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0032005265
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Myosins: Matching functions with motors
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Baker J.P., Titus M.A. Myosins: matching functions with motors. Curr Opin Cell Biol. 10:1998;80-86.
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Curr Opin Cell Biol
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Baker, J.P.1
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0032559349
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Unconventional myosins in cell movement, membrane traffic, and signal transduction
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Mermall V., Rost P.L., Mooseker M.S. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 279:1998;527-533.
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Mermall, V.1
Rost, P.L.2
Mooseker, M.S.3
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0033590558
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Direct interaction of microtubule- And actin-based transport motors
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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
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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.
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(1999)
Nature
, vol.397
, pp. 267-270
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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
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4
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0033566091
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The cloning and developmental expression of unconventional myosin IXA (MYO9A) a gene in the Bardet-Biedl syndrome (BBS4) region at chromosome 15q22-q23
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Gorman S.W., Haider N.B., Grieshammer U., Swiderski R.E., Kim E., Welch J.W., Searby C., Leng S., Carmi R., Sheffield V.C., Duhl D.M. The cloning and developmental expression of unconventional myosin IXA (MYO9A) a gene in the Bardet-Biedl syndrome (BBS4) region at chromosome 15q22-q23. Genomics. 59:1999;150-160.
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Genomics
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Gorman, S.W.1
Haider, N.B.2
Grieshammer, U.3
Swiderski, R.E.4
Kim, E.5
Welch, J.W.6
Searby, C.7
Leng, S.8
Carmi, R.9
Sheffield, V.C.10
Duhl, D.M.11
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5
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0032912744
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Twelve novel myosin VIIA mutations in 34 patients with Usher syndrome type I: Confirmation of genetic heterogeneity
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Janecke A.R., Meins M., Sadeghi M., Grundmann K., Apfelstedt-Sylla E., Zrenner E., Rosenberg T., Gal A. Twelve novel myosin VIIA mutations in 34 patients with Usher syndrome type I: confirmation of genetic heterogeneity. Hum Mutat. 13:1999;133-140.
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Hum Mutat
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Janecke, A.R.1
Meins, M.2
Sadeghi, M.3
Grundmann, K.4
Apfelstedt-Sylla, E.5
Zrenner, E.6
Rosenberg, T.7
Gal, A.8
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6
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0032942542
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Myosin IB from Entamoeba histolytica is involved in phagocytosis of human erythrocytes
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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.
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J Cell Sci
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Voigt, H.1
Olivo, J.2
Sansonetti, P.3
Guillen, N.4
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7
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0030592549
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Fifty ways to love your lever: Myosin motors
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Block S.M. Fifty ways to love your lever: myosin motors. Cell. 87:1996;151-157.
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, vol.87
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Block, S.M.1
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8
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0032478543
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Wag the tail: Structural dynamics of actomyosin
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Goldman Y.E. Wag the tail: structural dynamics of actomyosin. Cell. 93:1998;1-4.
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Cell
, vol.93
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Goldman, Y.E.1
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18144434716
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Lever arm model of force generation by actin-myosin-ATP
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Highsmith S. Lever arm model of force generation by actin-myosin-ATP. Biochemistry. 38:1999;9791-9797.
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Biochemistry
, vol.38
, pp. 9791-9797
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Highsmith, S.1
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0033600904
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Kinetic characterization of a monomeric unconventional myosin V construct
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Trybus K.M., Krementsova E., Freyzon Y. Kinetic characterization of a monomeric unconventional myosin V construct. J Biol Chem. 274:1999;27448-27456.
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J Biol Chem
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Trybus, K.M.1
Krementsova, E.2
Freyzon, Y.3
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12
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0033615015
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Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction
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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
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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.
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(1999)
Nature
, vol.400
, pp. 425-430
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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
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13
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0032848772
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Intradomain distances in the regulatory domain of the myosin head in prepower and postpower stroke states: Fluorescence energy transfer
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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.
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(1999)
Biochemistry
, vol.38
, pp. 13026-13034
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Palm, T.1
Sale, K.2
Brown, L.3
Li, H.4
Hambly, B.5
Fajer, P.G.6
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14
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0032569898
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Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps
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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
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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.
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(1998)
Nature
, vol.396
, pp. 380-383
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Suzuki, Y.1
Yasunaga, T.2
Ohkura, R.3
Wakabayashi, T.4
Sutoh, K.5
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15
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0032539847
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A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction
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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
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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.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 2944-2949
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Baker, J.E.1
Brust-Mascher, I.2
Ramachandran, S.3
Laconte, L.E.4
Thomas, D.D.5
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16
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0032433333
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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
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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.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 15309-15314
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Xiao, M.1
Li, H.2
Snyder, G.E.3
Cooke, R.4
Yount, R.G.5
Selvin, P.R.6
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17
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0032474429
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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
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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.
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(1998)
Biochemistry
, vol.37
, pp. 8035-8047
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Burghardt, T.P.1
Garamszegi, S.P.2
Park, S.3
Ajtai, K.4
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18
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0033580652
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Trinitrophenylated reactive lysine residue in myosin detects lever arm movement during the consecutive steps of ATP hydrolysis
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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.
