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Volumn 22, Issue 6, 2013, Pages 774-787

Membrane phospholipid bilayer as a determinant of monoacylglycerol lipase kinetic profile and conformational repertoire

Author keywords

Conformation; Hydrogen exchange; Mass spectrometry; Phospholipid bilayer nanodisc; Serine hydrolase

Indexed keywords

ACYLGLYCEROL LIPASE; MEMBRANE PHOSPHOLIPID; NANODISC;

EID: 84880620990     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2257     Document Type: Article
Times cited : (38)

References (65)
  • 1
    • 80054054097 scopus 로고    scopus 로고
    • The metabolic serine hydrolases and their functions in mammalian physiology and disease
    • Long JZ, Cravatt BF (2011) The metabolic serine hydrolases and their functions in mammalian physiology and disease. Chem Rev 111:6022-6063.
    • (2011) Chem Rev , vol.111 , pp. 6022-6063
    • Long, J.Z.1    Cravatt, B.F.2
  • 2
    • 6944247598 scopus 로고    scopus 로고
    • RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2- arachidonoylglycerol
    • Dinh TP, Kathuria S, Piomelli D (2004) RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2- arachidonoylglycerol. Mol Pharmacol 66:1260-1264.
    • (2004) Mol Pharmacol , vol.66 , pp. 1260-1264
    • Dinh, T.P.1    Kathuria, S.2    Piomelli, D.3
  • 3
    • 37149013708 scopus 로고    scopus 로고
    • A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol
    • Blankman JL, Simon GM, Cravatt BF (2007) A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol. Chem Biol 14:1347-1356.
    • (2007) Chem Biol , vol.14 , pp. 1347-1356
    • Blankman, J.L.1    Simon, G.M.2    Cravatt, B.F.3
  • 4
    • 84855359304 scopus 로고    scopus 로고
    • The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signaling through canmnabinoid receptors
    • Savinainen JR, Saario SM, Laitinen JT (2012) The serine hydrolases MAGL, ABHD6 and ABHD12 as guardians of 2-arachidonoylglycerol signaling through canmnabinoid receptors. Acta Physiol 204:267-276.
    • (2012) Acta Physiol , vol.204 , pp. 267-276
    • Savinainen, J.R.1    Saario, S.M.2    Laitinen, J.T.3
  • 5
    • 65549150497 scopus 로고    scopus 로고
    • Pharmacotherapeutic modulation of the endocannabinoid signaling system in psychiatric disorders: Drug-discovery strategies
    • Janero DR, Vadivel SK, Makriyannis A (2009) Pharmacotherapeutic modulation of the endocannabinoid signaling system in psychiatric disorders: drug-discovery strategies. Int Rev Psychiatry 21:122-133.
    • (2009) Int Rev Psychiatry , vol.21 , pp. 122-133
    • Janero, D.R.1    Vadivel, S.K.2    Makriyannis, A.3
  • 6
    • 84856481281 scopus 로고    scopus 로고
    • The role of the endocannabinoid system in the neuroendocrine regulation of energy balance
    • Bermudez-Silva FJ, Cardinal P, Cota D (2012) The role of the endocannabinoid system in the neuroendocrine regulation of energy balance. J Psychopharmacol 26:114-124.
    • (2012) J Psychopharmacol , vol.26 , pp. 114-124
    • Bermudez-Silva, F.J.1    Cardinal, P.2    Cota, D.3
  • 7
    • 84926231211 scopus 로고    scopus 로고
    • Peripheral antinociceptive effects of inhibitors of monoacylglycerol lipase in a rat model of inflammatory pain
    • Guindon J, Guijarro A, Piomelli D, Hohmann AG (2011) Peripheral antinociceptive effects of inhibitors of monoacylglycerol lipase in a rat model of inflammatory pain. Br J Pharmacol 163:1464-1478.
    • (2011) Br J Pharmacol , vol.163 , pp. 1464-1478
    • Guindon, J.1    Guijarro, A.2    Piomelli, D.3    Hohmann, A.G.4
  • 8
    • 84874649914 scopus 로고    scopus 로고
    • The monoacylglycerol lipase inhibitor JZL 184 suppresses inflammatory pain in the mouse carrageenan model
    • Gosh S, Wise LE, Chen Y, Guijar R, Mahadevan A, Cravatt BF, Lichtman AH (2013) The monoacylglycerol lipase inhibitor JZL 184 suppresses inflammatory pain in the mouse carrageenan model. Life Sci 92:498-505.
