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Volumn 80, Issue 4, 2012, Pages 1066-1077

Conformational dynamics of capping protein and interaction partners: Simulation studies

Author keywords

Actin polymerization; Allostery; Capping protein interacting (CPI); CARMIL; Conformational shift; Electrostatic; Myotrophin; Protein protein interaction; V 1; V1

Indexed keywords

ACTIN CAPPING PROTEIN; RECOMBINANT SOMATOMEDIN C;

EID: 84857786911     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24008     Document Type: Article
Times cited : (10)

References (72)
  • 1
    • 0029954225 scopus 로고    scopus 로고
    • Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein
    • Barkalow K, Witke W, Kwiatkowski DJ, Hartwig JH. Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. J Cell Biol 1996; 134: 389-399.
    • (1996) J Cell Biol , vol.134 , pp. 389-399
    • Barkalow, K.1    Witke, W.2    Kwiatkowski, D.J.3    Hartwig, J.H.4
  • 2
    • 48949106158 scopus 로고    scopus 로고
    • New insights into mechanism and regulation of actin capping protein
    • Cooper JA, Sept D. New insights into mechanism and regulation of actin capping protein. Int Rev Cell Mol Biol 2008; 267: 183-206.
    • (2008) Int Rev Cell Mol Biol , vol.267 , pp. 183-206
    • Cooper, J.A.1    Sept, D.2
  • 3
    • 0019256032 scopus 로고
    • An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions
    • Isenberg G, Aebi U, Pollard TD. An actin-binding protein from Acanthamoeba regulates actin filament polymerization and interactions. Nature 1980; 288: 455-459.
    • (1980) Nature , vol.288 , pp. 455-459
    • Isenberg, G.1    Aebi, U.2    Pollard, T.D.3
  • 5
    • 0042420366 scopus 로고    scopus 로고
    • How capping protein binds the barbed end of the actin filament
    • Wear MA, Yamashita A, Kim K, Maeda Y, Cooper JA. How capping protein binds the barbed end of the actin filament. Curr Biol 2003; 13: 1531-1537.
    • (2003) Curr Biol , vol.13 , pp. 1531-1537
    • Wear, M.A.1    Yamashita, A.2    Kim, K.3    Maeda, Y.4    Cooper, J.A.5
  • 6
    • 0023372284 scopus 로고
    • Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
    • Casella JF, Craig SW, Maack DJ, Brown AE. Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle. J Cell Biol 1987; 105: 371-379.
    • (1987) J Cell Biol , vol.105 , pp. 371-379
    • Casella, J.F.1    Craig, S.W.2    Maack, D.J.3    Brown, A.E.4
  • 7
    • 0027178964 scopus 로고
    • Localization of CapZ during myofibrillogenesis in cultured chicken muscle
    • Schafer DA, Waddle JA, Cooper JA. Localization of CapZ during myofibrillogenesis in cultured chicken muscle. Cell Motil Cytoskeleton 1993; 25: 317-335.
    • (1993) Cell Motil Cytoskeleton , vol.25 , pp. 317-335
    • Schafer, D.A.1    Waddle, J.A.2    Cooper, J.A.3
  • 8
    • 0026772439 scopus 로고
    • Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation
    • Schafer DA, Mooseker MS, Cooper JA. Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation. J Cell Biol 1992; 118: 335-346.
    • (1992) J Cell Biol , vol.118 , pp. 335-346
    • Schafer, D.A.1    Mooseker, M.S.2    Cooper, J.A.3
  • 9
    • 0026686092 scopus 로고
    • Purification, characterization, and immunofluorescence localization of Saccharomyces cerevisiae capping protein
    • Amatruda JF, Cooper JA. Purification, characterization, and immunofluorescence localization of Saccharomyces cerevisiae capping protein. J Cell Biol 1992; 117: 1067-1076.
    • (1992) J Cell Biol , vol.117 , pp. 1067-1076
    • Amatruda, J.F.1    Cooper, J.A.2
  • 10
    • 33751567905 scopus 로고    scopus 로고
    • Structural basis of actin filament capping at the barbed-end: a cryo-electron microscopy study
    • Narita A, Takeda S, Yamashita A, Maeda Y. Structural basis of actin filament capping at the barbed-end: a cryo-electron microscopy study. EMBO J 2006; 25: 5626-5633.
    • (2006) EMBO J , vol.25 , pp. 5626-5633
    • Narita, A.1    Takeda, S.2    Yamashita, A.3    Maeda, Y.4
  • 11
    • 33845700946 scopus 로고    scopus 로고
    • Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing
    • Miyoshi T, Tsuji T, Higashida C, Hertzog M, Fujita A, Narumiya S, Scita G, Watanabe N. Actin turnover-dependent fast dissociation of capping protein in the dendritic nucleation actin network: evidence of frequent filament severing. J Cell Biol 2006; 175: 947-955.
