메뉴 건너뛰기




Volumn 11, Issue 3, 2005, Pages 345-356

Computer-based strategy for modeling the interaction of AGRP and related peptide ligands with the AGRP-binding site of murine melanocortin receptors

Author keywords

AGRP; Cyclic peptide; G protein coupled receptor; Homology model; Membrane mimetic; Murine melanocortin receptors; Receptor bound conformation

Indexed keywords

AGOUTI RELATED PROTEIN; ANTIOBESITY AGENT; APPETITE STIMULANT; HISTIDINYLPHENYLALANYLARGINYLTRYPTOPHAN; MELANOCORTIN 4 RECEPTOR; MELANOCORTIN 4 RECEPTOR AGONIST; MELANOCORTIN 4 RECEPTOR ANTAGONIST; MUTANT PROTEIN; PEPTOID; UNCLASSIFIED DRUG;

EID: 14044262913     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/1381612053382188     Document Type: Review
Times cited : (6)

References (154)
  • 1
    • 0035081809 scopus 로고    scopus 로고
    • Melanocortin receptors: Their functions and regulation by physiological agonists and antagonists
    • Abdel-Malek ZA. Melanocortin receptors: their functions and regulation by physiological agonists and antagonists. Cell Mol Life Sci 2001; 58: 434-441.
    • (2001) Cell Mol. Life Sci. , vol.58 , pp. 434-441
    • Abdel-Malek, Z.A.1
  • 2
    • 0037561803 scopus 로고    scopus 로고
    • The melanocortin system and its role in obesity and cachexia
    • Goodfellow VS, Saunders, J. The melanocortin system and its role in obesity and cachexia. Curr Top Med Chem 2003; 3: 855-883.
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 855-883
    • Goodfellow, V.S.1    Saunders, J.2
  • 3
    • 0031251817 scopus 로고    scopus 로고
    • Modeling of the three-dimensional structure of the human melanocortin 1 receptor, using an automated method and docking of a rigid cyclic melanocyte-stimulating hormone core peptide
    • Prusis P, Schioth HB, Muceniece R, Herzyk P, Afshar M, Hubbard RE, et al. Modeling of the three-dimensional structure of the human melanocortin 1 receptor, using an automated method and docking of a rigid cyclic melanocyte-stimulating hormone core peptide. J Mol Graph Model 1997; 15: 307-317.
    • (1997) J. Mol. Graph. Model , vol.15 , pp. 307-317
    • Prusis, P.1    Schioth, H.B.2    Muceniece, R.3    Herzyk, P.4    Afshar, M.5    Hubbard, R.E.6
  • 5
    • 0041883731 scopus 로고    scopus 로고
    • Modeling and docking of the three-dimensional structure of the human melanocortin 4 receptor
    • Yang X, Wang Z, Dong W, Ling L, Yang H, Chen R. Modeling and docking of the three-dimensional structure of the human melanocortin 4 receptor. J Prot Chem 2003; 22: 335-344.
    • (2003) J. Prot. Chem. , vol.22 , pp. 335-344
    • Yang, X.1    Wang, Z.2    Dong, W.3    Ling, L.4    Yang, H.5    Chen, R.6
  • 7
    • 0028112970 scopus 로고
    • Agouti protein is an antagonist of the melanocyte-stimulating-hormone receptor
    • Lu DS, Willard D, Patel IR, Kadwell S, Overton L, Kost T, et al. Agouti protein is an antagonist of the melanocyte-stimulating-hormone receptor. Nature 1994; 371: 799-802.
    • (1994) Nature , vol.371 , pp. 799-802
    • Lu, D.S.1    Willard, D.2    Patel, I.R.3    Kadwell, S.4    Overton, L.5    Kost, T.6
  • 8
    • 0026731363 scopus 로고
    • Molecular cloning and expression of the human melanocyte stimulating hormone receptor cDNA
    • Chhajlani V, Wikberg JES. Molecular cloning and expression of the human melanocyte stimulating hormone receptor cDNA. FEBS Lett 1992; 309: 417-420.
    • (1992) FEBS Lett. , vol.309 , pp. 417-420
    • Chhajlani, V.1    Wikberg, J.E.S.2
  • 10
    • 0027227288 scopus 로고
    • Molecular cloning, expression, and gene localization of a 4th melanocortin receptor
    • Gantz I, Miwa H, Konda Y, Shimoto Y, Tashiro, T, Watson DJ, et al. Molecular cloning, expression, and gene localization of a 4th melanocortin receptor. J. Biol Chem 1993; 268: 15174-15179.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15174-15179
    • Gantz, I.1    Miwa, H.2    Konda, Y.3    Shimoto, Y.4    Tashiro, T.5    Watson, D.J.6
  • 12
    • 0028134706 scopus 로고
    • Localization of the melanocortin-4 receptor (MC4-R) in the neuroendocrine and autonomic control circuits in the brain
    • Mountjoy KG, Mortrud MT, Low MJ, Simerly RB, Cone RD. Localization of the melanocortin-4 receptor (MC4-R) in the neuroendocrine and autonomic control circuits in the brain. Mol Endocrinol 1994; 8: 1298-1308.
    • (1994) Mol. Endocrinol. , vol.8 , pp. 1298-1308
    • Mountjoy, K.G.1    Mortrud, M.T.2    Low, M.J.3    Simerly, R.B.4    Cone, R.D.5
  • 13
    • 0026800892 scopus 로고
    • The cloning of a family of genes that encode the melanocortin receptors
    • Mountjoy KG, Robbins LS, Mortrud MT, Cone RD. The cloning of a family of genes that encode the melanocortin receptors. Science 1992; 257: 1248-1251.
    • (1992) Science , vol.257 , pp. 1248-1251
    • Mountjoy, K.G.1    Robbins, L.S.2    Mortrud, M.T.3    Cone, R.D.4
  • 14
    • 0027436690 scopus 로고
    • Identification of a receptor for gamma-melanocortin and other proopiomelano-cortin peptides in the hypothalamus and limbic system
    • Roselli-Rehfuss L, Mountjoy KG, Robbins LS, Mortrud MT, Low MJ, Tatro JB, et al. Identification of a receptor for gamma-melanocortin and other proopiomelano-cortin peptides in the hypothalamus and limbic system. Proc Natl Acad Sci USA 1993; 90: 8856-8860.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8856-8860
    • Roselli-Rehfuss, L.1    Mountjoy, K.G.2    Robbins, L.S.3    Mortrud, M.T.4    Low, M.J.5    Tatro, J.B.6
  • 15
    • 0002293913 scopus 로고
    • Melanotropins: Structural, conformational, and biological considerations in the development of superpotent and superprolonged analogs
    • Hruby VJ, Wilkes BC, Cody WL, Sawyer TK, Hadley ME. Melanotropins: Structural, conformational, and biological considerations in the development of superpotent and superprolonged analogs. Pept Prot Rev 1984; 3: 1-64.
