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Volumn 2014, Issue 3, 2014, Pages

Small molecule-mediated refolding and activation of myosin motor function

Author keywords

[No Author keywords available]

Indexed keywords

5 [1 (3, 4 DIMETHOXYBENZOYL) 1, 2, 3, 4 TETRAHYDRO 6 QUINOLYL] 3, 6 DIHYDRO 6 METHYL 2H 1, 3, 4 THIADIAZIN 2 ONE; ADENOSINE TRIPHOSPHATASE; MYOSIN; UNCLASSIFIED DRUG; 5 [1 (3,4 DIMETHOXYBENZOYL) 1,2,3,4 TETRAHYDRO 6 QUINOLYL] 3,6 DIHYDRO 6 METHYL 2H 1,3,4 THIADIAZIN 2 ONE; ACTIN; ADENOSINE TRIPHOSPHATE; CARDIAC MYOSIN; CARDIOTONIC AGENT; ENZYME ACTIVATOR; QUINOLINE DERIVATIVE; RECOMBINANT PROTEIN; THIADIAZINE DERIVATIVE;

EID: 84898731649     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.01603     Document Type: Article
Times cited : (43)

References (54)
  • 1
    • 0036670189 scopus 로고    scopus 로고
    • Alpha(1)-and beta-adrenoceptor stimulation differentially activate p38-MAPK and atrial natriuretic peptide production in the perfused amphibian heart
    • Aggeli I-KS, Gaitanaki C, Lazou A, Beis I. 2002. Alpha(1)-and beta-adrenoceptor stimulation differentially activate p38-MAPK and atrial natriuretic peptide production in the perfused amphibian heart. The Journal of Experimental Biology 205:2387-2397.
    • (2002) The Journal of Experimental Biology , vol.205 , pp. 2387-2397
    • Aggeli, I.-K.S.1    Gaitanaki, C.2    Lazou, A.3    Beis, I.4
  • 4
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • doi: 10.1016/S0065-3233(08)60413-1
    • Anfinsen CB, Scheraga HA. 1975. Experimental and theoretical aspects of protein folding. Advances in Protein Chemistry 29:205-300. doi: 10.1016/S0065-3233(08)60413-1.
    • (1975) Advances in Protein Chemistry , vol.29 , pp. 205-300
    • Anfinsen, C.B.1    Scheraga, H.A.2
  • 6
    • 0035168989 scopus 로고    scopus 로고
    • Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle
    • Baldwin KM, Haddad F. 2001. Effects of different activity and inactivity paradigms on myosin heavy chain gene expression in striated muscle. Journal of Applied Physiology 90:345-357.
    • (2001) Journal of Applied Physiology , vol.90 , pp. 345-357
    • Baldwin, K.M.1    Haddad, F.2
  • 7
    • 66849106554 scopus 로고    scopus 로고
    • An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms
    • doi: 10.1038/nsmb.1592
    • Bartlett AI, Radford SE. 2009. An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms. Nature Structural & Molecular Biology 16:582-588. doi: 10.1038/nsmb.1592.
    • (2009) Nature Structural & Molecular Biology , vol.16 , pp. 582-588
    • Bartlett, A.I.1    Radford, S.E.2
  • 8
    • 0032854474 scopus 로고    scopus 로고
    • Functional characterisation of Dictyostelium myosin II with conserved tryptophanyl residue 501 mutated to tyrosine
    • doi: 10.1515/BC.1999.126
    • Batra R, Manstein DJ. 1999. Functional characterisation of Dictyostelium myosin II with conserved tryptophanyl residue 501 mutated to tyrosine. Biological Chemistry 380:1017-1023. doi: 10.1515/BC.1999.126.
    • (1999) Biological Chemistry , vol.380 , pp. 1017-1023
    • Batra, R.1    Manstein, D.J.2
  • 10
    • 0028098798 scopus 로고
    • Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase
    • doi: 10.1021/bi00193a013
    • Brune M, Hunter JL, Corrie JE, Webb MR. 1994. Direct, real-time measurement of rapid inorganic phosphate release using a novel fluorescent probe and its application to actomyosin subfragment 1 ATPase. Biochemistry 33:8262-8271. doi: 10.1021/bi00193a013.
