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Volumn 74, Issue 2 I, 1998, Pages 764-772

Determination of the gelsolin binding site on F-actin: Implications for severing and capping

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; GELSOLIN;

EID: 0031879577     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)74001-9     Document Type: Article
Times cited : (54)

References (69)
  • 1
    • 0028603483 scopus 로고
    • Gelsolin displaces phalloidin from actin filaments
    • Allen, P. G., and P. A. Janmey. 1994. Gelsolin displaces phalloidin from actin filaments. J. Biol. Chem. 269:32916-32923.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32916-32923
    • Allen, P.G.1    Janmey, P.A.2
  • 2
    • 0029787092 scopus 로고    scopus 로고
    • Dependence of fibroblast migration on actin severing activity of gelsolin
    • Arora, P. D., and C. A. G. McCulloch. 1996. Dependence of fibroblast migration on actin severing activity of gelsolin. J. Biol. Chem. 271: 20516-20523.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20516-20523
    • Arora, P.D.1    McCulloch, C.A.G.2
  • 3
    • 0026343343 scopus 로고
    • Direct observation of actin filament severing by gelsolin and binding by gCap39 and CapZ
    • Bearer, E. L. 1991. Direct observation of actin filament severing by gelsolin and binding by gCap39 and CapZ. J. Cell Biol. 115:1629-1538.
    • (1991) J. Cell Biol. , vol.115 , pp. 1629-11538
    • Bearer, E.L.1
  • 4
    • 0344482847 scopus 로고
    • Cambridge, MA
    • Biogen Annual Report. 1995. Cambridge, MA. 3.
    • (1995) Biogen Annual Report , pp. 3
  • 5
    • 0023894120 scopus 로고
    • Gelsolin has three actin-binding sites
    • Bryan, J. 1988. Gelsolin has three actin-binding sites. J. Cell Biol. 106: 1553-1562.
    • (1988) J. Cell Biol. , vol.106 , pp. 1553-1562
    • Bryan, J.1
  • 6
    • 0022551969 scopus 로고
    • 2+ regulatory domain in human brevin
    • 2+ regulatory domain in human brevin. J. Cell Biol. 102:1439-1446.
    • (1986) J. Cell Biol. , vol.102 , pp. 1439-1446
    • Bryan, J.1    Hwo, S.2
  • 7
    • 0021770684 scopus 로고
    • Actin-gelsolin interactions. Evidence for two actin-binding sites
    • Bryan, J., and M. C. Kurth. 1984. Actin-gelsolin interactions. Evidence for two actin-binding sites. J. Biol. Chem. 259:7480-7487.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7480-7487
    • Bryan, J.1    Kurth, M.C.2
  • 8
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: Implications for actin severing, capping and nucleation
    • Burtnick, L. D., E. K. Koepf, J. Grimes, E. Y. Jones, D. I. Stuart, P. J. McLaughlin, and R. C. Robinson. 1997. The crystal structure of plasma gelsolin: implications for actin severing, capping and nucleation. Cell. 90:661-670.
    • (1997) Cell , vol.90 , pp. 661-670
    • Burtnick, L.D.1    Koepf, E.K.2    Grimes, J.3    Jones, E.Y.4    Stuart, D.I.5    McLaughlin, P.J.6    Robinson, R.C.7
  • 9
    • 0001037624 scopus 로고
    • Algorithm for ribbon models of proteins
    • Carson, M., and C. E. Bugg. 1986. Algorithm for ribbon models of proteins. J. Mol. Graph. 4:121-122.
    • (1986) J. Mol. Graph. , vol.4 , pp. 121-122
    • Carson, M.1    Bugg, C.E.2
  • 10
    • 0023008203 scopus 로고
    • The actin filament-severing domain of plasma gelsolin
    • Chaponnier, C., P. A. Janmey, and H. L. Yin. 1986. The actin filament-severing domain of plasma gelsolin. J. Cell Biol. 103:1473-1481.
    • (1986) J. Cell Biol. , vol.103 , pp. 1473-1481
    • Chaponnier, C.1    Janmey, P.A.2    Yin, H.L.3
  • 12
    • 0014945329 scopus 로고
    • Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry
    • DeRosier, D. J., and P. B. Moore. 1970. Reconstruction of three-dimensional images from electron micrographs of structures with helical symmetry. J. Mol. Biol. 52:355-369.
