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Volumn 64, Issue 2, 2006, Pages 363-375

Interactions of the C2 domain of human factor V with a model membrane

Author keywords

Domain C2 of coagulation Factor V; Molecular dynamics; Peripheral membrane protein; POPE

Indexed keywords

BLOOD CLOTTING FACTOR 10A INHIBITOR; BLOOD CLOTTING FACTOR 5; PHOSPHATIDYLSERINE; PHOSPHOLIPID; WATER;

EID: 33745603727     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20986     Document Type: Article
Times cited : (12)

References (65)
  • 1
    • 0019977242 scopus 로고
    • Radioimmunoassay of Factor V in human plasma and platelets
    • Tracy PB, Eide LL, Bowie EJ, Mann KG. Radioimmunoassay of Factor V in human plasma and platelets. Blood 1982;60:59-63.
    • (1982) Blood , vol.60 , pp. 59-63
    • Tracy, P.B.1    Eide, L.L.2    Bowie, E.J.3    Mann, K.G.4
  • 2
    • 0023918199 scopus 로고
    • Blood coagulation Factors V and VIII: Structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders
    • Kane WH, Davie EW. Blood coagulation Factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders. Blood 1988;71:539-555.
    • (1988) Blood , vol.71 , pp. 539-555
    • Kane, W.H.1    Davie, E.W.2
  • 3
    • 0037567421 scopus 로고    scopus 로고
    • Exposure of platelet membrane phosphatidylserine regulates blood coagulation
    • Lentz BR. Exposure of platelet membrane phosphatidylserine regulates blood coagulation. Prog Lipid Res 2003;42:423-438.
    • (2003) Prog Lipid Res , vol.42 , pp. 423-438
    • Lentz, B.R.1
  • 4
    • 0018786088 scopus 로고
    • The subunit structure of thrombin-activated Factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity
    • Esmon CT. The subunit structure of thrombin-activated Factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity. J Biol Chem 1979;254:964-973.
    • (1979) J Biol Chem , vol.254 , pp. 964-973
    • Esmon, C.T.1
  • 5
    • 0024509988 scopus 로고
    • The reassociation of Factor Va from its isolated subunits
    • Krishnaswamy S, Russell GD, Mann KG. The reassociation of Factor Va from its isolated subunits. J Biol Chem 1989;264:3160-3168.
    • (1989) J Biol Chem , vol.264 , pp. 3160-3168
    • Krishnaswamy, S.1    Russell, G.D.2    Mann, K.G.3
  • 6
    • 0018622772 scopus 로고
    • The contribution of bovine Factor V and Factor Va to the activity of prothrombinase
    • Nesheim ME, Taswell JB, Mann KG. The contribution of bovine Factor V and Factor Va to the activity of prothrombinase. J Biol Chem 1979;254:10952-10962.
    • (1979) J Biol Chem , vol.254 , pp. 10952-10962
    • Nesheim, M.E.1    Taswell, J.B.2    Mann, K.G.3
  • 7
    • 1842426740 scopus 로고    scopus 로고
    • Trp2063 and Trp2064 in the Factor Va C2 domain are required for high-affinity binding to phospholipid membranes but not for assembly of the prothrombinase complex
    • Peng W, Quinn-Allen MA, Kim SW, Alexander KA, Kane WH. Trp2063 and Trp2064 in the Factor Va C2 domain are required for high-affinity binding to phospholipid membranes but not for assembly of the prothrombinase complex. Biochemistry 2004;43:4385-4393.
    • (2004) Biochemistry , vol.43 , pp. 4385-4393
    • Peng, W.1    Quinn-Allen, M.A.2    Kim, S.W.3    Alexander, K.A.4    Kane, W.H.5
  • 8
    • 0026709656 scopus 로고
    • Deletion analysis of recombinant human Factor V. Evidence for a phosphatidylserine binding site in the second C-type domain
    • Ortel TL, Devore-Carter D, Quinn-Allen M, Kane WH. Deletion analysis of recombinant human Factor V. Evidence for a phosphatidylserine binding site in the second C-type domain. J Biol Chem 1992;267:4189-4198.