    • (1994) Biochemistry , vol.33 , pp. 8262-8271
    • Brune, M.1    Hunter, J.L.2    Corrie, J.E.3    Webb, M.R.4
  • 11
    • 84866994902 scopus 로고    scopus 로고
    • Molecular pathology of natriuretic peptides in the myocardium with special regard to fatal intoxication, hypothermia, and hyperthermia
    • doi: 10.1007/s00414-012-0732-4
    • Chen J-H, Michiue T, Ishikawa T, Maeda H. 2012. Molecular pathology of natriuretic peptides in the myocardium with special regard to fatal intoxication, hypothermia, and hyperthermia. International Journal of Legal Medicine 126:747-756. doi: 10.1007/s00414-012-0732-4.
    • (2012) International Journal of Legal Medicine , vol.126 , pp. 747-756
    • Chen, J.-H.1    Michiue, T.2    Ishikawa, T.3    Maeda, H.4
  • 12
    • 84862889001 scopus 로고    scopus 로고
    • Identification of functional differences between recombinant human α and β cardiac myosin motors
    • doi: 10.1007/s00018-012-0927-3
    • Deacon JC, Bloemink MJ, Rezavandi H, Geeves MA, Leinwand LA. 2012. Identification of functional differences between recombinant human α and β cardiac myosin motors. Cellular and Molecular Life Sciences 69:2261-2277. doi: 10.1007/s00018-012-0927-3.
    • (2012) Cellular and Molecular Life Sciences , vol.69 , pp. 2261-2277
    • Deacon, J.C.1    Bloemink, M.J.2    Rezavandi, H.3    Geeves, M.A.4    Leinwand, L.A.5
  • 15
    • 14044259423 scopus 로고    scopus 로고
    • Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of a class I myosin
    • doi: 10.1074/jbc.M412473200
    • Fujita-Becker S, Dürrwang U, Erent M, Clark RJ, Geeves MA, Manstein DJ. 2005. Changes in Mg2+ ion concentration and heavy chain phosphorylation regulate the motor activity of a class I myosin. The Journal of Biological Chemistry 280:6064-6071. doi: 10.1074/jbc.M412473200.
    • (2005) The Journal of Biological Chemistry , vol.280 , pp. 6064-6071
    • Fujita-Becker, S.1    Dürrwang, U.2    Erent, M.3    Clark, R.J.4    Geeves, M.A.5    Manstein, D.J.6
  • 17
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • doi: 10.1021/bi972851y
    • Furch M, Geeves MA, Manstein DJ. 1998. Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain. Biochemistry 37:6317-6326. doi: 10.1021/bi972851y.
    • (1998) Biochemistry , vol.37 , pp. 6317-6326
    • Furch, M.1    Geeves, M.A.2    Manstein, D.J.3
  • 19
    • 79951552729 scopus 로고    scopus 로고
    • Interactions of the proteins of neuronal ceroid lipofuscinosis: Clues to function
    • doi: 10.1007/s00018-010-0468-6
    • Getty AL, Pearce DA. 2011. Interactions of the proteins of neuronal ceroid lipofuscinosis: clues to function. Cellular and Molecular Life Sciences 68:453-474. doi: 10.1007/s00018-010-0468-6.
    • (2011) Cellular and Molecular Life Sciences , vol.68 , pp. 453-474
    • Getty, A.L.1    Pearce, D.A.2
  • 20
    • 78449274362 scopus 로고    scopus 로고
    • A novel interaction of CLN3 with nonmuscle myosin-IIB and defects in cell motility of Cln3(-/-) cells
    • doi: 10.1016/j.yexcr.2010.09.007
    • Getty AL, Benedict JW, Pearce DA. 2011. A novel interaction of CLN3 with nonmuscle myosin-IIB and defects in cell motility of Cln3(-/-) cells. Experimental Cell Research 317:51-69. doi: 10.1016/j.yexcr.2010.09.007.
    • (2011) Experimental Cell Research , vol.317 , pp. 51-69
    • Getty, A.L.1    Benedict, J.W.2    Pearce, D.A.3
  • 21
    • 77953593304 scopus 로고    scopus 로고
    • The molecular basis of frictional loads in the in vitro motility assay with applications to the study of the loaded mechanochemistry of molecular motors
    • doi: 10.1002/cm.20441
    • Greenberg MJ, Moore JR. 2010. The molecular basis of frictional loads in the in vitro motility assay with applications to the study of the loaded mechanochemistry of molecular motors. Cytoskeleton (Hoboken) 67:273-285. doi: 10.1002/cm.20441.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 273-285
    • Greenberg, M.J.1    Moore, J.R.2
  • 22
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • doi: 10.1038/nature10317
    • Hartl FU, Bracher A, Hayer-Hartl M. 2011. Molecular chaperones in protein folding and proteostasis. Nature 475:324-332. doi: 10.1038/nature10317.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 24
    • 33745011604 scopus 로고    scopus 로고
    • JunD attenuates phenylephrine-mediated cardiomyocyte hypertrophy by negatively regulating AP-1 transcriptional activity
    • doi: 10.1016/j.cardiores.2006.02.032
    • Hilfiker-Kleiner D, Hilfiker A, Castellazzi M, Wollert KC, Trautwein C, Schunkert H, Drexler H. 2006. JunD attenuates phenylephrine-mediated cardiomyocyte hypertrophy by negatively regulating AP-1 transcriptional activity. Cardiovascular Research 71:108-117. doi: 10.1016/j.cardiores.2006.02.032.