    • (2013) Life Sci , vol.92 , pp. 498-505
    • Gosh, S.1    Wise, L.E.2    Chen, Y.3    Guijar, R.4    Mahadevan, A.5    Cravatt, B.F.6    Lichtman, A.H.7
  • 9
    • 35648973242 scopus 로고    scopus 로고
    • The inhibition of monoacylglycerol lipase by URB602 showed an anti-inflammatory and anti-nociceptive effect in a murine model of acute inflammation
    • Comelli F, Giagnoni G, Bettoni I, Colleoni M, Costa B (2007) The inhibition of monoacylglycerol lipase by URB602 showed an anti-inflammatory and anti-nociceptive effect in a murine model of acute inflammation. Br J Pharmacol 152:787-794.
    • (2007) Br J Pharmacol , vol.152 , pp. 787-794
    • Comelli, F.1    Giagnoni, G.2    Bettoni, I.3    Colleoni, M.4    Costa, B.5
  • 12
    • 79959977058 scopus 로고    scopus 로고
    • Enhancement of endocnnabinoid signaling with JZL184, an inhibitor of the 2-arachidonoylglycerol hydrolyzing enzyme monoacylglycerol lipase, produces anxiolytic effects under consitions of high environmental aversiveness in rats
    • Sciolino NR, Zhou W, Hohmann AG (2011) Enhancement of endocnnabinoid signaling with JZL184, an inhibitor of the 2-arachidonoylglycerol hydrolyzing enzyme monoacylglycerol lipase, produces anxiolytic effects under consitions of high environmental aversiveness in rats. Pharmacol Res 64:226-234.
    • (2011) Pharmacol Res , vol.64 , pp. 226-234
    • Sciolino, N.R.1    Zhou, W.2    Hohmann, A.G.3
  • 13
    • 84859067302 scopus 로고    scopus 로고
    • Inhibition of monoacylglycerol lipase attenuates vomiting in Suncus murinus and 2-arachdonoyl glycerol attenuates nausea in rats
    • Sticht MA, Long JZ, Rock EM, Limebeer CL, Mechoulam R, Cravatt BF, Parker LA (2012) Inhibition of monoacylglycerol lipase attenuates vomiting in Suncus murinus and 2-arachdonoyl glycerol attenuates nausea in rats. Br J Pharmacol 165:2425-2435.
    • (2012) Br J Pharmacol , vol.165 , pp. 2425-2435
    • Sticht, M.A.1    Long, J.Z.2    Rock, E.M.3    Limebeer, C.L.4    Mechoulam, R.5    Cravatt, B.F.6    Parker, L.A.7
  • 15
    • 73149109062 scopus 로고    scopus 로고
    • Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis
    • Nomura DK, Long JZ, Niessen S, Hoover HS, Ng SW, Cravatt BF (2010) Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis. Cell 140:49-61.
    • (2010) Cell , vol.140 , pp. 49-61
    • Nomura, D.K.1    Long, J.Z.2    Niessen, S.3    Hoover, H.S.4    Ng, S.W.5    Cravatt, B.F.6
  • 17
    • 84862742406 scopus 로고    scopus 로고
    • Monoacyglycerol lipase - A taregt for drug development?
    • Fowler CJ (2012) Monoacyglycerol lipase - a taregt for drug development? Br J Pharmacol 166:1568-1585.
    • (2012) Br J Pharmacol , vol.166 , pp. 1568-1585
    • Fowler, C.J.1
  • 18
    • 84874652001 scopus 로고    scopus 로고
    • Therapeutic potential of monoacylglycerol lipase inhibitors
    • Mulvihill MM, Nomura DK (2013) Therapeutic potential of monoacylglycerol lipase inhibitors. Life Sci 92:492-497.
