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Volumn 12, Issue 1, 2000, Pages 26-34

Actomyosin: Law and order in motility

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 0033952309     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)00053-8     Document Type: Review
Times cited : (40)

References (97)
  • 1
    • 0032005265 scopus 로고    scopus 로고
    • Myosins: Matching functions with motors
    • Baker J.P., Titus M.A. Myosins: matching functions with motors. Curr Opin Cell Biol. 10:1998;80-86.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 80-86
    • Baker, J.P.1    Titus, M.A.2
  • 2
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V., Rost P.L., Mooseker M.S. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 279:1998;527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Rost, P.L.2    Mooseker, M.S.3
  • 3
    • 0033590558 scopus 로고    scopus 로고
    • Direct interaction of microtubule- And actin-based transport motors
    • This paper provides evidence for direct interaction between myosin Va and kinesin. This interaction links the actin- and microtubule-based cytoskeletal systems and indicates that the two systems are coordinated in membrane traffic
    • Huang J.D., Brady S.T., Richards B.W., Stenolen D., Resau J.H., Copeland N.G., Jenkins N.A. Direct interaction of microtubule- and actin-based transport motors. Nature. 397:1999;267-270. This paper provides evidence for direct interaction between myosin Va and kinesin. This interaction links the actin- and microtubule-based cytoskeletal systems and indicates that the two systems are coordinated in membrane traffic.
    • (1999) Nature , vol.397 , pp. 267-270
    • Huang, J.D.1    Brady, S.T.2    Richards, B.W.3    Stenolen, D.4    Resau, J.H.5    Copeland, N.G.6    Jenkins, N.A.7
  • 6
    • 0032942542 scopus 로고    scopus 로고
    • Myosin IB from Entamoeba histolytica is involved in phagocytosis of human erythrocytes
    • Voigt H., Olivo J., Sansonetti P., Guillen N. Myosin IB from Entamoeba histolytica is involved in phagocytosis of human erythrocytes. J Cell Sci. 112:1999;1191-1201.
    • (1999) J Cell Sci , vol.112 , pp. 1191-1201
    • Voigt, H.1    Olivo, J.2    Sansonetti, P.3    Guillen, N.4
  • 7
    • 0030592549 scopus 로고    scopus 로고
    • Fifty ways to love your lever: Myosin motors
    • Block S.M. Fifty ways to love your lever: myosin motors. Cell. 87:1996;151-157.
    • (1996) Cell , vol.87 , pp. 151-157
    • Block, S.M.1
  • 8
    • 0032478543 scopus 로고    scopus 로고
    • Wag the tail: Structural dynamics of actomyosin
    • Goldman Y.E. Wag the tail: structural dynamics of actomyosin. Cell. 93:1998;1-4.
    • (1998) Cell , vol.93 , pp. 1-4
    • Goldman, Y.E.1
  • 9
    • 18144434716 scopus 로고    scopus 로고
    • Lever arm model of force generation by actin-myosin-ATP
    • Highsmith S. Lever arm model of force generation by actin-myosin-ATP. Biochemistry. 38:1999;9791-9797.
    • (1999) Biochemistry , vol.38 , pp. 9791-9797
    • Highsmith, S.1
  • 11
    • 0033600904 scopus 로고    scopus 로고
    • Kinetic characterization of a monomeric unconventional myosin V construct
    • Trybus K.M., Krementsova E., Freyzon Y. Kinetic characterization of a monomeric unconventional myosin V construct. J Biol Chem. 274:1999;27448-27456.
    • (1999) J Biol Chem , vol.274 , pp. 27448-27456
    • Trybus, K.M.1    Krementsova, E.2    Freyzon, Y.3
  • 12
    • 0033615015 scopus 로고    scopus 로고
    • Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction
    • In this study the myosin regulatory light chain was labeled with rhodamine. Both ends of this bifunctional fluorophore were bound to genetically engineered cysteines in different locations of the light chain. The fact that both ends, rather than one end, are fixed eliminates the possibility of the labels moving independently and allows much more precise and unambiguous measurements
    • Corrie J.E.T., Brandmeier B.D., Ferguson R.E., Trentham D.R., Kendrick Jones J., Hopkins S.C., Heide U.A.v.d., Goldman Y.E., Sabido-David C., Dale R.E.et al. Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction. Nature. 400:1999;425-430. In this study the myosin regulatory light chain was labeled with rhodamine. Both ends of this bifunctional fluorophore were bound to genetically engineered cysteines in different locations of the light chain. The fact that both ends, rather than one end, are fixed eliminates the possibility of the labels moving independently and allows much more precise and unambiguous measurements.
    • (1999) Nature , vol.400 , pp. 425-430
    • Corrie, J.E.T.1    Brandmeier, B.D.2    Ferguson, R.E.3    Trentham, D.R.4    Kendrick Jones, J.5    Hopkins, S.C.6    Heide, U.A.v.d.7    Goldman, Y.E.8    Sabido-David, C.9    Dale, R.E.10
  • 13
    • 0032848772 scopus 로고    scopus 로고
    • Intradomain distances in the regulatory domain of the myosin head in prepower and postpower stroke states: Fluorescence energy transfer
    • Palm T., Sale K., Brown L., Li H., Hambly B., Fajer P.G. Intradomain distances in the regulatory domain of the myosin head in prepower and postpower stroke states: fluorescence energy transfer. Biochemistry. 38:1999;13026-13034.
    • (1999) Biochemistry , vol.38 , pp. 13026-13034
    • Palm, T.1    Sale, K.2    Brown, L.3    Li, H.4    Hambly, B.5    Fajer, P.G.6
  • 14
    • 0032569898 scopus 로고    scopus 로고
    • Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps
    • This paper describes experiments using fluorescence resonance energy transfer. Two fluorescent molecules were attached to different points in myosin on either side of the presumed hinge of the lever arm movement. The energy transfer measurements were consistent with a swinging of the lever arm during the ATPase cycle where the power stroke occurs upon phosphate release
    • Suzuki Y., Yasunaga T., Ohkura R., Wakabayashi T., Sutoh K. Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps. Nature. 396:1998;380-383. This paper describes experiments using fluorescence resonance energy transfer. Two fluorescent molecules were attached to different points in myosin on either side of the presumed hinge of the lever arm movement. The energy transfer measurements were consistent with a swinging of the lever arm during the ATPase cycle where the power stroke occurs upon phosphate release.
