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Volumn 50, Issue 11, 2011, Pages 1839-1847

Binding properties of the calcium-activated F2 isoform of lethocerus troponin C

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROPERTIES; C-TERMINAL DOMAINS; CALCIUM SENSORS; FLIGHT MUSCLE; GLOBULAR DOMAINS; INSECT FLIGHT; ISOFORMS; MECHANICAL STRETCH; MODEL SYSTEM; ORDER OF MAGNITUDE; ORTHOLOGS; STRUCTURAL DIFFERENCES; TROPONIN; TROPONIN C; TROPONIN I;

EID: 79952793975     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi102076s     Document Type: Article
Times cited : (10)

References (41)
  • 1
    • 51249105761 scopus 로고    scopus 로고
    • Invertebrate muscles: Thin and thick filament structure; Molecular basis of contraction and its regulation, catch and asynchronous muscle
    • Hooper, S. L., Hobbs, K. H., and Thuma, J. B. (2008) Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle Prog. Neurobiol. 86, 72-127
    • (2008) Prog. Neurobiol. , vol.86 , pp. 72-127
    • Hooper, S.L.1    Hobbs, K.H.2    Thuma, J.B.3
  • 2
    • 17744382824 scopus 로고    scopus 로고
    • Structural based insights into the role of troponin in cardiac muscle pathophysiology
    • DOI 10.1007/s10974-004-5879-2
    • Li, M. X., Wang, X., and Sykes, B. D. (2004) Structural based insights into the role of troponin in cardiac muscle pathophysiol J. Muscle Res. Cell Motil. 25, 559-579 (Pubitemid 40575632)
    • (2004) Journal of Muscle Research and Cell Motility , vol.25 , Issue.7 , pp. 559-579
    • Li, M.X.1    Wang, X.2    Sykes, B.D.3
  • 3
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon, A. M., Homsher, E., and Regnier, M. (2000) Regulation of contraction in striated muscle Physiol. Rev. 80, 853
    • (2000) Physiol. Rev. , vol.80 , pp. 853
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 4
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • DOI 10.1006/jmbi.1996.0800
    • Vibert, P., Craig, R., and Lehman, W. H. (1997) Steric-model for activation of muscle thin filaments J. Mol. Biol. 266, 8-14 (Pubitemid 27170513)
    • (1997) Journal of Molecular Biology , vol.266 , Issue.1 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 5
    • 84934435143 scopus 로고    scopus 로고
    • Disposition and dynamics: Interdomain orientations in troponin
    • Hoffman, R. M. and Sykes, B. D. (2007) Disposition and dynamics: Interdomain orientations in troponin Adv. Exp. Med. Biol. 592, 59-70
    • (2007) Adv. Exp. Med. Biol. , vol.592 , pp. 59-70
    • Hoffman, R.M.1    Sykes, B.D.2
  • 6
    • 0015218120 scopus 로고
    • Reconstitution of troponin activity from three protein components
    • Greaser, M. L. and Gergely, J. (1971) Reconstitution of troponin activity from three protein components J. Biol. Chem. 246, 4226-4233
    • (1971) J. Biol. Chem. , vol.246 , pp. 4226-4233
    • Greaser, M.L.1    Gergely, J.2
  • 7
    • 0022001045 scopus 로고
    • Structure of the calcium regulatory muscle protein troponin-C at 2.8 A resolution
    • DOI 10.1038/313653a0
    • Herzberg, O. and James, M. N. G. (1985) Structure of the calcium regulatory muscle protein troponin C at 28 Å resolution Nature 313, 653-659 (Pubitemid 15172468)
    • (1985) Nature , vol.313 , Issue.6004 , pp. 653-659
    • Herzberg, O.1    James, M.N.G.2
  • 8
    • 0023771079 scopus 로고
    • Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution
    • Herzberg, O. and James, M. N. G. (1988) Refined crystal structure of troponin C from turkey skeletal muscle at 2.0 Å resolution J. Mol. Biol. 203, 761-779
    • (1988) J. Mol. Biol. , vol.203 , pp. 761-779
    • Herzberg, O.1    James, M.N.G.2
  • 10
    • 0028891899 scopus 로고
    • NMR solution structure of calcium saturated skeletal muscle troponin C
    • Slupsky, C. M. and Sykes, B. D. (1995) NMR solution structure of calcium saturated skeletal muscle troponin C Biochemistry 34, 15953-15964
    • (1995) Biochemistry , vol.34 , pp. 15953-15964
    • Slupsky, C.M.1    Sykes, B.D.2
  • 12
    • 0032574791 scopus 로고    scopus 로고
    • Crystal structure of troponin C in complex with troponin i fragment at 2.3-Å resolution
