메뉴 건너뛰기




Volumn 139, Issue 3, 1997, Pages 695-707

Tomographic three-dimensional reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol

Author keywords

[No Author keywords available]

Indexed keywords

ETHYLENE GLYCOL;

EID: 0030724661     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.139.3.695     Document Type: Article
Times cited : (29)

References (31)
  • 1
    • 0020018227 scopus 로고
    • Three-dimensional structure determinatiun by electron microscopy of two-dimensional crystals
    • Amos, L.A., R. Henderson, and P.N.T. Unwin. 1982. Three-dimensional structure determinatiun by electron microscopy of two-dimensional crystals. Prog. Biophys. Mol. Biol. 39:183-231.
    • (1982) Prog. Biophys. Mol. Biol. , vol.39 , pp. 183-231
    • Amos, L.A.1    Henderson, R.2    Unwin, P.N.T.3
  • 2
    • 0023654810 scopus 로고
    • New states of actomyosin
    • Applegate, D., and P. Flicker. 1987. New states of actomyosin. J. Biol. Chem. 262:6856-6863.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6856-6863
    • Applegate, D.1    Flicker, P.2
  • 3
    • 0025228709 scopus 로고
    • Binding of ADP and adenosine 5′-[β,γ-imido]triphosphate to insect flight muscle fibrils
    • Biosca, J.A., E. Eisenberg, M.C. Reedy, and M.K, Reedy. 1990. Binding of ADP and adenosine 5′-[β,γ-imido]triphosphate to insect flight muscle fibrils. Eur. J. Biochem. 189:395-399.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 395-399
    • Biosca, J.A.1    Eisenberg, E.2    Reedy, M.C.3    Reedy, M.K.4
  • 4
    • 0021346959 scopus 로고
    • Modification of crossbridge states by ethylene glycol in insect flight muscle
    • Chirke, M.L., C.D. Rodger, and R.T. Tregear. 1984. Modification of crossbridge states by ethylene glycol in insect flight muscle. J. Muscle Res. Cell Motil. 5:81-96.
    • (1984) J. Muscle Res. Cell Motil. , vol.5 , pp. 81-96
    • Chirke, M.L.1    Rodger, C.D.2    Tregear, R.T.3
  • 5
    • 0026580032 scopus 로고
    • Electron microscopy of the actin-myosin head complex in the presence of ATP
    • Frndo, L.-L., and R. Craig. 1992. Electron microscopy of the actin-myosin head complex in the presence of ATP. J. Mol. Biol. 223:391-397.
    • (1992) J. Mol. Biol. , vol.223 , pp. 391-397
    • Frndo, L.-L.1    Craig, R.2
  • 6
    • 0028915522 scopus 로고
    • The role of three-state docking of myoSin-S1 with actin in force generation
    • Geeves, M., and P.B. Conibear. 1995. The role of three-state docking of myoSin-S1 with actin in force generation. Biophys. J. 68:194S-199S.
    • (1995) Biophys. J. , vol.68
    • Geeves, M.1    Conibear, P.B.2
  • 7
    • 0019332185 scopus 로고
    • Dissociation of the actin-subfragment 1 complex by adenyl-5′-yl imidodiphosphate, ADP, and PPi
    • Green, L.E., and E. Eisenberg. 1980. Dissociation of the actin-subfragment 1 complex by adenyl-5′-yl imidodiphosphate, ADP, and PPi. J. Biol. Chem. 255:543-548.
    • (1980) J. Biol. Chem. , vol.255 , pp. 543-548
    • Green, L.E.1    Eisenberg, E.2
  • 8
    • 0015236610 scopus 로고
    • Proposed mechanism efforce generation in striated muscle
    • Huxley, A.F., and R.M. Simmons. 1971, Proposed mechanism efforce generation in striated muscle. Nature (Lond.). 233:533-538.
    • (1971) Nature (Lond.) , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 9
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A.. J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47:110-119.
    • (1991) Acta Cryst. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 11
    • 0021366761 scopus 로고
    • Modification of the interactions of myosin with actin and 5′-adenylyl imidodiphosphate by substitution of ethylene glycol for water
    • Marston, S.B., and R.T. Tregear. 1984. Modification of the interactions of myosin with actin and 5′-adenylyl imidodiphosphate by substitution of ethylene glycol for water. Biochem. J. 217:169-177.
