메뉴 건너뛰기




Volumn 111, Issue 43, 2014, Pages E4596-E4605

Structural basis of thymosin-β4/profilin exchange leading to actin filament polymerization

Author keywords

Crystallography; Fluorescence; Molecular dynamics; Protein complex; Thermodynamics

Indexed keywords

ACTIN; G ACTIN; PROFILIN; THYMOSIN BETA4; THYMOSIN; THYMOSIN BETA(4);

EID: 84908274470     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1412271111     Document Type: Article
Times cited : (75)

References (75)
  • 1
    • 0022881322 scopus 로고
    • Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments
    • Pollard TD (1986) Rate constants for the reactions of ATP- and ADP-actin with the ends of actin filaments. J Cell Biol 103(6 Pt 2):2747-2754.
    • (1986) J Cell Biol , vol.103 , Issue.6 , pp. 2747-2754
    • Pollard, T.D.1
  • 2
    • 62849096355 scopus 로고    scopus 로고
    • F- and G-actin concentrations in lamellipodia of moving cells
    • Koestler SA, et al. (2009) F- and G-actin concentrations in lamellipodia of moving cells. PLoS ONE 4(3):e4810.
    • (2009) PLoS ONE , vol.4 , Issue.3 , pp. e4810
    • Koestler, S.A.1
  • 3
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112(4):453-465.
    • (2003) Cell , vol.112 , Issue.4 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 4
    • 0037378124 scopus 로고    scopus 로고
    • Actin binding proteins: Regulation of cytoskeletal microfilaments
    • dos Remedios CG, et al. (2003) Actin binding proteins: Regulation of cytoskeletal microfilaments. Physiol Rev 83(2):433-473.
    • (2003) Physiol Rev , vol.83 , Issue.2 , pp. 433-473
    • Dos Remedios, C.G.1
  • 5
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: Cellular control of actin assembly
    • Campellone KG, Welch MD (2010) A nucleator arms race: Cellular control of actin assembly. Nat Rev Mol Cell Biol 11(4):237-251.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.4 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 6
    • 70450245305 scopus 로고    scopus 로고
    • Actin filament nucleation and elongation factors-structurefunction relationships
    • Dominguez R (2009) Actin filament nucleation and elongation factors-structurefunction relationships. Crit Rev Biochem Mol Biol 44(6):351-366.
    • (2009) Crit Rev Biochem Mol Biol , vol.44 , Issue.6 , pp. 351-366
    • Dominguez, R.1
  • 7
    • 0033601258 scopus 로고    scopus 로고
    • Profilin promotes barbed-end actin filament assembly without lowering the critical concentration
    • Kang F, Purich DL, Southwick FS (1999) Profilin promotes barbed-end actin filament assembly without lowering the critical concentration. J Biol Chem 274(52):36963-36972.
    • (1999) J Biol Chem , vol.274 , Issue.52 , pp. 36963-36972
    • Kang, F.1    Purich, D.L.2    Southwick, F.S.3
  • 8
    • 0027163104 scopus 로고
    • Modulation of the interaction between G-actin and thymosin beta 4 by the ATP/ADP ratio: Possible implication in the regulation of actin dynamics
    • Carlier MF, Jean C, Rieger KJ, Lenfant M, Pantaloni D (1993) Modulation of the interaction between G-actin and thymosin beta 4 by the ATP/ADP ratio: Possible implication in the regulation of actin dynamics. Proc Natl Acad Sci USA 90(11):5034-5038.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.11 , pp. 5034-5038
    • Carlier, M.F.1    Jean, C.2    Rieger, K.J.3    Lenfant, M.4    Pantaloni, D.5
  • 9
    • 4043074223 scopus 로고    scopus 로고
    • Effects of profilin and thymosin beta4 on the critical concentration of actin demonstrated in vitro and in cell extracts with a novel direct assay
    • Yarmola EG, Bubb MR (2004) Effects of profilin and thymosin beta4 on the critical concentration of actin demonstrated in vitro and in cell extracts with a novel direct assay. J Biol Chem 279(32):33519-33527.
    • (2004) J Biol Chem , vol.279 , Issue.32 , pp. 33519-33527
    • Yarmola, E.G.1    Bubb, M.R.2
  • 10
    • 0026708551 scopus 로고
    • Interaction of thymosin beta 4 with muscle and platelet actin: Implications for actin sequestration in resting platelets
    • Weber A, Nachmias VT, Pennise CR, Pring M, Safer D (1992) Interaction of thymosin beta 4 with muscle and platelet actin: Implications for actin sequestration in resting platelets. Biochemistry 31(27):6179-6185.
