophy induced by malignant hypertension
    • Tadokoro, K., Nishikimi, T., Mori, Y., Wang, X., Akimoto, K., and Matsuoka, H. (2003) Altered gene expression of adrenomedullin and its receptor system and molecular forms of tissue adrenomedullin in left ventricular hypertrophy induced by malignant hypertension. Regul. Pept. 112, 71-78
    • (2003) Regul. Pept. , vol.112 , pp. 71-78
    • Tadokoro, K.1    Nishikimi, T.2    Mori, Y.3    Wang, X.4    Akimoto, K.5    Matsuoka, H.6
  • 19
    • 84884644197 scopus 로고    scopus 로고
    • Are GPCRs still a source of new targets?
    • Garland, S. L. (2013) Are GPCRs still a source of new targets? J. Biomol. Screen. 18, 947-966
    • (2013) J. Biomol. Screen. , vol.18 , pp. 947-966
    • Garland, S.L.1
  • 22
    • 84892378394 scopus 로고    scopus 로고
    • Receptor activity-modifying protein-dependent effects of mutations in the calcitonin receptor-like receptor: Implications for adrenomedullin and calcitonin gene-related peptide pharmacology
    • Watkins, H. A., Walker, C. S., Ly, K. N., Bailey, R. J., Barwell, J., Poyner, D. R., and Hay, D. L. (2014) Receptor activity-modifying protein-dependent effects of mutations in the calcitonin receptor-like receptor: implications for adrenomedullin and calcitonin gene-related peptide pharmacology. Br. J. Pharmacol. 171, 772-788
    • (2014) Br. J. Pharmacol. , vol.171 , pp. 772-788
    • Watkins, H.A.1    Walker, C.S.2    Ly, K.N.3    Bailey, R.J.4    Barwell, J.5    Poyner, D.R.6    Hay, D.L.7
  • 23
    • 84872381155 scopus 로고    scopus 로고
    • Receptor activity-modifying protein-dependent impairment of calcitonin receptor splice variant Δ(1-47)hCT (a) function
    • Qi, T., Dong, M., Watkins, H. A., Wootten, D., Miller, L. J., and Hay, D. L. (2013) Receptor activity-modifying protein-dependent impairment of calcitonin receptor splice variant Δ(1-47)hCT (a) function. Br. J. Pharmacol. 168, 644-657
    • (2013) Br. J. Pharmacol. , vol.168 , pp. 644-657
    • Qi, T.1    Dong, M.2    Watkins, H.A.3    Wootten, D.4    Miller, L.J.5    Hay, D.L.6
  • 24
    • 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., and Poyner, D. R. (2011) 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 1813, 1906-1916
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1906-1916
    • Barwell, J.1    Conner, A.2    Poyner, D.R.3
  • 25
    • 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., and Hay, D. L. (2008) Identification of N-terminal receptor activity-modifying protein residues important for calcitonin gene-related peptide, adrenomedullin, and amylin receptor function. Mol. Pharmacol. 74, 1059-1071
    • (2008) Mol. Pharmacol. , vol.74 , pp. 1059-1071
    • Qi, T.1    Christopoulos, G.2    Bailey, R.J.3    Christopoulos, A.4    Sexton, P.M.5    Hay, D.L.6
  • 27
    • 33747276441 scopus 로고    scopus 로고
    • Pharmacology of the human CGRP1 receptor in Cos 7 cells
    • Bailey, R. J., and Hay, D. L. (2006) Pharmacology of the human CGRP1 receptor in Cos 7 cells. Peptides 27, 1367-1375
    • (2006) Peptides , vol.27 , pp. 1367-1375
    • Bailey, R.J.1    Hay, D.L.2
  • 28
    • 80053599294 scopus 로고    scopus 로고
    • An improved procedure for the preparation of aminomethyl polystyrene resin and its use in solid phase (peptide) synthesis
    • Harris, P. W. R., Yang, S. H., and Brimble, M. A. (2011) An improved procedure for the preparation of aminomethyl polystyrene resin and its use in solid phase (peptide) synthesis. Tetrahedron Lett. 52, 6024-6026
