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Volumn 416, Issue 4, 2012, Pages 543-557

Alternative relay and converter domains tune native muscle myosin isoform function in Drosophila

Author keywords

ATPase; Drosophila; motility; myofibril; myosin

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATASE (MAGNESIUM); ISOPROTEIN; MYOSIN;

EID: 84857371868     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.12.044     Document Type: Article
Times cited : (14)

References (54)
  • 1
    • 0020678384 scopus 로고
    • Drosophila muscle myosin heavy chain encoded by a single gene in a cluster of muscle mutations
    • DOI 10.1038/302393a0
    • Bernstein S.I., Mogami K., Donady J.J., and Emerson C.P. Jr Drosophila muscle myosin heavy chain encoded by a single gene in a cluster of muscle mutations Nature 302 1983 393 397 (Pubitemid 13164321)
    • (1983) Nature , vol.302 , Issue.5907 , pp. 393-397
    • Bernstein, S.I.1    Mogami, K.2    Donady, J.J.3    Emerson Jr., C.P.4
  • 2
    • 0024366590 scopus 로고
    • Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons
    • George E.L., Ober M.B., and Emerson C.P. Jr Functional domains of the Drosophila melanogaster muscle myosin heavy-chain gene are encoded by alternatively spliced exons Mol. Cell. Biol. 9 1989 2957 2974 (Pubitemid 19163060)
    • (1989) Molecular and Cellular Biology , vol.9 , Issue.7 , pp. 2957-2974
    • George, E.L.1    Ober, M.B.2    Emerson Jr., C.P.3
  • 3
    • 0025836145 scopus 로고
    • Myosin functional domains encoded by alternative exons are expressed in specific thoracic muscles of Drosophila
    • Hastings G.A., and Emerson C.P. Jr Myosin functional domains encoded by alternative exons are expressed in specific thoracic muscles of Drosophila J. Cell Biol. 114 1991 263 276 (Pubitemid 21909796)
    • (1991) Journal of Cell Biology , vol.114 , Issue.2 , pp. 263-276
    • Hastings, G.A.1    Emerson Jr., C.P.2
  • 4
    • 0020658044 scopus 로고
    • Drosophila has one myosin heavy-chain gene with three developmentally regulated transcripts
    • Rozek C.E., and Davidson N. Drosophila has one myosin heavy-chain gene with three developmentally regulated transcripts Cell 32 1983 23 34 (Pubitemid 13159142)
    • (1983) Cell , vol.32 , Issue.1 , pp. 23-34
    • Rozek, C.E.1    Davidson, N.2
  • 5
    • 0035119730 scopus 로고    scopus 로고
    • Spatially and temporally regulated expression of myosin heavy chain alternative exons during Drosophila embryogenesis
    • DOI 10.1016/S0925-4773(00)00549-9, PII S0925477300005499
    • Zhang S., and Bernstein S.I. Spatially and temporally regulated expression of myosin heavy chain alternative exons during Drosophila embryogenesis Mech. Dev. 101 2001 35 45 (Pubitemid 32192822)
    • (2001) Mechanisms of Development , vol.101 , Issue.1-2 , pp. 35-45
    • Zhang, S.1    Bernstein, S.I.2
  • 7
    • 0346118918 scopus 로고    scopus 로고
    • Kinetic Analysis of Drosophila Muscle Myosin Isoforms Suggests a Novel Mode of Mechanochemical Coupling
    • DOI 10.1074/jbc.M308318200
    • Miller B.M., Nyitrai M., Bernstein S.I., and Geeves M.A. Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling J. Biol. Chem. 278 2003 50293 50300 (Pubitemid 37548870)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.50 , pp. 50293-50300
    • Miller, B.M.1    Nyitrai, M.2    Bernstein, S.I.3    Geeves, M.A.4
  • 8
    • 0035805601 scopus 로고    scopus 로고
    • Alternative exon-encoded regions of Drosophila myosin heavy chain modulate ATPase rates and actin sliding velocity
    • Swank D.M., Bartoo M.L., Knowles A.F., Iliffe C., Bernstein S.I., Molloy J.E., and Sparrow J.C. Alternative exon-encoded regions of Drosophila myosin heavy chain modulate ATPase rates and actin sliding velocity J. Biol. Chem. 276 2001 15117 15124
