메뉴 건너뛰기




Volumn 73, Issue 2, 2008, Pages 338-350

Isoform-specific variation in the intrinsic disorder of troponin I

Author keywords

Dynamics; Native unfolding; Prediction; Sequence; Structural bioinformatics; Structure

Indexed keywords

INTRINSIC DISORDER PROTEIN; TROPOMYOSIN; TROPONIN I; TROPONIN T; UNCLASSIFIED DRUG;

EID: 52249099866     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22063     Document Type: Article
Times cited : (14)

References (78)
  • 1
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • Gordon AM, Homsher E, Regnier M. Regulation of contraction in striated muscle. Physiol Rev 2000;80:853
    • (2000) Physiol Rev , vol.80 , pp. 853
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 2
    • 0016213363 scopus 로고
    • Troponin, tropomyosin, and actin interactions in the Ca2+ regulation of muscle contraction
    • Potter JD, Gergely J. Troponin, tropomyosin, and actin interactions in the Ca2+ regulation of muscle contraction. Biochemistry 1974;13:2697.
    • (1974) Biochemistry , vol.13 , pp. 2697
    • Potter, J.D.1    Gergely, J.2
  • 3
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • Vibert P, Craig R, Lehman W. Steric-model for activation of muscle thin filaments. J Mol Biol 1997;266:8.
    • (1997) J Mol Biol , vol.266 , pp. 8
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 5
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • Geeves MA, Lehrer SS. Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit. Biophys J 1994;67:273.
    • (1994) Biophys J , vol.67 , pp. 273
    • Geeves, M.A.1    Lehrer, S.S.2
  • 6
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • McKillop DF, Geeves MA. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J 1993;65:693.
    • (1993) Biophys J , vol.65 , pp. 693
    • McKillop, D.F.1    Geeves, M.A.2
  • 7
    • 0023042847 scopus 로고
    • Tropomyosin crystal structure and muscle regulation
    • Phillips GNJ, Fillers JP, Cohen C. Tropomyosin crystal structure and muscle regulation. J Mol Biol 1986;192:111.
    • (1986) J Mol Biol , vol.192 , pp. 111
    • Phillips, G.N.J.1    Fillers, J.P.2    Cohen, C.3
  • 8
    • 33747767574 scopus 로고    scopus 로고
    • A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle
    • Poole KJV, Lorenz M, Evans G, Rosenbaum G, Pirani A, Craig R, Tobacman LS, Lehman W, Holmes KC. A comparison of muscle thin filament models obtained from electron microscopy reconstructions and low-angle X-ray fibre diagrams from non-overlap muscle. J Struct Biol 2006;155:273.
    • (2006) J Struct Biol , vol.155 , pp. 273
    • Poole, K.J.V.1    Lorenz, M.2    Evans, G.3    Rosenbaum, G.4    Pirani, A.5    Craig, R.6    Tobacman, L.S.7    Lehman, W.8    Holmes, K.C.9
  • 12
    • 0042624696 scopus 로고    scopus 로고
    • Pulling the calcium trigger
    • Sykes BD. Pulling the calcium trigger. Nat Struct Biol 2003;10:588.
    • (2003) Nat Struct Biol , vol.10 , pp. 588
    • Sykes, B.D.1
  • 13
    • 0022931544 scopus 로고
    • A model for the Ca2+-induced conformational transition of troponin C. A trigger for muscle contraction
    • Herzberg O, Moult J, James MNG. A model for the Ca2+-induced conformational transition of troponin C. A trigger for muscle contraction. J Biol Chem 1986;261:2638.
    • (1986) J Biol Chem , vol.261 , pp. 2638
    • Herzberg, O.1    Moult, J.2    James, M.N.G.3
  • 14
    • 0015935352 scopus 로고
    • Purification and properties of the components from troponin
    • Greaser ML, Gergely J. Purification and properties of the components from troponin. J Biol Chem 1973;248:2125.