    • (1984) Biochem. J. , vol.217 , pp. 169-177
    • Marston, S.B.1    Tregear, R.T.2
  • 14
    • 0023583644 scopus 로고
    • The structure of insect flight muscle in the presence of AMPPNP
    • Reedy, M.C., M.K. Reedy, and R.S. Goody. 1987. The structure of insect flight muscle in the presence of AMPPNP. J. Muscle Res. Cell Motil. 8:473-503.
    • (1987) J. Muscle Res. Cell Motil. , vol.8 , pp. 473-503
    • Reedy, M.C.1    Reedy, M.K.2    Goody, R.S.3
  • 15
    • 0024293416 scopus 로고
    • Two attached non-rigor crossbridge forms in insect flight muscle
    • Reedy, M.C., M.K. Reedy, and R.T. Tregear. 1988. Two attached non-rigor crossbridge forms in insect flight muscle. J. Mol. Biol. 204:357-383.
    • (1988) J. Mol. Biol. , vol.204 , pp. 357-383
    • Reedy, M.C.1    Reedy, M.K.2    Tregear, R.T.3
  • 16
    • 0028235402 scopus 로고
    • Gold/Fab immuno electron microscopy localization of troponin H and troponin T in Lethocerus flight muscle
    • Reedy, M.C., M.K. Reedy, K. Leonard, and B. Bullard. 1994. Gold/Fab immuno electron microscopy localization of troponin H and troponin T in Lethocerus flight muscle. J. Mol. Biol. 239:52-67.
    • (1994) J. Mol. Biol. , vol.239 , pp. 52-67
    • Reedy, M.C.1    Reedy, M.K.2    Leonard, K.3    Bullard, B.4
  • 17
    • 0014432527 scopus 로고
    • Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor crossbridge lattice
    • Reedy, M.K. 1968. Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor crossbridge lattice. J. Mol. Biol. 31:155-176.
    • (1968) J. Mol. Biol. , vol.31 , pp. 155-176
    • Reedy, M.K.1
  • 18
    • 0026785196 scopus 로고
    • Insect crossbridges, relaxed by spin-labeled nucleotide, show well-ordered 90° state by x-ray diffraction and electron microscopy, but spectra of electron paramagnetic resonance probes report disorder
    • Reedy, M.K., C. Lucaveche, N. Naber, and R. Cooke. 1992. Insect crossbridges, relaxed by spin-labeled nucleotide, show well-ordered 90° state by x-ray diffraction and electron microscopy, but spectra of electron paramagnetic resonance probes report disorder. J. Mol. Biol. 227:678-697.
    • (1992) J. Mol. Biol. , vol.227 , pp. 678-697
    • Reedy, M.K.1    Lucaveche, C.2    Naber, N.3    Cooke, R.4
  • 20
    • 0023257462 scopus 로고
    • ADP binding to myosin crossbridges and its effect on the crossbridge detachment rate constants
    • Schoenberg, M., and E. Eisenberg. 1987. ADP binding to myosin crossbridges and its effect on the crossbridge detachment rate constants. J. Gen. Physiol. 89:905-920.
    • (1987) J. Gen. Physiol. , vol.89 , pp. 905-920
    • Schoenberg, M.1    Eisenberg, E.2
  • 21
    • 0011828273 scopus 로고
    • 3-D reconstruction of paracrystalline biological specimens by tomography
    • G.W. Bailey, M.H. Ellisman, R.A. Hennigar, and N.J. Zaluzec, editors. Jones and Begell Publishing, New York
    • Taylor, K.A., and H. Winkler. 1995. 3-D reconstruction of paracrystalline biological specimens by tomography. In Proceedings Microscopy and Microanalysis. G.W. Bailey, M.H. Ellisman, R.A. Hennigar, and N.J. Zaluzec, editors. Jones and Begell Publishing, New York. 734-735.
    • (1995) Proceedings Microscopy and Microanalysis , pp. 734-735
    • Taylor, K.A.1    Winkler, H.2
  • 22
    • 15144347175 scopus 로고    scopus 로고
    • Tomography of paracrystalline specimens
    • G.W. Bailey, J.M. Corbett, R.V.W. Dimlich, J.R. Michael, and N.J. Zaluzec, editors. San Francisco Press, San Francisco, CA
    • Taylor, K. A., and H. Winkler. 1996. Tomography of paracrystalline specimens. In Proceedings Microscopy and Microanalysis. G.W. Bailey, J.M. Corbett, R.V.W. Dimlich, J.R. Michael, and N.J. Zaluzec, editors. San Francisco Press, San Francisco, CA. 586-587.
    • (1996) Proceedings Microscopy and Microanalysis , pp. 586-587