    • (2006) J Cell Biol , vol.175 , pp. 947-955
    • Miyoshi, T.1    Tsuji, T.2    Higashida, C.3    Hertzog, M.4    Fujita, A.5    Narumiya, S.6    Scita, G.7    Watanabe, N.8
  • 12
    • 34948838501 scopus 로고    scopus 로고
    • Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins
    • Kuhn JR, Pollard TD. Single molecule kinetic analysis of actin filament capping. Polyphosphoinositides do not dissociate capping proteins. J Biol Chem 2007; 282: 28014-28024.
    • (2007) J Biol Chem , vol.282 , pp. 28014-28024
    • Kuhn, J.R.1    Pollard, T.D.2
  • 13
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides
    • Schafer DA, Jennings PB, Cooper JA. Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides. J Cell Biol 1996; 135: 169-179.
    • (1996) J Cell Biol , vol.135 , pp. 169-179
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 14
    • 34247173028 scopus 로고    scopus 로고
    • Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actin-capping protein: implications for how capping protein binds the actin filament
    • Kim K, McCully ME, Bhattacharya N, Butler B, Sept D, Cooper JA. Structure/function analysis of the interaction of phosphatidylinositol 4, 5-bisphosphate with actin-capping protein: implications for how capping protein binds the actin filament. J Biol Chem 2007; 282: 5871-5879.
    • (2007) J Biol Chem , vol.282 , pp. 5871-5879
    • Kim, K.1    McCully, M.E.2    Bhattacharya, N.3    Butler, B.4    Sept, D.5    Cooper, J.A.6
  • 15
    • 17644371009 scopus 로고    scopus 로고
    • The pleckstrin homology domain-containing protein CKIP-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein
    • Canton DA, Olsten ME, Kim K, Doherty-Kirby A, Lajoie G, Cooper JA, Litchfield DW. The pleckstrin homology domain-containing protein CKIP-1 is involved in regulation of cell morphology and the actin cytoskeleton and interaction with actin capping protein. Mol Cell Biol 2005; 25: 3519-3534.
    • (2005) Mol Cell Biol , vol.25 , pp. 3519-3534
    • Canton, D.A.1    Olsten, M.E.2    Kim, K.3    Doherty-Kirby, A.4    Lajoie, G.5    Cooper, J.A.6    Litchfield, D.W.7
  • 16
    • 0037590956 scopus 로고    scopus 로고
    • Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85
    • Hutchings NJ, Clarkson N, Chalkley R, Barclay AN, Brown MH. Linking the T cell surface protein CD2 to the actin-capping protein CAPZ via CMS and CIN85. J Biol Chem 2003; 278: 22396-22403.
    • (2003) J Biol Chem , vol.278 , pp. 22396-22403
    • Hutchings, N.J.1    Clarkson, N.2    Chalkley, R.3    Barclay, A.N.4    Brown, M.H.5
  • 17
    • 0037458625 scopus 로고    scopus 로고
    • V-1, a protein expressed transiently during murine cerebellar development, regulates actin polymerization via interaction with capping protein
    • Taoka M, Ichimura T, Wakamiya-Tsuruta A, Kubota Y, Araki T, Obinata T, Isobe T. V-1, a protein expressed transiently during murine cerebellar development, regulates actin polymerization via interaction with capping protein. J Biol Chem 2003; 278: 5864-5870.
    • (2003) J Biol Chem , vol.278 , pp. 5864-5870
    • Taoka, M.1    Ichimura, T.2    Wakamiya-Tsuruta, A.3    Kubota, Y.4    Araki, T.5    Obinata, T.6    Isobe, T.7
  • 18
    • 22144462425 scopus 로고    scopus 로고
    • The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ
    • Eyers CE, McNeill H, Knebel A, Morrice N, Arthur SJ, Cuenda A, Cohen P. The phosphorylation of CapZ-interacting protein (CapZIP) by stress-activated protein kinases triggers its dissociation from CapZ. Biochem J 2005; 389(Part 1): 127-135.
    • (2005) Biochem J , vol.389 , Issue.PART. 1 , pp. 127-135
    • Eyers, C.E.1    McNeill, H.2    Knebel, A.3    Morrice, N.4    Arthur, S.J.5    Cuenda, A.6    Cohen, P.7
  • 20
    • 0032524455 scopus 로고    scopus 로고
    • The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin
    • Yang Y, Nanduri S, Sen S, Qin J. The structural basis of ankyrin-like repeat function as revealed by the solution structure of myotrophin. Structure 1998; 6: 619-626.
