spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Summary Freely available
Right arrow Full Text (PDF)
Right arrow Movies
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Reedy, M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Reedy, M. C.
Adhikari, B., Hideg, K. and Fajer, P. G (1997). Independent mobility of catalytic and regulatory domains of myosin heads. Proc. Nat. Acad. Sci. USA 94, 9643-9647.[Abstract/Free Full Text]

Allen, T. S., Sabido-David, C., Ling, N., Irving, M. and Goldman, Y. E (1995). Transients of fluorescence polarization in skeletal muscle fibers labeled with rhodamine on the regulatory light chain. Biophys. J 68, 81-.[Abstract/Free Full Text]

Baker, J. E., Brust-Mascher, I., Ramachandran, S., LaConte, L. E. and Thomas, D. D (1998). A large and distinct rotation of the myosin light chain domain occurs upon muscle contraction [see comments]. Proc. Nat. Acad. Sci. USA 95, 2944-2949.[Abstract/Free Full Text]

Berger, C. L., Craik, J. S., Trentham, D. R., Corrie, J. E. and Goldman, Y. E (1996). Fluorescence polarization of skeletal muscle fibers labeled with rhodamine isomers on the myosin heavy chain. Biophys. J 71, 3330-3343.[Abstract/Free Full Text]

Bershitsky, S., Tsaturyan, A., Bershitskaya, O., Mashanov, G., Brown, P., Burns, R. and Ferenczi, M (1997). Muscle force is generated by myosin heads stereospecifically atttached to actin. Nature 388, 186-190.[Medline]

Block, S. M (1996). Fifty ways to love your lever: Myosin motors. Cell 87, 151-157.[Medline]

Bobkova, E. A., Bobkov, A. A., Levitsky, D. I. and Reisler, E (1999). Effects of SH1 and SH2 modifications on myosin: similarities and differences. Biophys. J 76, 1001-1007.[Abstract/Free Full Text]

Cooke, R (1997). Actomyosin interaction in striated muscle. Physiol. Rev 77, 671-697.[Abstract/Free Full Text]

Corrie, J. E., Brandmeier, B. D., Ferguson, R. E., Trentham, D. R., Kendrick-Jones, J., Hopkins, S. C., van der Heide, U. A., Goldman, Y. E., Sabido-David, C., Dale, R. E., Criddle, S. and Irving, M (1999). Dynamic measurement of myosin light chain domain tilt and twist in musle contraction. Nature 400, 425-430.[Medline]

Dantzig, J. A., Barsotti, R. J., Manz, S., Sweeney, H. L. and Goldman, Y. E (1999). The ADP release step of the smooth muscle cross-bridge cycle is not directly associated with force generation. Biophys. J 77, 386-397.[Abstract/Free Full Text]

De La Cruz, E. M., Wells, A. L., Rosenfeld, S. S., Ostap, E. M. and Sweeney, H. L (1999). The kinetic mechanism of myosin V. Proc. Nat. Acad. Sci. USA 96, 13726-13731.[Abstract/Free Full Text]

Dobbie, I., Linari, M., Piazzesi, G., Reconditi, M., Koubassova, N., Ferenczi, M. A., Lombardi, V. and Irving, M (1998). Elastic bending and active tilting of myosin heads during muscle contraction [see comments]. Nature 396, 383-387.[Medline]

Dominguez, R., Freyzon, Y., Trybus, K. M. and Cohen, C (1998). 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, 559-571.[Medline]

Duke, T (2000). Cooperativity of myosin molecules through strain-dependent chemistry. Phil. Trans. Roy Soc. Lond. B Biol. Sci 355, 529-538.[Medline]

Fisher, A. J., Smith, C. A., Thoden, J., Smith, R., Sutoh, K., Holden, H. M. and Rayment, I (1995). Structural studies of myosin:nucleotide complexes: A revised model for the molecular basis of muscle contraction. Biophys. J 68, 19-.

Fisher, A. J., Smith, C. A., Thoden, J. B., Smith, R., Sutoh, K., Holden, H. M. and Rayment, I (1995). X-ray structures of the myosin motor domain of Dictyostelium discoideum complexed with MgADPBeF x and MgADPAlF4. Biochemistry 34, 8960-8972.[Medline]

Geeves, M. A. and Holmes, K. C (1999). Structural mechanism of muscle contraction. Annu. Rev. Biochem 68, 687-728.[Medline]

Goldman, Y. E (1998). Wag the tail: structural dynamics of actomyosin. Cell 93, 1-4.[Medline]