    • (2013) Life Sci , vol.92 , pp. 492-497
    • Mulvihill, M.M.1    Nomura, D.K.2
  • 20
    • 78349281122 scopus 로고    scopus 로고
    • Solvent-induced lid opening in lipases: A molecular dynamics study
    • Rehm S, Trodler P, Pleiss J (2010) Solvent-induced lid opening in lipases: a molecular dynamics study. Protein Sci 19:2122-2130.
    • (2010) Protein Sci , vol.19 , pp. 2122-2130
    • Rehm, S.1    Trodler, P.2    Pleiss, J.3
  • 21
    • 0026786234 scopus 로고
    • The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 A ° resolution
    • Derewenda ZS, Derewenda U, Dodson GG (1992) The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 A ° resolution. J Mol Biol 227:818-839.
    • (1992) J Mol Biol , vol.227 , pp. 818-839
    • Derewenda, Z.S.1    Derewenda, U.2    Dodson, G.G.3
  • 22
    • 0028295251 scopus 로고
    • Conformational lability of lipases observed in the absence of an oil-water interface: Crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar
    • Derewenda U, Swenson L, Wei Y, Green R, Kobos PM, Joerger R, Haas MJ, Derewenda ZS (1994) Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar. J Lipid Res 35:524-534.
    • (1994) J Lipid Res , vol.35 , pp. 524-534
    • Derewenda, U.1    Swenson, L.2    Wei, Y.3    Green, R.4    Kobos, P.M.5    Joerger, R.6    Haas, M.J.7    Derewenda, Z.S.8
  • 23
    • 0033567190 scopus 로고    scopus 로고
    • Biosynthesis and inactivation of the endocannabinoid 2- arachidonoylglycerol in circulating and tumoral macrophages
    • Di Marzo V, Bisogno T, De Petrocellis L, Melck D, Orlando P, Wagner JA, Kunos G (1999) Biosynthesis and inactivation of the endocannabinoid 2-arachidonoylglycerol in circulating and tumoral macrophages. Eur J Biochem 264:258-267.
    • (1999) Eur J Biochem , vol.264 , pp. 258-267
    • Di Marzo, V.1    Bisogno, T.2    De Petrocellis, L.3    Melck, D.4    Orlando, P.5    Wagner, J.A.6    Kunos, G.7
  • 25
    • 76649126721 scopus 로고    scopus 로고
    • Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling
    • Labar G, Bauvois C, Borel F, Ferrer JL, Wouters J, Lambert DM (2010) Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling. Chembiochem 11:218-227.
    • (2010) Chembiochem , vol.11 , pp. 218-227
    • Labar, G.1    Bauvois, C.2    Borel, F.3    Ferrer, J.L.4    Wouters, J.5    Lambert, D.M.6
  • 28
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • Nath A, Atkins WM, Sligar SG (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry 46:2059- 2069.
    • (2007) Biochemistry , vol.46 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 29
    • 0035980050 scopus 로고    scopus 로고
    • Detergents as tools in membrane biochemistry
    • Garavito RM, Ferguson-Miller S (2001) Detergents as tools in membrane biochemistry. J Biol Chem 276:32403-32406.
    • (2001) J Biol Chem , vol.276 , pp. 32403-32406
    • Garavito, R.M.1    Ferguson-Miller, S.2
  • 30
    • 0037139592 scopus 로고    scopus 로고
    • Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel
    • Chou JJ, Kaufman JD, Stahl SJ, Wingfield PT, Bax A (2002) Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. J Am Chem Soc 124:2450-2451.
    • (2002) J Am Chem Soc , vol.124 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, S.J.3    Wingfield, P.T.4    Bax, A.5
  • 31
    • 77953480345 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: What is it and what can it tell us?
    • Marcsisin SR, Engen JR (2010) Hydrogen exchange mass spectrometry: what is it and what can it tell us? Anal Bioanal Chem 397:967-972.
    • (2010) Anal Bioanal Chem , vol.397 , pp. 967-972
    • Marcsisin, S.R.1    Engen, J.R.2
  • 33
    • 70349437270 scopus 로고    scopus 로고
    • The nanodisc: A novel tool for membrane protein studies
    • Borch J, Hamann T (2009) The nanodisc: a novel tool for membrane protein studies. Biol Chem 390:805-814.