    • (2006) Cardiovascular Research , vol.71 , pp. 108-117
    • Hilfiker-Kleiner, D.1    Hilfiker, A.2    Castellazzi, M.3    Wollert, K.C.4    Trautwein, C.5    Schunkert, H.6    Drexler, H.7
  • 25
    • 77954762928 scopus 로고    scopus 로고
    • Continuous glycoprotein-130-mediated signal transducer and activator of transcription-3 activation promotes inflammation, left ventricular rupture, and adverse outcome in subacute myocardial infarction
    • doi: 10.1161/CIRCULATIONAHA.109.933127
    • Hilfiker-Kleiner D, Shukla P, Klein G, Schaefer A, Stapel B, Hoch M, Müller W, Scherr M, Theilmeier G, Ernst M, Hilfiker A, Drexler H. 2010. Continuous glycoprotein-130-mediated signal transducer and activator of transcription-3 activation promotes inflammation, left ventricular rupture, and adverse outcome in subacute myocardial infarction. Circulation 122:145-155. doi: 10.1161/CIRCULATIONAHA.109.933127.
    • (2010) Circulation , vol.122 , pp. 145-155
    • Hilfiker-Kleiner, D.1    Shukla, P.2    Klein, G.3    Schaefer, A.4    Stapel, B.5    Hoch, M.6    Müller, W.7    Scherr, M.8    Theilmeier, G.9    Ernst, M.10    Hilfiker, A.11    Drexler, H.12
  • 28
    • 0031033964 scopus 로고    scopus 로고
    • Force enhancement without changes in cross-bridge turnover kinetics: The effect of EMD 57033
    • doi: 10.1016/S0006-3495(97)78666-1
    • Kraft T, Brenner B. 1997. Force enhancement without changes in cross-bridge turnover kinetics: the effect of EMD 57033. Biophysical Journal 72:272-281. doi: 10.1016/S0006-3495(97)78666-1.
    • (1997) Biophysical Journal , vol.72 , pp. 272-281
    • Kraft, T.1    Brenner, B.2
  • 30
    • 0015526770 scopus 로고
    • Intrinsic fluorescence of actin
    • doi: 10.1021/bi00757a015
    • Lehrer SS, Kerwar G. 1972. Intrinsic fluorescence of actin. Biochemistry 11:1211-1217. doi: 10.1021/bi00757a015.
    • (1972) Biochemistry , vol.11 , pp. 1211-1217
    • Lehrer, S.S.1    Kerwar, G.2
  • 32
    • 0029055358 scopus 로고
    • Overexpression of myosin motor domains in Dictyostelium: Screening of transformants and purification of the affinity tagged protein
    • doi: 10.1007/BF00121141
    • Manstein DJ, Hunt DM. 1995. Overexpression of myosin motor domains in Dictyostelium: screening of transformants and purification of the affinity tagged protein. Journal of Muscle Research Cell Motility 16:325-332. doi: 10.1007/BF00121141.
    • (1995) Journal of Muscle Research Cell Motility , vol.16 , pp. 325-332
    • Manstein, D.J.1    Hunt, D.M.2
  • 33
    • 0020021291 scopus 로고
    • Preparation of myosin and its subfragments from rabbit skeletal muscle
    • Margossian SS, Lowey S. 1982. Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods in Enzymology 85:55-71.
    • (1982) Methods in Enzymology , vol.85 , pp. 55-71
    • Margossian, S.S.1    Lowey, S.2
  • 34
    • 84858019907 scopus 로고    scopus 로고
    • Rheumatic heart disease
    • doi: 10.1016/S0140-6736(11)61171-9
    • Marijon E, Mirabel M, Celermajer DS, Jouven X. 2012. Rheumatic heart disease. Lancet 379:953-964. doi: 10.1016/S0140-6736(11)61171-9.