    • (1973) J Biol Chem , vol.248 , pp. 2125
    • Greaser, M.L.1    Gergely, J.2
  • 15
    • 0031855272 scopus 로고    scopus 로고
    • Perry S. Troponin T. genetics, properties and function. J Muscle Res Cell Motil 1998;19:575.
    • Perry S. Troponin T. genetics, properties and function. J Muscle Res Cell Motil 1998;19:575.
  • 17
    • 34548014295 scopus 로고    scopus 로고
    • Tuning cardiac performance in ischemic heart disease and failure by modulating myofilament function
    • Day S, Westfall M, Metzger J. Tuning cardiac performance in ischemic heart disease and failure by modulating myofilament function. J Mol Med 2007.
    • (2007) J Mol Med
    • Day, S.1    Westfall, M.2    Metzger, J.3
  • 18
    • 0037470225 scopus 로고    scopus 로고
    • Differential regulation of the actomyosin interaction by skeletal and cardiac troponin isoforms
    • Maytum R, Westerdorf B, Jaquet K, Geeves MA. Differential regulation of the actomyosin interaction by skeletal and cardiac troponin isoforms. J Biol Chem 2003;278:6696.
    • (2003) J Biol Chem , vol.278 , pp. 6696
    • Maytum, R.1    Westerdorf, B.2    Jaquet, K.3    Geeves, M.A.4
  • 19
    • 34247642743 scopus 로고    scopus 로고
    • Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C
    • Davis JP, Norman C, Kobayashi T, Solaro RJ, Swartz DR, Tikunova SB. Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C. Biophys J 2007;92:3195.
    • (2007) Biophys J , vol.92 , pp. 3195
    • Davis, J.P.1    Norman, C.2    Kobayashi, T.3    Solaro, R.J.4    Swartz, D.R.5    Tikunova, S.B.6
  • 20
    • 0030992773 scopus 로고    scopus 로고
    • Slow skeletal troponin I gene transfer, expression, and myofilament incorporation enhances adult cardiac myocyte contractile function
    • Westfall MV, Rust EM, Metzger JM. Slow skeletal troponin I gene transfer, expression, and myofilament incorporation enhances adult cardiac myocyte contractile function. Proc Natl Acad Sci USA 1997;94:5444.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5444
    • Westfall, M.V.1    Rust, E.M.2    Metzger, J.M.3
  • 21
    • 0035947749 scopus 로고    scopus 로고
    • Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle
    • Kentish JC, McCloskey DT, Layland J, Palmer S, Leiden JM, Martin AF, Solaro RJ. Phosphorylation of troponin I by protein kinase A accelerates relaxation and crossbridge cycle kinetics in mouse ventricular muscle. Circ Res 2001;88:1059.
    • (2001) Circ Res , vol.88 , pp. 1059
    • Kentish, J.C.1    McCloskey, D.T.2    Layland, J.3    Palmer, S.4    Leiden, J.M.5    Martin, A.F.6    Solaro, R.J.7
  • 23
    • 14844344027 scopus 로고    scopus 로고
    • Regulation of cardiac contractile function by troponin I phosphorylation
    • Layland J, Solaro RJ, Shah AM. Regulation of cardiac contractile function by troponin I phosphorylation. Cardiovasc Res 2005;66:12.
    • (2005) Cardiovasc Res , vol.66 , pp. 12
    • Layland, J.1    Solaro, R.J.2    Shah, A.M.3
  • 24
    • 17744382824 scopus 로고    scopus 로고
    • Structural based insights into the role of troponin in cardiac muscle pathophysiology
    • Li MX, Wang X, Sykes BD. Structural based insights into the role of troponin in cardiac muscle pathophysiology. J Muscle Res Cell Motil 2004;25:559.
    • (2004) J Muscle Res Cell Motil , vol.25 , pp. 559
    • Li, M.X.1    Wang, X.2    Sykes, B.D.3
  • 25
    • 0033520429 scopus 로고    scopus 로고
    • In search of the proteins that cause myocardial stunning
    • Foster DB, Van Eyk JE. In search of the proteins that cause myocardial stunning. Circ Res 1999;85:470.