    • Vassylyev, D. G., Takeda, S., Wakatsuki, S., Maeda, K., and Maeda, Y. (1998) Crystal structure of troponin C in complex with troponin I fragment at 2.3-Å resolution Proc. Natl. Acad. Sci. U.S.A. 95, 4847-4852
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 4847-4852
    • Vassylyev, D.G.1    Takeda, S.2    Wakatsuki, S.3    Maeda, K.4    Maeda, Y.5
  • 13
    • 0035964181 scopus 로고    scopus 로고
    • Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I
    • DOI 10.1021/bi010748+
    • Mercier, P., Spyracopoulos, L., and Sykes, B. D. (2001) Structure, Dynamics, and Thermodynamics of the Structural Domain of Troponin C in Complex with the Regulatory Peptide 1-40 of Troponin I Biochemistry 40, 10063-10077 (Pubitemid 32800114)
    • (2001) Biochemistry , vol.40 , Issue.34 , pp. 10063-10077
    • Mercier, P.1    Spyracopoulos, L.2    Sykes, B.D.3
  • 16
    • 78651022505 scopus 로고
    • The excitation and contraction of the flight muscle of insects
    • Pringle, J. M. (1949) The excitation and contraction of the flight muscle of insects J. Physiol. 108, 226-232
    • (1949) J. Physiol. , vol.108 , pp. 226-232
    • Pringle, J.M.1
  • 18
    • 0020644351 scopus 로고
    • Role of cross-bridge distorsion in the small-signal mechanical dynamics of insect and rabbit striated muscle
    • Thorson, J. and White, D. C. (1983) Role of cross-bridge distorsion in the small-signal mechanical dynamics of insect and rabbit striated muscle J. Physiol. 343, 59-64
    • (1983) J. Physiol. , vol.343 , pp. 59-64
    • Thorson, J.1    White, D.C.2
  • 20
    • 1842562372 scopus 로고    scopus 로고
    • A troponin switch that regulates muscle contraction by stretch instead of calcium
    • DOI 10.1038/sj.emboj.7600097
    • Agianian, B., Kržič, U., Qiu, F., Linke, W. A., Leonard, K., and Bullard, B. (2004) A troponin switch that regulates muscle contraction by stretch instead of calcium EMBO J. 23, 772-779 (Pubitemid 38418744)
    • (2004) EMBO Journal , vol.23 , Issue.4 , pp. 772-779
    • Agianian, B.1    Krzic, U.2    Qiu, F.3    Linke, W.A.4    Leonard, K.5    Bullard, B.6
  • 21
    • 4143128692 scopus 로고    scopus 로고
    • Ca-activation and stretch-activation in insect flight muscle
    • DOI 10.1529/biophysj.103.037374
    • Linari, M., Reedy, M. K., Reedy, M. C., Lombardi, V., and Piazzesi, G. (2004) Ca-activation and stretch-activation in insect flight muscle Biophys. J. 87, 1101-1111 (Pubitemid 39095088)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 1101-1111
    • Linari, M.1    Reedy, M.K.2    Reedy, M.C.3    Lombardi, V.4    Piazzesi, G.5
  • 22
    • 33645231253 scopus 로고    scopus 로고
    • Role of calcium in the regulation of mechanical power in insect flight
    • Gordon, S. and Dickinson, M. H. (2006) Role of calcium in the regulation of mechanical power in insect flight Proc. Natl. Acad. Sci. U.S.A. 103, 4311-4315
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 4311-4315
    • Gordon, S.1    Dickinson, M.H.2
  • 23
    • 0037570580 scopus 로고    scopus 로고
    • Troponin C in different insect muscle types: Identification of two isoforms in Lethocerus, Drosophila and Anopheles that are specific to asynchronous flight muscle in the adult insect
    • DOI 10.1042/BJ20021814
    • Qiu, F., Lakey, A., Agianian, B., Hutchings, A., Butcher, G. W., Labeit, S., Leonard, K., and Bullard, B. (2003) Troponin C in different insect muscle types: Identification of two isoforms in Lethocerus, Drosophila and Anopheles that are specific to asynchronous flight muscle in the adult insect Biochem. J. 371, 811-821 (Pubitemid 36578880)
    • (2003) Biochemical Journal , vol.371 , Issue.3 , pp. 811-821
    • Qiu, F.1    Lakey, A.2    Agianian, B.3    Hutchings, A.4    Butcher, G.W.5    Labeit, S.6    Leonard, K.7    Bullard, B.8
  • 24
    • 77249147334 scopus 로고    scopus 로고
    • Regulation of oscillatory contraction in insect flight muscle by troponin
    • Kržič, U. and Rybin, V. 2010, Regulation of oscillatory contraction in insect flight muscle by troponin J. Mol. Biol. 397, 110-118