    • (1998) Nature , vol.396 , pp. 380-383
    • Suzuki, Y.1    Yasunaga, T.2    Ohkura, R.3    Wakabayashi, T.4    Sutoh, K.5
  • 15
    • 0032539847 scopus 로고    scopus 로고
    • A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction
    • Electron paramagnetic resonance was used in this study to show that large angular changes in the myosin light-chain domain occur and that these changes are associated with force production. The authors identify two distinct angles that are consistent with a power stroke of about 5 nm or more. The measurements also indicate that force may be generated by a transition from weak to strong actin binding
    • Baker J.E., Brust-Mascher I., Ramachandran S., LaConte L.E., Thomas D.D. A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction. Proc Natl Acad Sci USA. 95:1998;2944-2949. Electron paramagnetic resonance was used in this study to show that large angular changes in the myosin light-chain domain occur and that these changes are associated with force production. The authors identify two distinct angles that are consistent with a power stroke of about 5 nm or more. The measurements also indicate that force may be generated by a transition from weak to strong actin binding.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2944-2949
    • Baker, J.E.1    Brust-Mascher, I.2    Ramachandran, S.3    Laconte, L.E.4    Thomas, D.D.5
  • 16
    • 0032433333 scopus 로고    scopus 로고
    • Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: The effect of nucleotides and actin
    • Xiao M., Li H., Snyder G.E., Cooke R., Yount R.G., Selvin P.R. Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: the effect of nucleotides and actin. Proc Natl Acad Sci USA. 95:1998;15309-15314.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15309-15314
    • Xiao, M.1    Li, H.2    Snyder, G.E.3    Cooke, R.4    Yount, R.G.5    Selvin, P.R.6
  • 17
    • 0032474429 scopus 로고    scopus 로고
    • Tertiary structural changes in the cleft containing the ATP sensitive tryptophan and reactive thiol are consistent with pivoting of the myosin heavy chain at Gly699
    • Burghardt T.P., Garamszegi S.P., Park S., Ajtai K. Tertiary structural changes in the cleft containing the ATP sensitive tryptophan and reactive thiol are consistent with pivoting of the myosin heavy chain at Gly699. Biochemistry. 37:1998;8035-8047.
    • (1998) Biochemistry , vol.37 , pp. 8035-8047
    • Burghardt, T.P.1    Garamszegi, S.P.2    Park, S.3    Ajtai, K.4
  • 18
    • 0033580652 scopus 로고    scopus 로고
    • Trinitrophenylated reactive lysine residue in myosin detects lever arm movement during the consecutive steps of ATP hydrolysis
    • Ajtai K., Peyser Y.M., Park S., Burghardt T.P., Muhlrad A. Trinitrophenylated reactive lysine residue in myosin detects lever arm movement during the consecutive steps of ATP hydrolysis. Biochemistry. 38:1999;6428-6440.
    • (1999) Biochemistry , vol.38 , pp. 6428-6440
    • Ajtai, K.1    Peyser, Y.M.2    Park, S.3    Burghardt, T.P.4    Muhlrad, A.5
  • 20
    • 0030692707 scopus 로고    scopus 로고
    • Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis
    • Jontes J.D., Milligan R.A. Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis. J Cell Biol. 139:1997;683-693.
    • (1997) J Cell Biol , vol.139 , pp. 683-693
    • Jontes, J.D.1    Milligan, R.A.2
  • 21
    • 0032442461 scopus 로고    scopus 로고
    • Structural invariance of constitutively active and inactive mutants of Acanthamoeba myosin IC bound to F-actin in the rigor and ADP-bound states
    • In this study, the authors investigate two mutants of Acanthamoeba myosin IC by electron cryomicroscopy and image reconstruction. One mutant was trapped in an inactive ATPase state, the other was constitutively active. The authors find no difference in the mode of attachment of myosin to actin between the two mutants. They suggest that modulation of dynamic properties within the complex may play a role in the ATPase cycle
    • Carragher B.O., Cheng N., Wang Z.Y., Korn E.D., Reilein A., Belnap D.M., Hammer J.A., Steven A.C. Structural invariance of constitutively active and inactive mutants of Acanthamoeba myosin IC bound to F-actin in the rigor and ADP-bound states. Proc Natl Acad Sci USA. 95:1998;15206-15211. In this study, the authors investigate two mutants of Acanthamoeba myosin IC by electron cryomicroscopy and image reconstruction. One mutant was trapped in an inactive ATPase state, the other was constitutively active. The authors find no difference in the mode of attachment of myosin to actin between the two mutants. They suggest that modulation of dynamic properties within the complex may play a role in the ATPase cycle.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15206-15211
    • Carragher, B.O.1    Cheng, N.2    Wang, Z.Y.3    Korn, E.D.4    Reilein, A.5    Belnap, D.M.6    Hammer, J.A.7    Steven, A.C.8
  • 22
    • 0029774205 scopus 로고    scopus 로고
    • Fluorescence polarization of skeletal muscle fibers labeled with rhodamine isomers on the myosin heavy chain
    • Berger C.L., Craik J.S., Trentham D.R., Corrie J.E., Goldman Y.E. Fluorescence polarization of skeletal muscle fibers labeled with rhodamine isomers on the myosin heavy chain. Biophys J. 71:1996;3330-3343.
    • (1996) Biophys J , vol.71 , pp. 3330-3343
    • Berger, C.L.1    Craik, J.S.2    Trentham, D.R.3    Corrie, J.E.4    Goldman, Y.E.5
  • 23
    • 0030928755 scopus 로고    scopus 로고
    • Probes bound to myosin Cys-707 rotate during length transients in contraction
    • Burghardt T.P., Garamszegi S.P., Ajtai K. Probes bound to myosin Cys-707 rotate during length transients in contraction. Proc Natl Acad Sci USA. 94:1997;9631-9636.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9631-9636
    • Burghardt, T.P.1    Garamszegi, S.P.2    Ajtai, K.3
  • 24
    • 0033619258 scopus 로고    scopus 로고
    • Myosin VI is an actin-based motor that moves backwards
    • The authors show that myosin VI moves backwards on actin and provide a structural model for this mechanism. The direction of movement was determined by in vitro motility assays. Electron cryomicroscopy experiments in the presence and absence of ADP indicate that the lever arm moves towards the pointed end of the filament (up) upon ADP release rather than towards the barbed end (down)
    • Wells A.L., Lin A.W., Chen L-Q., Safer D., Cain S.A., Hasson T., Carragher B.O., Milligan R.A., Sweeney H.L. Myosin VI is an actin-based motor that moves backwards. Nature. 401:1999;505-508. The authors show that myosin VI moves backwards on actin and provide a structural model for this mechanism. The direction of movement was determined by in vitro motility assays. Electron cryomicroscopy experiments in the presence and absence of ADP indicate that the lever arm moves towards the pointed end of the filament (up) upon ADP release rather than towards the barbed end (down).