    • (1999) Circ Res , vol.85 , pp. 470
    • Foster, D.B.1    Van Eyk, J.E.2
  • 26
    • 0242469193 scopus 로고    scopus 로고
    • C-terminal truncation of cardiac troponin I causes divergent effects on ATPase and force: Implications for the pathophysiology of myocardial stunning
    • Foster DB, Noguchi T, VanBuren P, Murphy AM, Van Eyk JE. C-terminal truncation of cardiac troponin I causes divergent effects on ATPase and force: implications for the pathophysiology of myocardial stunning. Circ Res 2003;93:917.
    • (2003) Circ Res , vol.93 , pp. 917
    • Foster, D.B.1    Noguchi, T.2    VanBuren, P.3    Murphy, A.M.4    Van Eyk, J.E.5
  • 27
    • 34748818674 scopus 로고    scopus 로고
    • Phosphorylation -dependent Conformational Transition of the Cardiac-Specific N-Extension of Troponin I in Cardiac Troponin
    • Howarth JW, Meller J, Solaro RJ, Trewhella J, Rosevear PR. Phosphorylation -dependent Conformational Transition of the Cardiac-Specific N-Extension of Troponin I in Cardiac Troponin. J Mol Biol 2007;373:706.
    • (2007) J Mol Biol , vol.373 , pp. 706
    • Howarth, J.W.1    Meller, J.2    Solaro, R.J.3    Trewhella, J.4    Rosevear, P.R.5
  • 28
    • 2442429819 scopus 로고    scopus 로고
    • NMR and mutagenesis studies on the phosphorylation region of human cardiac troponin I
    • Ward D, Brewer S, Gallon C, Gao Y, Levine B, Trayer I. NMR and mutagenesis studies on the phosphorylation region of human cardiac troponin I. Biochemistry 2004;43:5772.
    • (2004) Biochemistry , vol.43 , pp. 5772
    • Ward, D.1    Brewer, S.2    Gallon, C.3    Gao, Y.4    Levine, B.5    Trayer, I.6
  • 29
    • 0034696575 scopus 로고    scopus 로고
    • Role of the structural domain of troponin C in muscle regulation: NMR studies of Ca2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I
    • Mercier P, Li MX, Sykes BD. Role of the structural domain of troponin C in muscle regulation: NMR studies of Ca2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I. Biochemistry 2000;39:2902.
    • (2000) Biochemistry , vol.39 , pp. 2902
    • Mercier, P.1    Li, M.X.2    Sykes, B.D.3
  • 30
    • 0037588762 scopus 로고    scopus 로고
    • Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form
    • Takeda S, Yamashita A, Maeda K, Maeda Y. Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form. Nature 2003;424:35.
    • (2003) Nature , vol.424 , pp. 35
    • Takeda, S.1    Yamashita, A.2    Maeda, K.3    Maeda, Y.4
  • 32
    • 0031554903 scopus 로고    scopus 로고
    • Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca2+-dependent regulation of muscle contraction
    • Tripet B, Van Eyk JE, Hodges RS. Mapping of a second actin-tropomyosin and a second troponin C binding site within the C terminus of troponin I, and their importance in the Ca2+-dependent regulation of muscle contraction. J Mol Biol 1997;271:728.
    • (1997) J Mol Biol , vol.271 , pp. 728
    • Tripet, B.1    Van Eyk, J.E.2    Hodges, R.S.3
  • 34
    • 23944457539 scopus 로고    scopus 로고
    • Structural Basis for Ca(2+)-regulated Muscle Relaxation at Interaction Sites of Troponin with Actin and Tropomyosin
    • Murakami K, Yumoto F, Ohki SY, Yasunaga T, Tanokura M, Wakabayashi T. Structural Basis for Ca(2+)-regulated Muscle Relaxation at Interaction Sites of Troponin with Actin and Tropomyosin. J Mol Biol 2005;352:178.