    • (1984) Pept. Prot. Rev. , vol.3 , pp. 1-64
    • Hruby, V.J.1    Wilkes, B.C.2    Cody, W.L.3    Sawyer, T.K.4    Hadley, M.E.5
  • 16
    • 0032230291 scopus 로고    scopus 로고
    • A ligand-mimetic model for constitutive activation of the melanocortin-1 receptor
    • Lu DS, Väge DI, Cone RD. A ligand-mimetic model for constitutive activation of the melanocortin-1 receptor. Mol Endocrinol 1998; 12: 592-604.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 592-604
    • Lu, D.S.1    Väge, D.I.2    Cone, R.D.3
  • 17
    • 0038051071 scopus 로고    scopus 로고
    • Knockout studies defining different roles for melanocortin receptors in energy homeostasis
    • Butler AA, Cone RD. Knockout studies defining different roles for melanocortin receptors in energy homeostasis. Ann NY Acad Sci 2003; 994: 240-245.
    • (2003) Ann. NY Acad. Sci. , vol.994 , pp. 240-245
    • Butler, A.A.1    Cone, R.D.2
  • 18
    • 0033818103 scopus 로고    scopus 로고
    • Inactivation of the mouse melanocortin-3 receptor results in increased fat mass and reduced lean body mass
    • Chen AS, Marsh DJ, Trumbauer ME, Frazier EG, Guan XM, Yu H, et al. Inactivation of the mouse melanocortin-3 receptor results in increased fat mass and reduced lean body mass. Nat Genet 2000; 26: 97-102.
    • (2000) Nat. Genet. , vol.26 , pp. 97-102
    • Chen, A.S.1    Marsh, D.J.2    Trumbauer, M.E.3    Frazier, E.G.4    Guan, X.M.5    Yu, H.6
  • 21
    • 0031442053 scopus 로고    scopus 로고
    • Exocrine gland dysfunction in MC5-R-deficient mice: Evidence for coordinated regulation of exocrine gland function by melanocortin peptides
    • Chen W, Kelly MA, Opitz-Araya X, Thomas RE, Low MJ, Cone RD. Exocrine gland dysfunction in MC5-R-deficient mice: Evidence for coordinated regulation of exocrine gland function by melanocortin peptides. Cell 1997; 91: 789-798.
    • (1997) Cell , vol.91 , pp. 789-798
    • Chen, W.1    Kelly, M.A.2    Opitz-Araya, X.3    Thomas, R.E.4    Low, M.J.5    Cone, R.D.6
  • 23
    • 0038381508 scopus 로고    scopus 로고
    • The role of melanocortins and their receptors in inflammatory processes, nerve regeneration and nociception
    • Starowicz K, Przewlocka B. The role of melanocortins and their receptors in inflammatory processes, nerve regeneration and nociception. Life Sci 2003; 73: 823-847.
    • (2003) Life Sci. , vol.73 , pp. 823-847
    • Starowicz, K.1    Przewlocka, B.2
  • 24
    • 0037274843 scopus 로고    scopus 로고
    • The role of melanocortin peptides and receptors in regulation of energy balance
    • Zimanyi IA, Pelleymounter MA. The role of melanocortin peptides and receptors in regulation of energy balance. Curr Pharm Des 2003; 9: 627-641.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 627-641
    • Zimanyi, I.A.1    Pelleymounter, M.A.2
  • 25
    • 0029855290 scopus 로고    scopus 로고
    • Truncation studies of alpha-melanotropin peptides identify tripeptide analogues exhibiting prolonged agonist bioactivity
    • Haskell-Luevano C, Sawyer TK, Hendrata S, North C, Panahinia L, Stum M, et al. Truncation studies of alpha-melanotropin peptides identify tripeptide analogues exhibiting prolonged agonist bioactivity. Peptides 1996; 17: 995-1002.
    • (1996) Peptides , vol.17 , pp. 995-1002
    • Haskell-Luevano, C.1    Sawyer, T.K.2    Hendrata, S.3    North, C.4    Panahinia, L.5    Stum, M.6
  • 27
    • 0344495976 scopus 로고    scopus 로고
    • Design and pharmacology of peptoids and peptide-peptoid hybrids based on the melanocortin agonists core tetrapeptide sequence
    • Holder JR, Bauzo RM, Xiang ZM, Scott J, Haskell-Luevano C. Design and pharmacology of peptoids and peptide-peptoid hybrids based on the melanocortin agonists core tetrapeptide sequence. J Med Chem 2003; 13: 4505-4509.
    • (2003) J. Med. Chem. , vol.13 , pp. 4505-4509
    • Holder, J.R.1    Bauzo, R.M.2    Xiang, Z.M.3    Scott, J.4    Haskell-Luevano, C.5
  • 28
    • 0027256438 scopus 로고
    • Cloning of the mouse agouti gene predicts a secreted protein ubiquitously expressed in mice carrying the lethal-yellow mutation
    • Miller MW, Duhl DMJ, Vrieling H, Cordes SP, Ollmann, MM, Winkes BM, et al. Cloning of the mouse agouti gene predicts a secreted protein ubiquitously expressed in mice carrying the lethal-yellow mutation. Genes Dev 1993; 7: 454-467.
    • (1993) Genes Dev. , vol.7 , pp. 454-467
    • Miller, M.W.1    Duhl, D.M.J.2    Vrieling, H.3    Cordes, S.P.4    Ollmann, M.M.5    Winkes, B.M.6
  • 29
    • 0030764741 scopus 로고    scopus 로고
    • Antagonism of central melanocortin receptors in vitro and in vivo by agouti-related protein
    • Ollmann MM, Wilson BD, Yang Y-K, Kerns JA, Chen Y, Gantz I, et al. Antagonism of central melanocortin receptors in vitro and in vivo by agouti-related protein. Science 1997; 278: 135-138.
    • (1997) Science , vol.278 , pp. 135-138
    • Ollmann, M.M.1    Wilson, B.D.2    Yang, Y.-K.3    Kerns, J.A.4    Chen, Y.5    Gantz, I.6
  • 30
    • 0141924530 scopus 로고    scopus 로고
    • The physiological function of the agouti-related peptide gene: The control of weight and metabolic rate
    • Mizuno TM, Makimura H, Mobbs CV. The physiological function of the agouti-related peptide gene: the control of weight and metabolic rate. Ann Med 2003; 35: 425-433.
    • (2003) Ann. Med. , vol.35 , pp. 425-433
    • Mizuno, T.M.1    Makimura, H.2    Mobbs, C.V.3
  • 32
    • 0034629465 scopus 로고    scopus 로고
    • Agouti and agouti-related protein: Analogies and contrasts
    • Dinulescu DM, Cone RD. Agouti and agouti-related protein: Analogies and contrasts. J Biol Chem 2000; 275: 6695-6698.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6695-6698
    • Dinulescu, D.M.1    Cone, R.D.2
  • 35
    • 0029742992 scopus 로고    scopus 로고
    • Coupled site-directed mutagenesis/transgenesis identifies important functional domains of the mouse agouti protein
    • Perry WL, Nakamura T, Swing DA, Secrest L, Eagleson B, Hustad CM, et al. Coupled site-directed mutagenesis/transgenesis identifies important functional domains of the mouse agouti protein. Genetics 1996; 144: 255-264.