    • (2012) Lancet , vol.379 , pp. 953-964
    • Marijon, E.1    Mirabel, M.2    Celermajer, D.S.3    Jouven, X.4
  • 36
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • doi: 10.1002/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B
    • Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, Belew RK, Olson AJ. 1998. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. Journal of Computational Chemistry 19:1639-1662. doi: 10.1002/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B.
    • (1998) Journal of Computational Chemistry , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 38
    • 33745674468 scopus 로고    scopus 로고
    • Drug discovery in the ubiquitin-proteasome system
    • doi: 10.1038/nrd2056
    • Nalepa G, Rolfe M, Harper JW. 2006. Drug discovery in the ubiquitin-proteasome system. Nature Reviews Drug Discovery 5:596-613. doi: 10.1038/nrd2056.
    • (2006) Nature Reviews Drug Discovery , vol.5 , pp. 596-613
    • Nalepa, G.1    Rolfe, M.2    Harper, J.W.3
  • 39
    • 0028955588 scopus 로고
    • Molecular biology and biochemistry of natriuretic peptide family
    • doi: 10.1111/j.1440-1681.1995.tb01918.x
    • Ogawa Y, Itoh H, Nakao K. 1995. Molecular biology and biochemistry of natriuretic peptide family. Clinical and Experimental Pharmacology and Physiology 22:49-53. doi: 10.1111/j.1440-1681.1995.tb01918.x.
    • (1995) Clinical and Experimental Pharmacology and Physiology , vol.22 , pp. 49-53
    • Ogawa, Y.1    Itoh, H.2    Nakao, K.3
  • 40
    • 34247554304 scopus 로고    scopus 로고
    • Hereditary myosin myopathies
    • doi: 10.1016/j.nmd.2007.02.008
    • Oldfors A. 2007. Hereditary myosin myopathies. Neuromuscular Disorders 17:355-367. doi: 10.1016/j.nmd.2007.02.008.
    • (2007) Neuromuscular Disorders , vol.17 , pp. 355-367
    • Oldfors, A.1
  • 41
    • 70349655895 scopus 로고    scopus 로고
    • Removal of the cardiac myosin regulatory light chain increases isometric force production
    • doi: 10.1096/fj.08-126672
    • Pant K, Watt J, Greenberg M, Jones M, Szczesna-Cordary D, Moore JR. 2009. Removal of the cardiac myosin regulatory light chain increases isometric force production. FASEB Journal 23:3571-3580. doi: 10.1096/fj.08-126672.
    • (2009) FASEB Journal , vol.23 , pp. 3571-3580
    • Pant, K.1    Watt, J.2    Greenberg, M.3    Jones, M.4    Szczesna-Cordary, D.5    Moore, J.R.6
  • 42
    • 84874337312 scopus 로고    scopus 로고
    • Transportation of nanoscale cargoes by myosin propelled actin filaments
    • doi: 10.1371/journal.pone.0055931
    • Persson M, Gullberg M, Tolf C, Lindberg AM, Månsson A, Kocer A. 2013. Transportation of nanoscale cargoes by myosin propelled actin filaments. PLOS ONE 8:e55931. doi: 10.1371/journal.pone.0055931.
    • (2013) PLOS ONE , vol.8
    • Persson, M.1    Gullberg, M.2    Tolf, C.3    Lindberg, A.M.4    Månsson, A.5    Kocer, A.6
  • 43
    • 0034681913 scopus 로고    scopus 로고
    • Charge changes in loop 2 affect the thermal unfolding of the myosin motor domain bound to F-actin
    • doi: 10.1021/bi992420a
    • Ponomarev MA, Furch M, Levitsky DI, Manstein DJ. 2000. Charge changes in loop 2 affect the thermal unfolding of the myosin motor domain bound to F-actin. Biochemistry 39:4527-4532. doi: 10.1021/bi992420a.
    • (2000) Biochemistry , vol.39 , pp. 4527-4532
    • Ponomarev, M.A.1    Furch, M.2    Levitsky, D.I.3    Manstein, D.J.4
  • 44
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • doi: 10.1006/jmbi.1993.1626
    • Sali A, Blundell TL. 1993. Comparative protein modelling by satisfaction of spatial restraints. Journal of Molecular Biology 234:779-815. doi: 10.1006/jmbi.1993.1626.
    • (1993) Journal of Molecular Biology , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 45
    • 0033397980 scopus 로고    scopus 로고
    • Python: A programming language for software integration and development
    • Sanner MF. 1999. Python: a programming language for software integration and development. Journal of Molecular Graphics & Modelling 17:57-61.