    • (1999) Nature , vol.401 , pp. 505-508
    • Wells, A.L.1    Lin, A.W.2    Chen, L.-Q.3    Safer, D.4    Cain, S.A.5    Hasson, T.6    Carragher, B.O.7    Milligan, R.A.8    Sweeney, H.L.9
  • 25
    • 0029159959 scopus 로고
    • X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-
    • Fisher A.J., Smith C.A., Thoden J.B., Smith R., Sutoh K., Holden H.M., Rayment I. X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-. Biochemistry. 34:1995;8960-8972.
    • (1995) Biochemistry , vol.34 , pp. 8960-8972
    • Fisher, A.J.1    Smith, C.A.2    Thoden, J.B.3    Smith, R.4    Sutoh, K.5    Holden, H.M.6    Rayment, I.7
  • 26
    • 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
    • This paper describes the crystal structure of smooth muscle myosin in the transition state. In contrast to earlier studies on Dictyostelium discoideum myosin, a substantial portion of the lever arm is present in this structure. This proves the important point that the converter movement detected in the Dictyostelium studies was not an artifact of the lever-arm truncation
    • Dominguez R., Freyzon Y., Trybus K.M., 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. This paper describes the crystal structure of smooth muscle myosin in the transition state. In contrast to earlier studies on Dictyostelium discoideum myosin, a substantial portion of the lever arm is present in this structure. This proves the important point that the converter movement detected in the Dictyostelium studies was not an artifact of the lever-arm truncation.
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 27
    • 0029913456 scopus 로고    scopus 로고
    • The neck region of the myosin motor domain acts as a lever arm to generate movement
    • Uyeda T.Q., Abramson P.D., Spudich J.A. The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc Natl Acad Sci USA. 93:1996;4459-4464.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4459-4464
    • Uyeda, T.Q.1    Abramson, P.D.2    Spudich, J.A.3
  • 29
    • 0029960235 scopus 로고    scopus 로고
    • X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
    • Smith C.A., Rayment I. X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution. Biochemistry. 35:1996;5404-5417.
    • (1996) Biochemistry , vol.35 , pp. 5404-5417
    • Smith, C.A.1    Rayment, I.2
  • 30
    • 0030768794 scopus 로고    scopus 로고
    • X-ray structures of the MgADP, MgATPγS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain
    • Gulick A.M., Bauer C.B., Thoden J.B., Rayment I. X-ray structures of the MgADP, MgATPγS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry. 36:1997;11619-11628.
    • (1997) Biochemistry , vol.36 , pp. 11619-11628
    • Gulick, A.M.1    Bauer, C.B.2    Thoden, J.B.3    Rayment, I.4
  • 31
    • 0018868611 scopus 로고
    • Reaction of 5,5′-dithiobis(2-nitrobenzoic acid) with myosin subfragment one: Evidence for formation of a single protein disulfide with trapping of metal nucleotide at the active site
    • Wells J.A., Yount R.G. Reaction of 5,5′-dithiobis(2-nitrobenzoic acid) with myosin subfragment one: evidence for formation of a single protein disulfide with trapping of metal nucleotide at the active site. Biochemistry. 19:1980;1711-1717.
    • (1980) Biochemistry , vol.19 , pp. 1711-1717
    • Wells, J.A.1    Yount, R.G.2
  • 32
    • 0032564445 scopus 로고    scopus 로고
    • Probing the conformational states of the SH1 SH2 helix in myosin: A cross-linking approach
    • This paper provides an answer to the long-standing question of why the reactive thiols in myosin can be crosslinked by a variety of crosslinkers of different length. The study focuses on the analysis of the reaction kinetics of the crosslinking process and detects that many conformational states of the SH1-SH2 helix must coexist and that the probability of a particular state is dependent on the nucleotide
    • Nitao L.K., Reisler E. Probing the conformational states of the SH1 SH2 helix in myosin: a cross-linking approach. Biochemistry. 37:1998;16704-16710. This paper provides an answer to the long-standing question of why the reactive thiols in myosin can be crosslinked by a variety of crosslinkers of different length. The study focuses on the analysis of the reaction kinetics of the crosslinking process and detects that many conformational states of the SH1-SH2 helix must coexist and that the probability of a particular state is dependent on the nucleotide.
    • (1998) Biochemistry , vol.37 , pp. 16704-16710
    • Nitao, L.K.1    Reisler, E.2
  • 33
    • 0033543224 scopus 로고    scopus 로고
    • : Thiol-specific cross-linkers of variable length reveal a similar separation of SH1 and SH2 in myosin subfragment 1 in the presence and absence of MgADP
    • Kliche W., Pfannstiel J., Tiepold M., Stoeva S., Faulstich H. : Thiol-specific cross-linkers of variable length reveal a similar separation of SH1 and SH2 in myosin subfragment 1 in the presence and absence of MgADP. Biochemistry. 38:1999;10307-10317.
    • (1999) Biochemistry , vol.38 , pp. 10307-10317
    • Kliche, W.1    Pfannstiel, J.2    Tiepold, M.3    Stoeva, S.4    Faulstich, H.5
  • 34
    • 1642340974 scopus 로고    scopus 로고
    • Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel conformation of the myosin head
    • The crystal structure of scallop myosin subfragment 1 is described in this paper. Both light chains are present in this construct. The conformation of the molecule has not been seen before and does not readily fit into the current idea of the ATPase cycle. The domains seem only loosely connected and the SH1-SH2 helix is not resolved. The authors argue that, even though crystallized in the presence of ADP, the structure represents an ATP-related state
    • Houdusse A., Kalabokis V.N., Himmel D., Szent-Györgyi A.G., Cohen C. Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head. Cell. 97:1999;459-470. The crystal structure of scallop myosin subfragment 1 is described in this paper. Both light chains are present in this construct. The conformation of the molecule has not been seen before and does not readily fit into the current idea of the ATPase cycle. The domains seem only loosely connected and the SH1-SH2 helix is not resolved. The authors argue that, even though crystallized in the presence of ADP, the structure represents an ATP-related state.
    • (1999) Cell , vol.97 , pp. 459-470
    • Houdusse, A.1    Kalabokis, V.N.2    Himmel, D.3    Szent-Györgyi, A.G.4    Cohen, C.5
  • 35
    • 0033545955 scopus 로고    scopus 로고
    • Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region
    • Batra R., Geeves M.A., Manstein D.J. Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region. Biochemistry. 38:1999;6126-6134.
    • (1999) Biochemistry , vol.38 , pp. 6126-6134
    • Batra, R.1    Geeves, M.A.2    Manstein, D.J.3
  • 36
    • 0032867566 scopus 로고    scopus 로고
    • Dictyostelium myosin II G680V suppressors exhibit overlapping spectra of biochemical phenotypes including facilitated phosphate release
    • In this study 13 intragenetic suppressors of the Gly680→Val mutation of Dictyostelium discoideum myosin are biochemically characterized. The authors conclude from this analysis that the Gly680→Val mutation affects the release of inorganic phosphate
    • Wu Y., Nejad M., Patterson B. Dictyostelium myosin II G680V suppressors exhibit overlapping spectra of biochemical phenotypes including facilitated phosphate release. Genetics. 153:1999;107-116. In this study 13 intragenetic suppressors of the Gly680→Val mutation of Dictyostelium discoideum myosin are biochemically characterized. The authors conclude from this analysis that the Gly680→Val mutation affects the release of inorganic phosphate.