    • (1992) J Biol Chem , vol.267 , pp. 4189-4198
    • Ortel, T.L.1    Devore-Carter, D.2    Quinn-Allen, M.3    Kane, W.H.4
  • 9
    • 0001252591 scopus 로고    scopus 로고
    • Identification of functionally important amino acid residues within the C2-domain of human factor V using alanine-scanningmutagenesis
    • Kim SW, Quinn-Allen MA, Camp JT, Macedo-Ribeiro S, Fuentes-Prior P, Bode W, Kane WH. Identification of functionally important amino acid residues within the C2-domain of human factor V using alanine-scanningmutagenesis. Biochemistry 2000;39:1951-1958.
    • (2000) Biochemistry , vol.39 , pp. 1951-1958
    • Kim, S.W.1    Quinn-Allen, M.A.2    Camp, J.T.3    Macedo-Ribeiro, S.4    Fuentes-Prior, P.5    Bode, W.6    Kane, W.H.7
  • 10
    • 0033953116 scopus 로고    scopus 로고
    • Mutations in a potential phospholipid binding loop in the C2 domain of Factor V affecting the assembly of the prothrombinase complex
    • Nicolaes GA, Villoutreix BO, Dahlback B. Mutations in a potential phospholipid binding loop in the C2 domain of Factor V affecting the assembly of the prothrombinase complex. Blood Coagul Fibrinolysis 2000;11:89-100.
    • (2000) Blood Coagul Fibrinolysis , vol.11 , pp. 89-100
    • Nicolaes, G.A.1    Villoutreix, B.O.2    Dahlback, B.3
  • 11
    • 0035902543 scopus 로고    scopus 로고
    • Soluble phosphatidylserine binds to a single identified site in the C2 domain of human Factor Va
    • Srivastava A, Quinn-Allen MA, Kim SW, Kane WH, Lentz BR. Soluble phosphatidylserine binds to a single identified site in the C2 domain of human Factor Va. Biochemistry 2001;40:8246-8255.
    • (2001) Biochemistry , vol.40 , pp. 8246-8255
    • Srivastava, A.1    Quinn-Allen, M.A.2    Kim, S.W.3    Kane, W.H.4    Lentz, B.R.5
  • 12
    • 0028013675 scopus 로고
    • Factor Va-membrane interaction is mediated by two regions located on the light chain of the cofactor
    • Kalafatis M, Rand MD, Mann KG. Factor Va-membrane interaction is mediated by two regions located on the light chain of the cofactor. Biochemistry 1994;33:486-493.
    • (1994) Biochemistry , vol.33 , pp. 486-493
    • Kalafatis, M.1    Rand, M.D.2    Mann, K.G.3
  • 13
    • 1642556716 scopus 로고    scopus 로고
    • The Factor V C1 domain is involved in membrane binding: Identification of functionally important amino acid residues within the C1 domain of Factor V using alanine scanningmutagenesis
    • Saleh M, Peng W, Quinn-Allen MA, Macedo-Ribeiro S, Fuentes-Prior P, Bode W, Kane WH. The Factor V C1 domain is involved in membrane binding: identification of functionally important amino acid residues within the C1 domain of Factor V using alanine scanningmutagenesis. Thromb Haemost 2004;91:16-27.
    • (2004) Thromb Haemost , vol.91 , pp. 16-27
    • Saleh, M.1    Peng, W.2    Quinn-Allen, M.A.3    Macedo-Ribeiro, S.4    Fuentes-Prior, P.5    Bode, W.6    Kane, W.H.7
  • 14
    • 20844460991 scopus 로고    scopus 로고
    • Mutation of Hydrophobic residues in the Factor Va C1 and C 2 domains blocks membrane-dependent prothrombin activation
    • Peng W, Quinn-Allen MA, Kane WH. Mutation of Hydrophobic residues in the Factor Va C1 and C 2 domains blocks membrane-dependent prothrombin activation. J Thromb Haemost 2005;3:351-354.