    • (1996) Genetics , vol.144 , pp. 255-264
    • Perry, W.L.1    Nakamura, T.2    Swing, D.A.3    Secrest, L.4    Eagleson, B.5    Hustad, C.M.6
  • 37
    • 0029093708 scopus 로고
    • Agouti structure and function - Characterization of a potent alpha-melanocyte-stimulating hormone-receptor antagonist
    • Willard DH, Bodnar W, Harris C, Kiefer L, Nichols JS, Blanchard S, et al. Agouti structure and function - Characterization of a potent alpha-melanocyte-stimulating hormone-receptor antagonist. Biochemistry 1995; 34: 12341-12346.
    • (1995) Biochemistry , vol.34 , pp. 12341-12346
    • Willard, D.H.1    Bodnar, W.2    Harris, C.3    Kiefer, L.4    Nichols, J.S.5    Blanchard, S.6
  • 38
    • 0031042075 scopus 로고    scopus 로고
    • Mutations in the carboxyl terminus of the agouti protein decrease agouti inhibition of ligand binding to the melanocortin receptors
    • Kiefer LL, Ittoop ORR, Bunce K, Truesdale AT, Willard DH, Nichols JS, et al. Mutations in the carboxyl terminus of the agouti protein decrease agouti inhibition of ligand binding to the melanocortin receptors. Biochemistry 1997; 36: 2084-2090.
    • (1997) Biochemistry , vol.36 , pp. 2084-2090
    • Kiefer, L.L.1    Ittoop, O.R.R.2    Bunce, K.3    Truesdale, A.T.4    Willard, D.H.5    Nichols, J.S.6
  • 39
    • 0032570249 scopus 로고    scopus 로고
    • Melanocortin receptor binding determinants in the agouti protein
    • Kiefer LL, Veal JM, Mountjoy KG, Wilkison WO. Melanocortin receptor binding determinants in the agouti protein. Biochemistry 1998; 37: 991-997.
    • (1998) Biochemistry , vol.37 , pp. 991-997
    • Kiefer, L.L.1    Veal, J.M.2    Mountjoy, K.G.3    Wilkison, W.O.4
  • 40
    • 0035951058 scopus 로고    scopus 로고
    • High-resolution NMR structure of the chemically-synthesized melanocortin receptor binding domain AGRP(87-132) of the agouti-related protein
    • McNulty JC, Thompson DA, Bolin KA, Wilken J, Barsh GS, Millhauser GL. High-resolution NMR structure of the chemically-synthesized melanocortin receptor binding domain AGRP(87-132) of the agouti-related protein. Biochemistry 2001; 40: 15520-15527.
    • (2001) Biochemistry , vol.40 , pp. 15520-15527
    • McNulty, J.C.1    Thompson, D.A.2    Bolin, K.A.3    Wilken, J.4    Barsh, G.S.5    Millhauser, G.L.6
  • 41
    • 0032951699 scopus 로고    scopus 로고
    • NMR structure of a minimized human agouti-related protein prepared by chemical synthesis
    • Bolin KA, Anderson DJ, Trulson JA, Thompson DA, Wilken J, Kent SB, et al. NMR structure of a minimized human agouti-related protein prepared by chemical synthesis. FEBS Lett 1999; 451: 125-131.
    • (1999) FEBS Lett. , vol.451 , pp. 125-131
    • Bolin, K.A.1    Anderson, D.J.2    Trulson, J.A.3    Thompson, D.A.4    Wilken, J.5    Kent, S.B.6
  • 42
    • 0032169519 scopus 로고    scopus 로고
    • Determination of disulfide structure in agouti-related protein (AGRP) by stepwise reduction and alkylation
    • Bures EJ, Hui JO, Young, Y, Chow DT, Katta V, Rohde MF, et al. Determination of disulfide structure in agouti-related protein (AGRP) by stepwise reduction and alkylation. Biochemistry 1998; 37: 12172-12177.
    • (1998) Biochemistry , vol.37 , pp. 12172-12177
    • Bures, E.J.1    Hui, J.O.2    Young, Y.3    Chow, D.T.4    Katta, V.5    Rohde, M.F.6
  • 43
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik DJ, Daly NL, Waine C. The cystine knot motif in toxins and implications for drug design. Toxicon 2001; 39: 43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 46
    • 0037044844 scopus 로고    scopus 로고
    • Structure of a novel P-superfamily spasmodic conotoxin reveals an inhibitory cystine knot
    • Miles LA, Dy CY, Nielsen J, Barnham KJ, Hinds MG, Olivera BM, et al. Structure of a novel P-superfamily spasmodic conotoxin reveals an inhibitory cystine knot. J Biol Chem 2002; 277: 43033-43040.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43033-43040
    • Miles, L.A.1    Dy, C.Y.2    Nielsen, J.3    Barnham, K.J.4    Hinds, M.G.5    Olivera, B.M.6
  • 47
    • 0030467905 scopus 로고    scopus 로고
    • Three-dimensional molecular models of the hMC1R melanocortin receptor: Complexes with melanotropin peptide agonists
    • Haskell-Luevano C, Sawyer TK, Trumpp-Kallmeyer S, Bikker JA, Humblet C, Gantz I, et al. Three-dimensional molecular models of the hMC1R melanocortin receptor: complexes with melanotropin peptide agonists. Drug Des Discov 1996; 14:197-211.
    • (1996) Drug Des. Discov. , vol.14 , pp. 197-211
    • Haskell-Luevano, C.1    Sawyer, T.K.2    Trumpp-Kallmeyer, S.3    Bikker, J.A.4    Humblet, C.5    Gantz, I.6
  • 49
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • Teller DC, Okada T, Behnke CA, Palczewski K, Stenkamp RE. Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 2001; 40: 7761-7772.
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 51
    • 0037494099 scopus 로고    scopus 로고
    • The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors
    • Filipek S, Teller DC, Palczewski K, Stenkamp R. The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors. Annu Rev Biophys Biomol Struct 2003; 32: 375-397.
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 375-397
    • Filipek, S.1    Teller, D.C.2    Palczewski, K.3    Stenkamp, R.4
  • 52
    • 0034791894 scopus 로고    scopus 로고
    • Theoretical implications of receptor coupling to multiple G proteins based on analysis of a three-state model
    • Scaramellini C, Leff P. Theoretical implications of receptor coupling to multiple G proteins based on analysis of a three-state model. Methods Enzymol 2002; 343: 17-29.
    • (2002) Methods Enzymol. , vol.343 , pp. 17-29
    • Scaramellini, C.1    Leff, P.2
  • 53
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors
    • Ballesteros JA, Weinstein H. Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. Methods Neurosci 1995; 25: 366-428.