    • (1999) Genetics , vol.153 , pp. 107-116
    • Wu, Y.1    Nejad, M.2    Patterson, B.3
  • 37
    • 0010299503 scopus 로고    scopus 로고
    • Double-headed smooth and skeletal myosins generate displacements by cooperative action of the two heads
    • Guilford W.H., Dupuis D.E., Warshaw D.M., Waller G.S., Trybus K.M., Lowey S. Double-headed smooth and skeletal myosins generate displacements by cooperative action of the two heads. Biophys J. 74:1998;A225.
    • (1998) Biophys J , vol.74 , pp. 225
    • Guilford, W.H.1    Dupuis, D.E.2    Warshaw, D.M.3    Waller, G.S.4    Trybus, K.M.5    Lowey, S.6
  • 38
    • 0032559298 scopus 로고    scopus 로고
    • Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin
    • The study described in this paper is based on single molecule analysis of myosin using optical traps and total internal reflection fluorescence microscopy. The results indicate that force production can occur several hundred milliseconds after product release. This suggests that force generation is not directly coupled to the release of bound ligands
    • Ishijima A., Kojima H., Funatsu T., Tokunaga M., Higuchi H., Tanaka H., Yanagida T. Simultaneous observation of individual ATPase and mechanical events by a single myosin molecule during interaction with actin. Cell. 92:1998;161-171. The study described in this paper is based on single molecule analysis of myosin using optical traps and total internal reflection fluorescence microscopy. The results indicate that force production can occur several hundred milliseconds after product release. This suggests that force generation is not directly coupled to the release of bound ligands.
    • (1998) Cell , vol.92 , pp. 161-171
    • Ishijima, A.1    Kojima, H.2    Funatsu, T.3    Tokunaga, M.4    Higuchi, H.5    Tanaka, H.6    Yanagida, T.7
  • 39
    • 0033535556 scopus 로고    scopus 로고
    • The motor protein myosin-I produces its working stroke in two steps
    • This study, based on single molecule analysis of myosin I using optical tweezers, indicates that the power stroke occurs in two steps. The authors detected a step at the beginning of each interaction and then, 100-300 milliseconds later, another step
    • Veigel C., Coluccio L.M., Jontes J.D., Sparrow J.C., Milligan R.A., Molloy J.E. The motor protein myosin-I produces its working stroke in two steps. Nature. 398:1999;530-533. This study, based on single molecule analysis of myosin I using optical tweezers, indicates that the power stroke occurs in two steps. The authors detected a step at the beginning of each interaction and then, 100-300 milliseconds later, another step.
    • (1999) Nature , vol.398 , pp. 530-533
    • Veigel, C.1    Coluccio, L.M.2    Jontes, J.D.3    Sparrow, J.C.4    Milligan, R.A.5    Molloy, J.E.6
  • 40
    • 0033552942 scopus 로고    scopus 로고
    • A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
    • This study used single myosin molecules attached to the tip of a scanning-probe microscope, moved close to a bundle of actin filaments in the presence of ATP. These experiments indicate that myosin moves in a series of up to five sub-steps of 5.3 nm per ATP hydrolysis
    • Kitamura K., Tokunaga M., Iwane A.H., Yanagida T. A single myosin head moves along an actin filament with regular steps of 5.3 nanometres. Nature. 397:1999;129-134. This study used single myosin molecules attached to the tip of a scanning-probe microscope, moved close to a bundle of actin filaments in the presence of ATP. These experiments indicate that myosin moves in a series of up to five sub-steps of 5.3 nm per ATP hydrolysis.
    • (1999) Nature , vol.397 , pp. 129-134
    • Kitamura, K.1    Tokunaga, M.2    Iwane, A.H.3    Yanagida, T.4
  • 42
    • 0033551045 scopus 로고    scopus 로고
    • Two heads of myosin are better than one for generating force and motion
    • Single molecule study using an optical-trap transducer on single- and double-headed muscle myosins. Analysis of the signal was done by mean-variance analysis, a statistical method originally developed for ion-channel studies. The results of the study indicate that muscle myosins require both heads to generate maximal force
    • Tyska M.J., Dupuis D.E., Guilford W.H., Patlak J.B., Waller G.S., Trybus K.M., Warshaw D.M., Lowey S. Two heads of myosin are better than one for generating force and motion. Proc Natl Acad Sci USA. 96:1999;4402-4407. Single molecule study using an optical-trap transducer on single- and double-headed muscle myosins. Analysis of the signal was done by mean-variance analysis, a statistical method originally developed for ion-channel studies. The results of the study indicate that muscle myosins require both heads to generate maximal force.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4402-4407
    • Tyska, M.J.1    Dupuis, D.E.2    Guilford, W.H.3    Patlak, J.B.4    Waller, G.S.5    Trybus, K.M.6    Warshaw, D.M.7    Lowey, S.8
  • 44
    • 0032975880 scopus 로고    scopus 로고
    • The ADP release step of the smooth muscle cross-bridge cycle is not directly associated with force generation
    • Dantzig J.A., Barsotti R.J., Manz S., Sweeney H.L., Goldman Y.E. The ADP release step of the smooth muscle cross-bridge cycle is not directly associated with force generation. Biophys J. 77:1999;386-397.
    • (1999) Biophys J , vol.77 , pp. 386-397
    • Dantzig, J.A.1    Barsotti, R.J.2    Manz, S.3    Sweeney, H.L.4    Goldman, Y.E.5
  • 45
    • 0029914905 scopus 로고    scopus 로고
    • Active site comparisons highlight structural similarities between myosin and other P-loop proteins
    • Smith C.A., Rayment I. Active site comparisons highlight structural similarities between myosin and other P-loop proteins. Biophys J. 70:1996;1590-1602.
    • (1996) Biophys J , vol.70 , pp. 1590-1602
    • Smith, C.A.1    Rayment, I.2
  • 46
    • 0011364439 scopus 로고
    • Structural studies of myosin:nucleotide complexes: A revised model for the molecular basis of muscle contraction
    • Fisher A.J., Smith C.A., Thoden J., Smith R., Sutoh K., Holden H.M., Rayment I. Structural studies of myosin:nucleotide complexes: a revised model for the molecular basis of muscle contraction. Biophys J. 68:1995;19S-28S.