    • (2009) Biol Chem , vol.390 , pp. 805-814
    • Borch, J.1    Hamann, T.2
  • 35
    • 84861895328 scopus 로고    scopus 로고
    • Measurements and implications of the membrane dipole potential
    • Wang L (2012) Measurements and implications of the membrane dipole potential. Annu Rev Biochem 81:615-635.
    • (2012) Annu Rev Biochem , vol.81 , pp. 615-635
    • Wang, L.1
  • 36
    • 49449086026 scopus 로고    scopus 로고
    • Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification
    • Zvonok N, Williams J, Johnston M, Pandarinathan L, Janero DR, Li J, Krishnan SC, Makriyannis A (2008) Full mass spectrometric characterization of human monoacylglycerol lipase generated by large-scale expression and single-step purification. J Proteome Res 7:2158-2164.
    • (2008) J Proteome Res , vol.7 , pp. 2158-2164
    • Zvonok, N.1    Williams, J.2    Johnston, M.3    Pandarinathan, L.4    Janero, D.R.5    Li, J.6    Krishnan, S.C.7    Makriyannis, A.8
  • 38
    • 34547764348 scopus 로고    scopus 로고
    • Effect of nonionic surfactants on Rhizopus homothallicus lipase activity
    • Diaz JCM, Cordova J, Baratti J, Carriere F, Abousalham A (2007) Effect of nonionic surfactants on Rhizopus homothallicus lipase activity. Mol Biotechnol 35:205-214.
    • (2007) Mol Biotechnol , vol.35 , pp. 205-214
    • Jcm, D.1    Cordova, J.2    Baratti, J.3    Carriere, F.4    Abousalham, A.5
  • 40
    • 69549084345 scopus 로고    scopus 로고
    • A/b-Hydrolase fold: An update
    • Carr PD, Ollis DL (2009) a/b-Hydrolase fold: an update. Protein Pept Lett 16:1137-1148.
    • (2009) Protein Pept Lett , vol.16 , pp. 1137-1148
    • Carr, P.D.1    Ollis, D.L.2
  • 41
    • 72849117351 scopus 로고    scopus 로고
    • Refined homology model of monoacylglycerol lipase: Toward a selective inhibitor
    • Bowman AL, Makriyannis A (2009) Refined homology model of monoacylglycerol lipase: toward a selective inhibitor. J Comput Aided Mol Des 23:799-806.
    • (2009) J Comput Aided Mol des , vol.23 , pp. 799-806
    • Bowman, A.L.1    Makriyannis, A.2
  • 42
    • 49449092396 scopus 로고    scopus 로고
    • Covalent inhibitors of human monoacylglycerol lipase: Ligand-assisted characterization of the catalytic site by mass spectrometry and mutational anlaysis
    • Zvonok N, Pandarinathan L, Williams J, Johnston M, Karageorgos I, Janero DR, Krishnan SC, Makriyannis A (2008) Covalent inhibitors of human monoacylglycerol lipase: ligand-assisted characterization of the catalytic site by mass spectrometry and mutational anlaysis. Chem Biol 25:854-862.
    • (2008) Chem Biol , vol.25 , pp. 854-862
    • Zvonok, N.1    Pandarinathan, L.2    Williams, J.3    Johnston, M.4    Karageorgos, I.5    Janero, D.R.6    Krishnan, S.C.7    Makriyannis, A.8
  • 43
    • 49549083949 scopus 로고    scopus 로고
    • Membrane proteins: Molecular dynamics simulations
    • Lindhal E, Sansom MSP (2008) Membrane proteins: molecular dynamics simulations. Curr Opin Struct Biol 18:425-431.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 425-431
    • Lindhal, E.1    Msp, S.2
  • 44
    • 15844374570 scopus 로고    scopus 로고
    • The conformational properties of the highly selective cannabinoid receptor ligand CP-55,940
    • Xie X-Q, Melvin LS, Makriyannis A (1996) The conformational properties of the highly selective cannabinoid receptor ligand CP-55,940. J Biol Chem 271:10640- 10647.