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 54
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin JM. The probable arrangement of the helices in G protein-coupled receptors. EMBO J 1993; 12: 1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 55
    • 0031565726 scopus 로고    scopus 로고
    • An alpha-carbon template for the transmembrane helices in the rhodopsin family of G protein-coupled receptors
    • Baldwin JM, Schertler GFX, Unger VM. An alpha-carbon template for the transmembrane helices in the rhodopsin family of G protein-coupled receptors. J Mol Biol 1997; 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
  • 56
    • 0032562699 scopus 로고    scopus 로고
    • Functional microdomains in G-protein-coupled receptors: The conserved arginine-cage motif in the gonadotropin-releasing hormone receptor
    • Ballesteros J, Kitanovic S, Guarnieri F, Davies P, Fromme BJ, Konvicka K, et al. Functional microdomains in G-protein-coupled receptors: The conserved arginine-cage motif in the gonadotropin-releasing hormone receptor. J Biol Chem 1998; 273: 10445-10453.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10445-10453
    • Ballesteros, J.1    Kitanovic, S.2    Guarnieri, F.3    Davies, P.4    Fromme, B.J.5    Konvicka, K.6
  • 57
    • 0037066181 scopus 로고    scopus 로고
    • Structural motifs as functional microdomains in G protein-coupled receptors: Energetic considerations in the mechanism of activation of the serotonin 5-HT2A receptor by disruption of the ionic lock of the arginine cage
    • Visiers I, Ebersole BJ, Dracheva S, Ballesteros J, Sealfon SC, Weinstein H. Structural motifs as functional microdomains in G protein-coupled receptors: Energetic considerations in the mechanism of activation of the serotonin 5-HT2A receptor by disruption of the ionic lock of the arginine cage. Int J Quantum Chem 2002; 88: 65-75,
    • (2002) Int. J. Quantum. Chem. , vol.88 , pp. 65-75
    • Visiers, I.1    Ebersole, B.J.2    Dracheva, S.3    Ballesteros, J.4    Sealfon, S.C.5    Weinstein, H.6
  • 58
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • Visiers I, Ballesteros JA, Weinstein H. Three-dimensional representations of G protein-coupled receptor structures and mechanisms. Methods Enzymol 2002; 343: 329-371.
    • (2002) Methods Enzymol. , vol.343 , pp. 329-371
    • Visiers, I.1    Ballesteros, J.A.2    Weinstein, H.3
  • 59
    • 0035933839 scopus 로고    scopus 로고
    • A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor
    • Govaerts, C, Lefort A, Costagliola S, Wodak SJ, Ballesteros JA, Van Sande J, et al. A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor. J Biol Chem 2001; 276: 22991-22999.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22991-22999
    • Govaerts, C.1    Lefort, A.2    Costagliola, S.3    Wodak, S.J.4    Ballesteros, J.A.5    Van Sande, J.6
  • 60
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the beta(2)-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • Ballesteros JA, Jensen AD, Liapakis G, Rasmussen SGF, Shi L, Gether U, et al. Activation of the beta(2)-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J Biol Chem 2001; 276: 29171-29177.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.F.4    Shi, L.5    Gether, U.6
  • 62
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros JA, Shi L, Javitch JA. Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors. Mol Pharmacol 2001; 60: 1-19.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 63
    • 0034633933 scopus 로고    scopus 로고
    • The fourth transmembrane segment of the dopamine D2 receptor: Accessibility in the binding-site crevice and position in the transmembrane bundle
    • Javitch JA, Shi L, Simpson MM, Chen J, Chiappa V, Visiers I, et al. The fourth transmembrane segment of the dopamine D2 receptor: Accessibility in the binding-site crevice and position in the transmembrane bundle. Biochemistry 2000; 39: 12190-12199.
    • (2000) Biochemistry , vol.39 , pp. 12190-12199
    • Javitch, J.A.1    Shi, L.2    Simpson, M.M.3    Chen, J.4    Chiappa, V.5    Visiers, I.6
  • 64
    • 0032221749 scopus 로고    scopus 로고
    • Recent advances in molecular dynamics simulation towards the realistic representation of biomolecules in solution
    • Brooks BR, Cheatham, TE. Recent advances in molecular dynamics simulation towards the realistic representation of biomolecules in solution. Theor Chem Acc 1998; 99: 279-288.
    • (1998) Theor. Chem. Acc. , vol.99 , pp. 279-288
    • Brooks, B.R.1    Cheatham, T.E.2
  • 65
    • 0001031179 scopus 로고
    • Proteins: A theoretical perspective of dynamics, structure and thermodynamics
    • Brooks CL III, Karplus M, Pettit BM. Proteins: A theoretical perspective of dynamics, structure and thermodynamics. Adv Chem Phys 1988; 71: 1-259.
    • (1988) Adv. Chem. Phys. , vol.71 , pp. 1-259
    • Brooks III, C.L.1    Karplus, M.2    Pettit, B.M.3
  • 67
    • 0344541116 scopus 로고    scopus 로고
    • Recent developments for the efficient crystallographic refinement of macromolecular structures
    • Brunger AT, Adams PD, Rice LM. Recent developments for the efficient crystallographic refinement of macromolecular structures. Curr Op Struct Biol 1998; 8: 600-611.
    • (1998) Curr. Op. Struct. Biol. , vol.8 , pp. 600-611
    • Brunger, A.T.1    Adams, P.D.2    Rice, L.M.3
  • 68
    • 0032504237 scopus 로고    scopus 로고
    • G protein-coupled receptors I. Diversity of receptor-ligand interactions
    • Ji TH, Grossmann M, Ji IH. G protein-coupled receptors I. Diversity of receptor-ligand interactions. J Biol Chem 1998; 273: 17299-17302.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17299-17302
    • Ji, T.H.1    Grossmann, M.2    Ji, I.H.3
  • 69
    • 0031914895 scopus 로고    scopus 로고
    • Steric hindrance mutagenesis versus alanine scan in mapping of ligand binding sites in the tachykinin NK1 receptor
    • Holst B, Zoffmann S, Elling CE, Hjorth SA, Schwartz TW. Steric hindrance mutagenesis versus alanine scan in mapping of ligand binding sites in the tachykinin NK1 receptor. Mol Pharmacol 1998; 53: 166-175.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 166-175
    • Holst, B.1    Zoffmann, S.2    Elling, C.E.3    Hjorth, S.A.4    Schwartz, T.W.5
  • 70
    • 0011073909 scopus 로고    scopus 로고
    • Extracellular domains of the bradykinin B2 receptor involved in ligand binding and agonist sensing defined by anti-peptide antibodies
    • Alla SA, Quitterer U, Grigoriev S, Maidhof A, Haasemann M, Jarnagin K, et al. Extracellular domains of the bradykinin B2 receptor involved in ligand binding and agonist sensing defined by anti-peptide antibodies. J Biol Chem 1996; 271: 1748-1755.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1748-1755
    • Alla, S.A.1    Quitterer, U.2    Grigoriev, S.3    Maidhof, A.4    Haasemann, M.5    Jarnagin, K.6
  • 71
    • 0038174859 scopus 로고    scopus 로고
    • Key issues in the computational simulation of GPCR function: Representation of loop domains
    • Mehler EL, Periole X, Hassan SA, Weinstein H. Key issues in the computational simulation of GPCR function: representation of loop domains. J Comput-Aided Mol Des 2002; 16: 841-853.
    • (2002) J. Comput-Aided Mol. Des. , vol.16 , pp. 841-853
    • Mehler, E.L.1    Periole, X.2    Hassan, S.A.3    Weinstein, H.4
  • 72
    • 0001450853 scopus 로고    scopus 로고
    • Solvation in simulated annealing and high-temperature molecular dynamics of proteins: A restrained water droplet model
    • Sankararamakrishnan R, Konvicka K, Mehler EL, Weinstein H. Solvation in simulated annealing and high-temperature molecular dynamics of proteins: A restrained water droplet model. Int J Quantum Chem 2000; 77: 174-185.