    • (1970) J. Mol. Biol. , vol.52 , pp. 355-369
    • DeRosier, D.J.1    Moore, P.B.2
  • 13
    • 0028067048 scopus 로고
    • Nucleation of actin polymerization by gelsolin
    • Ditsch, A., and A. Wegner. 1994. Nucleation of actin polymerization by gelsolin. Eur. J. Biochem. 224:223-227.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 223-227
    • Ditsch, A.1    Wegner, A.2
  • 14
    • 0028921170 scopus 로고
    • Definition of an interface implicated in gelsolin binding to the sides of actin filaments
    • Feinberg, J., Y. Benyamin, and C. Roustan. 1995. Definition of an interface implicated in gelsolin binding to the sides of actin filaments. Biochem. Biophys. Res. Commun. 17:426-432.
    • (1995) Biochem. Biophys. Res. Commun. , vol.17 , pp. 426-432
    • Feinberg, J.1    Benyamin, Y.2    Roustan, C.3
  • 15
    • 0026554080 scopus 로고
    • In vivo analysis of functional domains from villin and gelsolin
    • Finidori, J., E. Friederich, D. J. Kwiatkowski, and D. Louvard. 1992. In vivo analysis of functional domains from villin and gelsolin. J. Cell. Biol. 116:1145-1155.
    • (1992) J. Cell. Biol. , vol.116 , pp. 1145-1155
    • Finidori, J.1    Friederich, E.2    Kwiatkowski, D.J.3    Louvard, D.4
  • 17
    • 0027258984 scopus 로고
    • The Ca-induced conformational change of gelsolin is located in the carboxy-terminal half of the molecule
    • Hellweg, T., H. Hinssen, and W. Eimer. 1993. The Ca-induced conformational change of gelsolin is located in the carboxy-terminal half of the molecule. Biophys. J. 65:799-805.
    • (1993) Biophys. J. , vol.65 , pp. 799-805
    • Hellweg, T.1    Hinssen, H.2    Eimer, W.3
  • 18
    • 0027134875 scopus 로고
    • The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation
    • Hesterkamp, T., A. G. Weeds, and H. G. Mannherz. 1993. The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation. Eur. J. Biochem. 218:507-513.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 507-513
    • Hesterkamp, T.1    Weeds, A.G.2    Mannherz, H.G.3
  • 19
    • 0030927201 scopus 로고    scopus 로고
    • Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: Effects of caldesmon
    • Hodgkinson, J. L., S. B. Marston, R. Craig, P. Vibert, and W. Lehman. 1997. Three-dimensional image reconstruction of reconstituted smooth muscle thin filaments: effects of caldesmon. Biophys. J. 72:2398-2404.
    • (1997) Biophys. J. , vol.72 , pp. 2398-2404
    • Hodgkinson, J.L.1    Marston, S.B.2    Craig, R.3    Vibert, P.4    Lehman, W.5
  • 20
  • 21
    • 0026724890 scopus 로고
    • Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin
    • Janmey, P. A., J. Lamb, P. G. Allen, and P. T. Matsudaira. 1992. Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin. J. Biol. Chem. 267:11818-11823.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11818-11823
    • Janmey, P.A.1    Lamb, J.2    Allen, P.G.3    Matsudaira, P.T.4
  • 22
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey, P. A., and T. P. Stossel. 1987. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature. 325:362-364.
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 23
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J. Y. Zou, C. Cowan, and M. Kjeldgaard. 1991. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47:110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, C.3    Kjeldgaard, M.4
  • 25
    • 0030872052 scopus 로고    scopus 로고
    • Conformational changes in actin induced by its interaction with gelsolin
    • Khaitlina, S., and H. Hinssen. 1997. Conformational changes in actin induced by its interaction with gelsolin. Biophys. J. 73:929-937.
    • (1997) Biophys. J. , vol.73 , pp. 929-937
    • Khaitlina, S.1    Hinssen, H.2
  • 26
    • 0030467026 scopus 로고    scopus 로고
    • Kinetics of gelsolin interaction with phalloidin-stabilized F-actin. Rate constants for binding and severing
    • Kinosian, H. J., L. A. Selden, J. E. Estes, and L. C. Gershman. 1996. Kinetics of gelsolin interaction with phalloidin-stabilized F-actin. Rate constants for binding and severing. Biochemistry. 35:16550-16556.
    • (1996) Biochemistry , vol.35 , pp. 16550-16556
    • Kinosian, H.J.1    Selden, L.A.2    Estes, J.E.3    Gershman, L.C.4
  • 28
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
    • Kwiatkowski, D. J., T. P. Stossel, S. H. Orkin, J. E. Mole, H. R. Colten, and H. L. Yin. 1986. Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature. 323:455-458.