    • (1992) Biochemistry , vol.31 , Issue.27 , pp. 6179-6185
    • Weber, A.1    Nachmias, V.T.2    Pennise, C.R.3    Pring, M.4    Safer, D.5
  • 11
    • 0027510119 scopus 로고
    • Thymosin beta 10 and thymosin beta 4 are both actin monomer sequestering proteins
    • Yu FX, Lin SC, Morrison-Bogorad M, Atkinson MA, Yin HL (1993) Thymosin beta 10 and thymosin beta 4 are both actin monomer sequestering proteins. J Biol Chem 268(1):502-509.
    • (1993) J Biol Chem , vol.268 , Issue.1 , pp. 502-509
    • Yu, F.X.1    Lin, S.C.2    Morrison-Bogorad, M.3    Atkinson, M.A.4    Yin, H.L.5
  • 13
    • 0025340881 scopus 로고
    • The actin released from profilin-actin complexes is insufficient to account for the increase in F-actin in chemoattractant-stimulated polymorphonuclear leukocytes
    • Southwick FS, Young CL (1990) The actin released from profilin-actin complexes is insufficient to account for the increase in F-actin in chemoattractant-stimulated polymorphonuclear leukocytes. J Cell Biol 110(6):1965-1973.
    • (1990) J Cell Biol , vol.110 , Issue.6 , pp. 1965-1973
    • Southwick, F.S.1    Young, C.L.2
  • 14
    • 0033788467 scopus 로고    scopus 로고
    • Interdependence of profilin, cation, and nucleotide binding to vertebrate non-muscle actin
    • Kinosian HJ, Selden LA, Gershman LC, Estes JE (2000) Interdependence of profilin, cation, and nucleotide binding to vertebrate non-muscle actin. Biochemistry 39(43):13176-13188.
    • (2000) Biochemistry , vol.39 , Issue.43 , pp. 13176-13188
    • Kinosian, H.J.1    Selden, L.A.2    Gershman, L.C.3    Estes, J.E.4
  • 15
    • 0025355476 scopus 로고
    • Isolation of a 5-kilodalton actin-sequestering peptide from human blood platelets
    • Safer D, Golla R, Nachmias VT (1990) Isolation of a 5-kilodalton actin-sequestering peptide from human blood platelets. Proc Natl Acad Sci USA 87(7):2536-2540.
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.7 , pp. 2536-2540
    • Safer, D.1    Golla, R.2    Nachmias, V.T.3
  • 16
    • 0025856003 scopus 로고
    • Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable
    • Safer D, Elzinga M, Nachmias VT (1991) Thymosin beta 4 and Fx, an actin-sequestering peptide, are indistinguishable. J Biol Chem 266(7):4029-4032.
    • (1991) J Biol Chem , vol.266 , Issue.7 , pp. 4029-4032
    • Safer, D.1    Elzinga, M.2    Nachmias, V.T.3
  • 17
    • 0034121422 scopus 로고    scopus 로고
    • Thymosin-beta(4) changes the conformation and dynamics of actin monomers
    • De La Cruz EM, et al. (2000) Thymosin-beta(4) changes the conformation and dynamics of actin monomers. Biophys J 78(5):2516-2527.
    • (2000) Biophys J , vol.78 , Issue.5 , pp. 2516-2527
    • De La Cruz, E.M.1
  • 19
    • 2542492280 scopus 로고    scopus 로고
    • Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance
    • Domanski M, et al. (2004) Coupling of folding and binding of thymosin beta4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. J Biol Chem 279(22):23637-23645.
    • (2004) J Biol Chem , vol.279 , Issue.22 , pp. 23637-23645
    • Domanski, M.1
  • 20
    • 0027146350 scopus 로고
    • Conformation of thymosin beta 4 in water determined by NMR spectroscopy
    • Czisch M, Schleicher M, Hörger S, Voelter W, Holak TA (1993) Conformation of thymosin beta 4 in water determined by NMR spectroscopy. Eur J Biochem 218(2):335-344.
    • (1993) Eur J Biochem , vol.218 , Issue.2 , pp. 335-344
    • Czisch, M.1    Schleicher, M.2    Hörger, S.3    Voelter, W.4    Holak, T.A.5
  • 21
    • 0031000223 scopus 로고    scopus 로고
    • Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends
    • Safer D, Sosnick TR, Elzinga M (1997) Thymosin beta 4 binds actin in an extended conformation and contacts both the barbed and pointed ends. Biochemistry 36(19):5806-5816.
