메뉴 건너뛰기




Volumn 288, Issue 1, 2013, Pages 709-722

Kinetic characterization of nonmuscle myosin IIB at the single molecule level

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN FILAMENT; CELL MOTILITY; DUAL-BEAM; DUTY RATIOS; FLUORESCENCE IMAGING; HEAVY MEROMYOSIN; IN-VITRO; KINETIC CHARACTERIZATION; OPTICALTRAPPING; PHOSPHATE RELEASE; POWER STROKES; RATE LIMITING; SINGLE MOLECULE EXPERIMENTS; SINGLE MOLECULE LEVEL; TOTAL INTERNAL REFLECTION FLUORESCENCE; TRANSIENT KINETIC STUDIES; VITRO MOTILITY;

EID: 84872064814     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.424671     Document Type: Article
Times cited : (61)

References (67)
  • 1
    • 37549069575 scopus 로고    scopus 로고
    • Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species
    • Odronitz, F., and Kollmar, M. (2007) Drawing the tree of eukaryotic life based on the analysis of 2,269 manually annotated myosins from 328 species. Genome Biol. 8, R196
    • (2007) Genome Biol. , vol.8
    • Odronitz, F.1    Kollmar, M.2
  • 4
    • 33646410929 scopus 로고    scopus 로고
    • Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration
    • Betapudi, V., Licate, L. S., and Egelhoff, T. T. (2006) Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration. Cancer Res. 66, 4725-4733
    • (2006) Cancer Res. , vol.66 , pp. 4725-4733
    • Betapudi, V.1    Licate, L.S.2    Egelhoff, T.T.3
  • 5
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • DOI 10.1083/jcb.200612043
    • Vicente-Manzanares, M., Zareno, J., Whitmore, L., Choi, C. K., and Horwitz, A. F. (2007) Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells. J. Cell Biol. 176, 573-580 (Pubitemid 46333973)
    • (2007) Journal of Cell Biology , vol.176 , Issue.5 , pp. 573-580
    • Vicente-Manzanares, M.1    Zareno, J.2    Whitmore, L.3    Choi, C.K.4    Horwitz, A.F.5
  • 6
    • 26244455734 scopus 로고    scopus 로고
    • Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts
    • DOI 10.1091/mbc.E05-04-0330
    • Shewan, A. M., Maddugoda, M., Kraemer, A., Stehbens, S. J., Verma, S., Kovacs, E. M., and Yap, A. S. (2005) Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts. Mol. Biol. Cell 16, 4531-4542 (Pubitemid 41416439)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 4531-4542
    • Shewan, A.M.1    Maddugoda, M.2    Kraemer, A.3    Stehbens, S.J.4    Verma, S.5    Kovacs, E.M.6    Yap, A.S.7
  • 7
    • 66749172932 scopus 로고    scopus 로고
    • Protein kinase C activation disrupts epithelial apical junctions via ROCK-II dependent stimulation of actomyosin contractility
    • Ivanov, A. I., Samarin, S. N., Bachar, M., Parkos, C. A., and Nusrat, A. (2009) Protein kinase C activation disrupts epithelial apical junctions via ROCK-II dependent stimulation of actomyosin contractility. BMC Cell Biol. 10, 36
    • (2009) BMC Cell Biol. , vol.10 , pp. 36
    • Ivanov, A.I.1    Samarin, S.N.2    Bachar, M.3    Parkos, C.A.4    Nusrat, A.5
  • 8
    • 4744364577 scopus 로고    scopus 로고
    • Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice
    • DOI 10.1074/jbc.C400352200
    • Conti, M. A., Even-Ram, S., Liu, C., Yamada, K. M., and Adelstein, R. S. (2004) Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice. J. Biol. Chem. 279, 41263-41266 (Pubitemid 39313562)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.40 , pp. 41263-41266
    • Conti, M.A.1    Even-Ram, S.2    Liu, C.3    Yamada, K.M.4    Adelstein, R.S.5
  • 9
    • 75749110614 scopus 로고    scopus 로고
    • Mechanics of cytokinesis in eukaryotes
    • Pollard, T. D. (2010) Mechanics of cytokinesis in eukaryotes. Curr. Opin. Cell Biol. 22, 50-56
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 50-56
    • Pollard, T.D.1
  • 10
    • 84872354665 scopus 로고    scopus 로고
    • Nonmuscle myosin-2: Mix and match
    • DOI 10.1007/s00018-012-1002-9
    • Heissler, S. M., and Manstein, D. J. (2012) Nonmuscle myosin-2: mix and match. Cell Mol. Life Sci., DOI 10.1007/s00018-012-1002-9
    • (2012) Cell Mol. Life Sci.