    • (2005) J Thromb Haemost , vol.3 , pp. 351-354
    • Peng, W.1    Quinn-Allen, M.A.2    Kane, W.H.3
  • 17
    • 0031826798 scopus 로고    scopus 로고
    • The discoidin domain family revisited: New members from prokaryotes and a homology-based fold prediction
    • Baumgartner S, Hofmann K, Chiquet-Ehrismann R, Bucher P. The discoidin domain family revisited: new members from prokaryotes and a homology-based fold prediction. Protein Sci 1998;7:1626-1631.
    • (1998) Protein Sci , vol.7 , pp. 1626-1631
    • Baumgartner, S.1    Hofmann, K.2    Chiquet-Ehrismann, R.3    Bucher, P.4
  • 18
    • 0026709656 scopus 로고
    • Deletion analysis of recombinant human Factor V. Evidence for a phosphatidylserine binding site in the second C-type domain
    • Ortel TL, Devore-Carter D, Quinn-Allen M, Kane WH. Deletion analysis of recombinant human Factor V. Evidence for a phosphatidylserine binding site in the second C-type domain. J Biol Chem 1992;267:4189-4198.
    • (1992) J Biol Chem , vol.267 , pp. 4189-4198
    • Ortel, T.L.1    Devore-Carter, D.2    Quinn-Allen, M.3    Kane, W.H.4
  • 19
    • 0030066652 scopus 로고    scopus 로고
    • Insights into the complex association of bovine Factor Va with acidic-lipid-containing synthetic membranes
    • Cutsforth GA, Koppaka V, Krishnaswamy S, Wu JR, Mann KG, Lentz BR. Insights into the complex association of bovine Factor Va with acidic-lipid-containing synthetic membranes. Biophys J 1996;70:2938-2949.
    • (1996) Biophys J , vol.70 , pp. 2938-2949
    • Cutsforth, G.A.1    Koppaka, V.2    Krishnaswamy, S.3    Wu, J.R.4    Mann, K.G.5    Lentz, B.R.6
  • 20
    • 0030043115 scopus 로고    scopus 로고
    • Binding of bovine Factor Va to phosphatidylcholine membranes
    • Koppaka V, Lentz BR. Binding of bovine Factor Va to phosphatidylcholine membranes. Biophys J 1996;70:2930-2937.
    • (1996) Biophys J , vol.70 , pp. 2930-2937
    • Koppaka, V.1    Lentz, B.R.2
  • 22
    • 11244346546 scopus 로고    scopus 로고
    • Molecular dynamics simulations of discoidal bilayers assembled from truncated human lipoproteins
    • Shih AY, Denisov IG, Phillips JC, Sligar SG, Schulten K. Molecular dynamics simulations of discoidal bilayers assembled from truncated human lipoproteins. Biophys J 2005;88:548-556.
    • (2005) Biophys J , vol.88 , pp. 548-556
    • Shih, A.Y.1    Denisov, I.G.2    Phillips, J.C.3    Sligar, S.G.4    Schulten, K.5
  • 23
    • 0043167827 scopus 로고    scopus 로고
    • Molecular dynamics simulations of pentapeptides at interfaces: Salt bridge and cation-Pi interactions
    • Aliste MP, MacCallum 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    MacCallum, J.L.2    Tieleman, D.P.3
  • 24
    • 0036841855 scopus 로고    scopus 로고
    • Analysis and evaluation of channel models: Simulations of alamethicin
    • Tieleman DP, Hess B, Sansom MS. 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.3
  • 26
    • 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 MS, Berendsen HJ. 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.3    Berendsen, H.J.4
  • 27
    • 20544436458 scopus 로고    scopus 로고
    • Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: Applications to C2 domains
    • Malmberg NJ, Falke JJ. Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains. Annu Rev Biophys Biomol Struct 2005;34:71-90.
