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Volumn 49, Issue 18, 2010, Pages 3919-3927

Antiparallel dimer and actin assembly

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN FILAMENT; ACTIN POLYMERIZATION; BIFUNCTIONAL; CHEMICAL CROSS-LINKING; CONFORMATIONAL TRANSITIONS; MALEIMIDES; NEUTRAL PH; NEW SYSTEM; P-PHENYLENE; PHYSIOLOGICAL CONDITION; POLYLYSINE; POLYMERIZATION REACTION; SEDIMENTATION EQUILIBRIUM; YEAST ACTIN;

EID: 77951925394     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1002663     Document Type: Article
Times cited : (15)

References (28)
  • 1
    • 0023840623 scopus 로고
    • Probing actin polymerization by intermolecular cross-linking
    • Millonig, R., Salvo, H., and Aebi, U. (1988) Probing actin polymerization by intermolecular cross-linking J. Cell Biol. 106, 785-796 (Pubitemid 18089979)
    • (1988) Journal of Cell Biology , vol.106 , Issue.3 , pp. 785-796
    • Millonig, R.1    Salvo, H.2    Aebi, U.3
  • 2
    • 0030804033 scopus 로고    scopus 로고
    • A correlative analysis of actin filament assembly, structure, and dynamics
    • DOI 10.1083/jcb.138.3.559
    • Steinmetz, M. O., Goldie, K. N., and Aebi, U. (1997) A correlative analysis of actin filament assembly, structure, and dynamics J. Cell Biol. 138, 559-574 (Pubitemid 27349838)
    • (1997) Journal of Cell Biology , vol.138 , Issue.3 , pp. 559-574
    • Steinmetz, M.O.1    Goldie, K.N.2    Aebi, U.3
  • 3
    • 62649135278 scopus 로고    scopus 로고
    • New aspects of the spontaneous polymerization of actin in the presence of salts
    • Galinska-Rakoczy, A., Wawro, B., and Strzelecka-Golaszewska, H. (2009) New aspects of the spontaneous polymerization of actin in the presence of salts J. Mol. Biol. 387, 869-882
    • (2009) J. Mol. Biol. , vol.387 , pp. 869-882
    • Galinska-Rakoczy, A.1    Wawro, B.2    Strzelecka-Golaszewska, H.3
  • 5
    • 0018436709 scopus 로고
    • Nucleation of polar actin filament assembly by a positively charged surface
    • Brown, S. S. and Spudich, J. A. (1979) Nucleation of polar actin filament assembly by a positively charged surface J. Cell Biol. 80, 499-504
    • (1979) J. Cell Biol. , vol.80 , pp. 499-504
    • Brown, S.S.1    Spudich, J.A.2
  • 6
    • 0017897643 scopus 로고
    • Polyamine-induced actin polymerization
    • Oriol-Audit, C. (1978) Polyamine-induced actin polymerization Eur. J. Biochem. 87, 371-376 (Pubitemid 8355179)
    • (1978) European Journal of Biochemistry , vol.87 , Issue.2 , pp. 371-376
    • Oriol-Audit, C.1
  • 7
    • 0020626339 scopus 로고
    • Supramolecular forms of actin induced by polyamines: An electron microscopic study
    • Grant, N. J., Oriol-Audit, C., and Dickens, M. J. (1983) Supramolecular forms of actin induced by polyamines: An electron microscopic study Eur. J. Cell Biol. 30, 67-73 (Pubitemid 13085820)
    • (1983) European Journal of Cell Biology , vol.30 , Issue.1 , pp. 67-73
    • Grant, N.J.1    Oriol Audit, C.2    Dickens, M.J.3
  • 8
    • 0029032728 scopus 로고
    • Polyamine involvement in the cell cycle, apoptosis, and autoimmunity
    • Brooks, W. H. (1995) Polyamine involvement in the cell cycle, apoptosis, and autoimmunity Med. Hypotheses 44, 331-338
    • (1995) Med. Hypotheses , vol.44 , pp. 331-338
    • Brooks, W.H.1
  • 9
    • 12144276287 scopus 로고    scopus 로고
    • Signal transduction pathways linking polyamines to apoptosis
    • DOI 10.1007/s00726-004-0115-3
    • Pignatti, C., Tantini, B., Stefanelli, C., and Flamigni, F. (2004) Signal transduction pathways linking polyamines to apoptosis Amino Acids 27, 359-365 (Pubitemid 40110081)
    • (2004) Amino Acids , vol.27 , Issue.3-4 , pp. 359-365
    • Pignatti, C.1    Tantini, B.2    Stefanelli, C.3    Flamigni, F.4
  • 10
    • 33748487414 scopus 로고    scopus 로고
    • Myelin basic protein: A multifunctional protein
    • DOI 10.1007/s00018-006-6094-7
    • Boggs, J. (2006) Myelin basic protein: A multifunctional protein Cell. Mol. Life Sci. 63, 1945-1961 (Pubitemid 44359737)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.17 , pp. 1945-1961
    • Boggs, J.M.1
  • 11
  • 12
    • 0035960656 scopus 로고    scopus 로고
    • Fesselin, a synaptopodin-like protein, stimulates actin nucleation and polymerization
    • DOI 10.1021/bi011806u
    • Beall, B. and Chalovich, J. M. (2001) Fesselin, a synaptopodin-like protein, stimulates actin nucleation and polymerization Biochemistry 40, 14252-14259 (Pubitemid 33081629)