    • (2011) Tetrahedron Lett. , vol.52 , pp. 6024-6026
    • Harris, P.W.R.1    Yang, S.H.2    Brimble, M.A.3
  • 29
    • 57349087747 scopus 로고    scopus 로고
    • The synthesis of phosphopeptides using microwave-assisted solid phase peptide synthesis
    • Harris, P. W. R., Williams, G. M., Shepherd, P., and Brimble, M. A. (2008) The synthesis of phosphopeptides using microwave-assisted solid phase peptide synthesis. Int. J. Pept. Res. Ther. 14, 387-392
    • (2008) Int. J. Pept. Res. Ther. , vol.14 , pp. 387-392
    • Harris, P.W.R.1    Williams, G.M.2    Shepherd, P.3    Brimble, M.A.4
  • 30
    • 84872233573 scopus 로고    scopus 로고
    • Similarity between class A and class B G-protein-coupled receptors exemplified through calcitonin gene-related peptide receptor modelling and mutagenesis studies
    • Vohra, S., Taddese, B., Conner, A. C., Poyner, D. R., Hay, D. L., Barwell, J., Reeves, P. J., Upton, G. J., and Reynolds, C. A. (2013) Similarity between class A and class B G-protein-coupled receptors exemplified through calcitonin gene-related peptide receptor modelling and mutagenesis studies. J. R. Soc. Interface 10, 20120846
    • (2013) J. R. Soc. Interface , vol.10
    • Vohra, S.1    Taddese, B.2    Conner, A.C.3    Poyner, D.R.4    Hay, D.L.5    Barwell, J.6    Reeves, P.J.7    Upton, G.J.8    Reynolds, C.9
  • 31
    • 77952581108 scopus 로고    scopus 로고
    • A key role for tryptophan 84 in receptor activity-modifying protein 1 in the amylin 1 receptor
    • Gingell, J. J., Qi, T., Bailey, R. J., and Hay, D. L. (2010) A key role for tryptophan 84 in receptor activity-modifying protein 1 in the amylin 1 receptor. Peptides 31, 1400-1404
    • (2010) Peptides , vol.31 , pp. 1400-1404
    • Gingell, J.J.1    Qi, T.2    Bailey, R.J.3    Hay, D.L.4
  • 33
    • 34347349008 scopus 로고    scopus 로고
    • Agonist-dependent consequences of proline to alanine substitution in the transmembrane helices of the calcitonin receptor
    • Bailey, R. J., and Hay, D. L. (2007) Agonist-dependent consequences of proline to alanine substitution in the transmembrane helices of the calcitonin receptor. Br. J. Pharmacol. 151, 678-687
    • (2007) Br. J. Pharmacol. , vol.151 , pp. 678-687
    • Bailey, R.J.1    Hay, D.L.2
  • 34
    • 11244331476 scopus 로고    scopus 로고
    • A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: Implications for family B G-protein-coupled receptors
    • Conner, A. C., Hay, D. L., Simms, J., Howitt, S. G., Schindler, M., Smith, D. M., Wheatley, M., and Poyner, D. R. (2005) A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors. Mol. Pharmacol. 67, 20-31
    • (2005) Mol. Pharmacol. , vol.67 , pp. 20-31
    • Conner, A.C.1    Hay, D.L.2    Simms, J.3    Howitt, S.G.4    Schindler, M.5    Smith, D.M.6    Wheatley, M.7    Poyner, D.R.8
  • 36
    • 84949115675 scopus 로고    scopus 로고
    • One motif to bind them: A small-XXX-small motif affects transmembrane domain 1 oligomerization, function, localization, and cross-talk between two yeast GPCRs
    • Lock, A., Forfar, R., Weston, C., Bowsher, L., Upton, G. J. G., Reynolds, C. A., Ladds, G., and Dixon, A. M. (2014) One motif to bind them: a small-XXX-small motif affects transmembrane domain 1 oligomerization, function, localization, and cross-talk between two yeast GPCRs. Biochim. Biophys. Acta 1838, 3036-3051