    • (1995) Biophys J , vol.68
    • Fisher, A.J.1    Smith, C.A.2    Thoden, J.3    Smith, R.4    Sutoh, K.5    Holden, H.M.6    Rayment, I.7
  • 47
    • 0032766063 scopus 로고    scopus 로고
    • Role of the salt-bridge between switch-1 and switch-2 of Dictyostelium myosin
    • Furch M., Fujita-Becker S., Geeves M.A., Holmes K.C., Manstein D.J. Role of the salt-bridge between switch-1 and switch-2 of Dictyostelium myosin. J Mol Biol. 290:1999;797-809.
    • (1999) J Mol Biol , vol.290 , pp. 797-809
    • Furch, M.1    Fujita-Becker, S.2    Geeves, M.A.3    Holmes, K.C.4    Manstein, D.J.5
  • 48
    • 0032499768 scopus 로고    scopus 로고
    • Functional transitions in myosin: Formation of a critical salt-bridge and transmission of effect to the sensitive tryptophan
    • Onishi H., Kojima S., Katoh K., Fujiwara K., Martinez H.M., Morales M.F. Functional transitions in myosin: formation of a critical salt-bridge and transmission of effect to the sensitive tryptophan. Proc Natl Acad Sci USA. 95:1998;6653-6658.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6653-6658
    • Onishi, H.1    Kojima, S.2    Katoh, K.3    Fujiwara, K.4    Martinez, H.M.5    Morales, M.F.6
  • 49
    • 0033522996 scopus 로고    scopus 로고
    • Functional significance of the conserved residues in the flexible hinge region of the myosin motor domain
    • Kambara T., Rhodes T.E., Ikebe R., Yamada M., White H.D., Ikebe M. Functional significance of the conserved residues in the flexible hinge region of the myosin motor domain. J Biol Chem. 274:1999;16400-16406.
    • (1999) J Biol Chem , vol.274 , pp. 16400-16406
    • Kambara, T.1    Rhodes, T.E.2    Ikebe, R.3    Yamada, M.4    White, H.D.5    Ikebe, M.6
  • 50
    • 0032411662 scopus 로고    scopus 로고
    • Smooth muscle myosin. Amino acid residues responsible for the hydrolysis of ATP
    • Onishi H., Morales M.F., Kojima S., Katoh K., Fujiwara K. Smooth muscle myosin. Amino acid residues responsible for the hydrolysis of ATP. Adv Exp Med Biol. 453:1998;99-103.
    • (1998) Adv Exp Med Biol , vol.453 , pp. 99-103
    • Onishi, H.1    Morales, M.F.2    Kojima, S.3    Katoh, K.4    Fujiwara, K.5
  • 51
    • 0032538442 scopus 로고    scopus 로고
    • Effects of mutations in the γ-phosphate binding site of myosin on its motor function
    • Li X.D., Rhodes T.E., Ikebe R., Kambara T., White H.D., Ikebe M. Effects of mutations in the γ-phosphate binding site of myosin on its motor function. J Biol Chem. 273:1998;27404-27411.
    • (1998) J Biol Chem , vol.273 , pp. 27404-27411
    • Li, X.D.1    Rhodes, T.E.2    Ikebe, R.3    Kambara, T.4    White, H.D.5    Ikebe, M.6
  • 52
    • 0031672952 scopus 로고    scopus 로고
    • Structure-mutation analysis of the ATPase site of Dictyostelium discoideum myosin II
    • Sasaki N., Sutoh K. Structure-mutation analysis of the ATPase site of Dictyostelium discoideum myosin II. Adv Biophys. 35:1998;1-24.
    • (1998) Adv Biophys , vol.35 , pp. 1-24
    • Sasaki, N.1    Sutoh, K.2
  • 53
    • 0040833283 scopus 로고    scopus 로고
    • Conformational variability in actomyosin complexes
    • Hanein D., Ouyang G., DeRosier D. Conformational variability in actomyosin complexes. Biophys J. 76:1999;A145.
    • (1999) Biophys J , vol.76 , pp. 145
    • Hanein, D.1    Ouyang, G.2    Derosier, D.3
  • 54
    • 0031031962 scopus 로고    scopus 로고
    • An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms
    • Rovner A.S., Freyzon Y., Trybus K.M. An insert in the motor domain determines the functional properties of expressed smooth muscle myosin isoforms. J Musc Res Cell Motil. 18:1997;103-110.
    • (1997) J Musc Res Cell Motil , vol.18 , pp. 103-110
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 55
    • 15144351296 scopus 로고    scopus 로고
    • Conservation within the myosin motor domain: Implications for structure and function
    • Cope M.J.T., Whisstock J., Rayment I., Kendrick-Jones J. Conservation within the myosin motor domain: implications for structure and function. Structure. 4:1996;969-987.
    • (1996) Structure , vol.4 , pp. 969-987
    • Cope, M.J.T.1    Whisstock, J.2    Rayment, I.3    Kendrick-Jones, J.4
  • 56
    • 0033516510 scopus 로고    scopus 로고
    • Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: Implications for functional diversity
    • Weiss A., Schiaffino S., Leinwand L.A. Comparative sequence analysis of the complete human sarcomeric myosin heavy chain family: implications for functional diversity. J Mol Biol. 290:1999;61-75.
    • (1999) J Mol Biol , vol.290 , pp. 61-75
    • Weiss, A.1    Schiaffino, S.2    Leinwand, L.A.3
  • 57
    • 0033599347 scopus 로고    scopus 로고
    • Novel Dictyostelium unconventional myosin MyoK is a class I myosin with the longest loop-1 insert and the shortest tail
    • Yazu M., Adachi H., Sutoh K. Novel Dictyostelium unconventional myosin MyoK is a class I myosin with the longest loop-1 insert and the shortest tail. Biochem Biophys Res Commun. 255:1999;711-716.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 711-716
    • Yazu, M.1    Adachi, H.2    Sutoh, K.3
  • 58
    • 0032546576 scopus 로고    scopus 로고
    • Loop I can modulate ADP affinity, ATPase activity, and motility of different scallop myosins. Transient kinetic analysis of S1 isoforms
    • Kurzawa-Goertz S.E., Perreault-Micale C.L., Trybus K.M., Szent-Györgyi A.G., Geeves M.A. Loop I can modulate ADP affinity, ATPase activity, and motility of different scallop myosins. Transient kinetic analysis of S1 isoforms. Biochemistry. 37:1998;7517-7525.
    • (1998) Biochemistry , vol.37 , pp. 7517-7525
    • Kurzawa-Goertz, S.E.1    Perreault-Micale, C.L.2    Trybus, K.M.3    Szent-Györgyi, A.G.4    Geeves, M.A.5
  • 59
    • 0032510769 scopus 로고    scopus 로고
    • Dictyostelium myosin 25-50K loop substitutions specifically affect ADP release rates
    • Murphy C.T., Spudich J.A. Dictyostelium myosin 25-50K loop substitutions specifically affect ADP release rates. Biochemistry. 37:1998;6738-6744.