    • (1986) Nature , vol.323 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3    Mole, J.E.4    Colten, H.R.5    Yin, H.L.6
  • 29
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against x-ray fiber diffraction data by the use of the directed mutation algorithm
    • Lorenz, M., D. Popp, and K. Holmes. 1993. Refinement of the F-actin model against x-ray fiber diffraction data by the use of the directed mutation algorithm. J. Mol. Biol. 234:826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.3
  • 30
    • 0030754673 scopus 로고    scopus 로고
    • Delayed retraction of filopodia in gelsolin null mice
    • Lu, M., W. Witke, D. J. Kwiatkowski, and K. S. Kosick. 1997. Delayed retraction of filopodia in gelsolin null mice. J. Cell. Biol. 138: 1279-1287.
    • (1997) J. Cell. Biol. , vol.138 , pp. 1279-1287
    • Lu, M.1    Witke, W.2    Kwiatkowski, D.J.3    Kosick, K.S.4
  • 31
    • 0028158904 scopus 로고
    • Solution structure of villin 14T, a domain conserved among actin-severing proteins
    • Markus, M. A., T. Nakayama, P. Matsudaira, and G. Wagner. 1994. Solution structure of villin 14T, a domain conserved among actin-severing proteins. Protein Sci. 3:70-81.
    • (1994) Protein Sci. , vol.3 , pp. 70-81
    • Markus, M.A.1    Nakayama, T.2    Matsudaira, P.3    Wagner, G.4
  • 32
    • 0023707173 scopus 로고
    • Pieces in the actin-severing puzzle
    • Matudaira, P. T., and P. A. Janmey. 1988. Pieces in the actin-severing puzzle. Cell. 54:139-140.
    • (1988) Cell , vol.54 , pp. 139-140
    • Matudaira, P.T.1    Janmey, P.A.2
  • 33
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • McGough, A., B. Pope, W. Chiu, and A. Weeds. 1997. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138:771-781.
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 34
    • 0028863184 scopus 로고
    • Molecular model of an actin filament capped by a severing protein
    • McGough, A., and M. Way. 1995. Molecular model of an actin filament capped by a severing protein. J. Struct. Biol. 115:144-150.
    • (1995) J. Struct. Biol. , vol.115 , pp. 144-150
    • McGough, A.1    Way, M.2
  • 35
    • 0028176006 scopus 로고
    • Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis
    • McGough, A., M. Way, and D. DeRosier. 1994. Determination of the α-actinin binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 126:433-443.
    • (1994) J. Cell Biol. , vol.126 , pp. 433-443
    • McGough, A.1    Way, M.2    DeRosier, D.3
  • 36
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin, P. J., J. T. Gooch, H.-G. Mannherz, and A. G. Weeds. 1993. Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature. 364:685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.-G.3    Weeds, A.G.4
  • 37
    • 0023374114 scopus 로고
    • Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy
    • Milligan, R. A., and P. F. Flicker. 1987. Structural relationships of actin, myosin, and tropomyosin revealed by cryo-electron microscopy J. Cell Biol. 105:29-39.
    • (1987) J. Cell Biol. , vol.105 , pp. 29-39
    • Milligan, R.A.1    Flicker, P.F.2
  • 38
    • 0023216026 scopus 로고
    • Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and alpha-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking
    • Mimura, N., and A. Asano. 1987. Further characterization of a conserved actin-binding 27-kDa fragment of actinogelin and alpha-actinins and mapping of their binding sites on the actin molecule by chemical cross-linking. J. Biol. Chem. 262:4717-4723.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4717-4723
    • Mimura, N.1    Asano, A.2
  • 40
    • 0028920157 scopus 로고
    • Structural dynamics of F-actin. II. Cooperativity in structural transitions
    • Orlova, A., E. Prochniewicz, and E. H. Egelman. 1995. Structural dynamics of F-actin. II. Cooperativity in structural transitions. J. Mol. Biol. 245:598-607.
    • (1995) J. Mol. Biol. , vol.245 , pp. 598-607
    • Orlova, A.1    Prochniewicz, E.2    Egelman, E.H.3
  • 41
    • 0027340549 scopus 로고
    • A 13 Å map of the actin-scruin filament from the Limulus acrosomal process
    • Owen, C., and D. DeRosier. 1993. A 13 Å map of the actin-scruin filament from the Limulus acrosomal process. J. Cell Biol. 123:337-344.