    • (1998) Structure , vol.6 , pp. 619-626
    • Yang, Y.1    Nanduri, S.2    Sen, S.3    Qin, J.4
  • 25
    • 0029928608 scopus 로고    scopus 로고
    • Changes in the gene expression of a protein with the cdc10/SWI6 motif, V-1, during rat follicular development and corpus luteum formation
    • Song SY, Asakai R, Kenmotsu N, Taoka M, Isobe T, Yamakuni T. Changes in the gene expression of a protein with the cdc10/SWI6 motif, V-1, during rat follicular development and corpus luteum formation. Endocrinology 1996; 137: 1423-1428.
    • (1996) Endocrinology , vol.137 , pp. 1423-1428
    • Song, S.Y.1    Asakai, R.2    Kenmotsu, N.3    Taoka, M.4    Isobe, T.5    Yamakuni, T.6
  • 26
    • 0035954433 scopus 로고    scopus 로고
    • The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains
    • Jung G, Remmert K, Wu X, Volosky JM, Hammer JA, III. The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains. J Cell Biol 2001; 153: 1479-1497.
    • (2001) J Cell Biol , vol.153 , pp. 1479-1497
    • Jung, G.1    Remmert, K.2    Wu, X.3    Volosky, J.M.4    Hammer III, J.A.5
  • 27
    • 33744521654 scopus 로고    scopus 로고
    • CARMIL is a potent capping protein antagonist: identification of a conserved CARMIL domain that inhibits the activity of capping protein and uncaps capped actin filaments
    • Uruno T, Remmert K, Hammer JA, III. CARMIL is a potent capping protein antagonist: identification of a conserved CARMIL domain that inhibits the activity of capping protein and uncaps capped actin filaments. J Biol Chem 2006; 281: 10635-10650.
    • (2006) J Biol Chem , vol.281 , pp. 10635-10650
    • Uruno, T.1    Remmert, K.2    Hammer III, J.A.3
  • 28
    • 0037010186 scopus 로고    scopus 로고
    • CIN85/CMS family of adaptor molecules
    • Dikic I. CIN85/CMS family of adaptor molecules. FEBS Lett 2002; 529: 110-115.
    • (2002) FEBS Lett , vol.529 , pp. 110-115
    • Dikic, I.1
  • 29
    • 33750063180 scopus 로고    scopus 로고
    • Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end
    • Bhattacharya N, Ghosh S, Sept D, Cooper JA. Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. J Biol Chem 2006; 281: 31021-31030.
    • (2006) J Biol Chem , vol.281 , pp. 31021-31030
    • Bhattacharya, N.1    Ghosh, S.2    Sept, D.3    Cooper, J.A.4
  • 31
    • 77955488192 scopus 로고    scopus 로고
    • Structural basis for capping protein sequestration by myotrophin (V-1)
    • Zwolak A, Fujiwara I, Hammer JA, III, Tjandra N. Structural basis for capping protein sequestration by myotrophin (V-1). J Biol Chem 2010; 285: 25767-25781.
    • (2010) J Biol Chem , vol.285 , pp. 25767-25781
    • Zwolak, A.1    Fujiwara, I.2    Hammer III, J.A.3    Tjandra, N.4
  • 32
    • 77449152025 scopus 로고    scopus 로고
    • Direct observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain 3
    • Fujiwara I, Remmert K, Hammer JA, III. Direct observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain 3. J Biol Chem 2010; 285: 2707-2720.
    • (2010) J Biol Chem , vol.285 , pp. 2707-2720
    • Fujiwara, I.1    Remmert, K.2    Hammer III, J.A.3
  • 33
    • 79956194275 scopus 로고    scopus 로고
    • Actin capping protein and its inhibitor CARMIL: how intrinsically disordered regions function
    • Takeda S, Koike R, Nitanai Y, Minakata S, Maeda Y, Ota M. Actin capping protein and its inhibitor CARMIL: how intrinsically disordered regions function. Phys Biol 2011; 8:035005.
    • (2011) Phys Biol , vol.8 , pp. 035005
    • Takeda, S.1    Koike, R.2    Nitanai, Y.3    Minakata, S.4    Maeda, Y.5    Ota, M.6
  • 34
    • 78649529338 scopus 로고    scopus 로고
    • The interaction of capping protein with the barbed end of the actin filament
    • Kim T, Cooper JA, Sept D. The interaction of capping protein with the barbed end of the actin filament. J Mol Biol 2010; 404: 794-802.