    • (1998) Biochemistry , vol.37 , pp. 6738-6744
    • Murphy, C.T.1    Spudich, J.A.2
  • 61
    • 0033583079 scopus 로고    scopus 로고
    • Specialized conservation of surface loops of myosin: Evidence that loops are involved in determining functional characteristics
    • Analysis of relative rates of evolutionary changes in surface loops 1 and 2 of myosin. The study shows that the sequences of these loops are evolutionarily more constrained than the rest of the myosin molecule when myosins are compared that are known to be kinetically or developmentally similar
    • Goodson H.V., Warrick H.M., Spudich J.A. Specialized conservation of surface loops of myosin: evidence that loops are involved in determining functional characteristics. J Mol Biol. 287:1999;173-185. Analysis of relative rates of evolutionary changes in surface loops 1 and 2 of myosin. The study shows that the sequences of these loops are evolutionarily more constrained than the rest of the myosin molecule when myosins are compared that are known to be kinetically or developmentally similar.
    • (1999) J Mol Biol , vol.287 , pp. 173-185
    • Goodson, H.V.1    Warrick, H.M.2    Spudich, J.A.3
  • 62
    • 0032779888 scopus 로고    scopus 로고
    • Quantitative fitting of atomic models into observed densities derived by electron microscopy
    • This paper describes a powerful quantitative approach to fitting atomic models into three-dimensional reconstructions derived by electron microscopy. The procedure relies on a global, statistical analysis based on real-space correlation. An application of this technique to actin filaments decorated with chicken skeletal myosin subfragment 1 showed that the light-chain position needs to be modified relative to the unbound crystal structure. The analysis also indicated that loop 1 is stabilized upon binding of myosin to actin
    • Volkmann N., Hanein D. Quantitative fitting of atomic models into observed densities derived by electron microscopy. J Struct Biol. 125:1999;176-184. This paper describes a powerful quantitative approach to fitting atomic models into three-dimensional reconstructions derived by electron microscopy. The procedure relies on a global, statistical analysis based on real-space correlation. An application of this technique to actin filaments decorated with chicken skeletal myosin subfragment 1 showed that the light-chain position needs to be modified relative to the unbound crystal structure. The analysis also indicated that loop 1 is stabilized upon binding of myosin to actin.
    • (1999) J Struct Biol , vol.125 , pp. 176-184
    • Volkmann, N.1    Hanein, D.2
  • 63
  • 64
    • 0033613155 scopus 로고    scopus 로고
    • Myosin light chain domain rotates upon muscle activation but not ATP hydrolysis
    • An electron paramagnetic resonance study on scallop muscle fibers using nucleotide analogs to trap myosin in certain states of the ATPase cycle is reported. The study indicates that the rotation of the light-chain domain is not directly coupled to ATP hydrolysis
    • Brust-Mascher I., LaConte L.E., Baker J.E., Thomas D.D. Myosin light chain domain rotates upon muscle activation but not ATP hydrolysis. Biochemistry. 38:1999;12607-12613. An electron paramagnetic resonance study on scallop muscle fibers using nucleotide analogs to trap myosin in certain states of the ATPase cycle is reported. The study indicates that the rotation of the light-chain domain is not directly coupled to ATP hydrolysis.
    • (1999) Biochemistry , vol.38 , pp. 12607-12613
    • Brust-Mascher, I.1    Laconte, L.E.2    Baker, J.E.3    Thomas, D.D.4
  • 65
    • 0029989974 scopus 로고    scopus 로고
    • Crystal structure of the kinesin motor domain reveals a structural similarity to myosin
    • Kull F.J., Sablin E.P., Lau R., Fletterick R.J., Vale R.D. Crystal structure of the kinesin motor domain reveals a structural similarity to myosin. Nature. 380:1996;550-555.
    • (1996) Nature , vol.380 , pp. 550-555
    • Kull, F.J.1    Sablin, E.P.2    Lau, R.3    Fletterick, R.J.4    Vale, R.D.5
  • 66
    • 0040241932 scopus 로고    scopus 로고
    • The structure of the nucleotide-binding site of kinesin
    • Crystal structures of kinesin in the presence of various nucleotide analogs were solved and compared. The structure of kinesin remains nearly unchanged, indicating that the conformational state of kinesin is not strongly dependent on the nucleotide
    • Möller J., Marx A., Sack S., Song Y.H., Mandelkow E. The structure of the nucleotide-binding site of kinesin. Biol Chem. 380:1999;981-992. Crystal structures of kinesin in the presence of various nucleotide analogs were solved and compared. The structure of kinesin remains nearly unchanged, indicating that the conformational state of kinesin is not strongly dependent on the nucleotide.
    • (1999) Biol Chem , vol.380 , pp. 981-992
    • Möller, J.1    Marx, A.2    Sack, S.3    Song, Y.H.4    Mandelkow, E.5
  • 67
    • 0344765475 scopus 로고    scopus 로고
    • Microsecond rotational dynamics of spin-labeled myosin regulatory light chain induced by relaxation and contraction of scallop muscle
    • Roopnarine O., Szent-Györgyi A.G., Thomas D.D. Microsecond rotational dynamics of spin-labeled myosin regulatory light chain induced by relaxation and contraction of scallop muscle. Biochemistry. 37:1998;14428-14436.
    • (1998) Biochemistry , vol.37 , pp. 14428-14436
    • Roopnarine, O.1    Szent-Györgyi, A.G.2    Thomas, D.D.3
  • 68
    • 0032976537 scopus 로고    scopus 로고
    • Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers
    • Tsaturyan A.K., Bershitsky S.Y., Burns R., Ferenczi M.A. Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibers. Biophys J. 77:1999;354-372.