    • (1999) Journal of Molecular Graphics & Modelling , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 46
    • 33751559579 scopus 로고    scopus 로고
    • Screening for ligands using a generic and high-throughput light-scattering-based assay
    • doi: 10.1177/1087057106294699
    • Senisterra GA, Markin E, Yamazaki K, Hui R, Vedadi M, Awrey DE. 2006. Screening for ligands using a generic and high-throughput light-scattering-based assay. Journal of Biomolecular Screening 11:940-948. doi: 10.1177/1087057106294699.
    • (2006) Journal of Biomolecular Screening , vol.11 , pp. 940-948
    • Senisterra, G.A.1    Markin, E.2    Yamazaki, K.3    Hui, R.4    Vedadi, M.5    Awrey, D.E.6
  • 47
    • 0034006394 scopus 로고    scopus 로고
    • Improved mechanoenergetics and cardiac rest and reserve function of in vivo failing heart by calcium sensitizer EMD-57033
    • doi: 10.1161/01.CIR.101.9.1040
    • Senzaki H, Isoda T, Paolocci N, Ekelund U, Hare JM, Kass DA. 2000. Improved mechanoenergetics and cardiac rest and reserve function of in vivo failing heart by calcium sensitizer EMD-57033. Circulation 101:1040-1048. doi: 10.1161/01.CIR.101.9.1040.
    • (2000) Circulation , vol.101 , pp. 1040-1048
    • Senzaki, H.1    Isoda, T.2    Paolocci, N.3    Ekelund, U.4    Hare, J.M.5    Kass, D.A.6
  • 50
    • 0036865662 scopus 로고    scopus 로고
    • Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium
    • doi: 10.1093/embo-reports/kvf214
    • Tsiavaliaris G, Fujita-Becker S, Batra R, Levitsky DI, Kull FJ, Geeves MA, Manstein DJ. 2002. Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium. EMBO Reports 3:1099-1105. doi: 10.1093/embo-reports/kvf214.
    • (2002) EMBO Reports , vol.3 , pp. 1099-1105
    • Tsiavaliaris, G.1    Fujita-Becker, S.2    Batra, R.3    Levitsky, D.I.4    Kull, F.J.5    Geeves, M.A.6    Manstein, D.J.7
  • 51
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • doi: 10.1038/nrm2993
    • Tyedmers J, Mogk A, Bukau B. 2010. Cellular strategies for controlling protein aggregation. Nature Reviews Molecular Cell Biology 11:777-788. doi: 10.1038/nrm2993.
    • (2010) Nature Reviews Molecular Cell Biology , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 52
    • 70350393411 scopus 로고    scopus 로고
    • Cardiomyopathy: A systematic review of disease-causing mutations in myosin heavy chain 7 and their phenotypic manifestations
    • doi: 10.1159/000252808
    • Walsh R, Rutland C, Thomas R, Loughna S. 2010. Cardiomyopathy: a systematic review of disease-causing mutations in myosin heavy chain 7 and their phenotypic manifestations. Cardiology 115:49-60. doi: 10.1159/000252808.
    • (2010) Cardiology , vol.115 , pp. 49-60
    • Walsh, R.1    Rutland, C.2    Thomas, R.3    Loughna, S.4
  • 53
    • 84855254333 scopus 로고    scopus 로고
    • Protein-binding assays in biological liquids using microscale thermophoresis
    • doi: 10.1038/ncomms1093
    • Wienken CJ, Baaske P, Rothbauer U, Braun D, Duhr S. 2010. Protein-binding assays in biological liquids using microscale thermophoresis. Nature Communications 1:100. doi: 10.1038/ncomms1093.
    • (2010) Nature Communications , vol.1 , pp. 100
    • Wienken, C.J.1    Baaske, P.2    Rothbauer, U.3    Braun, D.4    Duhr, S.5
  • 54
    • 84873034262 scopus 로고    scopus 로고
    • Proteotoxicity and cardiac dysfunction-Alzheimer's disease of the heart?
    • doi: 10.1056/NEJMra1106180
    • Willis MS, Patterson C. 2013. Proteotoxicity and cardiac dysfunction-Alzheimer's disease of the heart? The New England Journal of Medicine 368:455-464. doi: 10.1056/NEJMra1106180.
    • (2013) The New England Journal of Medicine , vol.368 , pp. 455-464
    • Willis, M.S.1    Patterson, C.2


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