    • (2000) Int. J. Quantum. Chem. , vol.77 , pp. 174-185
    • Sankararamakrishnan, R.1    Konvicka, K.2    Mehler, E.L.3    Weinstein, H.4
  • 75
    • 0037036419 scopus 로고    scopus 로고
    • Molecular determinants of human melanocortin-4 receptor responsible for antagonist SHU9119 selectivity
    • Yang YK, Chen M, Lai, YM, Gantz I, Georgeson KE, Harmon CM. Molecular determinants of human melanocortin-4 receptor responsible for antagonist SHU9119 selectivity. J Biol Chem 2002; 277: 20328-20335.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20328-20335
    • Yang, Y.K.1    Chen, M.2    Lai, Y.M.3    Gantz, I.4    Georgeson, K.E.5    Harmon, C.M.6
  • 76
    • 0035918601 scopus 로고    scopus 로고
    • Structure activity studies of the melanocortin-4 receptor by in vitro mutagenesis: Identification of agouti-related protein (AGRP), melanocortin agonist and synthetic peptide antagonist interaction determinants
    • Haskell-Luevano C, Cone RD, Monck EK, Wan Y-P. Structure activity studies of the melanocortin-4 receptor by in vitro mutagenesis: Identification of agouti-related protein (AGRP), melanocortin agonist and synthetic peptide antagonist interaction determinants. Biochemistry 2001; 40: 6164-6179.
    • (2001) Biochemistry , vol.40 , pp. 6164-6179
    • Haskell-Luevano, C.1    Cone, R.D.2    Monck, E.K.3    Wan, Y.-P.4
  • 77
    • 0034610311 scopus 로고    scopus 로고
    • Molecular determinants of ligand binding to the human melanocortin-4 receptor
    • Yang YK, Fong TM, Dickinson CJ, Mao C, Li JY, Tota MR, et al. Molecular determinants of ligand binding to the human melanocortin-4 receptor. Biochemistry 2000; 39: 14900-14911.
    • (2000) Biochemistry , vol.39 , pp. 14900-14911
    • Yang, Y.K.1    Fong, T.M.2    Dickinson, C.J.3    Mao, C.4    Li, J.Y.5    Tota, M.R.6
  • 78
    • 0030761093 scopus 로고    scopus 로고
    • Molecular basis for the interaction of [Nle(4), D-Phe(7)]melanocyte-stimulating hormone with the melanocortin-1 receptor (melanocyte alpha-MSH receptor)
    • Yang YK, Dickinson C, Haskell-Luevano C, Gantz I. Molecular basis for the interaction of [Nle(4), D-Phe(7)]melanocyte-stimulating hormone with the melanocortin-1 receptor (melanocyte alpha-MSH receptor). J Biol Chem 1997; 272: 23000-23010.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23000-23010
    • Yang, Y.K.1    Dickinson, C.2    Haskell-Luevano, C.3    Gantz, I.4
  • 79
    • 0029880599 scopus 로고    scopus 로고
    • Identification of ligand binding residues in extracellular loops of the melanocortin 1 receptor
    • Chhajlani V, Xu X, Blauw J, Sudarshi S. Identification of ligand binding residues in extracellular loops of the melanocortin 1 receptor. Biochem Biophys Res Commun 1996; 219: 521-525.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 521-525
    • Chhajlani, V.1    Xu, X.2    Blauw, J.3    Sudarshi, S.4
  • 80
    • 0030600559 scopus 로고    scopus 로고
    • Evidence indicating that the TM4, EL2, and TM5 of the melanocortin-3 receptor do not participate in ligand binding
    • Schioth HB, Muceniece R, Szardenings M, Prusis P, Wikberg JES. Evidence indicating that the TM4, EL2, and TM5 of the melanocortin-3 receptor do not participate in ligand binding. Biochem Biophys Res Commun 1996; 229: 687-692.
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 687-692
    • Schioth, H.B.1    Muceniece, R.2    Szardenings, M.3    Prusis, P.4    Wikberg, J.E.S.5
  • 81
    • 0038237053 scopus 로고    scopus 로고
    • Molecular determination of agouti-related protein binding to human melanocortin-4 receptor
    • Yang Y, Chen M, Lai YM, Gantz I, Yagmurlu A, Georgeson KE, et al. Molecular determination of agouti-related protein binding to human melanocortin-4 receptor. Mol Pharmacol 2003; 64: 94-103.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 94-103
    • Yang, Y.1    Chen, M.2    Lai, Y.M.3    Gantz, I.4    Yagmurlu, A.5    Georgeson, K.E.6
  • 82
  • 83
    • 0037129927 scopus 로고    scopus 로고
    • Design, pharmacology, and NMR structure of a minimized cystine knot with agouti-related protein activity
    • Jackson PJ, McNulty JC, Yang YK, Thompson DA, Chai BX, Gantz I, et al. Design, pharmacology, and NMR structure of a minimized cystine knot with agouti-related protein activity. Biochemistry 2002; 41: 7565-7572.
    • (2002) Biochemistry , vol.41 , pp. 7565-7572
    • Jackson, P.J.1    McNulty, J.C.2    Yang, Y.K.3    Thompson, D.A.4    Chai, B.X.5    Gantz, I.6
  • 85
    • 0033579822 scopus 로고    scopus 로고
    • Molecular interaction of agouti and agouti-related protein with human melanocortin receptors
    • Tota MR, Smith TS, Mao C, MacNeil T, Mosley RT, Van der Ploeg LHT, et al. Molecular interaction of agouti and agouti-related protein with human melanocortin receptors. Biochemistry 1999; 38: 897-904.
    • (1999) Biochemistry , vol.38 , pp. 897-904
    • Tota, M.R.1    Smith, T.S.2    Mao, C.3    MacNeil, T.4    Mosley, R.T.5    Van der Ploeg, L.H.T.6
  • 86
    • 0027416441 scopus 로고
    • Signal transduction by a 5-HT2 receptor: A mechanistic hypothesis from molecular dynamics simulations of the three-dimensional model of the receptor complexed to ligands
    • Zhang DQ, Weinstein H. Signal transduction by a 5-HT2 receptor: A mechanistic hypothesis from molecular dynamics simulations of the three-dimensional model of the receptor complexed to ligands. J Med Chem 1993; 36: 934-938.
    • (1993) J. Med. Chem. , vol.36 , pp. 934-938
    • Zhang, D.Q.1    Weinstein, H.2
  • 87
    • 0035117505 scopus 로고    scopus 로고
    • Insights into G protein-coupled receptor function using molecular models
    • Gershengorn M, Osman R. Insights into G protein-coupled receptor function using molecular models. Endocrinology 2001; 142: 2-10.
