메뉴 건너뛰기




Volumn 86, Issue 4, 2004, Pages 2329-2341

Bifunctional Rhodamine Probes of Myosin Regulatory Light Chain Orientation in Relaxed Skeletal Muscle Fibers

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; EDETIC ACID; LYSINE; MYOSIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; RHODAMINE;

EID: 1942423256     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74290-3     Document Type: Article
Times cited : (23)

References (40)
  • 1
    • 0035997056 scopus 로고    scopus 로고
    • Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges
    • Bell, M. G., R. E. Dale, U. A. van der Heide, and Y. E. Goldman. 2002. Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges. Biophys. J. 83:1050-1073.
    • (2002) Biophys. J. , vol.83 , pp. 1050-1073
    • Bell, M.G.1    Dale, R.E.2    Van Der Heide, U.A.3    Goldman, Y.E.4
  • 2
    • 0036094838 scopus 로고    scopus 로고
    • Rapid cryofixation of rabbit muscle fibres after a temperature jump
    • Bennett, P. M., A. Tsaturyan, and S. Bershitsky. 2002. Rapid cryofixation of rabbit muscle fibres after a temperature jump. J. Microsc. 206:152-160.
    • (2002) J. Microsc. , vol.206 , pp. 152-160
    • Bennett, P.M.1    Tsaturyan, A.2    Bershitsky, S.3
  • 3
    • 0032031751 scopus 로고    scopus 로고
    • A homobifunctional rhodamine for labeling proteins with defined orientations of a fluorophore
    • Corrie, J. E. T., J. S. Craik, and V. R. N. Munasinghe. 1998. A homobifunctional rhodamine for labeling proteins with defined orientations of a fluorophore. Bioconjug. Chem. 9:160-167.
    • (1998) Bioconjug. Chem. , vol.9 , pp. 160-167
    • Corrie, J.E.T.1    Craik, J.S.2    Munasinghe, V.R.N.3
  • 5
    • 0021813998 scopus 로고
    • Structure of the actin-myosin complex in the presence of ATP
    • Craig, R., L. E. Greene, and E. Eisenberg. 1985. Structure of the actin-myosin complex in the presence of ATP. Proc. Natl. Acad. Sci. USA. 82:3247-3251.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3247-3251
    • Craig, R.1    Greene, L.E.2    Eisenberg, E.3
  • 6
    • 0033029278 scopus 로고    scopus 로고
    • Model-independent analysis of the orientation of fluorescent probes with restricted mobility in muscle fibers
    • Dale, R. E., S. C. Hopkins, U. A. van der Heide, T. Marszalek, M. Irving, and Y. E. Goldman. 1999. Model-independent analysis of the orientation of fluorescent probes with restricted mobility in muscle fibers. Biophys. J. 76:1606-1618.
    • (1999) Biophys. J. , vol.76 , pp. 1606-1618
    • Dale, R.E.1    Hopkins, S.C.2    Van Der Heide, U.A.3    Marszalek, T.4    Irving, M.5    Goldman, Y.E.6
  • 7
    • 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., Y. Freyzon, K. M. Trybus, and C. Cohen. 1998. 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) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 8
    • 0021992946 scopus 로고
    • Muscle contraction and free energy transduction in biological systems
    • Eisenberg, E., and T. L. Hill. 1985. Muscle contraction and free energy transduction in biological systems. Science. 227:999-1006.
    • (1985) Science , vol.227 , pp. 999-1006
    • Eisenberg, E.1    Hill, T.L.2
  • 9
    • 0025989807 scopus 로고
    • Orientational disorder and motion of weakly attached cross-bridges
    • Fajer, P., E. A. Fajer, M. Schoenberg, and D. D. Thomas. 1991. Orientational disorder and motion of weakly attached cross-bridges. Biophys. J. 60:624-649.