Gollub, J., Cremo, C. R. and Cooke, R (1996). ADP release produces a rotation of the neck region of smooth myosin but not skeletal myosin. Nature Struct. Biol 3, 796-802.[Medline]

Gulick, A. M., Bauer, C. B., Thoden, J. B. and Rayment, I (1997). X-ray structures of the MgADP, MgATPgammaS and MgAMPPNP complexes of the Dictyostelium discoideum myosin motor domain. Biochemistry 36, 11619-11628.[Medline]

Highsmith, S (1999). Lever arm model of force generation by actin-myosin-ATP. Biochemistry 38, 9791-9797.[Medline]

Hirose, K. and Wakabayashi, T (1993). Structural change of crossbridges of rabbit skeletal muscle during isometric contraction. J. Muscle Res. Cell Motil 14, 432-445.[Medline]

Hirose, K., Franzini-Armstrong, C., Goldman, Y. E. and Murray, J. M (1994). Structural changes in muscle crossbridges accompanying force generation. J. Cell Biol 127, 763-778.[Abstract/Free Full Text]

Holmes, K. C., Tregear, R. T. and Barrington Leigh, J (1980). Interpretation of the low angle X-ray diffraction from insect muscle in rigor. Proc. Royal Soc. Lond. B Biol 207, 13-33.

Holmes, K. C. and Goody, R. S (1984). The nature of the actin cross-bridge interaction. Advan. Exp. Med. Biol 170, 373-384.[Medline]

Holmes, K. C., Popp, D., Gebhard, W. and Kabsch, W (1990). Atomic model of the actin filament. Nature 347, 44-49.[Medline]

Holmes, K. C (1996). Muscle proteins\320their actions and interactions. Curr. Opin. Struct. Biol 6, 781-789.[Medline]

Holmes, K. C (1997). The swinging lever-arm hypothesis of muscle contraction. Curr. Biol 7, 112-118.[Medline]

Holmes, K. C. ad Geeves, M. A (2000). The structural basis of muscle contraction. Phil. Trans. Roy Soc. Lond. B Biol 355, 419-431.[Medline]

Hopkins, S. C., Sabido-David, C., Corrie, J. E., Irving, M. and Goldman, Y. E (1998). Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers. Biophys. J 74, 3093-3110.[Abstract/Free Full Text]

Houdusse, A. and Cohen, C (1996). Structure of the regulatory domain of scallop myosin at 2 \201 resolution: Implications for regulation. Structure 4, 21-32.[Medline]

Houdusse, A., Kalabokis, V. N., Himmel, D., Szent-Gyorgyi, A. G. and Cohen, C (1999). Atomic structure of scallop myosin subfragment S1 complexed with MgADP: a novel conformation of the myosin head [In Process Citation]. Cell 97, 459-470.[Medline]

Huxley, A. F. and Niedergerke, R (1954). Structural changes in muscle during contraction. Nature 173, 971-973.[Medline]

Huxley, A. F. and Simmons, R. M (1971). Proposed mechanism of force generation in striated muscle. Nature 233, 533-538.[Medline]

Huxley, A. F (1974). Muscular contraction. J. Physiol 243, 1-43.

Huxley, H. E. and Hanson, J (1954). Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 173, 973-976.[Medline]

Huxley, H. E (1969). The mechanism of muscular contraction. Science 164, 1356-1366.[Free Full Text]

Huxley, H. E. and Kress, M (1985). Crossbridge behaviour during muscle contraction. J. Muscle Res. Cell Motil 6, 153-161.[Medline]

Huxley, H. E (1990). Sliding filaments and molecular motile systems. J. Biol. Chem 265, 8347-8350.[Free Full Text]

Irving, M., St Claire Allen, T., Sabido-David, C., Craik, J. S., Brandmeier, B., Kendrick-Jones, J., Corrie, J. E. T., Trentham, D. R. and Goldman, Y. E (1995). Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle. Nature 375, 688-691.[Medline]

Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F. and Holmes, K. C (1990). Atomic structure of the actin: DNase I complex. Nature 347, 37-44.[Medline]

Kurzawa-Goertz, S. E., Perreault-Micale, C. L., Trybus, K. M., Szent-Gyorgyi, A. G. and Geeves, M. A (1998). Loop I can modulate ADP affinity, ATPase activity and motility of different scallop myosins. Transient kinetic analysis of S1 isoforms. Biochemistry 37, 7517-7525.[Medline]

Lenart, T. D., Murray, J. M., Franzini-Armstrong, C. and Goldman, Y. E (1996). Structure and periodicities of crossbridges in relaxation and during contraction initiated by photolysis of caged calcium. Biophys. J 71, 2289-2306.[Abstract/Free Full Text]