    • (1993) J. Cell Biol. , vol.123 , pp. 337-344
    • Owen, C.1    DeRosier, D.2
  • 42
    • 0025175562 scopus 로고
    • Size, shape parameters, and calcium-induced conformational change of the gelsolin molecule: A dynamic light scattering study
    • Patowski, A., J. Seils, H. Hinssen, and T. Dorfmuller. 1990. Size, shape parameters, and calcium-induced conformational change of the gelsolin molecule: a dynamic light scattering study. Biopolymers. 30:427-435.
    • (1990) Biopolymers , vol.30 , pp. 427-435
    • Patowski, A.1    Seils, J.2    Hinssen, H.3    Dorfmuller, T.4
  • 43
    • 0028957131 scopus 로고
    • Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites
    • Pope, B., S. Maciver, and A. Weeds. 1995. Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites. Biochemistry. 34:1583-1588.
    • (1995) Biochemistry , vol.34 , pp. 1583-1588
    • Pope, B.1    Maciver, S.2    Weeds, A.3
  • 44
    • 0026089715 scopus 로고
    • Two of the three actin-binding domains of gelsolin bind to the same subdomain of actin
    • Pope, B., M. Way, and A. G. Weeds. 1991. Two of the three actin-binding domains of gelsolin bind to the same subdomain of actin. FEBS Lett. 280:70-74.
    • (1991) FEBS Lett. , vol.280 , pp. 70-74
    • Pope, B.1    Way, M.2    Weeds, A.G.3
  • 45
    • 0030564835 scopus 로고    scopus 로고
    • Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament
    • Prochniewicz, E., Q. Zhang, P. A. Janmey, and D. D. Thomas. 1996. Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament. J. Mol. Biol. 260: 756-766.
    • (1996) J. Mol. Biol. , vol.260 , pp. 756-766
    • Prochniewicz, E.1    Zhang, Q.2    Janmey, P.A.3    Thomas, D.D.4
  • 47
    • 0022556940 scopus 로고
    • Characterization of the calcium-induced conformational changes in gelsolin and identification of interaction regions between actin and gelsolin
    • Rouayrenc, J. F., A. Fattoum, C. Mejean, and R. Kassab. 1986. Characterization of the calcium-induced conformational changes in gelsolin and identification of interaction regions between actin and gelsolin. Biochemistry. 13:3859-3867.
    • (1986) Biochemistry , vol.13 , pp. 3859-3867
    • Rouayrenc, J.F.1    Fattoum, A.2    Mejean, C.3    Kassab, R.4
  • 48
    • 0028115630 scopus 로고
    • Three-dimensional structure of a single filament in the Limulus acrosomal bundle: Scruin binds to homologous helix-loop-beta motifs in actin
    • Schmid, M. F., J. M. Agris, J. Jakana, P. Matsudaira, and W. Chiu. 1994. Three-dimensional structure of a single filament in the Limulus acrosomal bundle: scruin binds to homologous helix-loop-beta motifs in actin. J. Cell Biol. 124:341-350.
    • (1994) J. Cell Biol. , vol.124 , pp. 341-350
    • Schmid, M.F.1    Agris, J.M.2    Jakana, J.3    Matsudaira, P.4    Chiu, W.5
  • 51
    • 0029928871 scopus 로고    scopus 로고
    • SUPRIM: Easily modified image processing software
    • Schroeter, J. P., and J.-P. Bretaudiere. 1996. SUPRIM: easily modified image processing software. J. Struct. Biol. 116:131-137.
    • (1996) J. Struct. Biol. , vol.116 , pp. 131-137
    • Schroeter, J.P.1    Bretaudiere, J.-P.2
  • 53
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J. A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 54
    • 0023252082 scopus 로고
    • The variable twist of actin and its modulation by actin-binding proteins
    • Stokes, D. L., and D. J. DeRosier. 1987. The variable twist of actin and its modulation by actin-binding proteins. J. Cell Biol. 104:1005-1017.
    • (1987) J. Cell Biol. , vol.104 , pp. 1005-1017
    • Stokes, D.L.1    DeRosier, D.J.2
  • 55
    • 0028773922 scopus 로고
    • The E. Donnall Thomas Lecture, 1993. The machinery of blood cell movements
    • Stossel, T. P. 1994a. The E. Donnall Thomas Lecture, 1993. The machinery of blood cell movements. Blood. 84:367-379.
    • (1994) Blood , vol.84 , pp. 367-379
    • Stossel, T.P.1
  • 56
    • 0344051618 scopus 로고
    • Gelsolin: Another potential therapy for CF sputum!
    • article 40 (CFRI, Palo Alto, CA)
    • Stossel, T. P. 1994b. Gelsolin: another potential therapy for CF sputum! CFRI News. Fall: article 40 (CFRI, Palo Alto, CA).