    • (2001) J. Biol. Chem. , vol.276 , pp. 15117-15124
    • Swank, D.M.1    Bartoo, M.L.2    Knowles, A.F.3    Iliffe, C.4    Bernstein, S.I.5    Molloy, J.E.6    Sparrow, J.C.7
  • 10
    • 0029790426 scopus 로고    scopus 로고
    • Myosin heavy chain isoforms regulate muscle function but not myofibril assembly
    • Wells L., Edwards K.A., and Bernstein S.I. Myosin heavy chain isoforms regulate muscle function but not myofibril assembly EMBO J. 15 1996 4454 4459 (Pubitemid 26294563)
    • (1996) EMBO Journal , vol.15 , Issue.17 , pp. 4454-4459
    • Wells, L.1    Edwards, K.A.2    Bernstein, S.I.3
  • 12
    • 0031559585 scopus 로고    scopus 로고
    • Fine tuning a molecular motor: The location of alternative domains in the Drosophila myosin head
    • DOI 10.1006/jmbi.1997.1160
    • Bernstein S.I., and Milligan R.A. Fine tuning a molecular motor: the location of alternative domains in the Drosophila myosin head J. Mol. Biol 271 1997 1 6 (Pubitemid 27338762)
    • (1997) Journal of Molecular Biology , vol.271 , Issue.1 , pp. 1-6
    • Bernstein, S.I.1    Milligan, R.A.2
  • 13
    • 0037435594 scopus 로고    scopus 로고
    • Dictyostelium myosin II mutations that uncouple the converter swing and ATP hydrolysis cycle
    • DOI 10.1021/bi026051l
    • Sasaki N., Ohkura R., and Sutoh K. Dictyostelium myosin II mutations that uncouple the converter swing and ATP hydrolysis cycle Biochemistry 42 2003 90 95 (Pubitemid 36083854)
    • (2003) Biochemistry , vol.42 , Issue.1 , pp. 90-95
    • Sasaki, N.1    Ohkura, R.2    Sutoh, K.3
  • 15
    • 0042733142 scopus 로고    scopus 로고
    • Requirement of domain-domain interaction for conformational change and functional ATP hydrolysis in myosin
    • DOI 10.1074/jbc.M304138200
    • Ito K., Uyeda T.Q., Suzuki Y., Sutoh K., and Yamamoto K. Requirement of domain-domain interaction for conformational change and functional ATP hydrolysis in myosin J. Biol. Chem. 278 2003 31049 31057 (Pubitemid 36994619)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 31049-31057
    • Ito, K.1    Uyeda, T.Q.P.2    Suzuki, Y.3    Sutoh, K.4    Yamamoto, K.5
  • 17
    • 35148894521 scopus 로고    scopus 로고
    • Predicting Allosteric Communication in Myosin via a Pathway of Conserved Residues
    • DOI 10.1016/j.jmb.2007.08.059, PII S0022283607011412
    • Tang S., Liao J.C., Dunn A.R., Altman R.B., Spudich J.A., and Schmidt J.P. Predicting allosteric communication in myosin via a pathway of conserved residues J. Mol. Biol. 373 2007 1361 1373 (Pubitemid 47539487)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.5 , pp. 1361-1373
    • Tang, S.1    Liao, J.-C.2    Dunn, A.R.3    Altman, R.B.4    Spudich, J.A.5    Schmidt, J.P.6
  • 18
    • 65849096732 scopus 로고    scopus 로고
    • Alternative exon 9-encoded relay domains affect more than one communication pathway in the Drosophila myosin head
    • Bloemink M.J., Dambacher C.M., Knowles A.F., Melkani G.C., Geeves M.A., and Bernstein S.I. Alternative exon 9-encoded relay domains affect more than one communication pathway in the Drosophila myosin head J. Mol. Biol. 389 2009 707 721
    • (2009) J. Mol. Biol. , vol.389 , pp. 707-721
    • Bloemink, M.J.1    Dambacher, C.M.2    Knowles, A.F.3    Melkani, G.C.4    Geeves, M.A.5    Bernstein, S.I.6
  • 19
    • 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
    • DOI 10.1016/S0092-8674(00)81598-6
    • Dominguez R., Freyzon Y., Trybus K.M., and Cohen C. 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 1998 559 571 (Pubitemid 28427575)
    • (1998) Cell , vol.94 , Issue.5 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 21
    • 25144488608 scopus 로고    scopus 로고
    • An alternative domain near the nucleotide-binding site of Drosophila muscle myosin affects ATPase kinetics