    • Heissler, S.M.1    Manstein, D.J.2
  • 12
    • 39449101285 scopus 로고    scopus 로고
    • Nonmuscle myosin II moves in new directions
    • DOI 10.1242/jcs.007112
    • Conti, M. A., and Adelstein, R. S. (2008) Nonmuscle myosin II moves in new directions. J. Cell Sci. 121, 11-18 (Pubitemid 351265698)
    • (2008) Journal of Cell Science , vol.121 , Issue.1 , pp. 11-18
    • Conti, M.A.1    Adelstein, R.S.2
  • 13
    • 0035895901 scopus 로고    scopus 로고
    • Dedicated myosin light chain kinases with diverse cellular functions
    • Kamm, K. E., and Stull, J. T. (2001) Dedicated myosin light chain kinases with diverse cellular functions. J. Biol. Chem. 276, 4527-4530
    • (2001) J. Biol. Chem. , vol.276 , pp. 4527-4530
    • Kamm, K.E.1    Stull, J.T.2
  • 14
    • 21744445075 scopus 로고    scopus 로고
    • Regulation of myosin II during cytokinesis in higher eukaryotes
    • Matsumura, F. (2005) Regulation of myosin II during cytokinesis in higher eukaryotes. Trends Cell Biol. 15, 371-377
    • (2005) Trends Cell Biol. , vol.15 , pp. 371-377
    • Matsumura, F.1
  • 16
    • 0042347443 scopus 로고    scopus 로고
    • Kinetic mechanism of non-muscle myosin IIB. Functional adaptations for tension generation and maintenance
    • DOI 10.1074/jbc.M302510200
    • Wang, F., Kovacs, M., Hu, A., Limouze, J., Harvey, E. V., and Sellers, J. R. (2003) Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance. J. Biol. Chem. 278, 27439-27448 (Pubitemid 36899926)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27439-27448
    • Wang, F.1    Kovacs, M.2    Hu, A.3    Limouze, J.4    Harvey, E.V.5    Sellers, J.R.6
  • 17
    • 1642448472 scopus 로고    scopus 로고
    • Functional divergence of human cytoplasmic myosin II. Kinetic characterization of the non-muscle IIA isoform
    • DOI 10.1074/jbc.M305453200
    • Kovacs, M., Wang, F., Hu, A., Zhang, Y., and Sellers. J. R. (2003) Functional divergence of human cytoplasmic myosin II: kinetic characterization of the non-muscle IIA isoform. J. Biol. Chem. 278, 38132-38140 (Pubitemid 37221701)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 38132-38140
    • Kovacs, M.1    Wang, F.2    Hu, A.3    Zhang, Y.4    Sellers, J.R.5
  • 19
    • 79958703016 scopus 로고    scopus 로고
    • Comparative kinetic and functional characterization of the motor domains of human nonmuscle myosin-2C isoforms
    • Heissler, S. M., and Manstein, D. J. (2011) Comparative kinetic and functional characterization of the motor domains of human nonmuscle myosin-2C isoforms. J. Biol. Chem. 286, 21191-21202
    • (2011) J. Biol. Chem. , vol.286 , pp. 21191-21202
    • Heissler, S.M.1    Manstein, D.J.2
  • 20
    • 49549162361 scopus 로고
    • Substructure of the myosin molecule. 3. Preparation of single-headed derivatives of myosin
    • Margossian, S. S., and Lowey, S. (1973) Substructure of the myosin molecule. 3. Preparation of single-headed derivatives of myosin. J. Mol. Biol. 74, 301-311
    • (1973) J. Mol. Biol. , vol.74 , pp. 301-311
    • Margossian, S.S.1    Lowey, S.2
  • 21
    • 0026029783 scopus 로고
    • Chicken nonmuscle myosin heavy chains: Differential expression of two mRNAs and evidence for two different polypeptides
    • Kawamoto, S., and Adelstein, R. S. (1991) Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol. 112, 915-924 (Pubitemid 21909638)
    • (1991) Journal of Cell Biology , vol.112 , Issue.5 , pp. 915-924
    • Kawamoto, S.1    Adelstein, R.S.2
  • 22
    • 0027999246 scopus 로고
    • Differential localization of myosin-II isozymes in human cultured cells and blood cells