    • Taylor, K.A.1    Winkler, H.2
  • 23
    • 0021176612 scopus 로고
    • 3-D structure of insect flight muscle in rigor from tilted thin sections
    • Taylor, K.A., M.C. Reedy, L, Cordova, and M.K Reedy. 1984. 3-D structure of insect flight muscle in rigor from tilted thin sections. Nature (Lond.). 310: 285-291.
    • (1984) Nature (Lond.) , vol.310 , pp. 285-291
    • Taylor, K.A.1    Reedy, M.C.2    Cordova, L.3    Reedy, M.K.4
  • 24
    • 0024725008 scopus 로고
    • Three-dimensional image reconstruction of insect flight muscle. I. The rigor myac layer
    • Taylor, K.A., M.C. Reedy, L. Córdova, and M.K. Reedy. 1989a. Three-dimensional image reconstruction of insect flight muscle. I. The rigor myac layer. J. Cell Biol. 109:1085-1102.
    • (1989) J. Cell Biol. , vol.109 , pp. 1085-1102
    • Taylor, K.A.1    Reedy, M.C.2    Córdova, L.3    Reedy, M.K.4
  • 25
    • 0024727974 scopus 로고
    • Three-dimensional image reconstruction of insect flight muscle. II. The rigor actin layer
    • Taylor, K.A., M.C. Reedy, L. Córdova, and M.K. Reedy. 1989b. Three-dimensional image reconstruction of insect flight muscle. II. The rigor actin layer. J. Cell Biol. 109:1103-1123.
    • (1989) J. Cell Biol. , vol.109 , pp. 1103-1123
    • Taylor, K.A.1    Reedy, M.C.2    Córdova, L.3    Reedy, M.K.4
  • 26
    • 0021669735 scopus 로고
    • The process of muscle relaxation by the combined action of MgAMPPNP and ethylene glycol
    • Tregear, R.T., C.S. Terry, and A.J. Sayers. 1984. The process of muscle relaxation by the combined action of MgAMPPNP and ethylene glycol. J. Muscle Res. Cell Motil. 5:687-696.
    • (1984) J. Muscle Res. Cell Motil. , vol.5 , pp. 687-696
    • Tregear, R.T.1    Terry, C.S.2    Sayers, A.J.3
  • 27
    • 0025292139 scopus 로고
    • X-ray diffraction and electron microscopy from Lethocerus flight muscle partially relaxed by adenylylimidodiphosphate and ethylene glycol
    • Tregear, R.T., K. Wakabayashi, H. Tanaka, H. Iwamoto, M.C. Reedy, M.K. Reedy, H. Sugi, and Y. Amemiya. 1990. X-ray diffraction and electron microscopy from Lethocerus flight muscle partially relaxed by adenylylimidodiphosphate and ethylene glycol. J. Mol. Biol. 214:129-141.
    • (1990) J. Mol. Biol. , vol.214 , pp. 129-141
    • Tregear, R.T.1    Wakabayashi, K.2    Tanaka, H.3    Iwamoto, H.4    Reedy, M.C.5    Reedy, M.K.6    Sugi, H.7    Amemiya, Y.8
  • 28
    • 17144450693 scopus 로고
    • Millisecond time resolution electron cryo-microscopy of the M-ATP transient kinetic state of the acto-myosin ATPase
    • Walker, M., J. Trinick, and H. White. 1995. Millisecond time resolution electron cryo-microscopy of the M-ATP transient kinetic state of the acto-myosin ATPase. Biophys. J. 68:87S-91S.
    • (1995) Biophys. J. , vol.68
    • Walker, M.1    Trinick, J.2    White, H.3
  • 30
    • 0030175214 scopus 로고    scopus 로고
    • Three-dimensional distortion correction applied to tomographic reconstructions of sectioned crystals
    • Winkler, H., and K.A. Taylor. 1996. Three-dimensional distortion correction applied to tomographic reconstructions of sectioned crystals. Ultramicroscopy. 63:125-132.
    • (1996) Ultramicroscopy , vol.63 , pp. 125-132
    • Winkler, H.1    Taylor, K.A.2
  • 31
    • 0030606281 scopus 로고    scopus 로고
    • 3-D structure of nucleotide bearing crossbridges in situ: Oblique section reconstruction of insect flight muscle in aqueous AMPPNP
    • Winkler, H., M.C. Reedy, M.K. Reedy, R.T. Tregear, and K.A. Taylor. 1996. 3-D structure of nucleotide bearing crossbridges in situ: oblique section reconstruction of insect flight muscle in aqueous AMPPNP. J. Mol. Biol. 264:302-322.
    • (1996) J. Mol. Biol. , vol.264 , pp. 302-322
    • Winkler, H.1    Reedy, M.C.2    Reedy, M.K.3    Tregear, R.T.4    Taylor, K.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.