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Volumn 170, Issue 2, 2010, Pages 307-312

Curvature variation along the tropomyosin molecule

Author keywords

Actin; Coiled coils; Electron microscopy; Molecular dynamics; Tropomyosin

Indexed keywords

ALANINE; ALPHA TROPOMYOSIN;

EID: 77951975707     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2009.12.017     Document Type: Article
Times cited : (24)

References (22)
  • 1
    • 26844510875 scopus 로고    scopus 로고
    • Regulation of muscle contraction by tropomyosin and troponin: how structure illuminates function
    • Brown J.H., Cohen C. Regulation of muscle contraction by tropomyosin and troponin: how structure illuminates function. Adv. Protein Chem. 2005, 71:121-159.
    • (2005) Adv. Protein Chem. , vol.71 , pp. 121-159
    • Brown, J.H.1    Cohen, C.2
  • 4
    • 0025130161 scopus 로고
    • Structural features in the heptad substructure and longer range repeats of two-stranded alpha-fibrous proteins
    • Conway J.F., Parry D.A.D. Structural features in the heptad substructure and longer range repeats of two-stranded alpha-fibrous proteins. Int. J. Biol. Macromol. 1990, 12:328-334.
    • (1990) Int. J. Biol. Macromol. , vol.12 , pp. 328-334
    • Conway, J.F.1    Parry, D.A.D.2
  • 5
    • 0000920828 scopus 로고
    • The packing of alpha-helices: simple coiled-coils
    • Crick F.H.C. The packing of alpha-helices: simple coiled-coils. Acta Crystallogr. 1953, 6:689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 6
    • 62449145371 scopus 로고    scopus 로고
    • Gestalt-binding of tropomyosin to actin filaments
    • Holmes K.C., Lehman W. Gestalt-binding of tropomyosin to actin filaments. J. Muscle Res. Cell Motil. 2008, 29:213-219.
    • (2008) J. Muscle Res. Cell Motil. , vol.29 , pp. 213-219
    • Holmes, K.C.1    Lehman, W.2
  • 8
    • 67349282758 scopus 로고    scopus 로고
    • Structural basis for the activation of muscle contraction by troponin and tropomyosin
    • Lehman W., Galińska-Rakoczy A., Hatch V., Tobacman L.S., Craig R. Structural basis for the activation of muscle contraction by troponin and tropomyosin. J. Mol. Biol. 2009, 388:673-681.
    • (2009) J. Mol. Biol. , vol.388 , pp. 673-681
    • Lehman, W.1    Galińska-Rakoczy, A.2    Hatch, V.3    Tobacman, L.S.4    Craig, R.5
  • 10
    • 73149102752 scopus 로고    scopus 로고
    • The shape and flexibility of tropomyosin coiled-coils: implications for actin filament assembly and regulation
    • Li X.E., Holmes K.C., Lehman W., Jung H., Fischer S. The shape and flexibility of tropomyosin coiled-coils: implications for actin filament assembly and regulation. J. Mol. Biol. 2010, 395:327-339.
    • (2010) J. Mol. Biol. , vol.395 , pp. 327-339
    • Li, X.E.1    Holmes, K.C.2    Lehman, W.3    Jung, H.4    Fischer, S.5
  • 11
    • 0028940312 scopus 로고
    • An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels
    • Lorenz M., Poole K.J.V., Popp D., Rosenbaum G., Holmes K.C. An atomic model of the unregulated thin filament obtained by X-ray fiber diffraction on oriented actin-tropomyosin gels. J. Mol. Biol. 1995, 246:108-119.
    • (1995) J. Mol. Biol. , vol.246 , pp. 108-119
    • Lorenz, M.1    Poole, K.J.V.2    Popp, D.3    Rosenbaum, G.4    Holmes, K.C.5
  • 12
    • 0017136639 scopus 로고
    • The 14-fold periodicity in alpha-tropomyosin and the interaction with actin
    • McLachlan A.D., Stewart M. The 14-fold periodicity in alpha-tropomyosin and the interaction with actin. J. Mol. Biol. 1976, 103:271-298.
    • (1976) J. Mol. Biol. , vol.103 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 15
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T., Iwasa M., Aihara T., Maéda Y., Narita A. The nature of the globular- to fibrous-actin transition. Nature 2009, 457:441-445.
    • (2009) Nature , vol.457 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maéda, Y.4    Narita, A.5
  • 16
    • 0016777712 scopus 로고
    • Analysis of the primary sequence of alpha-tropomyosin from rabbit skeletal muscle
    • Parry D.A.D. Analysis of the primary sequence of alpha-tropomyosin from rabbit skeletal muscle. J. Mol. Biol. 1975, 98:519-535.
    • (1975) J. Mol. Biol. , vol.98 , pp. 519-535
    • Parry, D.A.D.1
  • 18
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips G.N., Fillers J.P., Cohen C. Tropomyosin crystal structure and muscle regulation. J. Mol. Biol. 1986, 192:111-131.
    • (1986) J. Mol. Biol. , vol.192 , pp. 111-131
    • Phillips, G.N.1    Fillers, J.P.2    Cohen, C.3
  • 19
    • 0344198181 scopus 로고    scopus 로고
    • Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding
    • Singh A., Hitchcock-DeGregori S.E. Local destabilization of the tropomyosin coiled coil gives the molecular flexibility required for actin binding. Biochemistry 2003, 42:14114-14121.
    • (2003) Biochemistry , vol.42 , pp. 14114-14121
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 20
    • 33644795360 scopus 로고    scopus 로고
    • Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin
    • Singh A., Hitchcock-DeGregori S.E. Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin. Structure 2006, 14:43-50.
    • (2006) Structure , vol.14 , pp. 43-50
    • Singh, A.1    Hitchcock-DeGregori, S.E.2
  • 21
    • 0016765447 scopus 로고
    • Fourteen actin-binding sites on tropomyosin?
    • Stewart M., McLachlan A.D. Fourteen actin-binding sites on tropomyosin?. Nature 1975, 257:331-333.
    • (1975) Nature , vol.257 , pp. 331-333
    • Stewart, M.1    McLachlan, A.D.2
  • 22
    • 0017853508 scopus 로고
    • 2-terminal half and complete sequence
    • 2-terminal half and complete sequence. J. Biol. Chem. 1978, 253:1137-1148.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1137-1148
    • Stone, D.1    Smillie, L.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.