    • Maupin, P., Phillips, C. L., Adelstein, R. S., and Pollard, T. D. (1994) Differential localization of myosin-II isozymes in human cultured cells and blood cells. J. Cell Sci. 107, 3077-3090 (Pubitemid 24365211)
    • (1994) Journal of Cell Science , vol.107 , Issue.11 , pp. 3077-3090
    • Maupin, P.1    Phillips, C.L.2    Adelstein, R.S.3    Pollard, T.D.4
  • 23
    • 0029586312 scopus 로고
    • Localization of myosin II A and B isoforms in cultured neurons
    • Rochlin, M. W., Itoh, K., Adelstein, R. S., and Bridgman, P. C. (1995) Localization of myosin II A and B isoforms in cultured neurons. J. Cell Sci. 108, 3661-3670 (Pubitemid 26003199)
    • (1995) Journal of Cell Science , vol.108 , Issue.12 , pp. 3661-3670
    • Rochlin, M.W.1    Itoh, K.2    Adelstein, R.S.3    Bridgman, P.C.4
  • 24
    • 0029782819 scopus 로고    scopus 로고
    • Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities
    • Kelley, C. A., Sellers, J. R., Gard, D. L., Bui, D., Adelstein, R. S., and Baines, I. C. (1996) Xenopus nonmuscle myosin heavy chain isoforms have different subcellular localizations and enzymatic activities. J. Cell Biol. 134, 675-687 (Pubitemid 26269140)
    • (1996) Journal of Cell Biology , vol.134 , Issue.3 , pp. 675-687
    • Kelley, C.A.1    Sellers, J.R.2    Gard, D.L.3    Bui, D.4    Adelstein, R.S.5    Baines, I.C.6
  • 26
    • 0036144267 scopus 로고    scopus 로고
    • The gated gait of the processive molecular motor, myosin V
    • DOI 10.1038/ncb732
    • Veigel, C., Wang, F., Bartoo, M. L., Sellers, J. R., and Molloy, J. E. (2002) The gated gait of the processive molecular motor, myosin V. Nat. Cell Biol. 4, 59-65 (Pubitemid 34071981)
    • (2002) Nature Cell Biology , vol.4 , Issue.1 , pp. 59-65
    • Veigel, C.1    Wang, F.2    Bartoo, M.L.3    Sellers, J.R.4    Molloy, J.E.5
  • 27
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • DOI 10.1146/annurev.biochem.68.1.687
    • Geeves, M. A., and Holmes, K. C. (1999) Structural mechanism of muscle contraction. Annu. Rev. Biochem. 68, 687-728 (Pubitemid 29449207)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 29
    • 0016826285 scopus 로고
    • Human platelet myosin. II. In vitro assembly and structure of myosin filaments
    • Niederman, R., and Pollard, T. D. (1975) Human platelet myosin. II. In vitro assembly and structure of myosin filaments. J. Cell Biol. 67, 72-92
    • (1975) J. Cell Biol. , vol.67 , pp. 72-92
    • Niederman, R.1    Pollard, T.D.2
  • 30
    • 0028818253 scopus 로고
    • Myosin II filament assemblies in the active lamella of fibroblasts: Their morphogenesis and role in the formation of actin filament bundles
    • Verkhovsky, A. B., Svitkina, T. M., and Borisy, G. G. (1995) Myosin II filament assemblies in the active lamella of fibroblasts: their morphogenesis and role in the formation of actin filament bundles. J. Cell Biol. 131, 989-1002
    • (1995) J. Cell Biol. , vol.131 , pp. 989-1002
    • Verkhovsky, A.B.1    Svitkina, T.M.2    Borisy, G.G.3
  • 31
    • 77957602527 scopus 로고    scopus 로고
    • Non-muscle myosin IIA with a GFP fused to the N terminus of the regulatory light chain is regulated normally
    • Kengyel, A., Wolf, W. A., Chisholm, R. L., and Sellers, J. R. (2010) Non-muscle myosin IIA with a GFP fused to the N terminus of the regulatory light chain is regulated normally. J. Muscle Res. Cell Motil. 31, 163-170
    • (2010) J. Muscle Res. Cell Motil. , vol.31 , pp. 163-170
    • Kengyel, A.1    Wolf, W.A.2    Chisholm, R.L.3    Sellers, J.R.4
  • 32
    • 0034625126 scopus 로고    scopus 로고
    • A conserved negatively charged amino acid modulates function in human nonmuscle myosin IIA
    • DOI 10.1021/bi000133x