    • (2014) Biochim. Biophys. Acta , vol.1838 , pp. 3036-3051
    • Lock, A.1    Forfar, R.2    Weston, C.3    Bowsher, L.4    Upton, G.J.G.5    Reynolds, C.A.6    Ladds, G.7    Dixon, A.M.8
  • 38
    • 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., and Hay, D. L. (2012) The structure of secretin family GPCR peptide ligands: implications for receptor pharmacology and drug development. Drug Discov. Today 17, 1006-1014
    • (2012) Drug Discov. Today , vol.17 , pp. 1006-1014
    • Watkins, H.A.1    Au, M.2    Hay, D.L.3
  • 42
    • 45549086826 scopus 로고    scopus 로고
    • Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain
    • Runge, S., Thøgersen, H., Madsen, K., Lau, J., and Rudolph, R. (2008) Crystal structure of the ligand-bound glucagon-like peptide-1 receptor extracellular domain. J. Biol. Chem. 283, 11340-11347
    • (2008) J. Biol. Chem. , vol.283 , pp. 11340-11347
    • Runge, S.1    Thøgersen, H.2    Madsen, K.3    Lau, J.4    Rudolph, R.5
  • 46
    • 0027180507 scopus 로고
    • Verification of protein structures: Patterns of nonbonded atomic interactions
    • Colovos, C., and Yeates, T. O. (1993) Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci. 2, 1511-1519
    • (1993) Protein Sci. , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 49
    • 0031565726 scopus 로고    scopus 로고
    • An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • Baldwin, J. M., Schertler, G. F. X., and Unger, V. M. (1997) An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors, J. Mol. Biol. 272, 144-164
    • (1997) J. Mol. Biol. , vol.272 , pp. 144-164
    • Baldwin, J.M.1    Schertler, G.F.X.2    Unger, V.M.3
  • 52
    • 84979862178 scopus 로고    scopus 로고
    • PockDrug-Server: A new web server for predicting pocket druggability on holo and apo proteins
    • Hussein, H. A., Borrel, A., Geneix, C., Petitjean, M., Regad, L., and Camproux, A. C. (2015) PockDrug-Server: a new web server for predicting pocket druggability on holo and apo proteins. Nucleic Acids Res. 43, W436-W442
    • (2015) Nucleic Acids Res. , vol.43 , pp. W436-W442
    • Hussein, H.A.1    Borrel, A.2    Geneix, C.3    Petitjean, M.4    Regad, L.5    Camproux, A.C.6
  • 53
    • 84928681155 scopus 로고    scopus 로고
    • Pock drug: A model for predicting pocket druggability that overcomes pocket estimation uncertainties
    • Borrel, A., Regad, L., Xhaard, H., Petitjean, M., and Camproux, A. C. (2015) Pock drug: a model for predicting pocket druggability that overcomes pocket estimation uncertainties. J. Chem. Inf. Model. 55, 882-895
    • (2015) J. Chem. Inf. Model. , vol.55 , pp. 882-895
    • Borrel, A.1    Regad, L.2    Xhaard, H.3    Petitjean, M.4    Camproux, A.C.5
  • 54
    • 84865132980 scopus 로고    scopus 로고
    • DoGSite-Scorer: A web server for automatic binding site prediction, analysis and druggability assessment
    • Volkamer, A., Kuhn, D., Rippmann, F., and Rarey, M. (2012) DoGSite-Scorer: a web server for automatic binding site prediction, analysis and druggability assessment. Bioinformatics 28, 2074-2075
    • (2012) Bioinformatics , vol.28 , pp. 2074-2075
    • Volkamer, A.1    Kuhn, D.2    Rippmann, F.3    Rarey, M.4
  • 55
    • 84875533946 scopus 로고    scopus 로고
    • Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations
    • Wootten, D., Simms, J., Miller, L. J., Christopoulos, A., and Sexton, P. M. (2013) Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations. Proc. Natl. Acad. Sci. U.S.A. 110, 5211-5216
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 5211-5216
    • Wootten, D.1    Simms, J.2    Miller, L.J.3    Christopoulos, A.4    Sexton, P.M.5
  • 60
    • 71549119499 scopus 로고    scopus 로고
    • Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor
    • Harikumar, K. G., Simms, J., Christopoulos, G., Sexton, P. M., and Miller, L. J. (2009) Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor. Biochemistry 48, 11773-11785
    • (2009) Biochemistry , vol.48 , pp. 11773-11785
    • Harikumar, K.G.1    Simms, J.2    Christopoulos, G.3    Sexton, P.M.4    Miller, L.J.5
  • 61
    • 84856731249 scopus 로고    scopus 로고
    • Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) has a critical role in GLP-1 peptide binding and receptor activation
    • Koole, C., Wootten, D., Simms, J., Miller, L. J., Christopoulos, A., and Sexton, P. M. (2012) Second extracellular loop of human glucagon-like peptide-1 receptor (GLP-1R) has a critical role in GLP-1 peptide binding and receptor activation. J. Biol. Chem. 287, 3642-3658
    • (2012) J. Biol. Chem. , vol.287 , pp. 3642-3658
    • Koole, C.1    Wootten, D.2    Simms, J.3    Miller, L.J.4    Christopoulos, A.5    Sexton, P.M.6
  • 64
    • 84964961766 scopus 로고    scopus 로고
    • Calcitonin and amylin receptor peptide interaction mechanisms: Insights into peptide-binding modes and allosteric modulation of the calcitonin receptor by receptor activity-modifying proteins
    • Lee S. M., Hay, D. L., and Pioszak, A. A. (2016) Calcitonin and amylin receptor peptide interaction mechanisms: insights into peptide-binding modes and allosteric modulation of the calcitonin receptor by receptor activity-modifying proteins. J. Biol. Chem. 291, 8686-8700
    • (2016) J. Biol. Chem. , vol.291 , pp. 8686-8700
    • Lee, S.M.1    Hay, D.L.2    Pioszak, A.A.3
  • 66
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SOU, and stability analysis in CAPRI rounds 13-19
    • Kozakov, D., Hall, D. R., Beglov, D., Brenke, R., Comeau, S. R., Shen, Y., Li, K., Zheng, J., Vakili, P., Paschalidis, I. C., and Vajda, S. (2010) Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SOU, and stability analysis in CAPRI rounds 13-19. Proteins 78, 3124-3130
    • (2010) Proteins , vol.78 , pp. 3124-3130
    • Kozakov, D.1    Hall, D.R.2    Beglov, D.3    Brenke, R.4    Comeau, S.R.5    Shen, Y.6    Li, K.7    Zheng, J.8    Vakili, P.9    Paschalidis, I.C.10    Vajda, S.11
  • 67
    • 77957968798 scopus 로고    scopus 로고
    • Detection and refinement of encounter complexes for protein-protein docking: Taking account of macromolecular crowding
    • Li, X., Moal, I. H., and Bates, P. A. (2010) Detection and refinement of encounter complexes for protein-protein docking: taking account of macromolecular crowding. Proteins 78, 3189-3196
    • (2010) Proteins , vol.78 , pp. 3189-3196
    • Li, X.1    Moal, I.H.2    Bates, P.A.3
  • 68
    • 34548317146 scopus 로고    scopus 로고
    • FireDock: Fast interaction refinement in molecular docking
    • Andrusier, N., Nussinov, R., and Wolfson, H. J. (2007) FireDock: fast interaction refinement in molecular docking. Proteins 69, 139-159
    • (2007) Proteins , vol.69 , pp. 139-159
    • Andrusier, N.1    Nussinov, R.2    Wolfson, H.J.3
