메뉴 건너뛰기




Volumn 112, Issue 31, 2015, Pages E4168-E4177

Vascular disease-causing mutation R258C in ACTA2 disrupts actin dynamics and interaction with myosin

Author keywords

Actin; Myosin ii; Smooth muscle; Thoracic aortic aneurysms; Vascular disease

Indexed keywords

ALPHA SMOOTH MUSCLE ACTIN; COFILIN; DEOXYRIBONUCLEASE; G ACTIN; GELSOLIN; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN; PROFILIN; TROPOMYOSIN; ACTA2 PROTEIN, HUMAN; ACTIN; ACTIN DEPOLYMERIZING FACTOR; GREEN FLUORESCENT PROTEIN; MUTANT PROTEIN; PROTEIN BINDING;

EID: 84938652684     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1507587112     Document Type: Article
Times cited : (48)

References (52)
  • 2
    • 52949141431 scopus 로고    scopus 로고
    • Genetic basis of thoracic aortic aneurysms and dissections: Focus on smooth muscle cell contractile dysfunction
    • Milewicz DM, et al. (2008) Genetic basis of thoracic aortic aneurysms and dissections: Focus on smooth muscle cell contractile dysfunction. Annu Rev Genomics Hum Genet 9:283-302.
    • (2008) Annu Rev Genomics Hum Genet , vol.9 , pp. 283-302
    • Milewicz, D.M.1
  • 3
    • 36549071997 scopus 로고    scopus 로고
    • Mutations in smooth muscle alpha-actin (ACTA2) lead to thoracic aortic aneurysms and dissections
    • Guo DC, et al. (2007) Mutations in smooth muscle alpha-actin (ACTA2) lead to thoracic aortic aneurysms and dissections. Nat Genet 39(12):1488-1493.
    • (2007) Nat Genet , vol.39 , Issue.12 , pp. 1488-1493
    • Guo, D.C.1
  • 4
    • 73349127492 scopus 로고    scopus 로고
    • Mutation of ACTA2 gene as an important cause of familial and nonfamilial nonsyndromatic thoracic aortic aneurysm and/or dissection (TAAD)
    • Morisaki H, et al. (2009) Mutation of ACTA2 gene as an important cause of familial and nonfamilial nonsyndromatic thoracic aortic aneurysm and/or dissection (TAAD). Hum Mutat 30(10):1406-1411.
    • (2009) Hum Mutat , vol.30 , Issue.10 , pp. 1406-1411
    • Morisaki, H.1
  • 5
    • 84936947295 scopus 로고    scopus 로고
    • Aortic disease presentation and outcome associated with ACTA2 mutations
    • Regalado ES, et al. (2015) Aortic Disease Presentation and Outcome Associated with ACTA2 Mutations. Circ Cardiovasc Genet 8(3):457-464.
    • (2015) Circ Cardiovasc Genet , vol.8 , Issue.3 , pp. 457-464
    • Regalado, E.S.1
  • 6
    • 65149088429 scopus 로고    scopus 로고
    • Mutations in smooth muscle alpha-actin (ACTA2) cause coronary artery disease, stroke, and Moyamoya disease, along with thoracic aortic disease
    • Guo DC, et al. (2009) Mutations in smooth muscle alpha-actin (ACTA2) cause coronary artery disease, stroke, and Moyamoya disease, along with thoracic aortic disease. Am J Hum Genet 84(5):617-627.
    • (2009) Am J Hum Genet , vol.84 , Issue.5 , pp. 617-627
    • Guo, D.C.1
  • 7
    • 0021220505 scopus 로고
    • A vascular smooth muscle alpha-isoactin biosynthetic intermediate in BC3H1 cells. Identification of acetylcysteine at the NH2 terminus
    • Strauch AR, Rubenstein PA (1984) A vascular smooth muscle alpha-isoactin biosynthetic intermediate in BC3H1 cells. Identification of acetylcysteine at the NH2 terminus. J Biol Chem 259(11):7224-7229.