    • DOI 10.1016/j.jmb.2005.08.012, PII S0022283605009356
    • Miller B.M., Zhang S., Suggs J.A., Swank D.M., Littlefield K.P., Knowles A.F., and Bernstein S.I. An alternative domain near the nucleotide-binding site of Drosophila muscle myosin affects ATPase kinetics J. Mol. Biol. 353 2005 14 25 (Pubitemid 41338836)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.1 , pp. 14-25
    • Miller, B.M.1    Zhang, S.2    Suggs, J.A.3    Swank, D.M.4    Littlefield, K.P.5    Knowles, A.F.6    Bernstein, S.I.7
  • 22
    • 43449134103 scopus 로고    scopus 로고
    • Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function
    • Kronert W.A., Dambacher C.M., Knowles A.F., Swank D.M., and Bernstein S.I. Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function J. Mol. Biol. 379 2008 443 456
    • (2008) J. Mol. Biol. , vol.379 , pp. 443-456
    • Kronert, W.A.1    Dambacher, C.M.2    Knowles, A.F.3    Swank, D.M.4    Bernstein, S.I.5
  • 23
    • 0001568287 scopus 로고
    • The mesoderm and its derivatives
    • M. Bate, A.M. Arias, Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • Bate M. The mesoderm and its derivatives M. Bate, A.M. Arias, The Development of Drosophila melanogaster vol. II 1993 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 1013 1090
    • (1993) The Development of Drosophila Melanogaster , vol.2 , pp. 1013-1090
    • Bate, M.1
  • 24
    • 0025291420 scopus 로고
    • Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed
    • Collier V.L., Kronert W.A., O'Donnell P.T., Edwards K.A., and Bernstein S.I. Alternative myosin hinge regions are utilized in a tissue-specific fashion that correlates with muscle contraction speed Genes Dev. 4 1990 885 895
    • (1990) Genes Dev. , vol.4 , pp. 885-895
    • Collier, V.L.1    Kronert, W.A.2    O'Donnell, P.T.3    Edwards, K.A.4    Bernstein, S.I.5
  • 25
    • 43749090655 scopus 로고    scopus 로고
    • The mechanism of the reverse recovery step, phosphate release, and actin activation of Dictyostelium myosin II
    • Gyimesi M., Kintses B., Bodor A., Perczel A., Fischer S., Bagshaw C.R., and Malnasi-Csizmadia A. The mechanism of the reverse recovery step, phosphate release, and actin activation of Dictyostelium myosin II J. Biol. Chem. 283 2008 8153 8163
    • (2008) J. Biol. Chem. , vol.283 , pp. 8153-8163
    • Gyimesi, M.1    Kintses, B.2    Bodor, A.3    Perczel, A.4    Fischer, S.5    Bagshaw, C.R.6    Malnasi-Csizmadia, A.7
  • 26
    • 33847181200 scopus 로고    scopus 로고
    • The principal motions involved in the coupling mechanism of the recovery stroke of the myosin motor
    • Mesentean S., Koppole S., Smith J.C., and Fischer S. The principal motions involved in the coupling mechanism of the recovery stroke of the myosin motor J. Mol. Biol. 367 2007 591 602
    • (2007) J. Mol. Biol. , vol.367 , pp. 591-602
    • Mesentean, S.1    Koppole, S.2    Smith, J.C.3    Fischer, S.4
  • 27
    • 34447276474 scopus 로고    scopus 로고
    • The Structural Coupling between ATPase Activation and Recovery Stroke in the Myosin II Motor
    • DOI 10.1016/j.str.2007.06.008, PII S0969212607002146
    • Koppole S., Smith J.C., and Fischer S. The structural coupling between ATPase activation and recovery stroke in the myosin II motor Structure 15 2007 825 837 (Pubitemid 47042437)
    • (2007) Structure , vol.15 , Issue.7 , pp. 825-837
    • Koppole, S.1    Smith, J.C.2    Fischer, S.3
  • 28
    • 33646468356 scopus 로고    scopus 로고
    • Insights into the chemomechanical coupling of the myosin motor from simulation of its ATP hydrolysis mechanism
    • Schwarzl S.M., Smith J.C., and Fischer S. Insights into the chemomechanical coupling of the myosin motor from simulation of its ATP hydrolysis mechanism Biochemistry 45 2006 5830 5847