    • (2001) Biochemistry , vol.40 , Issue.47 , pp. 14252-14259
    • Beall, B.1    Chalovich, J.M.2
  • 13
    • 0030845631 scopus 로고    scopus 로고
    • Opposite effects of electrostatics and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes
    • DOI 10.1021/bi9711386
    • Tang, J. X., Ito, T., Tao, T., Traub, P., and Janmey, P. A. (1997) Opposite effects of electrostatics and steric exclusion on bundle formation by F-actin and other filamentous polyelectrolytes Biochemistry 36, 12600-12607 (Pubitemid 27446685)
    • (1997) Biochemistry , vol.36 , Issue.41 , pp. 12600-12607
    • Tang, J.X.1    Ito, T.2    Tao, T.3    Traub, P.4    Janmey, P.A.5
  • 15
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction
    • Spudich, J. A. and Watt, S. (1971) The regulation of rabbit skeletal muscle contraction J. Biol. Chem. 246, 4866-4871
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 17
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin
    • Kouyama, T. and Mihashi, K. (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin Eur. J. Biochem. 114, 33-38
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0031013484 scopus 로고    scopus 로고
    • Beryllium fluoride and phalloidin restore polymerizability of a mutant yeast actin (V266G,L267G) with severely decreased hydrophobicity in a subdomain 3/4 loop
    • DOI 10.1074/jbc.272.2.1237
    • Kuang, B. and Rubenstein, P. A. (1997) Beryllium fluoride and phalloidin restore polymerizability of a mutant yeast actin (V266G,L267G) with severely decreased hydrophobicity in a subdomain 3/4 loop J. Biol. Chem. 272, 1237-1247 (Pubitemid 27034623)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 1237-1247
    • Kuang, B.1    Ruhenstein, P.A.2
  • 22
    • 0030919291 scopus 로고    scopus 로고
    • Intramolecular Pyrene Excimer Fluorescence: A Probe of Proximity and Protein Conformational Change
    • Academic Press, San Diego
    • Lehrer, S. S. (1997) Intramolecular Pyrene Excimer Fluorescence: A Probe of Proximity and Protein Conformational Change. In Methods in Enzymology: Fluorescence Spectroscopy (Brand, L. and Johnson, M. L., Eds.) pp 286 ? 295, Academic Press, San Diego.
    • (1997) Methods in Enzymology: Fluorescence Spectroscopy , pp. 286-295
    • Lehrer, S.S.1    Brand, L.2    Johnson, M.L.3
  • 24
    • 0036971460 scopus 로고    scopus 로고
    • Actin in the nucleus: What form and what for?
    • DOI 10.1016/S1047-8477(02)00528-2, PII S1047847702005282
    • Pederson, T. and Aebi, U. (2003) Actin in the nucleus: What form and what for? J. Struct. Biol. 140, 3-9 (Pubitemid 36139841)
    • (2002) Journal of Structural Biology , vol.140 , Issue.1-3 , pp. 3-9
    • Pederson, T.1    Aebi, U.2
  • 25
    • 0025075012 scopus 로고
    • A polymorphism peculiar to bipolar actin bundles
    • Francis, N. R. and DeRosier, D. J. (1990) A polymorphism peculiar to bipolar actin bundles Biophys. J. 58, 771-776
    • (1990) Biophys. J. , vol.58 , pp. 771-776
    • Francis, N.R.1    Derosier, D.J.2
  • 26
    • 0032525166 scopus 로고    scopus 로고
    • An atomic model of crystalline actin tubes: Combining electron microscopy with X-ray crystallography
    • DOI 10.1006/jmbi.1998.1717
    • Steinmetz, M. O., Hoenger, A., Tittmann, P., Fuchs, K. H., Gross, H., and Aebi, U. (1998) An atomic model of crystalline actin tubes: Combining electron microscopy with X-ray crystallography J. Mol. Biol. 278, 703-711 (Pubitemid 28224890)
    • (1998) Journal of Molecular Biology , vol.278 , Issue.4 , pp. 703-711
    • Steinmetz, M.O.1    Hoenger, A.2    Tittmann, P.3    Fuchs, K.H.4    Gross, H.5    Aebi, U.6
  • 27
    • 0035921432 scopus 로고    scopus 로고
    • Abp1p and cortactin, new hand-holds for actin
    • Olazabal, I. M. and Machesky, L. M. (2001) Abp1p and cortactin, new hand-holds for actin J. Cell Biol. 154, 679-682
    • (2001) J. Cell Biol. , vol.154 , pp. 679-682
    • Olazabal, I.M.1    MacHesky, L.M.2
  • 28
    • 0027134875 scopus 로고
    • The actin monomers in the ternary gelsolin: 2 actin complex are in an antiparallel orientation
    • DOI 10.1111/j.1432-1033.1993.tb18403.x
    • Hesterkamp, T., Weeds, A. G., and Mannherz, H. G. (1993) The actin monomers in the ternary gelsolin:2 actin complex are in an antiparallel orientation Eur. J. Biochem. 218, 507-513 (Pubitemid 24003767)
    • (1993) European Journal of Biochemistry , vol.218 , Issue.2 , pp. 507-513
    • Hesterkamp, T.1    Weeds, A.G.2    Mannherz, H.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.