    • (1984) J Biol Chem , vol.259 , Issue.11 , pp. 7224-7229
    • Strauch, A.R.1    Rubenstein, P.A.2
  • 8
    • 77957996302 scopus 로고    scopus 로고
    • Direct visualization of secondary structures of F-actin by electron cryomicroscopy
    • Fujii T, Iwane AH, Yanagida T, Namba K (2010) Direct visualization of secondary structures of F-actin by electron cryomicroscopy. Nature 467(7316):724-728.
    • (2010) Nature , vol.467 , Issue.7316 , pp. 724-728
    • Fujii, T.1    Iwane, A.H.2    Yanagida, T.3    Namba, K.4
  • 10
    • 58749091822 scopus 로고    scopus 로고
    • The nature of the globular- to fibrous-actin transition
    • Oda T, Iwasa M, Aihara T, Maéda Y, Narita A (2009) The nature of the globular- to fibrous-actin transition. Nature 457(7228):441-445.
    • (2009) Nature , vol.457 , Issue.7228 , pp. 441-445
    • Oda, T.1    Iwasa, M.2    Aihara, T.3    Maéda, Y.4    Narita, A.5
  • 11
    • 84925512097 scopus 로고    scopus 로고
    • Structure of the F-actin-tropomyosin complex
    • von der Ecken J, et al. (2015) Structure of the F-actin-tropomyosin complex. Nature 519(7541):114-117.
    • (2015) Nature , vol.519 , Issue.7541 , pp. 114-117
    • Von Der Ecken, J.1
  • 12
    • 53449100875 scopus 로고    scopus 로고
    • Actin cytoskeletal dynamics in smooth muscle: A new paradigm for the regulation of smooth muscle contraction
    • Gunst SJ, Zhang W (2008) Actin cytoskeletal dynamics in smooth muscle: A new paradigm for the regulation of smooth muscle contraction. Am J Physiol Cell Physiol 295(3):C576-C587.
    • (2008) Am J Physiol Cell Physiol , vol.295 , Issue.3 , pp. C576-C587
    • Gunst, S.J.1    Zhang, W.2
  • 13
    • 84930211518 scopus 로고    scopus 로고
    • Role of mechanotransduction in vascular biology: Focus on thoracic aortic aneurysms and dissections
    • Humphrey JD, Schwartz MA, Tellides G, Milewicz DM (2015) Role of mechanotransduction in vascular biology: Focus on thoracic aortic aneurysms and dissections. Circ Res 116(8):1448-1461.
    • (2015) Circ Res , vol.116 , Issue.8 , pp. 1448-1461
    • Humphrey, J.D.1    Schwartz, M.A.2    Tellides, G.3    Milewicz, D.M.4
  • 14
    • 34948868986 scopus 로고    scopus 로고
    • A novel system for expressing toxic actin mutants in Dictyostelium and purification and characterization of a dominant lethal yeast actin mutant
    • Noguchi TQ, Kanzaki N, Ueno H, Hirose K, Uyeda TQ (2007) A novel system for expressing toxic actin mutants in Dictyostelium and purification and characterization of a dominant lethal yeast actin mutant. J Biol Chem 282(38):27721-27727.
    • (2007) J Biol Chem , vol.282 , Issue.38 , pp. 27721-27727
    • Noguchi, T.Q.1    Kanzaki, N.2    Ueno, H.3    Hirose, K.4    Uyeda, T.Q.5
  • 15
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: Cellular control of actin assembly
    • Campellone KG, Welch MD (2010) A nucleator arms race: Cellular control of actin assembly. Nat Rev Mol Cell Biol 11(4):237-251.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.4 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 16
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone MA, DuPage AG, Goode BL (2010) Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat Rev Mol Cell Biol 11(1):62-74.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.1 , pp. 62-74
    • Chesarone, M.A.1    DuPage, A.G.2    Goode, B.L.3
  • 17
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg JR (1999) Proteins of the ADF/cofilin family: Essential regulators of actin dynamics. Annu Rev Cell Dev Biol 15:185-230.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 18
    • 43949104415 scopus 로고    scopus 로고
    • Physiologic properties and regulation of the actin cytoskeleton in vascular smooth muscle
    • Tang DD, Anfinogenova Y (2008) Physiologic properties and regulation of the actin cytoskeleton in vascular smooth muscle. J Cardiovasc Pharmacol Ther 13(2):130-140.