    • (2006) Biochemistry , vol.45 , pp. 5830-5847
    • Schwarzl, S.M.1    Smith, J.C.2    Fischer, S.3
  • 29
    • 33746513207 scopus 로고    scopus 로고
    • Simulations of the Myosin II Motor Reveal a Nucleotide-state Sensing Element that Controls the Recovery Stroke
    • DOI 10.1016/j.jmb.2006.06.022, PII S0022283606007650
    • Koppole S., Smith J.C., and Fischer S. Simulations of the myosin II motor reveal a nucleotide-state sensing element that controls the recovery stroke J. Mol. Biol. 361 2006 604 616 (Pubitemid 44137359)
    • (2006) Journal of Molecular Biology , vol.361 , Issue.3 , pp. 604-616
    • Koppole, S.1    Smith, J.C.2    Fischer, S.3
  • 30
    • 77956578914 scopus 로고    scopus 로고
    • The influence of myosin converter and relay domains on cross-bridge kinetics of Drosophila indirect flight muscle
    • Yang C., Kaplan C.N., Thatcher M.L., and Swank D.M. The influence of myosin converter and relay domains on cross-bridge kinetics of Drosophila indirect flight muscle Biophys. J. 99 2010 1546 1555
    • (2010) Biophys. J. , vol.99 , pp. 1546-1555
    • Yang, C.1    Kaplan, C.N.2    Thatcher, M.L.3    Swank, D.M.4
  • 31
    • 58149356271 scopus 로고    scopus 로고
    • Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics
    • Yang C., Ramanath S., Kronert W.A., Bernstein S.I., Maughan D.W., and Swank D.M. Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics Biophys. J. 95 2008 5228 5237
    • (2008) Biophys. J. , vol.95 , pp. 5228-5237
    • Yang, C.1    Ramanath, S.2    Kronert, W.A.3    Bernstein, S.I.4    Maughan, D.W.5    Swank, D.M.6
  • 32
    • 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., and Manstein D.J. Functional characterisation of Dictyostelium myosin II with conserved tryptophanyl residue 501 mutated to tyrosine Biol. Chem. 380 1999 1017 1023 (Pubitemid 29412763)
    • (1999) Biological Chemistry , vol.380 , Issue.7-8 , pp. 1017-1023
    • Batra, R.1    Manstein, D.J.2
  • 33
    • 0034718527 scopus 로고    scopus 로고
    • Isolating and localizing ATP-sensitive tryptophan emission in skeletal myosin subfragment 1
    • Park S., and Burghardt T.P. Isolating and localizing ATP-sensitive tryptophan emission in skeletal myosin subfragment 1 Biochemistry 39 2000 11732 11741
    • (2000) Biochemistry , vol.39 , pp. 11732-11741
    • Park, S.1    Burghardt, T.P.2
  • 34
    • 0034682824 scopus 로고    scopus 로고
    • Tryptophan 512 is sensitive to conformational changes in the rigid relay loop of smooth muscle myosin during the MgATPase cycle
    • Yengo C.M., Chrin L.R., Rovner A.S., and Berger C.L. Tryptophan 512 is sensitive to conformational changes in the rigid relay loop of smooth muscle myosin during the MgATPase cycle J. Biol. Chem. 275 2000 25481 25487
    • (2000) J. Biol. Chem. , vol.275 , pp. 25481-25487
    • Yengo, C.M.1    Chrin, L.R.2    Rovner, A.S.3    Berger, C.L.4
  • 35
    • 77952301315 scopus 로고    scopus 로고
    • Mutating the converter-relay interface of Drosophila myosin perturbs ATPase activity, actin motility, myofibril stability and flight ability
    • Kronert W.A., Melkani G.C., Melkani A., and Bernstein S.I. Mutating the converter-relay interface of Drosophila myosin perturbs ATPase activity, actin motility, myofibril stability and flight ability J. Mol. Biol. 398 2010 625 632
    • (2010) J. Mol. Biol. , vol.398 , pp. 625-632
    • Kronert, W.A.1    Melkani, G.C.2    Melkani, A.3    Bernstein, S.I.4
  • 36
    • 80052442162 scopus 로고    scopus 로고
    • Disrupting the myosin converter-relay interface impairs Drosophila indirect flight muscle performance
    • Ramanath S., Wang Q., Bernstein S.I., and Swank D.M. Disrupting the myosin converter-relay interface impairs Drosophila indirect flight muscle performance Biophys. J. 101 2011 1114 1122