    • (1991) Biophys. J. , vol.60 , pp. 624-649
    • Fajer, P.1    Fajer, E.A.2    Schoenberg, M.3    Thomas, D.D.4
  • 10
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves, M. A., and K. C. Holmes. 1999. Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68:687-728.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 11
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and P. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.2
  • 12
    • 0020724788 scopus 로고
    • Improved methodology for analysis and quantitation of proteins on one-dimensional silver stained slab gels
    • Giulian, G. G., R. L. Moss, and M. L. Greaser. 1983. Improved methodology for analysis and quantitation of proteins on one-dimensional silver stained slab gels. Anal. Biochem. 129:277-287.
    • (1983) Anal. Biochem. , vol.129 , pp. 277-287
    • Giulian, G.G.1    Moss, R.L.2    Greaser, M.L.3
  • 13
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., S. R. Adams, and R. Y. Tsien. 1998. Specific covalent labeling of recombinant protein molecules inside live cells. Science. 281:269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 14
    • 0031806323 scopus 로고    scopus 로고
    • Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers
    • Hopkins, S. C., C. Sabido-David, J. E. T. Corrie, M. Irving, and Y. E. Goldman. 1998. Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers. Biophys. J. 74:3093-3110.
    • (1998) Biophys. J. , vol.74 , pp. 3093-3110
    • Hopkins, S.C.1    Sabido-David, C.2    Corrie, J.E.T.3    Irving, M.4    Goldman, Y.E.5
  • 16
    • 0030729013 scopus 로고    scopus 로고
    • Myosin head configuration in relaxed fish muscle: Resting state myosin heads must swing axially by up to 150Å or turn upside down to reach rigor
    • Hudson, L., J. J. Harford, R. C. Denny, and J. M. Squire. 1997. Myosin head configuration in relaxed fish muscle: resting state myosin heads must swing axially by up to 150Å or turn upside down to reach rigor. J. Mol. Biol. 273:440-455.
    • (1997) J. Mol. Biol. , vol.273 , pp. 440-455
    • Hudson, L.1    Harford, J.J.2    Denny, R.C.3    Squire, J.M.4
  • 18
    • 0029005992 scopus 로고
    • Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: Additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation
    • Kraft, T., J. M. Chalovich, L. C. Yu, and B. Brenner. 1995. Parallel inhibition of active force and relaxed fiber stiffness by caldesmon fragments at physiological ionic strength and temperature conditions: additional evidence that weak cross-bridge binding to actin is an essential intermediate for force generation. Biophys. J. 68:2404-2418.
    • (1995) Biophys. J. , vol.68 , pp. 2404-2418
    • Kraft, T.1    Chalovich, J.M.2    Yu, L.C.3    Brenner, B.4
  • 19
    • 0031663377 scopus 로고    scopus 로고
    • Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains
    • Levine, R. J. C., Z. Yang, N. D. Epstein, L. Fananapazir, J. T. Stull, and H. L. Sweeney. 1998. Structural and functional responses of mammalian thick filaments to alterations in myosin regulatory light chains. J. Struct. Biol. 122:149-161.
    • (1998) J. Struct. Biol. , vol.122 , pp. 149-161
    • Levine, R.J.C.1    Yang, Z.2    Epstein, N.D.3    Fananapazir, L.4    Stull, J.T.5    Sweeney, H.L.6
  • 21
    • 0029863187 scopus 로고    scopus 로고
    • Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle
    • Ling, N., C. Shrimpton, J. Sleep, J. Kendrick-Jones, and M. Irving. 1996. Fluorescent probes of the orientation of myosin regulatory light chains in relaxed, rigor, and contracting muscle. Biophys. J. 70:1836-1846.
    • (1996) Biophys. J. , vol.70 , pp. 1836-1846
    • Ling, N.1    Shrimpton, C.2    Sleep, J.3    Kendrick-Jones, J.4    Irving, M.5
  • 22
    • 0026043263 scopus 로고
    • X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles
    • Lowy, J., D. Popp, and A. A. Stewart. 1991. X-ray studies of order-disorder transitions in the myosin heads of skinned rabbit psoas muscles. Biophys. J. 60:812-824.