    • (2008) J Cardiovasc Pharmacol Ther , vol.13 , Issue.2 , pp. 130-140
    • Tang, D.D.1    Anfinogenova, Y.2
  • 19
    • 84871919065 scopus 로고    scopus 로고
    • The role of actin filament dynamics in the myogenic response of cerebral resistance arteries
    • Walsh MP, Cole WC (2013) The role of actin filament dynamics in the myogenic response of cerebral resistance arteries. J Cereb Blood Flow Metab 33(1):1-12.
    • (2013) J Cereb Blood Flow Metab , vol.33 , Issue.1 , pp. 1-12
    • Walsh, M.P.1    Cole, W.C.2
  • 20
    • 84922159978 scopus 로고    scopus 로고
    • A novel role for RhoA GTPase in the regulation of airway smooth muscle contraction
    • Zhang W, Huang Y, Wu Y, Gunst SJ (2015) A novel role for RhoA GTPase in the regulation of airway smooth muscle contraction. Can J Physiol Pharmacol 93(2): 129-136.
    • (2015) Can J Physiol Pharmacol , vol.93 , Issue.2 , pp. 129-136
    • Zhang, W.1    Huang, Y.2    Wu, Y.3    Gunst, S.J.4
  • 21
    • 53449101190 scopus 로고    scopus 로고
    • Cytoskeletal remodeling in differentiated vascular smooth muscle is actin isoform dependent and stimulus dependent
    • Kim HR, Gallant C, Leavis PC, Gunst SJ, Morgan KG (2008) Cytoskeletal remodeling in differentiated vascular smooth muscle is actin isoform dependent and stimulus dependent. Am J Physiol Cell Physiol 295(3):C768-C778.
    • (2008) Am J Physiol Cell Physiol , vol.295 , Issue.3 , pp. C768-C778
    • Kim, H.R.1    Gallant, C.2    Leavis, P.C.3    Gunst, S.J.4    Morgan, K.G.5
  • 22
    • 17644379396 scopus 로고    scopus 로고
    • Activation of the Arp2/3 complex by N-WASp is required for actin polymerization and contraction in smooth muscle
    • Zhang W, Wu Y, Du L, Tang DD, Gunst SJ (2005) Activation of the Arp2/3 complex by N-WASp is required for actin polymerization and contraction in smooth muscle. Am J Physiol Cell Physiol 288(5):C1145-C1160.
    • (2005) Am J Physiol Cell Physiol , vol.288 , Issue.5 , pp. C1145-C1160
    • Zhang, W.1    Wu, Y.2    Du, L.3    Tang, D.D.4    Gunst, S.J.5
  • 23
    • 84874454662 scopus 로고    scopus 로고
    • Structure and dynamics of the actin-based smooth muscle contractile and cytoskeletal apparatus
    • Lehman W, Morgan KG (2012) Structure and dynamics of the actin-based smooth muscle contractile and cytoskeletal apparatus. J Muscle Res Cell Motil 33(6):461-469.
    • (2012) J Muscle Res Cell Motil , vol.33 , Issue.6 , pp. 461-469
    • Lehman, W.1    Morgan, K.G.2
  • 24
    • 84861631931 scopus 로고    scopus 로고
    • Rare, nonsynonymous variant in the smooth muscle-specific isoform of myosin heavy chain, MYH11, R247C, alters force generation in the aorta and phenotype of smooth muscle cells
    • Kuang SQ, et al. (2012) Rare, nonsynonymous variant in the smooth muscle-specific isoform of myosin heavy chain, MYH11, R247C, alters force generation in the aorta and phenotype of smooth muscle cells. Circ Res 110(11):1411-1422.