    • (2011) Biophys. J. , vol.101 , pp. 1114-1122
    • Ramanath, S.1    Wang, Q.2    Bernstein, S.I.3    Swank, D.M.4
  • 37
    • 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 D.I., Kull F.J., Geeves M.A., and Manstein D.J. Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium EMBO Rep. 3 2002 1099 1105 (Pubitemid 35469903)
    • (2002) EMBO Reports , vol.3 , Issue.11 , pp. 1099-1105
    • Tsiavaliaris, G.1    Fujita-Becker, S.2    Batra, R.3    Levitsky, D.I.4    Kill, F.J.5    Geeves, M.A.6    Manstein, D.J.7
  • 38
    • 0035379648 scopus 로고    scopus 로고
    • The myosin relay helix to converter interface remains intact throughout the actomyosin ATPase cycle
    • Shih W.M., and Spudich J.A. The myosin relay helix to converter interface remains intact throughout the actomyosin ATPase cycle J. Biol. Chem. 276 2001 19491 19494
    • (2001) J. Biol. Chem. , vol.276 , pp. 19491-19494
    • Shih, W.M.1    Spudich, J.A.2
  • 40
    • 68849085387 scopus 로고    scopus 로고
    • Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance
    • Seebohm B., Matinmehr F., Kohler J., Francino A., Navarro-Lopez F., and Perrot A. Cardiomyopathy mutations reveal variable region of myosin converter as major element of cross-bridge compliance Biophys. J. 97 2009 806 824
    • (2009) Biophys. J. , vol.97 , pp. 806-824
    • Seebohm, B.1    Matinmehr, F.2    Kohler, J.3    Francino, A.4    Navarro-Lopez, F.5    Perrot, A.6
  • 41
    • 39449118905 scopus 로고    scopus 로고
    • Myosin transducer mutations differentially affect motor function, myofibril structure, and the performance of skeletal and cardiac muscles
    • DOI 10.1091/mbc.E07-09-0890
    • Cammarato A., Dambacher C.M., Knowles A.F., Kronert W.A., Bodmer R., Ocorr K., and Bernstein S.I. Myosin transducer mutations differentially affect motor function, myofibril structure, and the performance of skeletal and cardiac muscles Mol. Biol. Cell 19 2008 553 562 (Pubitemid 351272144)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 553-562
    • Cammarato, A.1    Dambacher, C.M.2    Knowles, A.F.3    Kronert, W.A.4    Bodmer, R.5    Ocorr, K.6    Bernstein, S.I.7
  • 42
    • 0024230185 scopus 로고
    • Molecular and ultrastructural defects in a Drosophila myosin heavy chain mutant: Differential effects on muscle function produced by similar thick filament abnormalities
    • O'Donnell P.T., and Bernstein S.I. Molecular and ultrastructural defects in a Drosophila myosin heavy chain mutant: differential effects on muscle function produced by similar thick filament abnormalities J. Cell Biol. 107 1988 2601 2612
    • (1988) J. Cell Biol. , vol.107 , pp. 2601-2612
    • O'Donnell, P.T.1    Bernstein, S.I.2
  • 44
    • 0038530975 scopus 로고    scopus 로고
    • Suppression of muscle hypercontraction by mutations in the myosin heavy chain gene of Drosophila melanogaster
    • Nongthomba U., Cummins M., Clark S., Vigoreaux J.O., and Sparrow J.C. Suppression of muscle hypercontraction by mutations in the myosin heavy chain gene of Drosophila melanogaster Genetics 164 2003 209 222 (Pubitemid 36617706)
    • (2003) Genetics , vol.164 , Issue.1 , pp. 209-222
    • Nongthomba, U.1    Cummins, M.2    Clark, S.3    Vigoreaux, J.O.4    Sparrow, J.C.5
  • 45
    • 35748951592 scopus 로고    scopus 로고
    • Site directed mutagenesis of Drosophila flightin disrupts phosphorylation and impairs flight muscle structure and mechanics
    • DOI 10.1007/s10974-007-9120-y
    • Barton B., Ayer G., Maughan D.W., and Vigoreaux J.O. Site directed mutagenesis of Drosophila flightin disrupts phosphorylation and impairs flight muscle structure and mechanics J. Muscle Res. Cell Motil. 28 2007 219 230 (Pubitemid 350043632)
    • (2007) Journal of Muscle Research and Cell Motility , vol.28 , Issue.4-5 , pp. 219-230
