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Volumn 10, Issue 5, 2003, Pages 402-408

An actin-dependent conformational change in myosin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; COMPLEMENTARY DNA; CYSTEINE; EDETIC ACID; F ACTIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; POTASSIUM ION;

EID: 0037406442     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb916     Document Type: Article
Times cited : (25)

References (24)
  • 1
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment, I. et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261, 58-65 (1993).
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1
  • 2
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • Dominguez, R., Freyzon, Y., Trybus, K.M. & Cohen, C. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell 94, 559-571 (1998).
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 3
    • 1642340974 scopus 로고    scopus 로고
    • Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel formation of the myosin head
    • Houdusse, A., Kalabokis, V.N., Himmel, D., Szent-Györgyi, A.G. & Cohen, C. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel formation of the myosin head. Cell 97, 459-470 (1999).
    • (1999) Cell , vol.97 , pp. 459-470
    • Houdusse, A.1    Kalabokis, V.N.2    Himmel, D.3    Szent-Györgyi, A.G.4    Cohen, C.5
  • 4
    • 0033669710 scopus 로고    scopus 로고
    • Evidence for cleft closure in actomyosin upon ADP release
    • Volkmann, N. et al. Evidence for cleft closure in actomyosin upon ADP release. Nat. Struct. Biol. 7, 1147-1155 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1147-1155
    • Volkmann, N.1
  • 5
    • 0029176506 scopus 로고
    • A 35 Å movement of smooth muscle myosin on ADP release
    • Whittaker, M. et al. A 35 Å movement of smooth muscle myosin on ADP release. Nature 378, 748-751 (1995).
    • (1995) Nature , vol.378 , pp. 748-751
    • Whittaker, M.1
  • 6
    • 0029745362 scopus 로고    scopus 로고
    • ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin
    • Gollub, J., Cremo, C.R. & Cooke, R. ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin. Nat. Struct. Biol. 3, 796-802 (1996).
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 796-802
    • Gollub, J.1    Cremo, C.R.2    Cooke, R.3
  • 7
    • 0036085517 scopus 로고    scopus 로고
    • Principles and biophysical applications of luminescent lanthanide probes
    • Selvin, P.R. Principles and biophysical applications of luminescent lanthanide probes. Annu. Rev. Biophys. Biomol. Struct. 31, 275-302 (2002).
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 275-302
    • Selvin, P.R.1
  • 8
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment, I. et al. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-57 (1993).
    • (1993) Science , vol.261 , pp. 50-57
    • Rayment, I.1
  • 9
    • 0034264852 scopus 로고    scopus 로고
    • A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin
    • Shih, W.M., Gryczynski, Z., Lakowicz, J.R. & Spudich, J.A. A FRET-based sensor reveals large ATP hydrolysis-induced conformational changes and three distinct states of the molecular motor myosin. Cell 102, 683-694 (2000).
    • (2000) Cell , vol.102 , pp. 683-694
    • Shih, W.M.1    Gryczynski, Z.2    Lakowicz, J.R.3    Spudich, J.A.4
  • 11
    • 0035312384 scopus 로고    scopus 로고
    • Myosin motors: Missing structures and hidden springs
    • Houdusse, A. & Sweeney, H.L. Myosin motors: missing structures and hidden springs. Curr. Opin. Struct. Biol. 11, 182-194 (2001).
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 182-194
    • Houdusse, A.1    Sweeney, H.L.2
  • 12
    • 0023714467 scopus 로고
    • A short polypeptide marker sequence usefulfor recombinant protein identification and purification
    • Hopp, T.P. et al. A short polypeptide marker sequence usefulfor recombinant protein identification and purification. Biotechnology 6, 1205-1210 (1988).
