메뉴 건너뛰기




Volumn 289, Issue 29, 2014, Pages 20345-20358

The molecular basis of ligand interaction at free fatty acid receptor 4 (FFA4/GPR120)

Author keywords

[No Author keywords available]

Indexed keywords

FATTY ACIDS;

EID: 84904512037     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.561449     Document Type: Article
Times cited : (62)

References (39)
  • 1
    • 84872407744 scopus 로고    scopus 로고
    • Drug discovery opportunities and challenges at G protein coupled receptors for long chain free fatty acids
    • Holliday, N. D., Watson, S.-J., and Brown, A. J. (2011) Drug discovery opportunities and challenges at G protein coupled receptors for long chain free fatty acids. Front. Endocrinol. 2, 112
    • (2011) Front. Endocrinol. , vol.2 , pp. 112
    • Holliday, N.D.1    Watson, S.-J.2    Brown, A.J.3
  • 2
    • 84885169779 scopus 로고    scopus 로고
    • Drugs or diet?-developing novel therapeutic strategies targeting the free fatty acid family of GPCRs
    • Dranse, H. J., Kelly, M. E., and Hudson, B. D. (2013) Drugs or diet?-developing novel therapeutic strategies targeting the free fatty acid family of GPCRs. Br. J. Pharmacol. 170, 696-711
    • (2013) Br. J. Pharmacol. , vol.170 , pp. 696-711
    • Dranse, H.J.1    Kelly, M.E.2    Hudson, B.D.3
  • 5
    • 77956165390 scopus 로고    scopus 로고
    • GPR120 is an ω-3 fatty acid receptor mediating potent anti-inflammatory and insulin-sensitizing effects
    • Oh, D. Y., Talukdar, S., Bae, E. J., Imamura, T., Morinaga, H., Fan, W., Li, P., Lu, W. J., Watkins, S. M., and Olefsky, J. M. (2010) GPR120 is an ω-3 fatty acid receptor mediating potent anti-inflammatory and insulin-sensitizing effects. Cell 142, 687-698
    • (2010) Cell , vol.142 , pp. 687-698
    • Oh, D.Y.1    Talukdar, S.2    Bae, E.J.3    Imamura, T.4    Morinaga, H.5    Fan, W.6    Li, P.7    Lu, W.J.8    Watkins, S.M.9    Olefsky, J.M.10
  • 12
    • 84886060164 scopus 로고    scopus 로고
    • The pharmacology of a potent and selective agonist, TUG-891, demonstrates both potential opportunity and possible challenges to therapeutic agonism of FFA4 (GPR120)
    • Hudson, B. D., Shimpukade, B., Mackenzie, A. E., Butcher, A. J., Pediani, J. D., Christiansen, E., Heathcote, H., Tobin, A. B., Ulven, T., and Milligan, G. (2013) The pharmacology of a potent and selective agonist, TUG-891, demonstrates both potential opportunity and possible challenges to therapeutic agonism of FFA4 (GPR120). Mol. Pharmacol. 84, 710-725
    • (2013) Mol. Pharmacol. , vol.84 , pp. 710-725
    • Hudson, B.D.1    Shimpukade, B.2    Mackenzie, A.E.3    Butcher, A.J.4    Pediani, J.D.5    Christiansen, E.6    Heathcote, H.7    Tobin, A.B.8    Ulven, T.9    Milligan, G.10
  • 14
    • 84860513814 scopus 로고    scopus 로고
    • Structure-based drug screening for G-protein-coupled receptors
    • Shoichet, B. K., and Kobilka, B. K. (2012) Structure-based drug screening for G-protein-coupled receptors. Trends Pharmacol. Sci. 33, 268-272
    • (2012) Trends Pharmacol. Sci. , vol.33 , pp. 268-272
    • Shoichet, B.K.1    Kobilka, B.K.2
  • 18
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent treatment of internal and surface residues in empirical pKa predictions
    • Olsson, M. H., Søndergaard, C. R., Rostkowski, M., and Jensen, J. H. (2011) PROPKA3: Consistent treatment of internal and surface residues in empirical pKa predictions. J. Chem. Theory Comput. 7, 525-537