    • (2010) J Mol Biol , vol.404 , pp. 794-802
    • Kim, T.1    Cooper, J.A.2    Sept, D.3
  • 35
    • 0037387121 scopus 로고    scopus 로고
    • Crystal structure of CapZ: structural basis for actin filament barbed end capping
    • Yamashita A, Maeda K, Maeda Y. Crystal structure of CapZ: structural basis for actin filament barbed end capping. EMBO J 2003; 22: 1529-1538.
    • (2003) EMBO J , vol.22 , pp. 1529-1538
    • Yamashita, A.1    Maeda, K.2    Maeda, Y.3
  • 36
    • 59549088662 scopus 로고    scopus 로고
    • ProtorP: a protein-protein interaction analysis server
    • Reynolds C, Damerell D, Jones S. ProtorP: a protein-protein interaction analysis server. Bioinformatics 2009; 25: 413-414.
    • (2009) Bioinformatics , vol.25 , pp. 413-414
    • Reynolds, C.1    Damerell, D.2    Jones, S.3
  • 37
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007; 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 39
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: an automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations
    • Dolinsky TJ, JE Jen, McCammon JA, Baker NA. PDB2PQR: an automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 2004; 32: W665-W667.
    • (2004) Nucleic Acids Res , vol.32
    • Dolinsky, T.J.1    Jen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 40
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, Simmerling C. Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 2006; 65: 712-725.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 43
    • 33846823909 scopus 로고
    • Particle mesh Ewald-an NlogN method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle mesh Ewald-an NlogN 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
  • 44
    • 84946450438 scopus 로고
    • Algorithms for macromolecular dynamics and constraint dynamics
    • van Gunsteren WF, Berendsen HJ. Algorithms for macromolecular dynamics and constraint dynamics. Molecular Physics 1977; 34: 1311-1327.
    • (1977) Molecular Physics , vol.34 , pp. 1311-1327
    • van Gunsteren, W.F.1    Berendsen, H.J.2
  • 47
    • 0032560959 scopus 로고    scopus 로고
    • Continuum Solvent Studies of the Stability of DNA, RNA, and Phosphoramidate-DNA Helices
    • Srinivasan J, Cheatham ITE, Cieplak P, Kollman PA, Case DA. Continuum Solvent Studies of the Stability of DNA, RNA, and Phosphoramidate-DNA Helices. J Am Chem Soc 1998; 120: 9401-9408.
    • (1998) J Am Chem Soc , vol.120 , pp. 9401-9408
    • Srinivasan, J.1    Cheatham, I.T.E.2    Cieplak, P.3    Kollman, P.A.4    Case, D.A.5
  • 49
    • 14244273182 scopus 로고    scopus 로고
    • Theory and applications of the generalized Born solvation model in macromolecular simulations
    • Tsui V, Case DA. Theory and applications of the generalized Born solvation model in macromolecular simulations. Biopolymers 2000; 56: 275-291.
    • (2000) Biopolymers , vol.56 , pp. 275-291
    • Tsui, V.1    Case, D.A.2
  • 50
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser J, Shenkin PS, Still WC. Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO). J Comp Chem 1999; 20: 217-230.
    • (1999) J Comp Chem , vol.20 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 51
    • 0035928796 scopus 로고    scopus 로고
    • Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism
    • Osborne MJ, Schnell J, Benkovic SJ, Dyson HJ, Wright PE. Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. Biochemistry 2001; 40: 9846-9859.
    • (2001) Biochemistry , vol.40 , pp. 9846-9859
    • Osborne, M.J.1    Schnell, J.2    Benkovic, S.J.3    Dyson, H.J.4    Wright, P.E.5
  • 52
    • 47349099470 scopus 로고    scopus 로고
    • Mapping of two networks of residues that exhibit structural and dynamical changes upon binding in a PDZ domain protein
    • Dhulesia A, Gsponer J, Vendruscolo M. Mapping of two networks of residues that exhibit structural and dynamical changes upon binding in a PDZ domain protein. J Am Chem Soc 2008; 130: 8931-8939.
    • (2008) J Am Chem Soc , vol.130 , pp. 8931-8939
    • Dhulesia, A.1    Gsponer, J.2    Vendruscolo, M.3
  • 54
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui Q, Karplus M. Allostery and cooperativity revisited. Protein Sci 2008; 17: 1295-1307.
    • (2008) Protein Sci , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 55
    • 76249122268 scopus 로고    scopus 로고
    • An ensemble view of allostery
    • Hilser VJ. An ensemble view of allostery. Science 2010; 327: 653-654.