Lombardi, V., Piazzesi, G., Ferenczi, M. A., Thirlwell, H., Dobbie, I. and Irving, M (1995). Elastic distortion of myosin heads and repriming of the working stroke in muscle. Nature 374, 553-555.[Medline]

Molloy, J. E., Burns, J. E., Kendrick-Jones, J., Tregear, R. T. and White, D. C (1995). Movement and force produced by a single myosin head [see comments]. Nature 378, 209-212.[Medline]

Nitao, L. K. and Reisler, E (1998). Probing the conformational states of the SH1-SH2 helix in myosin: a cross-linking approach. Biochemistry 37, 16704-16710.[Medline]

Piazzesi, G., Koubassova, N., Irving, M. and Lombardi, V (1998). On the working stroke elicited by steps in length and temperature. Advan. Exp. Med. Biol 453, 259-263.[Medline]

Piazzesi, G., Reconditi, M., Dobbie, I., Linari, M., Boesecke, P., Diat, O., Irving, M. and Lombardi, V (1999). Changes in conformation of myosin heads during the development of isometric contraction and rapid shortening in single frog muscle fibres. J. Physiol. (Lond) 514, 305-312.[Abstract/Free Full Text]

Rayment, I., Holden, H. M., Whittaker, M., Yohn, C. B., Lorenz, M.,Holmes, K. C. and Milligan, R. A (1993). Structure of the actin-myosin complex and its implications for muscle contraction. Science 261, 58-65.[Abstract/Free Full Text]

Rayment, I., Rypniewsky, W. R., Schmidt-B\212se, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G. and Holden, H. M (1993). Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261, 50-58.[Abstract/Free Full Text]

Reedy, M. K., Holmes, K. C. and Tregear, R. T (1965). Induced changes in orientation of the cross-bridges of glycerinated insect flight muscle. Nature 207, 1276-1280.[Medline]

Rovner, A. S., Freyzon, Y. and Trybus, K. M (1995). Chimeric substitutions of the actin-binding loop activate dephosphorylated but not phosphorylated smooth muscle heavy meromyosin. J. Biol. Chem 270, 30260-30263.[Abstract/Free Full Text]

Sabido-David, C., Brandmeier, B., Craik, J. S., Corrie, J. E., Trentham, D. R. and Irving, M (1998). Steady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethylrhodamine. Biophys. J 74, 3083-3092.[Abstract/Free Full Text]

Schmitz, H., Reedy, M. C., Reedy, M. K., Tregear, R. T., Winkler, H. and Taylor, K. A (1996). Electron tomography of insect flight muscle in rigor and AMPPNP at 23C. J. Mol. Biol 264, 279-301.[Medline]

Schmitz, H., Reedy, M. C., Reedy, M. K., Tregear, R. T. and Taylor, K. A (1997). Tomographic three-dimensional reconstruction of insect flight muscle partially relaxed by AMPPNP and ethylene glycol. J. Cell Biol 139, 695-707.[Abstract/Free Full Text]

Sheetz, M. P. and Spudich, J. A (1983). Movement of myosin-coated fluorescent beads on actin cables in vitro. Nature 303, 31-35.[Medline]

Smith, C. A., Fisher, A. J., Smith, R., Sutoh, K. and Rayment, I (1995). The structure of the ATP-bound state of myosin. J. Muscle Res. Cell Motil 16, 145-.

Smith, C. A. and Rayment, I (1996). X-ray structure of the magnesium(II). ADP. vanadate complex of the Dictyostelium discoideum myosin motor domain to 1. 9 \201 resolution. Biochemistry 35, 5404-5417.[Medline]

Spudich, J. A., Finer, J., Simmons, B., Ruppel, K., Patterson, B. and Uyeda, T (1995). Myosin structure and function. Cold Spring Harbor Symp. Quant. Biol 60, 783-791.[Medline]

Sweeney, H. L., Rosenfeld, S. S., Brown, F., Faust, L., Smith, J., Xing, J., Stein, L. A. and Sellers, J. R (1998). Kinetic tuning of myosin via a flexible loop adjacent to the nucleotide binding pocket. J. Biol. Chem 273, 6262-6270.[Abstract/Free Full Text]

Taylor, K. A., Schmitz, H., Reedy, M. C., Goldman, Y. E., Franzini-Armstrong, C., Sasaki, H., Tregear, R. T., Poole, K. J. V., Lucaveche, C., Edwards, R. J., Chen, L. F., Winkler, H. and Reedy, M. K (1999). Tomographic 3-D reconstruction of quick frozen, Ca2+-activated contracting insect flight muscle. Cell 99, 421-431.[Medline]

Thomas, D. D., Ramachandran, S., Roopnarine, O., Hayden, D. W. and Ostap, E. M (1995). The mechanism of force generation in myosin: A disorder-to-order transition, coupled to internal structural changes. Biophys. J 68, 135-.