    • Wang, F., Harvey, E. V., Conti, M. A., Wei, D., and Sellers, J. R. (2000) A conserved negatively charged amino acid modulates function in human nonmuscle myosin IIA. Biochemistry 39, 5555-5560 (Pubitemid 30257098)
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5555-5560
    • Wang, F.1    Harvey, E.V.2    Conti, M.A.3    Wei, D.4    Sellers, J.R.5
  • 33
    • 27744519597 scopus 로고    scopus 로고
    • Molecular motors one at a time: FIONA to the rescue
    • DOI 10.1088/0953-8984/17/47/023, PII S0953898405062302
    • Kural, C., Balci, H., and Selvin, P. R. (2005) Molecular motors one at a time: FIONA to the rescue. J. Phys. Condens. Matter 17, S3979-3995 (Pubitemid 41607437)
    • (2005) Journal of Physics Condensed Matter , vol.17 , Issue.47
    • Kural, C.1    Balci, H.2    Selvin, P.R.3
  • 34
    • 4444384544 scopus 로고    scopus 로고
    • Nanometer localization of single fluorescent proteins: Evidence that myosin V walks hand-over-hand via telemark configuration
    • DOI 10.1529/biophysj.103.036897
    • Snyder, G. E., Sakamoto, T., Hammer, J. A., 3rd, Sellers, J. R., and Selvin, P. R. (2004) Nanometer localization of single green fluorescent proteins: evidence that myosinVwalks hand-over-hand via telemark configuration. Biophys. J. 87, 1776-1783 (Pubitemid 39167033)
    • (2004) Biophysical Journal , vol.87 , Issue.3 , pp. 1776-1783
    • Snyder, G.E.1    Sakamoto, T.2    Hammer III, J.A.3    Sellers, J.R.4    Selvin, P.R.5
  • 35
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • DOI 10.1038/368113a0
    • Finer, J. T., Simmons, R. M., and Spudich, J. A. (1994) Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature 368, 113-119 (Pubitemid 24101520)
    • (1994) Nature , vol.368 , Issue.6467 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 37
    • 24144498660 scopus 로고    scopus 로고
    • Mechanical studies of single ribosome/mRNA complexes
    • DOI 10.1529/biophysj.104.056283
    • Vanzi, F., Takagi, Y., Shuman, H., Cooperman, B. S., and Goldman, Y. E. (2005) Mechanical studies of single ribosome/mRNA complexes. Biophys. J. 89, 1909-1919 (Pubitemid 41233546)
    • (2005) Biophysical Journal , vol.89 , Issue.3 , pp. 1909-1919
    • Vanzi, F.1    Takagi, Y.2    Shuman, H.3    Cooperman, B.S.4    Goldman, Y.E.5
  • 38
    • 33645758327 scopus 로고    scopus 로고
    • Force generation in single conventional actomyosin complexes under high dynamic load
    • Takagi, Y., Homsher, E. E., Goldman, Y. E., and Shuman, H. (2006) Force generation in single conventional actomyosin complexes under high dynamic load. Biophys. J. 90, 1295-1307
    • (2006) Biophys. J. , vol.90 , pp. 1295-1307
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4
  • 41
    • 0031656226 scopus 로고    scopus 로고
    • The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer
    • Veigel, C., Bartoo, M. L., White, D. C., Sparrow, J. C., and Molloy, J. E. (1998) The stiffness of rabbit skeletal actomyosin cross-bridges determined with an optical tweezers transducer. Biophys. J. 75, 1424-1438 (Pubitemid 28397612)
    • (1998) Biophysical Journal , vol.75 , Issue.3 , pp. 1424-1438
    • Veigel, C.1    Bartoo, M.L.2    White, D.C.S.3    Sparrow, J.C.4    Molloy, J.E.5
  • 43
    • 46849089895 scopus 로고    scopus 로고
    • Myosin I can act as a molecular force sensor
    • DOI 10.1126/science.1159419
    • Laakso, J. M., Lewis, J. H., Shuman, H., and Ostap, E. M. (2008) Myosin I can act as a molecular force sensor. Science 321, 133-136 (Pubitemid 351956250)
    • (2008) Science , vol.321 , Issue.5885 , pp. 133-136
    • Laakso, J.M.1    Lewis, J.H.2    Shuman, H.3    Ostap, E.M.4
  • 44
    • 0034909695 scopus 로고    scopus 로고