    • (2005) J Mol Biol , vol.352 , pp. 178
    • Murakami, K.1    Yumoto, F.2    Ohki, S.Y.3    Yasunaga, T.4    Tanokura, M.5    Wakabayashi, T.6
  • 38
    • 0036436914 scopus 로고    scopus 로고
    • Equilibrium unfolding and conformational plasticity of troponin I and T
    • Martins SM, Chapeaurouge A, Ferreira ST. Equilibrium unfolding and conformational plasticity of troponin I and T. Eur J Biochem 2002;269:5484.
    • (2002) Eur J Biochem , vol.269 , pp. 5484
    • Martins, S.M.1    Chapeaurouge, A.2    Ferreira, S.T.3
  • 39
    • 33748280715 scopus 로고    scopus 로고
    • Abundance of intrinsic disorder in protein associated with cardiovascular disease
    • Cheng Y, LeGall T, Oldfield CJ, Dunker AK, Uversky VN. Abundance of intrinsic disorder in protein associated with cardiovascular disease. Biochemistry 2006;45:10448.
    • (2006) Biochemistry , vol.45 , pp. 10448
    • Cheng, Y.1    LeGall, T.2    Oldfield, C.J.3    Dunker, A.K.4    Uversky, V.N.5
  • 40
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker BA, Portman JJ, Wolynes PG. Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc Natl Acad Sci USA 2000;97:8868.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8868
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 41
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky VN. Natively unfolded proteins: a point where biology waits for physics. Protein Sci 2002;11:739.
    • (2002) Protein Sci , vol.11 , pp. 739
    • Uversky, V.N.1
  • 42
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky VN, Gillespie JR, Fink AL. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 2000;41:415.
    • (2000) Proteins , vol.41 , pp. 415
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 44
    • 33748258328 scopus 로고    scopus 로고
    • A practical overview of protein disorder prediction methods
    • Ferron F, Longhi S, Canard B, Karlin D. A practical overview of protein disorder prediction methods. Proteins 2006;65:1.
    • (2006) Proteins , vol.65 , pp. 1
    • Ferron, F.1    Longhi, S.2    Canard, B.3    Karlin, D.4
  • 46
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud C, Bissery V, Benchetrit T, Mornon JP. Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett 1987;224:149.
    • (1987) FEBS Lett , vol.224 , pp. 149
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 47
    • 33846630895 scopus 로고    scopus 로고
    • A generalized analysis of hydrophobic and loop clusters within globular protein sequences
    • Eudes R, Le Tuan K, Delettre J, Mornon JP, Callebaut I. A generalized analysis of hydrophobic and loop clusters within globular protein sequences. BMC Struct Biol 2007;7:2.
    • (2007) BMC Struct Biol , vol.7 , pp. 2
    • Eudes, R.1    Le Tuan, K.2    Delettre, J.3    Mornon, J.P.4    Callebaut, I.5
  • 48
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztányi Z, Csizmók V, Tompa P, Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 2005;21:3433.
    • (2005) Bioinformatics , vol.21 , pp. 3433
    • Dosztányi, Z.1    Csizmók, V.2    Tompa, P.3    Simon, I.4
  • 49
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztányi Z, Csizmók V, Tompa P, Simon I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J Mol Biol 2005;347:827.
    • (2005) J Mol Biol , vol.347 , pp. 827
    • Dosztányi, Z.1    Csizmók, V.2    Tompa, P.3    Simon, I.4
  • 53
    • 0242267500 scopus 로고    scopus 로고
    • Obradovic Z, Peng K, Vucetic S, Radivojac P, Brown CJ, Dunker AK. Predicting intrinsic disorder from amino acid sequence. Proteins 2003;53Suppl 6:566.
    • Obradovic Z, Peng K, Vucetic S, Radivojac P, Brown CJ, Dunker AK. Predicting intrinsic disorder from amino acid sequence. Proteins 2003;53Suppl 6:566.
  • 54
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 2004;337:635.
    • (2004) J Mol Biol , vol.337 , pp. 635
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 56
    • 0026475673 scopus 로고
    • Detection of secondary structure elements in proteins by hydrophobic cluster analysis
    • Woodcock S, Mornon J, Henrissat B. Detection of secondary structure elements in proteins by hydrophobic cluster analysis. Protein Eng 1992;5:629.