    • (1999) Biophys J , vol.77 , pp. 354-372
    • Tsaturyan, A.K.1    Bershitsky, S.Y.2    Burns, R.3    Ferenczi, M.A.4
  • 69
    • 0033582235 scopus 로고    scopus 로고
    • Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: Evidence that the start of the crossbridge power stroke in muscle has variable geometry
    • A combination of stopped-flow fluorescence and time-resolved electron microscopy is used in this study. A disordered transient intermediate after the stochastical collision complex between actin and myosin and before the stable, bound complex is identified. The authors conclude that a transition from disordered to ordered binding is likely to be part of force generation
    • Walker M., Zhang X.Z., Jiang W., Trinick J., White H.D. Observation of transient disorder during myosin subfragment-1 binding to actin by stopped-flow fluorescence and millisecond time resolution electron cryomicroscopy: evidence that the start of the crossbridge power stroke in muscle has variable geometry. Proc Natl Acad Sci USA. 96:1999;465-470. A combination of stopped-flow fluorescence and time-resolved electron microscopy is used in this study. A disordered transient intermediate after the stochastical collision complex between actin and myosin and before the stable, bound complex is identified. The authors conclude that a transition from disordered to ordered binding is likely to be part of force generation.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 465-470
    • Walker, M.1    Zhang, X.Z.2    Jiang, W.3    Trinick, J.4    White, H.D.5
  • 70
    • 0032493437 scopus 로고    scopus 로고
    • Myosin conformational states determined by single fluorophore polarization
    • Single molecule fluorescence polarization data indicate that the myosin light-chain domain adopts at least two states during the cyclic interaction of myosin with actin. One state is randomly disordered, the other one is ordered
    • Warshaw D.M., Hayes E., Gaffney D., Lauzon A.M., Wu J., Kennedy G., Trybus K., Lowey S., Berger C. Myosin conformational states determined by single fluorophore polarization. Proc Natl Acad Sci USA. 95:1998;8034-8039. Single molecule fluorescence polarization data indicate that the myosin light-chain domain adopts at least two states during the cyclic interaction of myosin with actin. One state is randomly disordered, the other one is ordered.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 8034-8039
    • Warshaw, D.M.1    Hayes, E.2    Gaffney, D.3    Lauzon, A.M.4    Wu, J.5    Kennedy, G.6    Trybus, K.7    Lowey, S.8    Berger, C.9
  • 71
    • 0030724661 scopus 로고    scopus 로고
    • Tomographic three-dimensional reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol
    • Schmitz H., Reedy M.C., Reedy M.K., Tregear R.T., Taylor K.A. Tomographic three-dimensional reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol. J Cell Biol. 139:1997;695-707.
    • (1997) J Cell Biol , vol.139 , pp. 695-707
    • Schmitz, H.1    Reedy, M.C.2    Reedy, M.K.3    Tregear, R.T.4    Taylor, K.A.5
  • 72
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz M., Popp D., Holmes K.C. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J Mol Biol. 234:1993;826-836.
    • (1993) J Mol Biol , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 75
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • Milligan R.A. Protein-protein interactions in the rigor actomyosin complex. Proc Natl Acad Sci USA. 93:1996;21-26.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 76
    • 0032489923 scopus 로고    scopus 로고
    • Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments
    • Jontes J.D., Ostap E.M., Pollard T.D., Milligan R.A. Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments. J Cell Biol. 141:1998;155-162.
    • (1998) J Cell Biol , vol.141 , pp. 155-162
    • Jontes, J.D.1    Ostap, E.M.2    Pollard, T.D.3    Milligan, R.A.4
  • 77
    • 0031581885 scopus 로고    scopus 로고
    • Three-dimensional structure of Brush Border Myosin-I at approximately 20 Å resolution by electron microscopy and image analysis
    • Jontes J.D., Milligan R.A. Three-dimensional structure of Brush Border Myosin-I at approximately 20 Å resolution by electron microscopy and image analysis. J Mol Biol. 266:1997;331-342.
    • (1997) J Mol Biol , vol.266 , pp. 331-342
    • Jontes, J.D.1    Milligan, R.A.2
  • 78
    • 0029991890 scopus 로고    scopus 로고
    • Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
    • Wirth J.A., Jensen K.A., Post P.L., Bement W.M., Mooseker M.S. Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. J Cell Sci. 109:1996;653-661.
    • (1996) J Cell Sci , vol.109 , pp. 653-661
    • Wirth, J.A.1    Jensen, K.A.2    Post, P.L.3    Bement, W.M.4    Mooseker, M.S.5
  • 79
    • 0029561337 scopus 로고
    • Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin
    • Rovner A.S., Freyzon Y., Trybus K.M. Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin. J Biol Chem. 270:1995;30260-30263.
    • (1995) J Biol Chem , vol.270 , pp. 30260-30263
    • Rovner, A.S.1    Freyzon, Y.2    Trybus, K.M.3
  • 80
    • 0028354078 scopus 로고
    • Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin
    • Uyeda T.Q., Ruppel K.M., Spudich J.A. Enzymatic activities correlate with chimaeric substitutions at the actin-binding face of myosin. Nature. 368:1994;567-569.
    • (1994) Nature , vol.368 , pp. 567-569
    • Uyeda, T.Q.1    Ruppel, K.M.2    Spudich, J.A.3
  • 81
    • 0033596962 scopus 로고    scopus 로고
    • The sequence of the myosin 50-20K loop affects myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity
    • Murphy C.T., Spudich J.A. The sequence of the myosin 50-20K loop affects myosin's affinity for actin throughout the actin-myosin ATPase cycle and its maximum ATPase activity. Biochemistry. 38:1999;3785-3792.
    • (1999) Biochemistry , vol.38 , pp. 3785-3792
    • Murphy, C.T.1    Spudich, J.A.2
  • 82
    • 0033575216 scopus 로고    scopus 로고
    • Disturbed communication between actin- And nucleotide-binding sites in a myosin II with truncated 50/20-kDa junction
    • Knetsch M.L., Uyeda T.Q., Manstein D.J. Disturbed communication between actin- and nucleotide-binding sites in a myosin II with truncated 50/20-kDa junction. J Biol Chem. 274:1999;20133-20138.
    • (1999) J Biol Chem , vol.274 , pp. 20133-20138
    • Knetsch, M.L.1    Uyeda, T.Q.2    Manstein, D.J.3
  • 83
    • 0032485859 scopus 로고    scopus 로고
    • Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain
    • Furch M., Geeves M.A., Manstein D.J. Modulation of actin affinity and actomyosin adenosine triphosphatase by charge changes in the myosin motor domain. Biochemistry. 37:1998;6317-6326.
    • (1998) Biochemistry , vol.37 , pp. 6317-6326
    • Furch, M.1    Geeves, M.A.2    Manstein, D.J.3
  • 84
    • 0032561361 scopus 로고    scopus 로고
    • A long, weakly charged actin-binding loop is required for phosphorylation-dependent regulation of smooth muscle myosin
    • Rovner A.S. A long, weakly charged actin-binding loop is required for phosphorylation-dependent regulation of smooth muscle myosin. J Biol Chem. 273:1998;27939-27944.
    • (1998) J Biol Chem , vol.273 , pp. 27939-27944
    • Rovner, A.S.1
  • 86
    • 0033604852 scopus 로고    scopus 로고
    • Nonspecific weak actomyosin interactions: Relocation of charged residues in subdomain 1 of actin does not alter actomyosin function
    • Relocation of charged residues in actin reveals that only the overall charge in subdomain 1 of actin is important for actomyosin function. The exact distribution of the charges does not seem to influence the function of the complex. This suggests that these charged residues are involved in nonspecific interactions with myosin
    • Wong W.W., Doyle T.C., Reisler E. Nonspecific weak actomyosin interactions: relocation of charged residues in subdomain 1 of actin does not alter actomyosin function. Biochemistry. 38:1999;1365-1370. Relocation of charged residues in actin reveals that only the overall charge in subdomain 1 of actin is important for actomyosin function. The exact distribution of the charges does not seem to influence the function of the complex. This suggests that these charged residues are involved in nonspecific interactions with myosin.