    • (2005) Annu Rev Biophys Biomol Struct , vol.34 , pp. 71-90
    • Malmberg, N.J.1    Falke, J.J.2
  • 28
    • 0031860932 scopus 로고    scopus 로고
    • A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer
    • Tieleman DP, Berendsen HJ. A molecular dynamics study of the pores formed by Escherichia coli OmpF porin in a fully hydrated palmitoyloleoylphosphatidylcholine bilayer. Biophys J 1998;74:2786-2801.
    • (1998) Biophys J , vol.74 , pp. 2786-2801
    • Tieleman, D.P.1    Berendsen, H.J.2
  • 29
    • 0029633168 scopus 로고
    • GROMACS: A message-passing parallel molecular dynamics implementation
    • Berendsen HJC, van der Spoel D, van Drunen R. GROMACS: a message-passing parallel molecular dynamics implementation. Comp Phys Comm 1995;91:43-56.
    • (1995) Comp Phys Comm , vol.91 , pp. 43-56
    • Berendsen, H.J.C.1    Van Der Spoel, D.2    Van Drunen, R.3
  • 31
    • 0030999097 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature
    • Berger O, Edholm O, Jahnig F. Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys J 1997;72:2002-2013.
    • (1997) Biophys J , vol.72 , pp. 2002-2013
    • Berger, O.1    Edholm, O.2    Jahnig, F.3
  • 33
    • 0000388705 scopus 로고    scopus 로고
    • LINGS: A linear constraint solver for molecular simulations
    • Hess B, Bekker H, Berendsen HJC, Fraaije J. LINGS: a linear constraint solver for molecular simulations. J Comput Chem 1997;18:1463-1472.
    • (1997) J Comput Chem , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 36
    • 0032574726 scopus 로고    scopus 로고
    • Phospholipid composition of the mammalian red cell membrane can be rationalized by a super-lattice model
    • Virtanen JA, Cheng KH, Somerharju P. Phospholipid composition of the mammalian red cell membrane can be rationalized by a super-lattice model. Proc Natl Acad Sci U S A 1998;95:4964-4969.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 4964-4969
    • Virtanen, J.A.1    Cheng, K.H.2    Somerharju, P.3
  • 37
    • 0016802611 scopus 로고
    • Determinants of the formation and activity of Factor V-phospholipid complexes. II. Molecular properties of the complexes
    • Kandall CL, Shohet SB, Akinbami TK, Colman RW. Determinants of the formation and activity of Factor V-phospholipid complexes. II. Molecular properties of the complexes. Thromb Diath Haemorrh 1975;34:271-284.
    • (1975) Thromb Diath Haemorrh , vol.34 , pp. 271-284
    • Kandall, C.L.1    Shohet, S.B.2    Akinbami, T.K.3    Colman, R.W.4
  • 38
    • 0036618993 scopus 로고    scopus 로고
    • Setting up and optimization of membrane protein simulations
    • Faraldo-Gomez JD, Smith GR, Sansom MS. Setting up and optimization of membrane protein simulations. Eur Biophys J 2002;31:217-227.
    • (2002) Eur Biophys J , vol.31 , pp. 217-227
    • Faraldo-Gomez, J.D.1    Smith, G.R.2    Sansom, M.S.3
  • 39
    • 0344236133 scopus 로고    scopus 로고
    • Lipid/protein interactions and the membrane/water interfacial region
    • Domene C, Bond PJ, Deol SS, Sansom MS. Lipid/protein interactions and the membrane/water interfacial region. J Am Chem Soc 2003;125:14966-14967.