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Olsson, M.H.1    Søndergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 19
    • 84871719063 scopus 로고    scopus 로고
    • Schrödinger, LLC (2012), Schrödinger, LLC, New York
    • Schrödinger, LLC (2012) MacroModel, Version 9.9 (2012), Schrödinger, LLC, New York
    • (2012) MacroModel, Version 9.9
  • 22
    • 84904514626 scopus 로고    scopus 로고
    • Schrödinger, LLC Schrödinger, LLC, New York
    • Schrödinger, LLC (2013) Prime, version 3.2, Schrödinger, LLC, New York
    • (2013) Prime, Version 3.2
  • 23
    • 77957055780 scopus 로고
    • Integrated methods for modeling G-protein coupled receptors
    • Ballesteros, J. A., and Weinstein, H. (1995) Integrated methods for modeling G-protein coupled receptors. Methods Neurosci. 366-428
    • (1995) Methods Neurosci. , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 24
    • 34347220548 scopus 로고    scopus 로고
    • Bidirectional, iterative approach to the structural delineation of the functional "chemoprint" in GPR40 for agonist recognition
    • DOI 10.1021/jm0614782
    • Tikhonova, I. G., Sum, C. S., Neumann, S., Thomas, C. J., Raaka, B. M., Costanzi, S., and Gershengorn, M. C. (2007) Bidirectional, iterative approach to the structural delineation of the functional "chemoprint" in GPR40 for agonist recognition. J. Med. Chem. 50, 2981-2989 (Pubitemid 47001241)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.13 , pp. 2981-2989
    • Tikhonova, I.G.1    Chi, S.S.2    Neumann, S.3    Thomas, C.J.4    Raaka, B.M.5    Costanzi, S.6    Gershengorn, M.C.7
  • 25
    • 57749112018 scopus 로고    scopus 로고
    • Conserved polar residues in transmembrane domains V, VI, and VII of free fatty acid receptor 2 and free fatty acid receptor 3 are required for the binding and function of short chain fatty acids
    • Stoddart, L. A., Smith, N. J., Jenkins, L., Brown, A. J., and Milligan, G. (2008) Conserved polar residues in transmembrane domains V, VI, and VII of free fatty acid receptor 2 and free fatty acid receptor 3 are required for the binding and function of short chain fatty acids. J. Biol. Chem. 283, 32913-32924
    • (2008) J. Biol. Chem. , vol.283 , pp. 32913-32924
    • Stoddart, L.A.1    Smith, N.J.2    Jenkins, L.3    Brown, A.J.4    Milligan, G.5
  • 27
    • 84859949278 scopus 로고    scopus 로고
    • Differential signaling by splice variants of the human free fatty acid receptor GPR120
    • Watson, S.-J., Brown, A. J., and Holliday, N. D. (2012) Differential signaling by splice variants of the human free fatty acid receptor GPR120. Mol. Pharmacol. 81, 631-642
    • (2012) Mol. Pharmacol. , vol.81 , pp. 631-642
    • Watson, S.-J.1    Brown, A.J.2    Holliday, N.D.3
  • 28
    • 80052684905 scopus 로고    scopus 로고
    • Experimental challenges to targeting poorly characterized GPCRs: Uncovering the therapeutic potential for free fatty acid receptors
    • Hudson, B. D., Smith, N. J., and Milligan, G. (2011) Experimental challenges to targeting poorly characterized GPCRs: uncovering the therapeutic potential for free fatty acid receptors. Adv. Pharmacol. 62, 175-218
    • (2011) Adv. Pharmacol. , vol.62 , pp. 175-218
    • Hudson, B.D.1    Smith, N.J.2    Milligan, G.3
  • 29
    • 84870021560 scopus 로고    scopus 로고
    • Are homology models sufficiently good for free-energy simulations?