    • (1999) Biochemistry , vol.38 , pp. 1365-1370
    • Wong, W.W.1    Doyle, T.C.2    Reisler, E.3
  • 87
    • 0032006681 scopus 로고    scopus 로고
    • The role of cytoskeletal proteins in cardiomyopathies
    • Towbin J.A. The role of cytoskeletal proteins in cardiomyopathies. Curr Opin Cell Biol. 10:1998;131-139.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 131-139
    • Towbin, J.A.1
  • 88
    • 0029024879 scopus 로고
    • Structural interpretation of the mutations in the β-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy
    • Rayment I., Holden H.M., Sellers J.R., Fananapazir L., Epstein N.D. Structural interpretation of the mutations in the β-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy. Proc Natl Acad Sci USA. 92:1995;3864-3868.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3864-3868
    • Rayment, I.1    Holden, H.M.2    Sellers, J.R.3    Fananapazir, L.4    Epstein, N.D.5
  • 89
    • 0031466513 scopus 로고    scopus 로고
    • Interaction of F-actin with synthetic peptides spanning the loop region of human cardiac β-myosin heavy chain containing Arg403
    • Bartegi A., Roustan C., Chavanieu A., Kassab R., Fattoum A. Interaction of F-actin with synthetic peptides spanning the loop region of human cardiac β-myosin heavy chain containing Arg403. Eur J Biochem. 250:1997;484-491.
    • (1997) Eur J Biochem , vol.250 , pp. 484-491
    • Bartegi, A.1    Roustan, C.2    Chavanieu, A.3    Kassab, R.4    Fattoum, A.5
  • 90
    • 0030832286 scopus 로고    scopus 로고
    • The structure of the acto-myosin subfragment 1 complex: Results of searches using data from electron microscopy and X-ray crystallography
    • Mendelson R., Morris E.P. The structure of the acto-myosin subfragment 1 complex: results of searches using data from electron microscopy and X-ray crystallography. Proc Natl Acad Sci USA. 94:1997;8533-8538.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8533-8538
    • Mendelson, R.1    Morris, E.P.2
  • 91
    • 0033517856 scopus 로고    scopus 로고
    • Intrinsic tryptophan fluorescence identifies specific conformational changes at the actomyosin interface upon actin binding and ADP-release
    • This study used intrinsic tryptophan fluorescence to analyze the dynamics of the tentative actomyosin interface upon ADP release. The study indicates that one portion of myosin remains tightly bound to actin while another adopts a more flexible and solvent exposed conformation upon ADP release
    • Yengo C.M., Chrin L., Rovner A.S., Berger C.L. Intrinsic tryptophan fluorescence identifies specific conformational changes at the actomyosin interface upon actin binding and ADP-release. Biochemistry. 38:1999;14515-14523. This study used intrinsic tryptophan fluorescence to analyze the dynamics of the tentative actomyosin interface upon ADP release. The study indicates that one portion of myosin remains tightly bound to actin while another adopts a more flexible and solvent exposed conformation upon ADP release.
    • (1999) Biochemistry , vol.38 , pp. 14515-14523
    • Yengo, C.M.1    Chrin, L.2    Rovner, A.S.3    Berger, C.L.4
  • 92
    • 0032573061 scopus 로고    scopus 로고
    • Smooth muscle myosin mutants containing a single tryptophan reveal molecular interactions at the actin-binding interface
    • Yengo C.M., Fagnant P.M., Chrin L., Rovner A.S., Berger C.L. Smooth muscle myosin mutants containing a single tryptophan reveal molecular interactions at the actin-binding interface. Proc Natl Acad Sci USA. 95:1998;12944-12949.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12944-12949
    • Yengo, C.M.1    Fagnant, P.M.2    Chrin, L.3    Rovner, A.S.4    Berger, C.L.5
  • 93
    • 0033554387 scopus 로고    scopus 로고
    • Detection of nucleotide- And F-actin-induced movements in the switch II helix of the skeletal myosin using its differential oxidative cleavage mediated by an iron-EDTA complex disulfide-linked to the strong actin binding site
    • Bertrand R., Capony J.P., Derancourt J., Kassab R. Detection of nucleotide- and F-actin-induced movements in the switch II helix of the skeletal myosin using its differential oxidative cleavage mediated by an iron-EDTA complex disulfide-linked to the strong actin binding site. Biochemistry. 38:1999;11914-11925.
    • (1999) Biochemistry , vol.38 , pp. 11914-11925
    • Bertrand, R.1    Capony, J.P.2    Derancourt, J.3    Kassab, R.4
  • 94
    • 0033565250 scopus 로고    scopus 로고
    • Actin and nucleotide induced conformational changes in the vicinity of Lys553 in myosin subfragment 1
    • Peyser Y.M., Muhlrad A. Actin and nucleotide induced conformational changes in the vicinity of Lys553 in myosin subfragment 1. Eur J Biochem. 263:1999;511-517.
    • (1999) Eur J Biochem , vol.263 , pp. 511-517
    • Peyser, Y.M.1    Muhlrad, A.2
  • 95
    • 0033020415 scopus 로고    scopus 로고
    • Interaction of 75-106 actin peptide with myosin subfragment-1 and its trypsin modified derivative
    • Labbe J.P., Chamayou S., Benyamin Y. Interaction of 75-106 actin peptide with myosin subfragment-1 and its trypsin modified derivative. Biochim Biophys Acta. 1427:1999;105-111.
    • (1999) Biochim Biophys Acta , vol.1427 , pp. 105-111
    • Labbe, J.P.1    Chamayou, S.2    Benyamin, Y.3
  • 96
    • 0033214659 scopus 로고    scopus 로고
    • Actin residue glu(93) is identified as an amino acid affecting myosin binding
    • Razzaq A., Schmitz S., Veigel C., Molloy J.E., Geeves M.A., Sparrow J.C. Actin residue glu(93) is identified as an amino acid affecting myosin binding. J Biol Chem. 274:1999;28321-28328.
    • (1999) J Biol Chem , vol.274 , pp. 28321-28328
    • Razzaq, A.1    Schmitz, S.2    Veigel, C.3    Molloy, J.E.4    Geeves, M.A.5    Sparrow, J.C.6
  • 97
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
    • Esnouf R. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J Mol Graph. 15:1997;132-134.
    • (1997) J Mol Graph , vol.15 , pp. 132-134
    • Esnouf, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.