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(1999)
Biochemistry
, vol.38
, pp. 6428-6440
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Ajtai, K.1
Peyser, Y.M.2
Park, S.3
Burghardt, T.P.4
Muhlrad, A.5
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19
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0029176506
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A 35-Å movement of smooth muscle myosin on ADP release
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Whittaker M., Wilson-Kubalek E.M., Smith J.E., Faust L., Milligan R.A., Sweeney H.L. A 35-Å movement of smooth muscle myosin on ADP release. Nature. 378:1995;748-751.
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(1995)
Nature
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Whittaker, M.1
Wilson-Kubalek, E.M.2
Smith, J.E.3
Faust, L.4
Milligan, R.A.5
Sweeney, H.L.6
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20
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0030692707
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Brush border myosin-I structure and ADP-dependent conformational changes revealed by cryoelectron microscopy and image analysis
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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.
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(1997)
J Cell Biol
, vol.139
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Jontes, J.D.1
Milligan, R.A.2
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21
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0032442461
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Structural invariance of constitutively active and inactive mutants of Acanthamoeba myosin IC bound to F-actin in the rigor and ADP-bound states
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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
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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.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 15206-15211
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-
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
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22
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0029774205
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Fluorescence polarization of skeletal muscle fibers labeled with rhodamine isomers on the myosin heavy chain
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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.
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Berger, C.L.1
Craik, J.S.2
Trentham, D.R.3
Corrie, J.E.4
Goldman, Y.E.5
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23
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0030928755
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Probes bound to myosin Cys-707 rotate during length transients in contraction
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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.
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Proc Natl Acad Sci USA
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Burghardt, T.P.1
Garamszegi, S.P.2
Ajtai, K.3
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24
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0033619258
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Myosin VI is an actin-based motor that moves backwards
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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)
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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).
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(1999)
Nature
, vol.401
, pp. 505-508
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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
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25
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0029159959
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X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADP.BeFx and MgADP.AlF4-
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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.
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Biochemistry
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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
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26
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0032483563
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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
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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
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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.
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(1998)
Cell
, vol.94
, pp. 559-571
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Dominguez, R.1
Freyzon, Y.2
Trybus, K.M.3
Cohen, C.4
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27
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0029913456
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The neck region of the myosin motor domain acts as a lever arm to generate movement
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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.
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Proc Natl Acad Sci USA
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Uyeda, T.Q.1
Abramson, P.D.2
Spudich, J.A.3
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28
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0027194702
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Three-dimensional structure of myosin subfragment-1: A molecular motor
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Rayment I., Rypniewski W.R., Schmidt-Base K., Smith R., Tomchick D.R., Benning M.M., Winkelmann D.A., Wesenberg G., Holden H.M. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science. 261:1993;50-58.
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Science
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Rayment, I.1
Rypniewski, W.R.2
Schmidt-Base, K.3
Smith, R.4
Tomchick, D.R.5
Benning, M.M.6
Winkelmann, D.A.7
Wesenberg, G.8
Holden, H.M.9
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29
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0029960235
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X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 Å resolution
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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.
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Biochemistry
, vol.35
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Smith, C.A.1
Rayment, I.2
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30
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0030768794
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X-ray structures of the MgADP, MgATPγS, and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain
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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.
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Biochemistry
, vol.36
, pp. 11619-11628
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Gulick, A.M.1
Bauer, C.B.2
Thoden, J.B.3
Rayment, I.4
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31
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0018868611
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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
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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.
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Biochemistry
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Yount, R.G.2
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32
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0032564445
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Probing the conformational states of the SH1 SH2 helix in myosin: A cross-linking approach
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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
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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.
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(1998)
Biochemistry
, vol.37
, pp. 16704-16710
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Nitao, L.K.1
Reisler, E.2
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33
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0033543224
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: 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
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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.
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(1999)
Biochemistry
, vol.38
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Kliche, W.1
Pfannstiel, J.2
Tiepold, M.3
Stoeva, S.4
Faulstich, H.5
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34
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1642340974
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Atomic structure of scallop myosin subfragment S1 complexed with MgADP: A novel conformation of the myosin head
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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
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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.
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(1999)
Cell
, vol.97
, pp. 459-470
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Houdusse, A.1
Kalabokis, V.N.2
Himmel, D.3
Szent-Györgyi, A.G.4
Cohen, C.5
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35
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0033545955
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Kinetic analysis of Dictyostelium discoideum myosin motor domains with glycine-to-alanine mutations in the reactive thiol region
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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.
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(1999)
Biochemistry
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Batra, R.1
Geeves, M.A.2
Manstein, D.J.3
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36
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0032867566
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Dictyostelium myosin II G680V suppressors exhibit overlapping spectra of biochemical phenotypes including facilitated phosphate release
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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
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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.
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(1999)
Genetics
, vol.153
, pp. 107-116
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Wu, Y.1
Nejad, M.2
Patterson, B.3
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37
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0010299503
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