    • (1997) Biochemistry , vol.36 , Issue.19 , pp. 5806-5816
    • Safer, D.1    Sosnick, T.R.2    Elzinga, M.3
  • 22
    • 0033944260 scopus 로고    scopus 로고
    • Structural requirements for thymosin beta4 in its contact with actin. An NMR-analysis of thymosin beta4 mutants in solution and correlation with their biological activity
    • Simenel C, Van Troys M, Vandekerckhove J, Ampe C, Delepierre M (2000) Structural requirements for thymosin beta4 in its contact with actin. An NMR-analysis of thymosin beta4 mutants in solution and correlation with their biological activity. Eur J Biochem 267(12):3530-3538.
    • (2000) Eur J Biochem , vol.267 , Issue.12 , pp. 3530-3538
    • Simenel, C.1    Van Troys, M.2    Vandekerckhove, J.3    Ampe, C.4    Delepierre, M.5
  • 23
    • 84857050647 scopus 로고    scopus 로고
    • How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly
    • Didry D, et al. (2012) How a single residue in individual β-thymosin/WH2 domains controls their functions in actin assembly. EMBO J 31(4):1000-1013.
    • (2012) EMBO J , vol.31 , Issue.4 , pp. 1000-1013
    • Didry, D.1
  • 24
    • 5044236672 scopus 로고    scopus 로고
    • Structural basis of actin sequestration by thymosin-beta4: Implications for WH2 proteins
    • Irobi E, et al. (2004) Structural basis of actin sequestration by thymosin-beta4: Implications for WH2 proteins. EMBO J 23(18):3599-3608.
    • (2004) EMBO J , vol.23 , Issue.18 , pp. 3599-3608
    • Irobi, E.1
  • 25
    • 2542421811 scopus 로고    scopus 로고
    • The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly
    • Hertzog M, et al. (2004) The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell 117(5):611-623.
    • (2004) Cell , vol.117 , Issue.5 , pp. 611-623
    • Hertzog, M.1
  • 26
    • 33644835262 scopus 로고    scopus 로고
    • The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins
    • Aguda AH, Xue B, Irobi E, Préat T, Robinson RC (2006) The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins. Structure 14(3):469-476.
    • (2006) Structure , vol.14 , Issue.3 , pp. 469-476
    • Aguda, A.H.1    Xue, B.2    Irobi, E.3    Préat, T.4    Robinson, R.C.5
  • 27
    • 35348931520 scopus 로고    scopus 로고
    • Models of the actin-bound forms of the betathymosins
    • Xue B, Aguda AH, Robinson RC (2007) Models of the actin-bound forms of the betathymosins. Ann N Y Acad Sci 1112:56-66.
    • (2007) Ann N Y Acad Sci , vol.1112 , pp. 56-66
    • Xue, B.1    Aguda, A.H.2    Robinson, R.C.3
  • 28
    • 34948868986 scopus 로고    scopus 로고
    • A novel system for expressing toxic actin mutants in Dictyostelium and purification and characterization of a dominant lethal yeast actin mutant
    • Noguchi TQ, Kanzaki N, Ueno H, Hirose K, Uyeda TQ (2007) A novel system for expressing toxic actin mutants in Dictyostelium and purification and characterization of a dominant lethal yeast actin mutant. J Biol Chem 282(38):27721-27727.
    • (2007) J Biol Chem , vol.282 , Issue.38 , pp. 27721-27727
    • Noguchi, T.Q.1    Kanzaki, N.2    Ueno, H.3    Hirose, K.4    Uyeda, T.Q.5
  • 29
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372(3):774-797.
    • (2007) J Mol Biol , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 31
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T, Iwasa M, Aihara T, Maéda Y, Narita A (2009) The nature of the globular- to fibrous-actin transition. Nature 457(7228):441-445.
    • (2009) Nature , vol.457 , Issue.7228 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maéda, Y.4    Narita, A.5
  • 32
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualization of secondary structures of F-actin by electron cryomicroscopy
    • Fujii T, Iwane AH, Yanagida T, Namba K (2010) Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 467(7316):724-728.