    • (1988) Biotechnology , vol.6 , pp. 1205-1210
    • Hopp, T.P.1
  • 14
    • 0032513032 scopus 로고    scopus 로고
    • Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket
    • Sweeney, H.L. et al. Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket. J. Biol. Chem. 273, 6262-6270 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 6262-6270
    • Sweeney, H.L.1
  • 15
    • 0020022509 scopus 로고
    • Assays for myosin
    • Pollard, T.D. Assays for myosin. Methods Enzymol. 85, 123-130 (1982).
    • (1982) Methods Enzymol. , vol.85 , pp. 123-130
    • Pollard, T.D.1
  • 16
    • 0020013525 scopus 로고
    • Special instrumentation and techniques for kinetic studies of contractile systems
    • White, H.D. Special instrumentation and techniques for kinetic studies of contractile systems. Methods Enzymol. 85, 698-708 (1982).
    • (1982) Methods Enzymol. , vol.85 , pp. 698-708
    • White, H.D.1
  • 17
    • 0033105255 scopus 로고    scopus 로고
    • Thiol-reactive luminescent lanthanide chelates
    • Chen, J. & Selvin, P.R. Thiol-reactive luminescent lanthanide chelates. Bioconjugate Chem. 10, 311-315 (1999).
    • (1999) Bioconjugate Chem. , vol.10 , pp. 311-315
    • Chen, J.1    Selvin, P.R.2
  • 18
    • 0000823408 scopus 로고    scopus 로고
    • Crystal structure and spectroscopic characterization of a luminescent europium chelate
    • Selvin, P.R., Jancarik, J., Li, M. & Hung, L.-W. Crystal structure and spectroscopic characterization of a luminescent europium chelate. Inorgan. Chem. 35, 700-705 (1996).
    • (1996) Inorgan. Chem. , vol.35 , pp. 700-705
    • Selvin, P.R.1    Jancarik, J.2    Li, M.3    Hung, L.-W.4
  • 19
    • 0032433333 scopus 로고    scopus 로고
    • Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: The effect of nucleotides and actin
    • Xiao, M. et al. Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: The effect of nucleotides and actin. Proc. Natl. Acad. Sci. USA 95, 15309-15314 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15309-15314
    • Xiao, M.1
  • 20
    • 0001277752 scopus 로고    scopus 로고
    • An improved instrument for measuring time-resolved lanthanide emission and resonance energy transfer
    • Xiao, M. & Selvin, P.R. An improved instrument for measuring time-resolved lanthanide emission and resonance energy transfer. Rev. Sci. Instrum. 70, 3877-3881 (1999).
    • (1999) Rev. Sci. Instrum. , vol.70 , pp. 3877-3881
    • Xiao, M.1    Selvin, P.R.2
  • 21
    • 0027394243 scopus 로고
    • Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer
    • Clegg, R.M., Murchie, A.I., Zechel, A. & Lilley, D.M. Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA 90, 2994-2998 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2994-2998
    • Clegg, R.M.1    Murchie, A.I.2    Zechel, A.3    Lilley, D.M.4
  • 22
    • 0029737547 scopus 로고    scopus 로고
    • Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5′ end of oligonucleotides: Multiple conformers of single-stranded and double-stranded dye-DNA complexes
    • Vamosi, G., Gohlke, C. & Clegg, R. Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5′ end of oligonucleotides: multiple conformers of single-stranded and double-stranded dye-DNA complexes. Biophys. J. 71, 972-994 (1996).
    • (1996) Biophys. J. , vol.71 , pp. 972-994
    • Vamosi, G.1    Gohlke, C.2    Clegg, R.3
  • 23
    • 0034822673 scopus 로고    scopus 로고
    • Quantum yields of luminescent lanthanide chelates and far-red dyes measured by resonance energy transfer
    • Xiao, M. & Selvin, P.R. Quantum yields of luminescent lanthanide chelates and far-red dyes measured by resonance energy transfer. J. Am. Chem. Soc. 123, 7067-7073 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7067-7073
    • Xiao, M.1    Selvin, P.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.