    • (2010) J. Mol. Biol. , vol.397 , pp. 110-118
    • Kržič, U.1    Rybin, V.2
  • 26
    • 34447263324 scopus 로고    scopus 로고
    • The Structure of Lethocerus Troponin C: Insights into the Mechanism of Stretch Activation in Muscles
    • DOI 10.1016/j.str.2007.05.007, PII S0969212607001876
    • De Nicola, G., Burkart, C., Qiu, F., Agianian, B., Labeit, S., and Martin, S. 2007, The structure of Lethocerus troponin C: Insights into the mechanism of stretch activation in muscles Structure 15, 813-824 (Pubitemid 47042429)
    • (2007) Structure , vol.15 , Issue.7 , pp. 813-824
    • De Nicola, G.1    Burkart, C.2    Qiu, F.3    Agianian, B.4    Labeit, S.5    Martin, S.6    Bullard, B.7    Pastore, A.8
  • 28
    • 12244269333 scopus 로고    scopus 로고
    • Kinetic analysis of the interactions between Troponin C (TnC) and Troponin I (TnI) binding peptides: Evidence for separate binding sites for the 'structural' N-terminus and the 'regulatory' C-terminus of TnI on TnC
    • DOI 10.1002/jmr.606
    • Tripet, B., de Crescenzo, G., Grothe, S., O'Connor-McCourt, M., and Hodges, R. S. (2003) Kinetic analysis of the interactions between Troponin C (TnC) and Troponin I (TnI) binding peptides: Evidence for separate binding sites for the 'structural' N-terminus and the 'regulatory' C-terminus of TnI on TnC J. Mol. Recognit. 16, 37-53 (Pubitemid 36198959)
    • (2003) Journal of Molecular Recognition , vol.16 , Issue.1 , pp. 37-53
    • Tripet, B.1    De Crescenzo, G.2    Grothe, S.3    O'Connor-McCourt, M.4    Hodges, R.S.5
  • 29
    • 0034696575 scopus 로고    scopus 로고
    • 2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I
    • DOI 10.1021/bi992579n
    • 2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I Biochemistry 39, 2902-2911 (Pubitemid 30159395)
    • (2000) Biochemistry , vol.39 , Issue.11 , pp. 2902-2911
    • Mercier, P.1    Li, M.X.2    Sykes, B.D.3
  • 31
    • 0025823438 scopus 로고
    • Calcium binding to calmodulin and its globular domains
    • Linse, S. A., Helmersson, A., and Forsen, S. (1991) Calcium binding to calmodulin and its globular domains J. Biol. Chem. 266, 8050-8054 (Pubitemid 21906473)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.13 , pp. 8050-8054
    • Linse, S.1    Helmersson, A.2    Forsen, S.3
  • 34
    • 77749290045 scopus 로고    scopus 로고
    • The solution structure of the apo C-terminal domain of Lethocerus F1 troponin C isoform
    • De Nicola, G., Martin, S., Bullard, B., and Pastore, A. (2010) The solution structure of the apo C-terminal domain of Lethocerus F1 troponin C isoform Biochemistry 49, 1719-1726
    • (2010) Biochemistry , vol.49 , pp. 1719-1726
    • De Nicola, G.1    Martin, S.2    Bullard, B.3    Pastore, A.4
  • 35
    • 0017280755 scopus 로고
    • The relationship between biological activity and primary structure of troponin i from white skeletal muscle of the rabbit
    • Syska, H., Wilkinson, J. M., Grand, R. J. A., and Perry, S. V. (1976) The relationship between biological activity and primary structure of troponin I from white skeletal muscle of the rabbit Biochem. J. 153, 375-387
    • (1976) Biochem. J. , vol.153 , pp. 375-387
    • Syska, H.1    Wilkinson, J.M.2    Grand, R.J.A.3    Perry, S.V.4
  • 40
    • 0028235402 scopus 로고
    • Gold/Fab immuno electron microscopy localization of troponin H and troponin T in Lethocerus flight muscle
    • DOI 10.1006/jmbi.1994.1350
    • Reedy, M. C., Reedy, M. K., Leonard, K. R., and Bullard, B. (1994) Gold/Fab immuno electron microscopy localisation of troponin H and troponin T in Lethocerus flight muscle J. Mol. Biol. 239, 52-67 (Pubitemid 24175081)
    • (1994) Journal of Molecular Biology , vol.239 , Issue.1 , pp. 52-67
    • Reedy, M.C.1    Reedy, M.K.2    Leonard, K.R.3    Bullard, B.4
  • 41
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • DOI 10.1006/abio.2000.4880
    • Sreerama, N. and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set Anal. Biochem. 287, 252-260 (Pubitemid 32006234)
    • (2000) Analytical Biochemistry , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.