    • (1994) CFRI News , vol.FALL
    • Stossel, T.P.1
  • 58
    • 0027514929 scopus 로고
    • Three-dimensional reconstruction of caldesmon-containing smooth muscle filaments
    • Vibert, P., R. Craig, and W. Lehman. 1993. Three-dimensional reconstruction of caldesmon-containing smooth muscle filaments. J. Cell Biol. 123:313-321.
    • (1993) J. Cell Biol. , vol.123 , pp. 313-321
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 59
    • 0024318706 scopus 로고
    • Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis
    • Way, M., J. Gooch, B. Pope, and A. G. Weeds. 1989. Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J. Cell Biol. 109:593-605.
    • (1989) J. Cell Biol. , vol.109 , pp. 593-605
    • Way, M.1    Gooch, J.2    Pope, B.3    Weeds, A.G.4
  • 60
    • 0026495427 scopus 로고
    • Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: Implications for the requirements of severing and capping
    • Way, M., B. Pope, and A. G. Weeds. 1992. Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping. J. Cell Biol. 119:835-842.
    • (1992) J. Cell Biol. , vol.119 , pp. 835-842
    • Way, M.1    Pope, B.2    Weeds, A.G.3
  • 61
    • 0024293322 scopus 로고
    • Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats
    • Way, M., and A. Weeds. 1988. Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats. J. Mol. Biol. 203:1127-1133.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1127-1133
    • Way, M.1    Weeds, A.2
  • 63
    • 0029311258 scopus 로고
    • PHOELIX: A package for automated helical reconstruction
    • Whittaker, M., B. O. Carragher, and R. A. Milligan. 1995b. PHOELIX: a package for automated helical reconstruction. Ultramicroscopy. 58: 245-260.
    • (1995) Ultramicroscopy , vol.58 , pp. 245-260
    • Whittaker, M.1    Carragher, B.O.2    Milligan, R.A.3
  • 65
    • 0028914814 scopus 로고
    • Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin
    • Witke, W., A. H. Sharpe, J. H. Hartwig, T. Azuma, T. P. Stossel, and D. J. Kwiatkowski. 1995. Hemostatic, inflammatory, and fibroblast responses are blunted in mice lacking gelsolin. Cell. 81:41-51.
    • (1995) Cell , vol.81 , pp. 41-51
    • Witke, W.1    Sharpe, A.H.2    Hartwig, J.H.3    Azuma, T.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 66
    • 0028823009 scopus 로고
    • Spectroscopic studies of phosphoinositide-binding peptide from gelsolin: Behavior in solutions of mixed solvent and anionic micelles
    • Xian, W., R. Vegners, P. A. Janmey, and W. H. Braunlin. 1995. Spectroscopic studies of phosphoinositide-binding peptide from gelsolin: behavior in solutions of mixed solvent and anionic micelles. Biophys. J. 69:2695-2702.
    • (1995) Biophys. J. , vol.69 , pp. 2695-2702
    • Xian, W.1    Vegners, R.2    Janmey, P.A.3    Braunlin, W.H.4
  • 67
    • 0023849688 scopus 로고
    • Identification of a polyphosphoinositide-regulated actin-modulated domain in gelsolin which binds to the sides of actin filaments
    • Yin, H. L., K. Iida, and P. A. Janmey. 1988. Identification of a polyphosphoinositide-regulated actin-modulated domain in gelsolin which binds to the sides of actin filaments. J. Cell Biol. 106:805-812.
    • (1988) J. Cell Biol. , vol.106 , pp. 805-812
    • Yin, H.L.1    Iida, K.2    Janmey, P.A.3
  • 68
    • 0018667209 scopus 로고
    • Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein
    • Yin, H. L., and T. P. Stossel. 1979. Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein. Nature. 281:585-586.
    • (1979) Nature , vol.281 , pp. 585-586
    • Yin, H.L.1    Stossel, T.P.2
  • 69
    • 0029928874 scopus 로고    scopus 로고
    • CTF determination of images of ice-embedded single particles using a graphics interface
    • Zhou, Z. H., S. Hardt, B. Wang, M. B. Sherman, J. Jakana, and W. Chiu. 1996. CTF determination of images of ice-embedded single particles using a graphics interface. J. Struct. Biol. 116:216-223.
    • (1996) J. Struct. Biol. , vol.116 , pp. 216-223
    • Zhou, Z.H.1    Hardt, S.2    Wang, B.3    Sherman, M.B.4    Jakana, J.5    Chiu, W.6


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