    • (1996) J Biol Chem , vol.271 , pp. 10640-10647
    • Xie, X.-Q.1    Melvin, L.S.2    Makriyannis, A.3
  • 45
    • 84862877720 scopus 로고    scopus 로고
    • Drug discovery for a new generation of covalent drugs
    • Kalgutkar A S, Dalvie DK (2012) Drug discovery for a new generation of covalent drugs. Expert Opin Drug Disc 7:561-581.
    • (2012) Expert Opin Drug Disc , vol.7 , pp. 561-581
    • Kalgutkar, A.S.1    Dalvie, D.K.2
  • 46
    • 4444297536 scopus 로고    scopus 로고
    • Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment
    • Baas BJ, Denisov IG, Sligar SG (2004) Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment. Arch Biochem Biophys 430:218-228.
    • (2004) Arch Biochem Biophys , vol.430 , pp. 218-228
    • Baas, B.J.1    Denisov, I.G.2    Sligar, S.G.3
  • 47
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size
    • Denisov IG, Grinkova YV, Lazarides AA, Sligar SG (2004) Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size. J Am Chem Soc 126:3477-3487.
    • (2004) J Am Chem Soc , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 48
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales TE, Engen JR (2006) Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom Rev 25:158-170.
    • (2006) Mass Spectrom Rev , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 49
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Zhang Z, Smith DL (1993) Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci 2:522- 531.
    • (1993) Protein Sci , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 50
    • 77954193701 scopus 로고    scopus 로고
    • Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry
    • Hebling CM, Morgan CR, Stafford DW, Jorgenson JW, Rand KD, Engen JR (2010) Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry. Anal Chem 82:5415-5419.
    • (2010) Anal Chem , vol.82 , pp. 5415-5419
    • Hebling, C.M.1    Morgan, C.R.2    Stafford, D.W.3    Jorgenson, J.W.4    Rand, K.D.5    Engen, J.R.6
  • 51
    • 79954547968 scopus 로고    scopus 로고
    • The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies
    • Houde D, Berkowitz SA, Engen JR (2011) The utility of hydrogen/deuterium exchange mass spectrometry in biopharmaceutical comparability studies. J Pharm Sci 100:2071-2086.
    • (2011) J Pharm Sci , vol.100 , pp. 2071-2086
    • Houde, D.1    Berkowitz, S.A.2    Engen, J.R.3
  • 53
    • 65249151900 scopus 로고    scopus 로고
    • Lipid models for united-atom molecular dynamics simulations of proteins
    • Kukol A (2009) Lipid models for united-atom molecular dynamics simulations of proteins. J Chem Theory Comput 5:615-626.
    • (2009) J Chem Theory Comput , vol.5 , pp. 615-626
    • Kukol, A.1
  • 54
    • 77957936649 scopus 로고    scopus 로고
    • Simulating POPC and POPC/POPG bilayers: Conserved packing and altered surface reactivity
    • Janosi L, Gorfe AA (2010) Simulating POPC and POPC/POPG bilayers: conserved packing and altered surface reactivity. J Chem Theory Comput 6:3267- 3273.
    • (2010) J Chem Theory Comput , vol.6 , pp. 3267-3273
    • Janosi, L.1    Gorfe, A.A.2
  • 59
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi G, Donadio D, Parrinello M (2007) Canonical sampling through velocity rescaling. J Chem Phys 126:014101.
    • (2007) J Chem Phys , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 60
    • 33846823909 scopus 로고
    • Particle mesh ewald-an nlog(n) method for ewald sums in large systems
    • Darden T, York D, Pedersen L (1993) Particle mesh Ewald-an N.Log(N) method for Ewald sums in large systems. J Chem Phys 98:10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 62
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen HJC, Fraaije J (1997) LINCS: a linear constraint solver for molecular simulations. J Comput Chem 18:1463-1472.
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Hjc, B.3    Fraaije, J.4
  • 63
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydration
    • Pullman B, Ed. Dordrecht, Netherlands: Reidel
    • Berendsen HJC, Postma JPM, van Gunsteren WF, Hermans J, Interaction models for water in relation to protein hydration. In: Pullman B, Ed. (1981) Intermolecular forces. Dordrecht, Netherlands: Reidel, pp 331- 342.
    • (1981) Intermolecular Forces , pp. 331-342
    • Hjc, B.1    Jpm, P.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 64
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4:435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4


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