    • (2001) Endocrinology , vol.142 , pp. 2-10
    • Gershengorn, M.1    Osman, R.2
  • 88
    • 0032541084 scopus 로고    scopus 로고
    • G protein-coupled receptors. II Mechanism of agonist activation
    • Gether U, Kobilka BK. G protein-coupled receptors. II Mechanism of agonist activation. J Biol Chem 1998; 273: 17979-17982.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17979-17982
    • Gether, U.1    Kobilka, B.K.2
  • 89
    • 0031018485 scopus 로고    scopus 로고
    • Structural instability of a constitutively active G protein-coupled receptor: Agonist-independent activation due to conformational flexibility
    • Gether U, Ballesteros JA, Seifert R, Sanders-Bush E, Weinstein H, Kobilka BK. Structural instability of a constitutively active G protein-coupled receptor: Agonist-independent activation due to conformational flexibility. J Biol Chem 1997; 272: 2587-2590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2587-2590
    • Gether, U.1    Ballesteros, J.A.2    Seifert, R.3    Sanders-Bush, E.4    Weinstein, H.5    Kobilka, B.K.6
  • 90
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the beta(2)-adrenoceptor
    • Gether U, Lin S, Ghanouni P, Ballesteros JA, Weinstein H, Kobilka BK. Agonists induce conformational changes in transmembrane domains III and VI of the beta(2)-adrenoceptor. EMBO J 1997; 16: 6737-6747.
    • (1997) EMBO J. , vol.16 , pp. 6737-6747
    • Gether, U.1    Lin, S.2    Ghanouni, P.3    Ballesteros, J.A.4    Weinstein, H.5    Kobilka, B.K.6
  • 91
    • 11144358080 scopus 로고    scopus 로고
    • Identification of putative agouti-related protein (87-132)/melanocortin-4 receptor interactions by homology molecular modeling and validation using chimeric peptide ligands
    • Wilczynski A, Wang XS, Joseph CG, Xiang Z, Bauzo RM, Scott JW, et al. Identification of putative agouti-related protein (87-132)/melanocortin-4 receptor interactions by homology molecular modeling and validation using chimeric peptide ligands. J Med Chem 2004; 47: 2194-2207.
    • (2004) J. Med. Chem. , vol.47 , pp. 2194-2207
    • Wilczynski, A.1    Wang, X.S.2    Joseph, C.G.3    Xiang, Z.4    Bauzo, R.M.5    Scott, J.W.6
  • 96
    • 0042626159 scopus 로고    scopus 로고
    • Structure of gramicidin A in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data
    • Allen TW, Anderson OS, Roux B. Structure of gramicidin A in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data. J Am Chem Soc 2003; 125: 9868-9877.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9868-9877
    • Allen, T.W.1    Anderson, O.S.2    Roux, B.3
  • 97
    • 0037168078 scopus 로고    scopus 로고
    • Kappa-opioid receptor model in a phospholipid bilayer: Molecular dynamics simulations
    • Iadanza M, Holtje M, Ronsisvalle G, Holtje HD. Kappa-opioid receptor model in a phospholipid bilayer: Molecular dynamics simulations. J Med Chem 2002; 45: 4838-4846.
    • (2002) J. Med. Chem. , vol.45 , pp. 4838-4846
    • Iadanza, M.1    Holtje, M.2    Ronsisvalle, G.3    Holtje, H.D.4
  • 98
    • 0347946756 scopus 로고    scopus 로고
    • Theory and simulation of water permeation in aquaporin-1
    • Zhu FQ, Tajkhorshid E, Schulten K. Theory and simulation of water permeation in aquaporin-1. Biophys J 2004; 86: 50-57.
    • (2004) Biophys. J. , vol.86 , pp. 50-57
    • Zhu, F.Q.1    Tajkhorshid, E.2    Schulten, K.3
  • 99
    • 0242269040 scopus 로고    scopus 로고
    • Electrostatic tuning of permeation and selectivity in aquaporin water channels
    • Jensen MO, Tajkhorshid E, Schulten K. Electrostatic tuning of permeation and selectivity in aquaporin water channels. Biophys J 2003; 85: 2884-2889.
    • (2003) Biophys. J. , vol.85 , pp. 2884-2889
    • Jensen, M.O.1    Tajkhorshid, E.2    Schulten, K.3
  • 100
    • 0344825877 scopus 로고    scopus 로고
    • What really prevents proton transport through aquaporin? Charge self-energy versus proton wire proposals
    • Burykin A, Warshel A. What really prevents proton transport through aquaporin? Charge self-energy versus proton wire proposals. Biophys J 2003; 85: 3696-3706.
    • (2003) Biophys. J. , vol.85 , pp. 3696-3706
    • Burykin, A.1    Warshel, A.2
  • 101
    • 0141534474 scopus 로고    scopus 로고
    • The mechanism of proton exclusion in the aquaporin-1 water channel
    • de Groot BL, Frigato T, Helms, V, Grubmuller H. The mechanism of proton exclusion in the aquaporin-1 water channel. J Mol Biol 2003; 333: 279-293.
    • (2003) J. Mol. Biol. , vol.333 , pp. 279-293
    • de Groot, B.L.1    Frigato, T.2    Helms, V.3    Grubmuller, H.4
  • 102
    • 0038514127 scopus 로고    scopus 로고
    • Simulation of pore formation in lipid bilayers by mechanical stress and electric fields
    • Tieleman DP, Leontiadou H, Mark AE, Marrink SJ. Simulation of pore formation in lipid bilayers by mechanical stress and electric fields. J Am Chem Soc 2003; 125: 6382-6383.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6382-6383
    • Tieleman, D.P.1    Leontiadou, H.2    Mark, A.E.3    Marrink, S.J.4
  • 103
    • 12244294449 scopus 로고    scopus 로고
    • Pores formed by the nicotinic receptor M2 delta peptide: A molecular dynamics simulation study
    • Law RJ, Tieleman DP, Sansom MSP. Pores formed by the nicotinic receptor M2 delta peptide: A molecular dynamics simulation study. Biophys J 2003; 84: 14-27.
    • (2003) Biophys. J. , vol.84 , pp. 14-27
    • Law, R.J.1    Tieleman, D.P.2    Sansom, M.S.P.3
  • 104
    • 0043167827 scopus 로고    scopus 로고
    • Molecular dynamics simulations of pentapeptides at interfaces: Salt bridge and cation-pi interactions
    • Aliste MP, MacCullum JL, Tieleman DP. Molecular dynamics simulations of pentapeptides at interfaces: Salt bridge and cation-pi interactions. Biochemistry 2003; 42: 8976-8987.
    • (2003) Biochemistry , vol.42 , pp. 8976-8987
    • Aliste, M.P.1    MacCullum, J.L.2    Tieleman, D.P.3
  • 105
    • 0036841535 scopus 로고    scopus 로고
    • Molecular dynamics simulation of spontaneous membrane fusion during a cubic-hexagonal phase transition
    • Marrinck SJ, Tieleman DP. Molecular dynamics simulation of spontaneous membrane fusion during a cubic-hexagonal phase transition. Biophys J 2002; 83: 2386-2392.
    • (2002) Biophys. J. , vol.83 , pp. 2386-2392
    • Marrinck, S.J.1    Tieleman, D.P.2
  • 106
    • 0036841855 scopus 로고    scopus 로고
    • Analysis and evaluation of channel models: Simulations of alamethicin
    • Tieleman DP, Hess B, Sansom MSP. Analysis and evaluation of channel models: Simulations of alamethicin. Biophys J 2002; 83: 2393-2407.