    • (1991) Biophys. J. , vol.60 , pp. 812-824
    • Lowy, J.1    Popp, D.2    Stewart, A.A.3
  • 23
    • 0030734902 scopus 로고    scopus 로고
    • Temperature-induced structural changes in the myosin thick filament of skinned rabbit psoas muscle
    • Malinchik, S., S. Xu, and L. C. Yu. 1997. Temperature-induced structural changes in the myosin thick filament of skinned rabbit psoas muscle. Biophys. J. 73:2304-2312.
    • (1997) Biophys. J. , vol.73 , pp. 2304-2312
    • Malinchik, S.1    Xu, S.2    Yu, L.C.3
  • 24
    • 0344490343 scopus 로고    scopus 로고
    • The NMR structure of a bifunctional rhodamine labeled troponin C in complex with the regulatory "switch" peptide from troponin I; implications for in situ fluorescence studies in muscle fibers
    • Mercier, P., R. E. Ferguson, M. Irving, J. E. T. Corrie, D. R. Trentham, and B. D. Sykes. 2003. The NMR structure of a bifunctional rhodamine labeled troponin C in complex with the regulatory "switch" peptide from troponin I; implications for in situ fluorescence studies in muscle fibers. Biochemistry. 15:4333-4348.
    • (2003) Biochemistry , vol.15 , pp. 4333-4348
    • Mercier, P.1    Ferguson, R.E.2    Irving, M.3    Corrie, J.E.T.4    Trentham, D.R.5    Sykes, B.D.6
  • 25
    • 0025356188 scopus 로고
    • Cryo-electron microscopic studies of relaxed striated muscle thick filaments
    • Menetret, J. F., R. R. Schroeder, and W. Hofmann. 1990. Cryo-electron microscopic studies of relaxed striated muscle thick filaments. J. Muscle Res. Cell Motil. 11:1-11.
    • (1990) J. Muscle Res. Cell Motil. , vol.11 , pp. 1-11
    • Menetret, J.F.1    Schroeder, R.R.2    Hofmann, W.3
  • 26
    • 0020615741 scopus 로고
    • Effects of EDTA treatment upon the protein subunit composition and mechanical properties of mammalian skeletal muscle fibers
    • Moss, R. L., G. G. Giulian, and M. L. Greaser. 1983. Effects of EDTA treatment upon the protein subunit composition and mechanical properties of mammalian skeletal muscle fibers. J. Cell Biol. 96:970-978.
    • (1983) J. Cell Biol. , vol.96 , pp. 970-978
    • Moss, R.L.1    Giulian, G.G.2    Greaser, M.L.3
  • 27
    • 0024457341 scopus 로고
    • Myosin crossbridge orientation in demembranated muscle-fibers studied by birefringence and x-ray diffraction measurements
    • Peckham, M., and M. Irving. 1989. Myosin crossbridge orientation in demembranated muscle-fibers studied by birefringence and x-ray diffraction measurements. J. Mol. Biol. 210:113-126.
    • (1989) J. Mol. Biol. , vol.210 , pp. 113-126
    • Peckham, M.1    Irving, M.2
  • 30
    • 0031806116 scopus 로고    scopus 로고
    • Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethyl-rhodamine
    • Sabido-David, C., B. D. Brandmeier, J. S. Craik, J. E. T. Corrie, D. R. Trentham, and M. Irving. 1998a. Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethyl-rhodamine. Biophys. J. 74:3083-3092.
    • (1998) Biophys. J. , vol.74 , pp. 3083-3092
    • Sabido-David, C.1    Brandmeier, B.D.2    Craik, J.S.3    Corrie, J.E.T.4    Trentham, D.R.5    Irving, M.6
  • 31
    • 0032486127 scopus 로고    scopus 로고
    • Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibers
    • Sabido-David, C., S. C. Hopkins, L. D. Saraswat, S. Lowey, Y. E. Goldman, and M. Irving. 1998b. Orientation changes of fluorescent probes at five sites on the myosin regulatory light chain during contraction of single skeletal muscle fibers. J. Mol. Biol. 279:387-402.
    • (1998) J. Mol. Biol. , vol.279 , pp. 387-402
    • Sabido-David, C.1    Hopkins, S.C.2    Saraswat, L.D.3    Lowey, S.4    Goldman, Y.E.5    Irving, M.6
  • 32
    • 0018940148 scopus 로고
    • Control of tension development in scallop muscle fibres with foreign regulatory light chains
    • Simmons, R. M., and A. G. Szent-Györgyi. 1980. Control of tension development in scallop muscle fibres with foreign regulatory light chains. Nature. 286:626-628.