    • (2003) J Am Chem Soc , vol.125 , pp. 14966-14967
    • Domene, C.1    Bond, P.J.2    Deol, S.S.3    Sansom, M.S.4
  • 40
    • 0027956509 scopus 로고
    • Structure of membrane-bound human Factor Va
    • Stoylova S, Mann KG, Brisson A. Structure of membrane-bound human Factor Va. FEBS Lett 1994;351:330-334.
    • (1994) FEBS Lett , vol.351 , pp. 330-334
    • Stoylova, S.1    Mann, K.G.2    Brisson, A.3
  • 41
    • 33745590809 scopus 로고    scopus 로고
    • Lipid-peptide interactions investigated by NMR
    • Gawrisch K, Koenig BW. Lipid-peptide interactions investigated by NMR. Curr Topics Membranes 2002;52:163-190.
    • (2002) Curr Topics Membranes , vol.52 , pp. 163-190
    • Gawrisch, K.1    Koenig, B.W.2
  • 42
    • 0036639910 scopus 로고    scopus 로고
    • Parameter optimized surfaces (POPS): Analysis of key interactions and conformational changes in the ribosome
    • Fraternali F, Cavallo L. Parameter optimized surfaces (POPS): analysis of key interactions and conformational changes in the ribosome. Nucleic Acids Res 2002;30:2950-2960.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2950-2960
    • Fraternali, F.1    Cavallo, L.2
  • 43
    • 23144459432 scopus 로고    scopus 로고
    • POPSCOMP: An automated interaction analysis of biomolecular complexes
    • Kleinjung J, Fraternali F. POPSCOMP: an automated interaction analysis of biomolecular complexes. Nucleic Acids Res 2005;33:W342-346.
    • (2005) Nucleic Acids Res , vol.33
    • Kleinjung, J.1    Fraternali, F.2
  • 44
    • 0347319167 scopus 로고    scopus 로고
    • Theoretical and experimental study of the D2194G mutation in the C2 domain of coagulation Factor V
    • Miteva MA, Brugge JM, Rosing J, Nicolaes GA, Villoutreix BO. Theoretical and experimental study of the D2194G mutation in the C2 domain of coagulation Factor V. Biophys J 2004;86:488-498.
    • (2004) Biophys J , vol.86 , pp. 488-498
    • Miteva, M.A.1    Brugge, J.M.2    Rosing, J.3    Nicolaes, G.A.4    Villoutreix, B.O.5
  • 45
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White SH, Wimley WC. Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct 1999;28:319-365.
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 46
    • 0034703270 scopus 로고    scopus 로고
    • Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: Molecular dynamics calculations
    • Petrache HI, Grossfield A, MacKenzie KR, Engelman DM, Woolf TB. Modulation of glycophorin A transmembrane helix interactions by lipid bilayers: molecular dynamics calculations. J Mol Biol 2000;302:727-746.
    • (2000) J Mol Biol , vol.302 , pp. 727-746
    • Petrache, H.I.1    Grossfield, A.2    MacKenzie, K.R.3    Engelman, D.M.4    Woolf, T.B.5
  • 47
    • 0011613265 scopus 로고    scopus 로고
    • Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane
    • Berneche S, Nina M, Roux B. Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane. Biophys J 1998;75:1603-1618.
    • (1998) Biophys J , vol.75 , pp. 1603-1618
    • Berneche, S.1    Nina, M.2    Roux, B.3
  • 48
    • 14844365793 scopus 로고    scopus 로고
    • Efficacy of soluble phospholipids in the prothrombinase reaction
    • Stone MD, Nelsestuen GL. Efficacy of soluble phospholipids in the prothrombinase reaction. Biochemistry 2005;44:4037-4041.
    • (2005) Biochemistry , vol.44 , pp. 4037-4041
    • Stone, M.D.1    Nelsestuen, G.L.2
  • 49
    • 0032467348 scopus 로고    scopus 로고
    • Homology models of the C domains of blood coagulation Factors V and VIII: A proposed membrane binding mode for FV and FVIII C2 domains
    • Pellequer JL, Gale AJ, Griffin JH, Getzoff ED. Homology models of the C domains of blood coagulation Factors V and VIII: a proposed membrane binding mode for FV and FVIII C2 domains. Blood Cells Mol Dis 1998;24:448-461.