    • (2012) Circ Res , vol.110 , Issue.11 , pp. 1411-1422
    • Kuang, S.Q.1
  • 25
    • 78249244459 scopus 로고    scopus 로고
    • Mutations in myosin light chain kinase cause familial aortic dissections
    • Wang L, et al. (2010) Mutations in myosin light chain kinase cause familial aortic dissections. Am J Hum Genet 87(5):701-707.
    • (2010) Am J Hum Genet , vol.87 , Issue.5 , pp. 701-707
    • Wang, L.1
  • 26
    • 84865230729 scopus 로고    scopus 로고
    • Thoracic aortic aneurysm (TAAD)-causing mutation in actin affects formin regulation of polymerization
    • Malloy LE, et al. (2012) Thoracic aortic aneurysm (TAAD)-causing mutation in actin affects formin regulation of polymerization. J Biol Chem 287(34):28398-28408.
    • (2012) J Biol Chem , vol.287 , Issue.34 , pp. 28398-28408
    • Malloy, L.E.1
  • 27
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier MF, et al. (1997) Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility. J Cell Biol 136(6):1307-1322.
    • (1997) J Cell Biol , vol.136 , Issue.6 , pp. 1307-1322
    • Carlier, M.F.1
  • 28
    • 84908466763 scopus 로고    scopus 로고
    • Cofilin-2 controls actin filament length in muscle sarcomeres
    • Kremneva E, et al. (2014) Cofilin-2 controls actin filament length in muscle sarcomeres. Dev Cell 31(2):215-226.
    • (2014) Dev Cell , vol.31 , Issue.2 , pp. 215-226
    • Kremneva, E.1
  • 30
    • 80054882370 scopus 로고    scopus 로고
    • Slingshot isoform-specific regulation of cofilin-mediated vascular smooth muscle cell migration and neointima formation
    • Torres RA, et al. (2011) Slingshot isoform-specific regulation of cofilin-mediated vascular smooth muscle cell migration and neointima formation. Arterioscler Thromb Vasc Biol 31(11):2424-2431.
    • (2011) Arterioscler Thromb Vasc Biol , vol.31 , Issue.11 , pp. 2424-2431
    • Torres, R.A.1
  • 31
    • 84919340291 scopus 로고    scopus 로고
    • Site-specific cation release drives actin filament severing by vertebrate cofilin
    • Kang H, et al. (2014) Site-specific cation release drives actin filament severing by vertebrate cofilin. Proc Natl Acad Sci USA 111(50):17821-17826.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.50 , pp. 17821-17826
    • Kang, H.1
  • 32
    • 60849116466 scopus 로고    scopus 로고
    • Tropomyosin and ADF/cofilin as collaborators and competitors
    • Kuhn TB, Bamburg JR (2008) Tropomyosin and ADF/cofilin as collaborators and competitors. Adv Exp Med Biol 644:232-249.
    • (2008) Adv Exp Med Biol , vol.644 , pp. 232-249
    • Kuhn, T.B.1    Bamburg, J.R.2
  • 33
    • 77951582061 scopus 로고    scopus 로고
    • Linking actin dynamics and gene transcription to drive cellular motile functions
    • Olson EN, Nordheim A (2010) Linking actin dynamics and gene transcription to drive cellular motile functions. Nat Rev Mol Cell Biol 11(5):353-365.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.5 , pp. 353-365
    • Olson, E.N.1    Nordheim, A.2
  • 34
    • 79959259657 scopus 로고    scopus 로고
    • Structure of a pentavalent G-actin∗MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator
    • Mouilleron S, Langer CA, Guettler S, McDonald NQ, Treisman R (2011) Structure of a pentavalent G-actin∗MRTF-A complex reveals how G-actin controls nucleocytoplasmic shuttling of a transcriptional coactivator. Sci Signal 4(177):ra40.
    • (2011) Sci Signal , vol.4 , Issue.177 , pp. ra40
    • Mouilleron, S.1    Langer, C.A.2    Guettler, S.3    McDonald, N.Q.4    Treisman, R.5
  • 35
    • 69949165706 scopus 로고    scopus 로고
    • Actin isoform-specific conformational differences observed with hydrogen/deuterium exchange and mass spectrometry
    • Stokasimov E, Rubenstein PA (2009) Actin isoform-specific conformational differences observed with hydrogen/deuterium exchange and mass spectrometry. J Biol Chem 284(37):25421-25430.