    • (1992) Protein Eng , vol.5 , pp. 629
    • Woodcock, S.1    Mornon, J.2    Henrissat, B.3
  • 57
    • 27744497723 scopus 로고    scopus 로고
    • The role of electrostatics in the interaction of the inhibitory region of troponin I with troponin C
    • Lindhout DA, Boyko RF, Corson DC, Li MX, Sykes BD. The role of electrostatics in the interaction of the inhibitory region of troponin I with troponin C. Biochemistry 2005;44:14750.
    • (2005) Biochemistry , vol.44 , pp. 14750
    • Lindhout, D.A.1    Boyko, R.F.2    Corson, D.C.3    Li, M.X.4    Sykes, B.D.5
  • 61
    • 6344277430 scopus 로고    scopus 로고
    • Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein
    • Weathers EA, Paulaitis ME, Woolf TB, Hoh JH. Reduced amino acid alphabet is sufficient to accurately recognize intrinsically disordered protein. FEBS Lett 2004;576:348.
    • (2004) FEBS Lett , vol.576 , pp. 348
    • Weathers, E.A.1    Paulaitis, M.E.2    Woolf, T.B.3    Hoh, J.H.4
  • 62
    • 0032734506 scopus 로고    scopus 로고
    • Kinetics of thin filament activation probed by fluorescence of N-((2-(Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1, 3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: Implications for regulation of muscle contraction
    • Brenner B, Chalovich J. Kinetics of thin filament activation probed by fluorescence of N-((2-(Iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1, 3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle contraction. Biophys J 1999;77:2692.
    • (1999) Biophys J , vol.77 , pp. 2692
    • Brenner, B.1    Chalovich, J.2
  • 63
    • 33847747433 scopus 로고    scopus 로고
    • Calcium regulation of troponin and its role in the dynamics of contraction and relaxation
    • Stehle R, Iorga B, Pfitzer G. Calcium regulation of troponin and its role in the dynamics of contraction and relaxation. Am J Physiol Regul Integr Comp Physiol 2007;292:R1125.
    • (2007) Am J Physiol Regul Integr Comp Physiol , vol.292
    • Stehle, R.1    Iorga, B.2    Pfitzer, G.3
  • 64
    • 34250174756 scopus 로고    scopus 로고
    • Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments
    • Boussouf SE, Maytum R, Jaquet K, Geeves MA. Role of tropomyosin isoforms in the calcium sensitivity of striated muscle thin filaments. J Muscle Res Cell Motil 2007;28:49.
    • (2007) J Muscle Res Cell Motil , vol.28 , pp. 49
    • Boussouf, S.E.1    Maytum, R.2    Jaquet, K.3    Geeves, M.A.4
  • 65
    • 0037144483 scopus 로고    scopus 로고
    • Single mutation (A162H) in human cardiac troponin I corrects acid pH sensitivity of Ca2+-regulated actomyosin S1 ATPase
    • Dargis R, Pearlstone JR, Barrette-Ng I, Edwards H, Smillie LB. Single mutation (A162H) in human cardiac troponin I corrects acid pH sensitivity of Ca2+-regulated actomyosin S1 ATPase. J Biol Chem 2002;277:34662.
    • (2002) J Biol Chem , vol.277 , pp. 34662
    • Dargis, R.1    Pearlstone, J.R.2    Barrette-Ng, I.3    Edwards, H.4    Smillie, L.B.5
  • 66
    • 34447572663 scopus 로고    scopus 로고
    • Single amino acid substitutions define isoform-specific effects of troponin I on myofilament Ca(2+) and pH sensitivity
    • Westfall M, Metzger J. Single amino acid substitutions define isoform-specific effects of troponin I on myofilament Ca(2+) and pH sensitivity. J Mol Cell Cardiol 2007.
    • (2007) J Mol Cell Cardiol
    • Westfall, M.1    Metzger, J.2
  • 67
    • 0033997037 scopus 로고    scopus 로고
    • Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes
    • Lavigne P, Bagu JR, Boyko R, Willard L, Holmes CF, Sykes BD. Structure-based thermodynamic analysis of the dissociation of protein phosphatase-1 catalytic subunit and microcystin-LR docked complexes. Protein Sci 2000;9:252.