Toyoshima, Y. Y., Kron, S. J., McNally, E. M., Niebling, K. R., Toyoshima, C. and Spudich, J. A (1987). Myosin subfragment-1 is sufficient to move actin filaments in vitro. Nature 328, 536-539.[Medline]

Tregear, R. T., Wakabayashi, K., Tanaka, H., Iwamoto, H., Reedy, M. C., Reedy, M. K., Sugi, H. and Amemiya, Y (1990). X-ray diffraction and electron microscopy from Lethocerus flight muscle partially relaxed by adenylylimidodiphosphate and ethylene glycol. J. Mol. Biol 214, 129-141.[Medline]

Tregear, R. T., Edwards, R. J., Irving, T. C., Poole, K. J. V., Reedy, M. C., Schmitz, H., Towns-Andrews, E. and Reedy, M. K (1998). X-ray diffraction indicates that active crossbridges bind to actin target zones in insect flight muscle. Biophys. J 74, 1439-1451.[Abstract/Free Full Text]

Tyska, M. J., Dupuis, D. E., Guilford, W. H., Patlak, J. B., Waller, G. S.,Trybus, K. M., Warshaw, D. M. and Lowey, S (1999). Two heads of myosin are better than one for generating force and motion. Proc. Nat. Acad. Sci. USA 96, 4402-4407.[Abstract/Free Full Text]

Uyeda, T., Abramson, P. and Spudich, J (1996). The neck region of the myosin motor domain acts as a lever arm to generate movement. Proc. Nat. Acad. Sci. USA 93, 4459-4464.[Abstract/Free Full Text]

Vale, R. D. and Milligan, R. A (2000). The way things move: looking under the hood of molecular motor proteins. Science 288, 88-95.[Abstract/Free Full Text]

Veigel, C., Coluccio, L. M., Jontes, J. D., Sparrow, J. C., Milligan, R. A. and Molloy, J. E (1999). The motor protein myosin-I produces its working stroke in two steps [see comments]. Nature 398, 530-533.[Medline]

Walker, M., Burgess, S., Sellers, J., Wang, F., Hammer, J., Trinick, J. and Knight, P (2000). Two-headed binding of a processive myosin to F-actin. Nature 405, 804-807.[Medline]

Warshaw, D. M., Hayes, E., Gaffney, D., Lauzon, A. M., Wu, J., Kennedy, G., Trybus, K., Lowey, S. and Berger, C (1998). Myosin conformational states determined by single fluorophore polarization. Proc. Nat. Acad. Sci. USA 95, 8034-8039.[Abstract/Free Full Text]

Wells, A. L., Lin, A. W., Chen, L. Q., Safer, D., Cain, S. M., Hasson, T., Carragher, B. O., Milligan, R. A. and Sweeney, H. L (1999). Myosin VI is an actin-based motor that moves backwards [see comments]. Nature 401, 505-508.[Medline]

Whittaker, M., Wilson-Kubalek, E. M., Smith, J. E., Faust, L., Milligan, R. A. and Sweeney, H. L (1995). A 35-\201 movement of smooth muscle myosin on ADP release. Nature 378, 748-751.[Medline]

Yanagida, T., Kitamura, K., Tanaka, H., Iwane, A. H. and Esaki, S (2000). Single molecule analysis of the actomyosin motor. Curr. Opin. Cell Biol 12, 20-25.[Medline]

Yanagida, T., Esaki, S., Iwane, A. H., Inoue, Y., Ishijima, A., Kitamura, K., Tanaka., H. and Tokunaga, M (2000). Single-motor mechanics and models of the myosin motor. Phil. Trans Roy. Soc. Lond. B Biol 355, 441-447.[Medline]

Yount, R. G., Lawson, D. and Rayment, I (1995). Is myosin a \324back door' enzyme?. Biophys. J 68, 44-.




This article has been cited by other articles:


Home page
BloodHome page
X. Lu, J. Chen, R. Malumbres, E. Cubedo Gil, D. M. Helfman, and I. S. Lossos
HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and mediates the effects of IL-6 on cell migration
Blood, December 15, 2007; 110(13): 4268 - 4277.
[Abstract] [Full Text] [PDF]


This Article
Right arrow Summary Freely available
Right arrow Full Text (PDF)
Right arrow Movies
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Reedy, M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Reedy, M. C.