    • (2010) Nature , vol.467 , Issue.7316 , pp. 724-728
    • Fujii, T.1    Iwane, A.H.2    Yanagida, T.3    Namba, K.4
  • 33
    • 28044470753 scopus 로고    scopus 로고
    • Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly
    • Chereau D, et al. (2005) Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc Natl Acad Sci USA 102(46):16644-16649.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.46 , pp. 16644-16649
    • Chereau, D.1
  • 34
    • 0027065504 scopus 로고
    • G- to F-actin modulation by a single amino acid substitution in the actin binding site of actobindin and thymosin beta 4
    • Vancompernolle K, Goethals M, Huet C, Louvard D, Vandekerckhove J (1992) G- to F-actin modulation by a single amino acid substitution in the actin binding site of actobindin and thymosin beta 4. EMBO J 11(13):4739-4746.
    • (1992) EMBO J , vol.11 , Issue.13 , pp. 4739-4746
    • Vancompernolle, K.1    Goethals, M.2    Huet, C.3    Louvard, D.4    Vandekerckhove, J.5
  • 36
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont PJ, et al. (1992) The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol Biol Cell 3(9):1015-1024.
    • (1992) Mol Biol Cell , vol.3 , Issue.9 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1
  • 37
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta 4
    • Pantaloni D, Carlier MF (1993) How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell 75(5):1007-1014.
    • (1993) Cell , vol.75 , Issue.5 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 38
    • 0035824653 scopus 로고    scopus 로고
    • Formation and implications of a ternary complex of profilin, thymosin beta 4, and actin
    • Yarmola EG, Parikh S, Bubb MR (2001) Formation and implications of a ternary complex of profilin, thymosin beta 4, and actin. J Biol Chem 276(49):45555-45563.
    • (2001) J Biol Chem , vol.276 , Issue.49 , pp. 45555-45563
    • Yarmola, E.G.1    Parikh, S.2    Bubb, M.R.3
  • 39
    • 35649021883 scopus 로고    scopus 로고
    • Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP
    • Ferron F, Rebowski G, Lee SH, Dominguez R (2007) Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J 26(21):4597-4606.
    • (2007) EMBO J , vol.26 , Issue.21 , pp. 4597-4606
    • Ferron, F.1    Rebowski, G.2    Lee, S.H.3    Dominguez, R.4
  • 40
    • 33646013893 scopus 로고    scopus 로고
    • Profilin: Emerging concepts and lingering misconceptions
    • Yarmola EG, Bubb MR (2006) Profilin: Emerging concepts and lingering misconceptions. Trends Biochem Sci 31(4):197-205.
    • (2006) Trends Biochem Sci , vol.31 , Issue.4 , pp. 197-205
    • Yarmola, E.G.1    Bubb, M.R.2
  • 41
    • 50149116323 scopus 로고    scopus 로고
    • Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding
    • Baek K, et al. (2008) Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding. Proc Natl Acad Sci USA 105(33):11748-11753.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.33 , pp. 11748-11753
    • Baek, K.1
  • 42
    • 0141426434 scopus 로고    scopus 로고
    • From the first to the second domain of gelsolin: A common path on the surface of actin?
    • Irobi E, Burtnick LD, Urosev D, Narayan K, Robinson RC (2003) From the first to the second domain of gelsolin: A common path on the surface of actin? FEBS Lett 552(2-3):86-90.
    • (2003) FEBS Lett , vol.552 , Issue.2-3 , pp. 86-90
    • Irobi, E.1    Burtnick, L.D.2    Urosev, D.3    Narayan, K.4    Robinson, R.C.5
  • 43
    • 0037610737 scopus 로고    scopus 로고
    • The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism
    • Vorobiev S, et al. (2003) The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism. Proc Natl Acad Sci USA 100(10):5760-5765.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.10 , pp. 5760-5765
    • Vorobiev, S.1
  • 44
    • 0037188362 scopus 로고    scopus 로고
    • Actin filament barbed end elongation with nonmuscle MgATP-actin and MgADP-actin in the presence of profilin
    • Kinosian HJ, Selden LA, Gershman LC, Estes JE (2002) Actin filament barbed end elongation with nonmuscle MgATP-actin and MgADP-actin in the presence of profilin. Biochemistry 41(21):6734-6743.
    • (2002) Biochemistry , vol.41 , Issue.21 , pp. 6734-6743
    • Kinosian, H.J.1    Selden, L.A.2    Gershman, L.C.3    Estes, J.E.4
  • 45
    • 84888428383 scopus 로고    scopus 로고
    • Guardians of the actin monomer
    • Xue B, Robinson RC (2013) Guardians of the actin monomer. Eur J Cell Biol 92(10-11):316-332.