    • (2010) Science , vol.327 , pp. 653-654
    • Hilser, V.J.1
  • 56
    • 32344434479 scopus 로고    scopus 로고
    • The changing landscape of protein allostery
    • Swain JF, Gierasch LM. The changing landscape of protein allostery. Curr Opin Struct Biol 2006; 16: 102-108.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 102-108
    • Swain, J.F.1    Gierasch, L.M.2
  • 57
    • 67349126528 scopus 로고    scopus 로고
    • The structural basis of allosteric regulation in proteins
    • Laskowski RA, Gerick F, Thornton JM. The structural basis of allosteric regulation in proteins. FEBS Lett 2009; 583: 1692-1698.
    • (2009) FEBS Lett , vol.583 , pp. 1692-1698
    • Laskowski, R.A.1    Gerick, F.2    Thornton, J.M.3
  • 58
    • 79959429733 scopus 로고    scopus 로고
    • Protein regulation: the statistical theory of allostery
    • Vendruscolo M. Protein regulation: the statistical theory of allostery. Nat Chem Biol 2011; 7: 411-412.
    • (2011) Nat Chem Biol , vol.7 , pp. 411-412
    • Vendruscolo, M.1
  • 59
    • 0029586726 scopus 로고
    • Essential dynamics of the cellular retinol-binding protein-evidence for ligand-induced conformational changes
    • van Aalten DM, Findlay JB, Amadei A, Berendsen HJ. Essential dynamics of the cellular retinol-binding protein-evidence for ligand-induced conformational changes. Protein Eng 1995; 8: 1129-1135.
    • (1995) Protein Eng , vol.8 , pp. 1129-1135
    • van Aalten, D.M.1    Findlay, J.B.2    Amadei, A.3    Berendsen, H.J.4
  • 60
    • 44649199260 scopus 로고    scopus 로고
    • Mapping the nucleotide and isoform-dependent structural and dynamical features of Ras proteins
    • Gorfe AA, Grant BJ, McCammon JA. Mapping the nucleotide and isoform-dependent structural and dynamical features of Ras proteins. Structure 2008; 16: 885-896.
    • (2008) Structure , vol.16 , pp. 885-896
    • Gorfe, A.A.1    Grant, B.J.2    McCammon, J.A.3
  • 62
    • 38949218425 scopus 로고    scopus 로고
    • Close correspondence between the motions from principal component analysis of multiple HIV-1 protease structures and elastic network modes
    • Yang L, Song G, Carriquiry A, Jernigan RL. Close correspondence between the motions from principal component analysis of multiple HIV-1 protease structures and elastic network modes. Structure 2008; 16: 321-330.
    • (2008) Structure , vol.16 , pp. 321-330
    • Yang, L.1    Song, G.2    Carriquiry, A.3    Jernigan, R.L.4
  • 64
    • 0031910020 scopus 로고    scopus 로고
    • Locally accessible conformations of proteins: multiple molecular dynamics simulations of crambin
    • Caves LS, Evanseck JD, Karplus M. Locally accessible conformations of proteins: multiple molecular dynamics simulations of crambin. Protein Sci 1998; 7: 649-666.
    • (1998) Protein Sci , vol.7 , pp. 649-666
    • Caves, L.S.1    Evanseck, J.D.2    Karplus, M.3
  • 65
    • 70149090164 scopus 로고    scopus 로고
    • The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding
    • Bakan A, Bahar I. The intrinsic dynamics of enzymes plays a dominant role in determining the structural changes induced upon inhibitor binding. Proc Natl Acad Sci USA 2009; 106: 14349-14354.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14349-14354
    • Bakan, A.1    Bahar, I.2
  • 67
    • 40949105259 scopus 로고    scopus 로고
    • Signal transduction via unstructured protein conduits
    • Dunker AK, Uversky VN. Signal transduction via unstructured protein conduits. Nat Chem Biol 2008; 4: 229-230.
    • (2008) Nat Chem Biol , vol.4 , pp. 229-230
    • Dunker, A.K.1    Uversky, V.N.2
  • 68
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N, Gammeltoft S, Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 1999; 294: 1351-1362.
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 72
    • 79551571786 scopus 로고    scopus 로고
    • Predicting novel binding modes of agonists to beta adrenergic receptors using all-atom molecular dynamics simulations
    • Vanni S, Neri M, Tavernelli I, Rothlisberger U. Predicting novel binding modes of agonists to beta adrenergic receptors using all-atom molecular dynamics simulations. PLoS Comput Biol 2011; 7: e1001053.
    • (2011) PLoS Comput Biol , vol.7
    • Vanni, S.1    Neri, M.2    Tavernelli, I.3    Rothlisberger, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.