    • (1998) Blood Cells Mol Dis , vol.24 , pp. 448-461
    • Pellequer, J.L.1    Gale, A.J.2    Griffin, J.H.3    Getzoff, E.D.4
  • 50
    • 0033709870 scopus 로고    scopus 로고
    • Three-dimensional model of coagulation Factor Va bound to activated protein C
    • Pellequer JL, Gale AJ, Getzoff ED, Griffin JH. Three-dimensional model of coagulation Factor Va bound to activated protein C. Thromb Haemost 2000;84:849-857.
    • (2000) Thromb Haemost , vol.84 , pp. 849-857
    • Pellequer, J.L.1    Gale, A.J.2    Getzoff, E.D.3    Griffin, J.H.4
  • 51
    • 12144254763 scopus 로고    scopus 로고
    • The phosphatidylserine binding site of the Factor Va C2 domain accounts for membrane binding but does not contribute to the assembly or activity of a human factor Xa-factor Va complex
    • Majumder R, Quinn-Allen MA, Kane WH, Lentz BR. The phosphatidylserine binding site of the Factor Va C2 domain accounts for membrane binding but does not contribute to the assembly or activity of a human factor Xa-factor Va complex. Biochemistry 2005;44:711-718.
    • (2005) Biochemistry , vol.44 , pp. 711-718
    • Majumder, R.1    Quinn-Allen, M.A.2    Kane, W.H.3    Lentz, B.R.4
  • 52
    • 0027957287 scopus 로고
    • Electrostatic and hydrophobic interactions are involved in Factor Va binding to membranes containing acidic phospholipids
    • Lecompte MF, Bouix G, Mann KG. Electrostatic and hydrophobic interactions are involved in Factor Va binding to membranes containing acidic phospholipids. J Biol Chem 1994;269:1905-1910.
    • (1994) J Biol Chem , vol.269 , pp. 1905-1910
    • Lecompte, M.F.1    Bouix, G.2    Mann, K.G.3
  • 53
    • 0001252591 scopus 로고    scopus 로고
    • Identification of functionally important amino acid residues within the C2-domain of human Factor V using alanine-scanning mutagenesis
    • Kim SW, Quinn-Allen MA, Camp JT, et al. Identification of functionally important amino acid residues within the C2-domain of human Factor V using alanine-scanning mutagenesis. Biochemistry 2000;39:1951-1958.
    • (2000) Biochemistry , vol.39 , pp. 1951-1958
    • Kim, S.W.1    Quinn-Allen, M.A.2    Camp, J.T.3
  • 54
    • 1542285301 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a palmitoyl-oleoyl phosphatidylserine bilayer with Na+ counterions and NaCl
    • Mukhopadhyay P, Monticelli L, Tieleman DP. Molecular dynamics simulation of a palmitoyl-oleoyl phosphatidylserine bilayer with Na+ counterions and NaCl. Biophys J 2004;86:1601-1609.
    • (2004) Biophys J , vol.86 , pp. 1601-1609
    • Mukhopadhyay, P.1    Monticelli, L.2    Tieleman, D.P.3
  • 55
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau WM, Wimley WC, Gawrisch K, White SH. The preference of tryptophan for membrane interfaces. Biochemistry 1998;37:14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 56
    • 12344330612 scopus 로고    scopus 로고
    • A study of the membrane-water interface region of membrane proteins
    • Granseth E, von Heijne G, Elofsson A. A study of the membrane-water interface region of membrane proteins. J Mol Biol 2005;346:377-385.