    • (2002) Biophys. J. , vol.83 , pp. 2393-2407
    • Tieleman, D.P.1    Hess, B.2    Sansom, M.S.P.3
  • 107
    • 0034499269 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the kinetics of spontaneous micelle formation
    • Marrinck SJ, Tieleman DP, Mark AE. Molecular dynamics simulation of the kinetics of spontaneous micelle formation. J Phys Chem B 2000; 104: 12165-12173.
    • (2000) J. Phys. Chem. B. , vol.104 , pp. 12165-12173
    • Marrinck, S.J.1    Tieleman, D.P.2    Mark, A.E.3
  • 108
    • 0032534843 scopus 로고    scopus 로고
    • Lipid properties and the orientation of aromatic residues in OmpF, influenza M2, and alamethicin systems: Molecular dynamics simulations
    • Tieleman DP, Forrest LR, Sansom MSP, Berendsen HJC. Lipid properties and the orientation of aromatic residues in OmpF, influenza M2, and alamethicin systems: Molecular dynamics simulations. Biochemistry 1998; 37: 17554-17561.
    • (1998) Biochemistry , vol.37 , pp. 17554-17561
    • Tieleman, D.P.1    Forrest, L.R.2    Sansom, M.S.P.3    Berendsen, H.J.C.4
  • 109
    • 0031438285 scopus 로고    scopus 로고
    • A computer perspective of membranes: Molecular dynamics studies of lipid bilayer systems
    • Tieleman DP, Marrinck SJ, Berendsen HJC. A computer perspective of membranes: Molecular dynamics studies of lipid bilayer systems. Biochim Biophys Acta 1997; 1331: 235-270.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 235-270
    • Tieleman, D.P.1    Marrinck, S.J.2    Berendsen, H.J.C.3
  • 110
    • 0034950310 scopus 로고    scopus 로고
    • Lipid-mediated interactions between intrinsic membrane proteins: Dependence on protein size and lipid composition
    • Lague P, Zuckermann MJ, Roux B. Lipid-mediated interactions between intrinsic membrane proteins: Dependence on protein size and lipid composition. Biophys J 2001; 81: 276-284.
    • (2001) Biophys. J. , vol.81 , pp. 276-284
    • Lague, P.1    Zuckermann, M.J.2    Roux, B.3
  • 111
    • 0037132616 scopus 로고    scopus 로고
    • Structures of neat and hydrated 1-octanol from computer simulations
    • MacCallum JL, Tieleman DP. Structures of neat and hydrated 1-octanol from computer simulations. J Am Chem Soc 2002; 124: 15085-15093.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 15085-15093
    • MacCallum, J.L.1    Tieleman, D.P.2
  • 113
    • 0034039621 scopus 로고    scopus 로고
    • The agouti-related protein decapeptide (Yc[CRFFNAFC]Y) possesses agonist activity at the murine melanocortin-1 receptor
    • Haskell-Luevano C, Monck EK, Wan YP, Schentrup AM. The agouti-related protein decapeptide (Yc[CRFFNAFC]Y) possesses agonist activity at the murine melanocortin-1 receptor. Peptides 2000; 21: 683-689.
    • (2000) Peptides , vol.21 , pp. 683-689
    • Haskell-Luevano, C.1    Monck, E.K.2    Wan, Y.P.3    Schentrup, A.M.4
  • 116
    • 0029670938 scopus 로고    scopus 로고
    • Passage of a delta-opioid receptor selective enkephalin, [D-penicillamine(2,5)]enkephalin, across the blood-brain and blood-cerebrospinal fluid barriers
    • Williams SA, Abbruscato TJ, Hruby VJ, Davis TP. Passage of a delta-opioid receptor selective enkephalin, [D-penicillamine(2,5)]enkephalin, across the blood-brain and blood-cerebrospinal fluid barriers. J Neurochem 1996; 66: 1289-1299.
    • (1996) J. Neurochem. , vol.66 , pp. 1289-1299
    • Williams, S.A.1    Abbruscato, T.J.2    Hruby, V.J.3    Davis, T.P.4
  • 117
    • 0027416441 scopus 로고
    • 2 receptor: A mechanistic hypothesis from molecular dynamics simulations of the three-dimensional model of the receptor complexed to ligands
    • 2 receptor: A mechanistic hypothesis from molecular dynamics simulations of the three-dimensional model of the receptor complexed to ligands. J Med Chem 1993; 36: 934-938.
    • (1993) J. Med. Chem. , vol.36 , pp. 934-938
    • Zhang, D.1    Weinstein, H.2
  • 119
    • 0029947902 scopus 로고    scopus 로고
    • A 3D model of the delta opioid receptor and ligand-receptor complexes
    • Alkorta I, Loew GH. A 3D model of the delta opioid receptor and ligand-receptor complexes. Prot Engin 1996; 9: 573-583.
    • (1996) Prot. Engin. , vol.9 , pp. 573-583
    • Alkorta, I.1    Loew, G.H.2
  • 120
    • 0032581639 scopus 로고    scopus 로고
    • G protein-coupled receptors: Models, mutagenesis, and drug design
    • Bikker JA, Trumpp-Kallmeyer S, Humblet C. G protein-coupled receptors: Models, mutagenesis, and drug design. J Med Chem 1998; 41: 2911-2927.
    • (1998) J. Med. Chem. , vol.41 , pp. 2911-2927
    • Bikker, J.A.1    Trumpp-Kallmeyer, S.2    Humblet, C.3
  • 121
    • 0026451988 scopus 로고
    • Molecular modeling of adenosine receptors. 1. The ligand binding site on the A1 receptor
    • Ijzerman AP, Van Galen PJM, Jacobson KA. Molecular modeling of adenosine receptors. 1. The ligand binding site on the A1 receptor. Drug Design Disc 1992; 9: 49-67.
    • (1992) Drug Design Disc. , vol.9 , pp. 49-67
    • Ijzerman, A.P.1    Van Galen, P.J.M.2    Jacobson, K.A.3
  • 123
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering the molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering the molecular mechanisms involved in activation of G protein-coupled receptors. Endocrinol Rev 2000; 21: 90-113.
    • (2000) Endocrinol. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 124
    • 0035132984 scopus 로고    scopus 로고
    • Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces
    • Tieleman DP, Berendsen HJC, Sansom MSP. Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces. Biophys J 2001; 80: 331-341.
    • (2001) Biophys. J. , vol.80 , pp. 331-341
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 125
    • 0035865532 scopus 로고    scopus 로고
    • Characterization of the molecular motions of constitutively active G protein-coupled receptors for parathyroid hormone
    • Rolz C, Mierke DF. Characterization of the molecular motions of constitutively active G protein-coupled receptors for parathyroid hormone. Biophys J 2001; 89: 119-128.
    • (2001) Biophys. J. , vol.89 , pp. 119-128
    • Rolz, C.1    Mierke, D.F.2
  • 126
    • 0033580648 scopus 로고    scopus 로고
    • Molecular characterization of the receptor-ligand complex for parathyroid hormone
    • Rolz C, Pellegrini M, Mierke DF. Molecular characterization of the receptor-ligand complex for parathyroid hormone. Biochemistry 1999; 38: 6397-6405.