    • Analysis of single-molecule mechanical recordings: Application to acto-myosin interactions
    • DOI 10.1016/S0079-6107(01)00010-4, PII S0079610701000104
    • Knight, A. E., Veigel, C., Chambers, C., and Molloy, J. E. (2001) Analysis of single-molecule mechanical recordings: application to acto-myosin interactions. Prog. Biophys. Mol. Biol. 77, 45-72 (Pubitemid 32709984)
    • (2001) Progress in Biophysics and Molecular Biology , vol.77 , Issue.1 , pp. 45-72
    • Knight, A.E.1    Veigel, C.2    Chambers, C.3    Molloy, J.E.4
  • 47
    • 79958726446 scopus 로고    scopus 로고
    • Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tetering properties
    • Guzik-Lendrum, S., Nagy, A., Takagi, Y., Houdusse, A., and Sellers, J. R. (2011) Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tetering properties. J. Biol. Chem. 286, 21755-21766
    • (2011) J. Biol. Chem. , vol.286 , pp. 21755-21766
    • Guzik-Lendrum, S.1    Nagy, A.2    Takagi, Y.3    Houdusse, A.4    Sellers, J.R.5
  • 48
    • 23744499004 scopus 로고    scopus 로고
    • Fluorescence imaging with one nanometer accuracy: Application to molecular motors
    • DOI 10.1021/ar040136s
    • Yildiz, A., and Selvin, P. R. (2005) Fluorescence imaging with one nanometer accuracy: application to molecular motors. Acc. Chem. Res. 38, 574-582 (Pubitemid 41128410)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.7 , pp. 574-582
    • Yildiz, A.1    Selvin, P.R.2
  • 49
    • 84355161386 scopus 로고    scopus 로고
    • Walking to work: Roles for class v myosins as cargo transporters
    • Hammer, J. A., 3rd, and Sellers, J. R. (2012) Walking to work: roles for class V myosins as cargo transporters. Nat. Rev. Mol. Cell Biol. 13, 13-26
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 13-26
    • Hammer III, J.A.1    Sellers, J.R.2
  • 51
    • 0019455883 scopus 로고
    • Comparison of the binding of heavy meromyosin and myosin subfragment 1 in F-actin
    • Greene, L. E. (1981) Comparison of the binding of heavy meromyosin and myosin subfragment 1 in F-actin. Biochemistry 20, 2120-2126
    • (1981) Biochemistry , vol.20 , pp. 2120-2126
    • Greene, L.E.1
  • 52
    • 0023664088 scopus 로고
    • Effect of phosphorylation on the binding of smooth muscle heavy meromyosin X ADP to actin
    • Greene, L. E., and Sellers, J. R. (1987) Effect of phosphorylation on the binding of smooth muscle heavy meromyosin X ADP to actin. J. Biol. Chem. 262, 4177-4181
    • (1987) J. Biol. Chem. , vol.262 , pp. 4177-4181
    • Greene, L.E.1    Sellers, J.R.2
  • 54
    • 0034718573 scopus 로고    scopus 로고
    • Stabilization of the actomyosin complex by negative charges on myosin
    • Furch, M., Remmel, B., Geeves, M. A., and Manstein, D. J. (2000) Stabilization of the actomyosin complex by negative charges on myosin. Biochemistry 39, 11602-11608
    • (2000) Biochemistry , vol.39 , pp. 11602-11608
    • Furch, M.1    Remmel, B.2    Geeves, M.A.3    Manstein, D.J.4
  • 55
    • 0030893622 scopus 로고    scopus 로고
    • In vitro actin filament sliding velocities produced by mixtures of different types of myosin
    • Cuda, G., Pate, E., Cooke, R., and Sellers, J. R. (1997) In vitro actin filament sliding velocities produced by mixtures of different types of myosin. Biophys. J. 72, 1767-1779 (Pubitemid 27133116)
    • (1997) Biophysical Journal , vol.72 , Issue.4 , pp. 1767-1779
    • Cuda, G.1    Pate, E.2    Cooke, R.3    Sellers, J.R.4
  • 56
    • 77954237525 scopus 로고    scopus 로고
    • Unconventional processive mechanics of non-muscle myosin IIB
    • Norstrom, M. F., Smithback, P. A., and Rock, R. S. (2010) Unconventional processive mechanics of non-muscle myosin IIB. J. Biol. Chem. 285, 26326-26334