    • (2009) J Biol Chem , vol.284 , Issue.37 , pp. 25421-25430
    • Stokasimov, E.1    Rubenstein, P.A.2
  • 36
    • 84856991361 scopus 로고    scopus 로고
    • Actin filaments as tension sensors
    • Galkin VE, Orlova A, Egelman EH (2012) Actin filaments as tension sensors. Curr Biol 22(3):R96-R101.
    • (2012) Curr Biol , vol.22 , Issue.3 , pp. R96-R101
    • Galkin, V.E.1    Orlova, A.2    Egelman, E.H.3
  • 37
    • 46249118002 scopus 로고    scopus 로고
    • Lifeact: A versatile marker to visualize F-actin
    • Riedl J, et al. (2008) Lifeact: A versatile marker to visualize F-actin. Nat Methods 5(7):605-607.
    • (2008) Nat Methods , vol.5 , Issue.7 , pp. 605-607
    • Riedl, J.1
  • 38
    • 34547455419 scopus 로고    scopus 로고
    • Polymerization kinetics of ADP- and ADP-Pi-actin determined by fluorescence microscopy
    • Fujiwara I, Vavylonis D, Pollard TD (2007) Polymerization kinetics of ADP- and ADP-Pi-actin determined by fluorescence microscopy. Proc Natl Acad Sci USA 104(21):8827-8832.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.21 , pp. 8827-8832
    • Fujiwara, I.1    Vavylonis, D.2    Pollard, T.D.3
  • 39
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • Kuhn JR, Pollard TD (2005) Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophys J 88(2):1387-1402.
    • (2005) Biophys J , vol.88 , Issue.2 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 40
    • 0034640134 scopus 로고    scopus 로고
    • Uncoupling actin filament fragmentation by cofilin from increased subunit turnover
    • Pope BJ, Gonsior SM, Yeoh S, McGough A, Weeds AG (2000) Uncoupling actin filament fragmentation by cofilin from increased subunit turnover. J Mol Biol 298(4): 649-661.
    • (2000) J Mol Biol , vol.298 , Issue.4 , pp. 649-661
    • Pope, B.J.1    Gonsior, S.M.2    Yeoh, S.3    McGough, A.4    Weeds, A.G.5
  • 41
    • 0035163855 scopus 로고    scopus 로고
    • Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast
    • Lu J, Pollard TD (2001) Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast. Mol Biol Cell 12(4):1161-1175.
    • (2001) Mol Biol Cell , vol.12 , Issue.4 , pp. 1161-1175
    • Lu, J.1    Pollard, T.D.2
  • 42
    • 2442473140 scopus 로고    scopus 로고
    • The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments
    • Harris ES, Li F, Higgs HN (2004) The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments. J Biol Chem 279(19):20076-20087.
    • (2004) J Biol Chem , vol.279 , Issue.19 , pp. 20076-20087
    • Harris, E.S.1    Li, F.2    Higgs, H.N.3
  • 43
    • 0034428543 scopus 로고    scopus 로고
    • Biochemical studies of myosin
    • Trybus KM (2000) Biochemical studies of myosin. Methods 22(4):327-335.
    • (2000) Methods , vol.22 , Issue.4 , pp. 327-335
    • Trybus, K.M.1
  • 44
    • 84875991378 scopus 로고    scopus 로고
    • A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin
    • Barua B, Fagnant PM, Winkelmann DA, Trybus KM, Hitchcock-DeGregori SE (2013) A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin. J Biol Chem 288(14):9602-9609.