    • Barton, B.1    Ayer, G.2    Maughan, D.W.3    Vigoreaux, J.O.4
  • 47
    • 1842456978 scopus 로고    scopus 로고
    • Characterization of a hypercontraction-induced myopathy in Drosophila caused by mutations in Mhc
    • DOI 10.1083/jcb.200308158
    • Montana E.S., and Littleton J.T. Characterization of a hypercontraction-induced myopathy in Drosophila caused by mutations in Mhc J. Cell Biol. 164 2004 1045 1054 (Pubitemid 38429130)
    • (2004) Journal of Cell Biology , vol.164 , Issue.7 , pp. 1045-1054
    • Montana, E.S.1    Littleton, J.T.2
  • 48
    • 0024260258 scopus 로고
    • Vectors for P-mediated transformation in Drosophila
    • Pirrotta V. Vectors for P-mediated transformation in Drosophila Biotechnology 10 1988 437 456
    • (1988) Biotechnology , vol.10 , pp. 437-456
    • Pirrotta, V.1
  • 49
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • Rubin G.M., and Spradling A.C. Genetic transformation of Drosophila with transposable element vectors Science 218 1982 348 353 (Pubitemid 12037603)
    • (1982) Science , vol.218 , Issue.4570 , pp. 348-353
    • Rubin, G.M.1    Spradling, A.C.2
  • 50
    • 0026571112 scopus 로고
    • Analysis of Drosophila paramyosin: Identification of a novel isoform which is restricted to a subset of adult muscles
    • Becker K.D., O'Donnell P.T., Heitz J.M., Vito M., and Bernstein S.I. Analysis of Drosophila paramyosin: identification of a novel isoform which is restricted to a subset of adult muscles J. Cell Biol. 116 1992 669 681
    • (1992) J. Cell Biol. , vol.116 , pp. 669-681
    • Becker, K.D.1    O'Donnell, P.T.2    Heitz, J.M.3    Vito, M.4    Bernstein, S.I.5
  • 51
    • 0024711230 scopus 로고
    • Ultrastructural and molecular analyses of homozygous-viable Drosophila melanogaster muscle mutants indicate there is a complex pattern of myosin heavy-chain isoform distribution
    • O'Donnell P.T., Collier V.L., Mogami K., and Bernstein S.I. Ultrastructural and molecular analyses of homozygous-viable Drosophila melanogaster muscle mutants indicate there is a complex pattern of myosin heavy-chain isoform distribution Genes Dev. 3 1989 1233 1246
    • (1989) Genes Dev. , vol.3 , pp. 1233-1246
    • O'Donnell, P.T.1    Collier, V.L.2    Mogami, K.3    Bernstein, S.I.4
  • 52
    • 0025794119 scopus 로고
    • Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster
    • Drummond D.R., Hennessey E.S., and Sparrow J.C. Characterisation of missense mutations in the Act88F gene of Drosophila melanogaster Mol. Gen. Genet. 226 1991 70 80
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 70-80
    • Drummond, D.R.1    Hennessey, E.S.2    Sparrow, J.C.3
  • 53
    • 0028926032 scopus 로고
    • Impairment of muscle function caused by mutations of phosphorylation sites in myosin regulatory light chain
    • Tohtong R., Yamashita H., Graham M., Haeberle J., Simcox A., and Maughan D. Impairment of muscle function caused by mutations of phosphorylation sites in myosin regulatory light chain Nature 374 1995 650 653
    • (1995) Nature , vol.374 , pp. 650-653
    • Tohtong, R.1    Yamashita, H.2    Graham, M.3    Haeberle, J.4    Simcox, A.5    Maughan, D.6
  • 54
    • 80051534185 scopus 로고    scopus 로고
    • Two Drosophila myosin transducer mutants with distinct cardiomyopathies have divergent ADP and actin affinities
    • Bloemink M.J., Melkani G.C., Dambacher C.M., Bernstein S.I., and Geeves M.A. Two Drosophila myosin transducer mutants with distinct cardiomyopathies have divergent ADP and actin affinities J. Biol. Chem. 286 2011 28435 28443
    • (2011) J. Biol. Chem. , vol.286 , pp. 28435-28443
    • Bloemink, M.J.1    Melkani, G.C.2    Dambacher, C.M.3    Bernstein, S.I.4    Geeves, M.A.5


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