    • (1999) Biochemistry , vol.38 , pp. 6397-6405
    • Rolz, C.1    Pellegrini, M.2    Mierke, D.F.3
  • 128
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Model 2001; 7: 306-317.
    • (2001) J. Mol. Model , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 131
    • 33846823909 scopus 로고
    • Particle Mesh Ewald - An Nlog(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle Mesh Ewald - An Nlog(N) method for Ewald sums in large systems. J Chem Phys 1993; 98: 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 132
    • 36549100991 scopus 로고
    • Monte Carlo simulation of liquid-liquid benzene water interface
    • Linse P. Monte Carlo simulation of liquid-liquid benzene water interface. J Chem Phys 1987; 86: 4177-4187.
    • (1987) J. Chem. Phys. , vol.86 , pp. 4177-4187
    • Linse, P.1
  • 133
    • 0000796912 scopus 로고
    • A molecular dynamics study of the hexane water interface
    • Carpenter IL, Hehre WJ. A molecular dynamics study of the hexane water interface. J Phys Chem 1990; 94: 531-536.
    • (1990) J. Phys. Chem. , vol.94 , pp. 531-536
    • Carpenter, I.L.1    Hehre, W.J.2
  • 134
    • 0037015153 scopus 로고    scopus 로고
    • Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations
    • Rohrig UF, Guidoni L, Röthlisberger U. Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations. Biochemistry 2002; 41: 10799-10809.
    • (2002) Biochemistry , vol.41 , pp. 10799-10809
    • Rohrig, U.F.1    Guidoni, L.2    Röthlisberger, U.3
  • 135
    • 84986532529 scopus 로고
    • Cluster analysis of molecular conformations
    • Shenkin PS, McDonald DQ. Cluster analysis of molecular conformations. J Comput Chem 1994; 15: 899-916.
    • (1994) J. Comput. Chem. , vol.15 , pp. 899-916
    • Shenkin, P.S.1    McDonald, D.Q.2
  • 137
    • 0026556022 scopus 로고
    • On the interpretation of biochemical data by molecular dynamics computer simulation
    • van Gunsteren WF, Mark AE. On the interpretation of biochemical data by molecular dynamics computer simulation. Eur J Biochem 1992; 204: 947-961.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 947-961
    • van Gunsteren, W.F.1    Mark, A.E.2
  • 139
    • 0035324944 scopus 로고    scopus 로고
    • Molecular complexity and its impact on the probability of finding leads for drug discovery
    • Hann MM, Leach AR, Harper G. Molecular complexity and its impact on the probability of finding leads for drug discovery. J Chem Inf Comput Sci 2001; 41: 856-864.
    • (2001) J. Chem. Inf. Comput. Sci. , vol.41 , pp. 856-864
    • Hann, M.M.1    Leach, A.R.2    Harper, G.3
  • 141
    • 0031024171 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski CA, Lombardo F, Dominy BW, Feeney PJ. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Delivery Rev 1997; 23: 3-25.
    • (1997) Adv. Drug Delivery Rev. , vol.23 , pp. 3-25
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 143
    • 0037785467 scopus 로고    scopus 로고
    • Novel tetrahydropyran-based peptidomimetics from a bioisosteric transformation of a tripeptide. Evidence of their activity at melanocortin receptors
    • Mazur AW, Kulesza A, Mishra RK, Cross-Doersen D, Russell AF, Ebetino FH. Novel tetrahydropyran-based peptidomimetics from a bioisosteric transformation of a tripeptide. Evidence of their activity at melanocortin receptors. Bioorg Med Chem 2003; 11: 3053-3063.
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 3053-3063
    • Mazur, A.W.1    Kulesza, A.2    Mishra, R.K.3    Cross-Doersen, D.4    Russell, A.F.5    Ebetino, F.H.6
  • 144
    • 0033851469 scopus 로고    scopus 로고
    • Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads
    • Hruby VJ, Balse PM. Conformational and topographical considerations in designing agonist peptidomimetics from peptide leads. Curr Med Chem 2000; 7: 945-970.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 945-970
    • Hruby, V.J.1    Balse, P.M.2
  • 145
    • 0036433436 scopus 로고    scopus 로고
    • Molecular modeling in the design of peptidomimetics and peptide surrogates
    • Perez JJ, Corcho F, Llorens O. Molecular modeling in the design of peptidomimetics and peptide surrogates. Curr Med Chem 2002; 9: 2209-2229.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 2209-2229
    • Perez, J.J.1    Corcho, F.2    Llorens, O.3
  • 146
    • 0141869940 scopus 로고    scopus 로고
    • Clinically validated peptides as templates for de novo peptidomimetic drug design at G protein-coupled receptors
    • Jones RM, Boatman PD, Semple G, Shin YJ, Tamura SY. Clinically validated peptides as templates for de novo peptidomimetic drug design at G protein-coupled receptors. Curr Op Pharmacol 2003; 3: 530-543.
    • (2003) Curr. Op. Pharmacol. , vol.3 , pp. 530-543
    • Jones, R.M.1    Boatman, P.D.2    Semple, G.3    Shin, Y.J.4    Tamura, S.Y.5
  • 147
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus M, McCammon JA. Molecular dynamics simulations of biomolecules. Nat Struct Biol 2002; 9: 646-652.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 150
    • 0023504970 scopus 로고
    • Structure-function analysis of proteins through the design, synthesis and study of peptide models
    • Taylor JW, Kaiser ET. Structure-function analysis of proteins through the design, synthesis and study of peptide models. Methods Enzymol 1987; 154: 473-498.
    • (1987) Methods Enzymol. , vol.154 , pp. 473-498
    • Taylor, J.W.1    Kaiser, E.T.2
  • 151
    • 0014307971 scopus 로고
    • The use of helical net-diagrams to represent protein structures
    • Dunnill P. The use of helical net-diagrams to represent protein structures. Biophys J 1968; 8: 865-875.
    • (1968) Biophys. J. , vol.8 , pp. 865-875
    • Dunnill, P.1
  • 153
    • 0037967309 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator (uPA) and its receptor (uPAR): Development of antagonists of uPA/uPAR interaction and their effects in vitro and in vivo
    • Reuning U, Sperl S, Kopitz C, Kessler H, Kruger A, Schmitt M, et al. Urokinase-type plasminogen activator (uPA) and its receptor (uPAR): development of antagonists of uPA/uPAR interaction and their effects in vitro and in vivo. Curr Pharm Design 2003; 9(19): 1529-43.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.19 , pp. 1529-1543
    • Reuning, U.1    Sperl, S.2    Kopitz, C.3    Kessler, H.4    Kruger, A.5    Schmitt, M.6
  • 154
    • 0037274843 scopus 로고    scopus 로고
    • The role of melanocortin peptides and receptors in regulation of energy balance
    • Zimanyi IA, Pelleymounter MA. The role of melanocortin peptides and receptors in regulation of energy balance. Curr Pharm Design 2003; 9(8): 627-41.
    • (2003) Curr. Pharm. Design , vol.9 , Issue.8 , pp. 627-641
    • Zimanyi, I.A.1    Pelleymounter, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.