    • (2013) Eur J Cell Biol , vol.92 , Issue.10-11 , pp. 316-332
    • Xue, B.1    Robinson, R.C.2
  • 47
    • 77649273530 scopus 로고    scopus 로고
    • Fifteen formins for an actin filament: A molecular view on the regulation of human formins
    • Schönichen A, Geyer M (2010) Fifteen formins for an actin filament: A molecular view on the regulation of human formins. Biochim Biophys Acta 1803(2):152-163.
    • (2010) Biochim Biophys Acta , vol.1803 , Issue.2 , pp. 152-163
    • Schönichen, A.1    Geyer, M.2
  • 48
    • 0020790453 scopus 로고
    • Actin from Thyone sperm assembles on only one end of an actin filament: A behavior regulated by profilin
    • Tilney LG, Bonder EM, Coluccio LM, Mooseker MS (1983) Actin from Thyone sperm assembles on only one end of an actin filament: A behavior regulated by profilin. J Cell Biol 97(1):112-124.
    • (1983) J Cell Biol , vol.97 , Issue.1 , pp. 112-124
    • Tilney, L.G.1    Bonder, E.M.2    Coluccio, L.M.3    Mooseker, M.S.4
  • 49
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • Pollard TD, Cooper JA (1984) Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 23(26):6631-6641.
    • (1984) Biochemistry , vol.23 , Issue.26 , pp. 6631-6641
    • Pollard, T.D.1    Cooper, J.A.2
  • 50
    • 70549106122 scopus 로고    scopus 로고
    • How depolymerization can promote polymerization: The case of actin and profilin
    • Yarmola EG, Bubb MR (2009) How depolymerization can promote polymerization: The case of actin and profilin. BioEssays 31(11):1150-1160.
    • (2009) BioEssays , vol.31 , Issue.11 , pp. 1150-1160
    • Yarmola, E.G.1    Bubb, M.R.2
  • 51
    • 84856295948 scopus 로고    scopus 로고
    • Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin
    • Jégou A, et al. (2011) Individual actin filaments in a microfluidic flow reveal the mechanism of ATP hydrolysis and give insight into the properties of profilin. PLoS Biol 9(9):e1001161.
    • (2011) PLoS Biol , vol.9 , Issue.9 , pp. e1001161
    • Jégou, A.1
  • 52
    • 0026589150 scopus 로고
    • Profilin-actin complexes directly elongate actin filaments at the barbed end
    • Pring M, Weber A, Bubb MR (1992) Profilin-actin complexes directly elongate actin filaments at the barbed end. Biochemistry 31(6):1827-1836.
    • (1992) Biochemistry , vol.31 , Issue.6 , pp. 1827-1836
    • Pring, M.1    Weber, A.2    Bubb, M.R.3
  • 53
    • 84884255029 scopus 로고    scopus 로고
    • Interaction of profilin with the barbed end of actin filaments
    • Courtemanche N, Pollard TD (2013) Interaction of profilin with the barbed end of actin filaments. Biochemistry 52(37):6456-6466.
    • (2013) Biochemistry , vol.52 , Issue.37 , pp. 6456-6466
    • Courtemanche, N.1    Pollard, T.D.2
  • 54
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246(15):4866-4871.
    • (1971) J Biol Chem , vol.246 , Issue.15 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 55
    • 69549101849 scopus 로고    scopus 로고
    • The crystal structure of the C-terminus of adseverin reveals the actin-binding interface
    • Chumnarnsilpa S, et al. (2009) The crystal structure of the C-terminus of adseverin reveals the actin-binding interface. Proc Natl Acad Sci USA 106(33):13719-13724.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.33 , pp. 13719-13724
    • Chumnarnsilpa, S.1
  • 56
    • 0025085655 scopus 로고
    • Ligation-independent cloning of PCR products (LICPCR)
    • Aslanidis C, de Jong PJ (1990) Ligation-independent cloning of PCR products (LICPCR). Nucleic Acids Res 18(20):6069-6074.
    • (1990) Nucleic Acids Res , vol.18 , Issue.20 , pp. 6069-6074
    • Aslanidis, C.1    De Jong, P.J.2
  • 57
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41(1):207-234.