    • (2010) J. Biol. Chem. , vol.285 , pp. 26326-26334
    • Norstrom, M.F.1    Smithback, P.A.2    Rock, R.S.3
  • 57
    • 28944449570 scopus 로고    scopus 로고
    • Step-size is determined by neck length in myosin V
    • DOI 10.1021/bi0512086
    • Sakamoto, T., Yildez, A., Selvin, P. R., and Sellers, J. R. (2005) Step-size is determined by neck length in myosin V. Biochemistry 44, 16203-16210 (Pubitemid 41785818)
    • (2005) Biochemistry , vol.44 , Issue.49 , pp. 16203-16210
    • Sakamoto, T.1    Yildez, A.2    Selvin, P.R.3    Sellers, J.R.4
  • 58
    • 0025002994 scopus 로고
    • Polarity and velocity of sliding filaments: Control of direction by actin and of speed by myosin
    • Sellers, J. R., and Kachar, B. (1990) Polarity and velocity of sliding filaments: control of direction by actin and of speed by myosin. Science 249, 406-408
    • (1990) Science , vol.249 , pp. 406-408
    • Sellers, J.R.1    Kachar, B.2
  • 59
    • 0030458632 scopus 로고    scopus 로고
    • Modification of the bi-directional sliding movement of actin filaments along native thick filaments isolated from a clam
    • DOI 10.1007/BF00154058
    • West, J. M., Higuchi, H., Ishijima, A., and Yanagida, T. (1996) Modification of the bi-directional sliding movement of actin filaments along native thick filaments isolated from a clam. J. Muscle Res. Cell Motil. 17, 637-646 (Pubitemid 27008033)
    • (1996) Journal of Muscle Research and Cell Motility , vol.17 , Issue.6 , pp. 637-646
    • West, J.M.1    Higuchi, H.2    Ishijima, A.3    Yanagida, T.4
  • 60
    • 84865827429 scopus 로고    scopus 로고
    • Molecular mechanics of cardiac myosin-binding protein C in native thick filaments
    • Previs, M. J., Beck Previs, S., Gulick, J., Robbins, J., and Warshaw, D. M. (2012) Molecular mechanics of cardiac myosin-binding protein C in native thick filaments. Science 337, 1215-1218
    • (2012) Science , vol.337 , pp. 1215-1218
    • Previs, M.J.1    Beck Previs, S.2    Gulick, J.3    Robbins, J.4    Warshaw, D.M.5
  • 62
    • 4444230478 scopus 로고    scopus 로고
    • How processive is the myosin-V motor?
    • Smith, D. A. (2004) How processive is the myosin-V motor? J. Muscle Res. Cell Motil. 25, 215-217
    • (2004) J. Muscle Res. Cell Motil. , vol.25 , pp. 215-217
    • Smith, D.A.1
  • 63
    • 0027272935 scopus 로고
    • Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
    • Harris, D. E., and Warshaw, D. M. (1993) Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro. J. Biol. Chem. 268, 14764-14768 (Pubitemid 23206617)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.20 , pp. 14764-14768
    • Harris, D.E.1    Warshaw, D.M.2
  • 64
    • 0242609969 scopus 로고    scopus 로고
    • Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
    • DOI 10.1038/ncb1060
    • Veigel, C., Molloy, J. E., Schmitz, S., and Kendrick-Jones, J. (2003) Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers. Nat. Cell Biol. 5, 980-986 (Pubitemid 37406911)
    • (2003) Nature Cell Biology , vol.5 , Issue.11 , pp. 980-986
    • Veigel, C.1    Molloy, J.E.2    Schmitz, S.3    Kendrick-Jones, J.4
  • 66
    • 26944449015 scopus 로고    scopus 로고
    • Load-dependent kinetics of myosin-V can explain its high processivity
    • DOI 10.1038/ncb1287, PII N1287
    • Veigel, C., Schmitz, S., Wang, F., and Sellers, J. R. (2005) Load-dependent kinetics of myosin-V can explain its high processivity. Nat. Cell Biol. 7, 861-869 (Pubitemid 41486286)
    • (2005) Nature Cell Biology , vol.7 , Issue.9 , pp. 861-869
    • Veigel, C.1    Schmitz, S.2    Wang, F.3    Sellers, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.