    • Genheden, S. (2012) Are homology models sufficiently good for free-energy simulations? J. Chem. Inf. Model. 52, 3013-3021
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 3013-3021
    • Genheden, S.1
  • 30
    • 84876712334 scopus 로고    scopus 로고
    • The therapeutic potential of allosteric ligands for free fatty acid sensitive GPCRs
    • Hudson, B. D., Ulven, T., and Milligan, G. (2013) The therapeutic potential of allosteric ligands for free fatty acid sensitive GPCRs. Curr. Top. Med. Chem. 13, 14-25
    • (2013) Curr. Top. Med. Chem. , vol.13 , pp. 14-25
    • Hudson, B.D.1    Ulven, T.2    Milligan, G.3
  • 32
    • 67349088738 scopus 로고    scopus 로고
    • Community-wide assessment of GPCR structure modelling and ligand docking: GPCR Dock 2008
    • GPCR Dock 2008 participants
    • Michino, M., Abola, E., GPCR Dock 2008 participants, Brooks, C. L., 3rd, Dixon, J. S., Moult, J., and Stevens, R. C. (2009) Community-wide assessment of GPCR structure modelling and ligand docking: GPCR Dock 2008. Nat. Rev. Drug Discov. 8, 455-463
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 455-463
    • Michino, M.1    Abola, E.2    Brooks III, C.L.3    Dixon, J.S.4    Moult, J.5    Stevens, R.C.6
  • 35
    • 79952488185 scopus 로고    scopus 로고
    • Therapeutic potential of β-arrestin- and G protein-biased agonists
    • Whalen, E. J., Rajagopal, S., and Lefkowitz, R. J. (2011) Therapeutic potential of β-arrestin- and G protein-biased agonists. Trends Mol. Med. 17, 126-139
    • (2011) Trends Mol. Med. , vol.17 , pp. 126-139
    • Whalen, E.J.1    Rajagopal, S.2    Lefkowitz, R.J.3
  • 36
    • 84904492656 scopus 로고    scopus 로고
    • Biased ligand modulation of seven transmembrane receptors (7TMRs): Functional implications for drug discovery
    • April 3, 10.1021/jm401677g
    • Correll, C. C., and McKittrick, B. A. (April 3, 2014) Biased ligand modulation of seven transmembrane receptors (7TMRs): functional implications for drug discovery. J. Med. Chem. 10.1021/jm401677g
    • (2014) J. Med. Chem.
    • Correll, C.C.1    McKittrick, B.A.2
  • 37
    • 84875227396 scopus 로고    scopus 로고
    • Signalling bias in new drug discovery: Detection, quantification and therapeutic impact
    • Kenakin, T., and Christopoulos, A. (2013) Signalling bias in new drug discovery: detection, quantification and therapeutic impact. Nat. Rev. Drug Discov. 12, 205-216
    • (2013) Nat. Rev. Drug Discov. , vol.12 , pp. 205-216
    • Kenakin, T.1    Christopoulos, A.2
  • 38
    • 84903513580 scopus 로고    scopus 로고
    • Concomitant action of structural elements and receptor phosphorylation determine arrestin-3 interaction with the free fatty acid receptor FFA4
    • Butcher, A. J., Hudson, B. D., Shimpukade, B., Alvarez-Curto, E., Prihandoko, R., Ulven, T., Milligan, G., and Tobin, A. B. (2014) Concomitant action of structural elements and receptor phosphorylation determine arrestin-3 interaction with the free fatty acid receptor FFA4. J. Biol. Chem. 289, 18451-18465
    • (2014) J. Biol. Chem. , vol.289 , pp. 18451-18465
    • Butcher, A.J.1    Hudson, B.D.2    Shimpukade, B.3    Alvarez-Curto, E.4    Prihandoko, R.5    Ulven, T.6    Milligan, G.7    Tobin, A.B.8
  • 39
    • 84897408090 scopus 로고    scopus 로고
    • Schrödinger Schrödinger, LLC, New York
    • Schrödinger (2013) LigPrep, version 2.6, Schrödinger, LLC, New York
    • (2013) LigPrep, Version 2.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.