  • 70
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations
    • Gray, J. J., Moughon, S., Wang, C., Schueler-Furman, O., Kuhlman, B., Rohl, C. A., and Baker, D. (2003) Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations. J. Mol. Biol. 331, 281-299
    • (2003) J. Mol. Biol. , vol.331 , pp. 281-299
    • Gray, J.J.1    Moughon, S.2    Wang, C.3    Schueler-Furman, O.4    Kuhlman, B.5    Rohl, C.A.6    Baker, D.7
  • 71
    • 84971286202 scopus 로고    scopus 로고
    • Homology modeling, docking and molecular dynamics simulation of class IHDACs
    • Wang, D. F., Wiest, O. G., and Helquist, P. (2005) Homology modeling, docking and molecular dynamics simulation of class IHDACs. Abstr. Papers Am. Chem. Soc. 230, U1360-U1361
    • (2005) Abstr. Papers Am. Chem. Soc. , vol.230 , pp. U1360-U1361
    • Wang, D.F.1    Wiest, O.G.2    Helquist, P.3
  • 72
    • 33750956018 scopus 로고    scopus 로고
    • Identification of some novel AHAS inhibitors via molecular docking and virtual screening approach
    • Wang, J. G., Xiao, Y. J., Li, Y. H., Ma, Y., and Li, Z. M. (2007) Identification of some novel AHAS inhibitors via molecular docking and virtual screening approach. Bioorg. Med. Chem. 15, 374-380
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 374-380
    • Wang, J.G.1    Xiao, Y.J.2    Li, Y.H.3    Ma, Y.4    Li, Z.M.5
  • 74
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky, T. J., Czodrowski, P., Li, H., Nielsen, J. E., Jensen, J. H., Klebe, G., and Baker, N. A. (2007) PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res. 35, W522-W525
    • (2007) Nucleic Acids Res. , vol.35 , pp. W522-W525
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3    Nielsen, J.E.4    Jensen, J.H.5    Klebe, G.6    Baker, N.A.7
  • 75
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-W667
    • (2004) Nucleic Acids Res. , vol.32 , pp. W665-W667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 77
    • 0027936280 scopus 로고
    • Correlating solvation free energies and surface tensions of hydrocarbon solutes
    • discussion 404-399
    • Sitkoff, D., Sharp, K. A., and Honig, B. (1994) Correlating solvation free energies and surface tensions of hydrocarbon solutes. Biophys. Chem. 51, 397-403; discussion 404-399
    • (1994) Biophys. Chem. , vol.51 , pp. 397-403
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 78
    • 47149096704 scopus 로고    scopus 로고
    • CHARMM-GUI: A Web-based graphical user interface for CHARMM
    • Jo, S., Kim, T., Iyer, V. G., and Im W. (2008) CHARMM-GUI: a Web-based graphical user interface for CHARMM. J. Comput. Chem. 29, 1859-1865
    • (2008) J. Comput. Chem. , vol.29 , pp. 1859-1865
    • Jo, S.1    Kim, T.2    Iyer, V.G.3    Im, W.4
  • 79
    • 79955540676 scopus 로고    scopus 로고
    • Refinement of glucagon-like peptide 1 docking to its intact receptor using mid-region photolabile probes and molecular modeling
    • Miller, L. J., Chen, Q., Lam, P. C., Pinon, D. I., Sexton, P. M., Abagyan, R., and Dong, M. (2011) Refinement of glucagon-like peptide 1 docking to its intact receptor using mid-region photolabile probes and molecular modeling. J. Biol. Chem. 286, 15895-15907
    • (2011) J. Biol. Chem. , vol.286 , pp. 15895-15907
    • Miller, L.J.1    Chen, Q.2    Lam, P.C.3    Pinon, D.I.4    Sexton, P.M.5    Abagyan, R.6    Dong, M.7


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