    • (2005) Protein Expr Purif , vol.41 , Issue.1 , pp. 207-234
    • Studier, F.W.1
  • 58
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Macromolecular Crystallography, Part A, eds Carter CW, Jr, Sweet RM (Academic, New York)
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology Vol 276: Macromolecular Crystallography, Part A, eds Carter CW, Jr, Sweet RM (Academic, New York), pp 307-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 59
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4):658-674.
    • (2007) J Appl Cryst , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 60
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 62
    • 33645158291 scopus 로고    scopus 로고
    • TLSMD web server for the generation of multi-group TLS models
    • Painter J, Merritt EA (2006) TLSMD web server for the generation of multi-group TLS models. J Appl Crystallogr 39(Pt 1):109-111.
    • (2006) J Appl Crystallogr , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 63
    • 79953737180 scopus 로고    scopus 로고
    • Overview of the CCP4 suite and current developments
    • Winn MD, et al. (2011) Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67(Pt 4):235-242.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 235-242
    • Winn, M.D.1
  • 64
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen VB, et al. (2010) MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66(Pt 1):12-21.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 12-21
    • Chen, V.B.1
  • 65
    • 84861708449 scopus 로고    scopus 로고
    • Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging
    • Breitsprecher D, et al. (2012) Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging. Science 336(6085):1164-1168.
    • (2012) Science , vol.336 , Issue.6085 , pp. 1164-1168
    • Breitsprecher, D.1
  • 66
    • 77950500990 scopus 로고    scopus 로고
    • Structural characterization of a capping protein interaction motif defines a family of actin filament regulators
    • Hernandez-Valladares M, et al. (2010) Structural characterization of a capping protein interaction motif defines a family of actin filament regulators. Nat Struct Mol Biol 17(4):497-503.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.4 , pp. 497-503
    • Hernandez-Valladares, M.1
  • 67
    • 0034623126 scopus 로고    scopus 로고
    • Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A
    • Yarmola EG, Somasundaram T, Boring TA, Spector I, Bubb MR (2000) Actin-latrunculin A structure and function. Differential modulation of actin-binding protein function by latrunculin A. J Biol Chem 275(36):28120-28127.
    • (2000) J Biol Chem , vol.275 , Issue.36 , pp. 28120-28127
    • Yarmola, E.G.1    Somasundaram, T.2    Boring, T.A.3    Spector, I.4    Bubb, M.R.5
  • 68
    • 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(3):435-447.
    • (2008) J Chem Theory Comput , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 69
    • 67649494492 scopus 로고    scopus 로고
    • Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides
    • Best RB, Hummer G (2009) Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides. J Phys Chem B 113(26):9004-9015.
    • (2009) J Phys Chem B , vol.113 , Issue.26 , pp. 9004-9015
    • Best, R.B.1    Hummer, G.2
  • 70
    • 77953513118 scopus 로고    scopus 로고
    • Improved side-chain torsion potentials for the Amber ff99SB protein force field
    • Lindorff-Larsen K, et al. (2010) Improved side-chain torsion potentials for the Amber ff99SB protein force field. Proteins 78(8):1950-1958.
    • (2010) Proteins , vol.78 , Issue.8 , pp. 1950-1958
    • Lindorff-Larsen, K.1
  • 71
    • 33645961739 scopus 로고
    • A smooth particle mesh Ewald method
    • Essmann U, et al. (1995) A smooth particle mesh Ewald method. J Chem Phys 103(19): 8577-8593.
    • (1995) J Chem Phys , vol.103 , Issue.19 , pp. 8577-8593
    • Essmann, U.1
  • 72
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • Hess B (2008) P-LINCS: A parallel linear constraint solver for molecular simulation. J Chem Theory Comput 4(1):116-122.
    • (2008) J Chem Theory Comput , vol.4 , Issue.1 , pp. 116-122
    • Hess, B.1
  • 73
    • 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(1):014101.
    • (2007) J Chem Phys , vol.126 , Issue.1 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 74
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello M, Rahman A (1981) Polymorphic transitions in single crystals: A new molecular dynamics method. J Appl Phys 52(12):7182-7190.
    • (1981) J Appl Phys , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 75
    • 0035478586 scopus 로고    scopus 로고
    • The Virtual Cell: A software environment for computational cell biology
    • Loew LM, Schaff JC (2001) The Virtual Cell: A software environment for computational cell biology. Trends Biotechnol 19(10):401-406.
    • (2001) Trends Biotechnol , vol.19 , Issue.10 , pp. 401-406
    • Loew, L.M.1    Schaff, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.