    • (2000) Protein Sci , vol.9 , pp. 252
    • Lavigne, P.1    Bagu, J.R.2    Boyko, R.3    Willard, L.4    Holmes, C.F.5    Sykes, B.D.6
  • 68
    • 0036708252 scopus 로고    scopus 로고
    • Mechanisms of action of novel cardiotonic agents
    • Endoh M. Mechanisms of action of novel cardiotonic agents. J Cardiovasc Pharmacol 2002;40:323.
    • (2002) J Cardiovasc Pharmacol , vol.40 , pp. 323
    • Endoh, M.1
  • 70
    • 33750999318 scopus 로고    scopus 로고
    • Disorder and sequence repeats in hub proteins and their implications for network evolution
    • Dosztányi Z, Chen J, Dunker AK, Simon I, Tompa P. Disorder and sequence repeats in hub proteins and their implications for network evolution. J Proteome Res 2006;5:2985.
    • (2006) J Proteome Res , vol.5 , pp. 2985
    • Dosztányi, Z.1    Chen, J.2    Dunker, A.K.3    Simon, I.4    Tompa, P.5
  • 71
    • 0036354279 scopus 로고    scopus 로고
    • Troponin I inhibits capillary endothelial cell proliferation by interaction with the cell's bFGF receptor
    • Feldman L, Rouleau C. Troponin I inhibits capillary endothelial cell proliferation by interaction with the cell's bFGF receptor. Microvasc Res 2002;63:41.
    • (2002) Microvasc Res , vol.63 , pp. 41
    • Feldman, L.1    Rouleau, C.2
  • 73
    • 0037457823 scopus 로고    scopus 로고
    • Polycystin-2 interacts with troponin I, an angiogenesis inhibitor
    • Li Q, Shen PY, Wu G, Chen XZ. Polycystin-2 interacts with troponin I, an angiogenesis inhibitor. Biochemistry 2003;42:450.
    • (2003) Biochemistry , vol.42 , pp. 450
    • Li, Q.1    Shen, P.Y.2    Wu, G.3    Chen, X.Z.4
  • 74
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa P, Szász C, Buday L. Structural disorder throws new light on moonlighting. Trends Biochem Sci 2005;30:484.
    • (2005) Trends Biochem Sci , vol.30 , pp. 484
    • Tompa, P.1    Szász, C.2    Buday, L.3
  • 75
    • 33646112404 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational switch in spin-labeled phospholamban bound to SERCA
    • Karim CB, Zhang Z, Howard EC, Torgersen KD, Thomas DD. Phosphorylation-dependent conformational switch in spin-labeled phospholamban bound to SERCA. J Mol Biol 2006;358:1032.
    • (2006) J Mol Biol , vol.358 , pp. 1032
    • Karim, C.B.1    Zhang, Z.2    Howard, E.C.3    Torgersen, K.D.4    Thomas, D.D.5
  • 76
    • 34547462095 scopus 로고    scopus 로고
    • Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity
    • Borg M, Mittag T, Pawson T, Tyers M, Forman-Kay JD, Chan HS. Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proc Natl Acad Sci USA 2007;104:9650.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 9650
    • Borg, M.1    Mittag, T.2    Pawson, T.3    Tyers, M.4    Forman-Kay, J.D.5    Chan, H.S.6
  • 78
    • 37349117667 scopus 로고    scopus 로고
    • Modulation of cardiac troponin C function by the cardiac-specific N-terminus of troponin I: Influence of PKA phosphorylation and involvement in cardiomyopathies
    • Baryshnikova OK, Li MX, Sykes BD. Modulation of cardiac troponin C function by the cardiac-specific N-terminus of troponin I: influence of PKA phosphorylation and involvement in cardiomyopathies. J Mol Biol 2008;375:735.
    • (2008) J Mol Biol , vol.375 , pp. 735
    • Baryshnikova, O.K.1    Li, M.X.2    Sykes, B.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.