    • (2013) J Biol Chem , vol.288 , Issue.14 , pp. 9602-9609
    • Barua, B.1    Fagnant, P.M.2    Winkelmann, D.A.3    Trybus, K.M.4    Hitchcock-DeGregori, S.E.5
  • 45
    • 0023050028 scopus 로고
    • A procedure for the immunoblotting of proteins separated on isoelectric focusing gels
    • Otey CA, Kalnoski MH, Bulinski JC (1986) A procedure for the immunoblotting of proteins separated on isoelectric focusing gels. Anal Biochem 157(1):71-76.
    • (1986) Anal Biochem , vol.157 , Issue.1 , pp. 71-76
    • Otey, C.A.1    Kalnoski, M.H.2    Bulinski, J.C.3
  • 46
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH (1975) High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250(10):4007-4021.
    • (1975) J Biol Chem , vol.250 , Issue.10 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 47
    • 0035654850 scopus 로고    scopus 로고
    • The affinity of chick cofilin for actin increases when actin is complexed with DNase I: Formation of a cofilin-actin-DNase I ternary complex
    • Nosworthy NJ, Kekic M, dos Remedios CG (2001) The affinity of chick cofilin for actin increases when actin is complexed with DNase I: Formation of a cofilin-actin-DNase I ternary complex. Proteomics 1(12):1513-1518.
    • (2001) Proteomics , vol.1 , Issue.12 , pp. 1513-1518
    • Nosworthy, N.J.1    Kekic, M.2    Dos Remedios, C.G.3
  • 48
    • 0034494362 scopus 로고    scopus 로고
    • R403Q and L908V mutant beta-cardiac myosin from patients with familial hypertrophic cardiomyopathy exhibit enhanced mechanical performance at the single molecule level
    • Palmiter KA, et al. (2000) R403Q and L908V mutant beta-cardiac myosin from patients with familial hypertrophic cardiomyopathy exhibit enhanced mechanical performance at the single molecule level. J Muscle Res Cell Motil 21(7):609-620.
    • (2000) J Muscle Res Cell Motil , vol.21 , Issue.7 , pp. 609-620
    • Palmiter, K.A.1
  • 49
    • 0029840916 scopus 로고    scopus 로고
    • Glycine 699 is pivotal for the motor activity of skeletal muscle myosin
    • Kinose F, Wang SX, Kidambi US, Moncman CL, Winkelmann DA (1996) Glycine 699 is pivotal for the motor activity of skeletal muscle myosin. J Cell Biol 134(4):895-909.
    • (1996) J Cell Biol , vol.134 , Issue.4 , pp. 895-909
    • Kinose, F.1    Wang, S.X.2    Kidambi, U.S.3    Moncman, C.L.4    Winkelmann, D.A.5
  • 50
    • 67650522936 scopus 로고    scopus 로고
    • Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion
    • Walcott S, Fagnant PM, Trybus KM, Warshaw DM (2009) Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion. J Biol Chem 284(27):18244-18251.
    • (2009) J Biol Chem , vol.284 , Issue.27 , pp. 18244-18251
    • Walcott, S.1    Fagnant, P.M.2    Trybus, K.M.3    Warshaw, D.M.4
  • 51
    • 72449125767 scopus 로고    scopus 로고
    • A nonprocessive class V myosin drives cargo processively when a kinesin-related protein is a passenger
    • Hodges AR, Bookwalter CS, Krementsova EB, Trybus KM (2009) A nonprocessive class V myosin drives cargo processively when a kinesin-related protein is a passenger. Curr Biol 19(24):2121-2125.
    • (2009) Curr Biol , vol.19 , Issue.24 , pp. 2121-2125
    • Hodges, A.R.1    Bookwalter, C.S.2    Krementsova, E.B.3    Trybus, K.M.4
  • 52
    • 78650651853 scopus 로고    scopus 로고
    • Simultaneous observation of tail and head movements of myosin V during processive motion
    • Lu H, Kennedy GG, Warshaw DM, Trybus KM (2010) Simultaneous observation of tail and head movements of myosin V during processive motion. J Biol Chem 285(53): 42068-42074.
    • (2010) J Biol Chem , vol.285 , Issue.53 , pp. 42068-42074
    • Lu, H.1    Kennedy, G.G.2    Warshaw, D.M.3    Trybus, K.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.