    • (2005) J Mol Biol , vol.346 , pp. 377-385
    • Granseth, E.1    Von Heijne, G.2    Elofsson, A.3
  • 57
    • 1842426740 scopus 로고    scopus 로고
    • Trp2063 and Trp2064 in the Factor Va C2 domain are required for high-affinity binding to phospholipid membranes but not for assembly of the prothrombinase complex
    • Peng W, Quinn-Allen MA, Kim SW, Alexander KA, Kane WH. Trp2063 and Trp2064 in the Factor Va C2 domain are required for high-affinity binding to phospholipid membranes but not for assembly of the prothrombinase complex. Biochemistry 2004;43:4385-4393.
    • (2004) Biochemistry , vol.43 , pp. 4385-4393
    • Peng, W.1    Quinn-Allen, M.A.2    Kim, S.W.3    Alexander, K.A.4    Kane, W.H.5
  • 58
    • 0035901553 scopus 로고    scopus 로고
    • Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: A surface plasmon resonance study on phospholipases A2
    • Stahelin RV, Cho W. Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: a surface plasmon resonance study on phospholipases A2. Biochemistry 2001;40:4672-4678.
    • (2001) Biochemistry , vol.40 , pp. 4672-4678
    • Stahelin, R.V.1    Cho, W.2
  • 59
    • 2342544065 scopus 로고    scopus 로고
    • Snorkeling preferences foster an amino acid composition bias in transmembrane helices
    • Chamberlain AK, Lee Y, Kim S, Bowie JU. Snorkeling preferences foster an amino acid composition bias in transmembrane helices. J Mol Biol 2004;339:471-479.
    • (2004) J Mol Biol , vol.339 , pp. 471-479
    • Chamberlain, A.K.1    Lee, Y.2    Kim, S.3    Bowie, J.U.4
  • 60
    • 0038694994 scopus 로고    scopus 로고
    • Snorkeling of lysine side chains in transmembrane helices: How easy can it get?
    • Strandberg E, Killian JA. Snorkeling of lysine side chains in transmembrane helices: how easy can it get? FEBS Lett 2003;544:69-73.
    • (2003) FEBS Lett , vol.544 , pp. 69-73
    • Strandberg, E.1    Killian, J.A.2
  • 61
    • 0035901553 scopus 로고    scopus 로고
    • Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: A surface plasmon resonance study on phospholipases A2
    • Stahelin RV, Cho W. Differential roles of ionic, aliphatic, and aromatic residues in membrane-protein interactions: a surface plasmon resonance study on phospholipases A2. Biochemistry 2001;40:4672-4678.
    • (2001) Biochemistry , vol.40 , pp. 4672-4678
    • Stahelin, R.V.1    Cho, W.2
  • 62
    • 2942669901 scopus 로고    scopus 로고
    • The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function
    • Adams TE, Hockin MF, Mann KG, Everse SJ. The crystal structure of activated protein C-inactivated bovine factor Va: implications for cofactor function. Proc Natl Acad Sci U S A 2004;101:8918-8923.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8918-8923
    • Adams, T.E.1    Hockin, M.F.2    Mann, K.G.3    Everse, S.J.4
  • 63
    • 5444228851 scopus 로고    scopus 로고
    • Disruption of protein-membrane binding and identification of small-molecule inhibitors of coagulation factor VIII
    • Spiegel PC, Kaiser SM, Simon JA, Stoddard BL. Disruption of protein-membrane binding and identification of small-molecule inhibitors of coagulation factor VIII. Chem Biol 2004;11:1413-1422.
    • (2004) Chem Biol , vol.11 , pp. 1413-1422
    • Spiegel, P.C.1    Kaiser, S.M.2    Simon, J.A.3    Stoddard, B.L.4
  • 65
    • 0032757340 scopus 로고    scopus 로고
    • Study of the electrostatics treatment in molecular dynamics simulations
    • Garemyr R, Elofsson A. Study of the electrostatics treatment in molecular dynamics simulations. Proteins 1999;37:417-428.
    • (1999) Proteins , vol.37 , pp. 417-428
    • Garemyr, R.1    Elofsson, A.2


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