    • (1980) Nature , vol.286 , pp. 626-628
    • Simmons, R.M.1    Szent-Györgyi, A.G.2
  • 33
    • 0028362281 scopus 로고
    • Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: Myofilament lengths
    • Sosa, H., D. Popp, G. Ouyang, and H. E. Huxley. 1994. Ultrastructure of skeletal muscle fibers studied by a plunge quick freezing method: myofilament lengths. Biophys. J. 67:283-292.
    • (1994) Biophys. J. , vol.67 , pp. 283-292
    • Sosa, H.1    Popp, D.2    Ouyang, G.3    Huxley, H.E.4
  • 34
    • 0022429789 scopus 로고
    • The rapid generation of oligonucleotide-directed mutations at high-frequency using phosphorothioate-modified DNA
    • Taylor, J. W., J. Ott, and F. Eckstein. 1985. The rapid generation of oligonucleotide-directed mutations at high-frequency using phosphorothioate-modified DNA. Nucleic Acids Res. 13:8765-8785.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 8765-8785
    • Taylor, J.W.1    Ott, J.2    Eckstein, F.3
  • 35
    • 0034071048 scopus 로고    scopus 로고
    • A maximum entropy analysis of protein orientations using fluorescence polarization data from multiple probes
    • van der Heide, U. A., S. C. Hopkins, and Y. E. Goldman. 2000. A maximum entropy analysis of protein orientations using fluorescence polarization data from multiple probes. Biophys. J. 78:2138-2150.
    • (2000) Biophys. J. , vol.78 , pp. 2138-2150
    • Van Der Heide, U.A.1    Hopkins, S.C.2    Goldman, Y.E.3
  • 36
    • 0028853517 scopus 로고
    • Protein production in three different expression vectors from a single polymerase chain-reaction product
    • Winder, S. J., and J. Kendrick-Jones. 1995. Protein production in three different expression vectors from a single polymerase chain-reaction product. Anal. Biochem. 231:271-273.
    • (1995) Anal. Biochem. , vol.231 , pp. 271-273
    • Winder, S.J.1    Kendrick-Jones, J.2
  • 37
    • 0001891718 scopus 로고
    • Structure of relaxed myosin filaments in relation to nucleotide state in vertebrate skeletal muscle
    • Abstr
    • Wray, J. S. 1987. Structure of relaxed myosin filaments in relation to nucleotide state in vertebrate skeletal muscle. J. Muscle Res. Cell Motil. 8:62a. (Abstr.)
    • (1987) J. Muscle Res. Cell Motil. , vol.8
    • Wray, J.S.1
  • 39
    • 0030833060 scopus 로고    scopus 로고
    • X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle
    • Xu, S., S. Malinchik, D. Gilroy, T. Kraft, B. Brenner, and L. C. Yu. 1997. X-ray diffraction studies of cross-bridges weakly bound to actin in relaxed skinned fibers of rabbit psoas muscle. Biophys. J. 73:2292-2303.
    • (1997) Biophys. J. , vol.73 , pp. 2292-2303
    • Xu, S.1    Malinchik, S.2    Gilroy, D.3    Kraft, T.4    Brenner, B.5    Yu, L.C.6
  • 40
    • 0032726350 scopus 로고    scopus 로고
    • The M·ADP·Pi state is required for helical order in the thick filaments of skeletal muscle
    • Xu, S., J. Gu, T. Rhodes, B. Belknap, G. Rosenbaum, G. Offer, H. White, and L. C. Yu. 1999. The M·ADP·Pi state is required for helical order in the thick filaments of skeletal muscle. Biophys. J. 77:2665-2676.
    • (1999) Biophys. J. , vol.77 , pp. 2665-2676
    • Xu, S.1    Gu, J.2    Rhodes, T.3    Belknap, B.4    Rosenbaum, G.5    Offer, G.6    White, H.7    Yu, L.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.