{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T07:44:40Z","timestamp":1790840680571,"version":"4.1.0"},"reference-count":156,"publisher":"MDPI AG","issue":"22","license":[{"start":{"date-parts":[[2019,11,14]],"date-time":"2019-11-14T00:00:00Z","timestamp":1573689600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Muscular contraction is a fundamental phenomenon in all animals; without it life as we know it would be impossible. The basic mechanism in muscle, including heart muscle, involves the interaction of the protein filaments myosin and actin. Motility in all cells is also partly based on similar interactions of actin filaments with non-muscle myosins. Early studies of muscle contraction have informed later studies of these cellular actin-myosin systems. In muscles, projections on the myosin filaments, the so-called myosin heads or cross-bridges, interact with the nearby actin filaments and, in a mechanism powered by ATP-hydrolysis, they move the actin filaments past them in a kind of cyclic rowing action to produce the macroscopic muscular movements of which we are all aware. In this special issue the papers and reviews address different aspects of the actin-myosin interaction in muscle as studied by a plethora of complementary techniques. The present overview provides a brief and elementary introduction to muscle structure and function and the techniques used to study it. It goes on to give more detailed descriptions of what is known about muscle components and the cross-bridge cycle using structural biology techniques, particularly protein crystallography, electron microscopy and X-ray diffraction. It then has a quick look at muscle mechanics and it summarises what can be learnt about how muscle works based on the other studies covered in the different papers in the special issue. A picture emerges of the main molecular steps involved in the force-producing process; steps that are also likely to be seen in non-muscle myosin interactions with cellular actin filaments. Finally, the remarkable advances made in studying the effects of mutations in the contractile assembly in causing specific muscle diseases, particularly those in heart muscle, are outlined and discussed.<\/jats:p>","DOI":"10.3390\/ijms20225715","type":"journal-article","created":{"date-parts":[[2019,11,14]],"date-time":"2019-11-14T10:56:34Z","timestamp":1573728994000},"page":"5715","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":91,"title":["Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview"],"prefix":"10.3390","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6656-7390","authenticated-orcid":false,"given":"John","family":"Squire","sequence":"first","affiliation":[{"name":"Muscle Contraction Group, School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol BS8 1TD, UK"},{"name":"Department of Surgery and Cancer, Faculty of Medicine, Imperial College London, London SW7 2BZ, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,11,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/S0096-4174(18)30128-8","article-title":"Muscle Structure and Theories of Contraction","volume":"7","author":"Huxley","year":"1957","journal-title":"Prog. Biophys. Biophys. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"a021931","DOI":"10.1101\/cshperspect.a021931","article-title":"Motor Proteins","volume":"10","author":"Sweeney","year":"2018","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Squire, J.M. (1981). The Structural Basis of Muscular Contraction, Plenum Publishing Co.. Now reprinted.","DOI":"10.1007\/978-1-4613-3183-4"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1038\/173973a0","article-title":"Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation","volume":"173","author":"Huxley","year":"1954","journal-title":"Nature"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1038\/173971a0","article-title":"Structural changes in muscle during contraction; interference microscopy of living muscle fibres","volume":"173","author":"Huxley","year":"1954","journal-title":"Nature"},{"key":"ref_6","first-page":"e201611","article-title":"Muscle contraction: Sliding filament history, sarcomere dynamics and the two Huxleys","volume":"2016","author":"Squire","year":"2016","journal-title":"Glob. Cardiol. Sci. Pract."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Sugi, H. (2017). Studies of Muscle Contraction Using X-ray Diffraction. Muscle Contraction and Cell Motility: Fundamentals and Developments, Pan Stanford Publishing.","DOI":"10.1201\/9781315364674"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/0022-2836(72)90390-7","article-title":"Structural basis of contraction in vertebrate smooth muscle","volume":"67","author":"Small","year":"1972","journal-title":"J. Mol. Biol."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1083\/jcb.134.1.53","article-title":"Myosin filament structure in vertebrate smooth muscle","volume":"134","author":"Xu","year":"1996","journal-title":"J. Cell Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"11","DOI":"10.4137\/BBI.S8451","article-title":"Structural and Functional Insights on the Myosin superfamily","volume":"6","author":"Syamaladevi","year":"2012","journal-title":"Bioinform. Biol. Insights"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0022-2836(69)90483-5","article-title":"Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation","volume":"42","author":"Lowey","year":"1969","journal-title":"J. Mol. Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1126\/science.8316857","article-title":"Three-dimensional structure of myosin subfragment-1: A molecular motor","volume":"261","author":"Rayment","year":"1993","journal-title":"Science"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/0022-2836(73)90337-9","article-title":"General model of myosin filament structure III: Molecular packing arrangements in myosin filaments","volume":"77","author":"Squire","year":"1973","journal-title":"J. Mol. Biol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"e1600058","DOI":"10.1126\/sciadv.1600058","article-title":"Structure of myosin filaments from relaxed Lethocerus flight muscle by cryo-EM at 6 \u00c5 resolution","volume":"2","author":"Hu","year":"2016","journal-title":"Sci. Adv."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/0022-2836(72)90074-5","article-title":"General model of myosin filament structure II: Myosin filaments and crossbridge interactions in vertebrate striated and insect flight muscles","volume":"72","author":"Squire","year":"1972","journal-title":"J. Mol. Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1242\/jcs.105.3.841","article-title":"The relaxed crossbridge pattern in isolated rabbit psoas muscle thick filaments","volume":"105","author":"Kensler","year":"1983","journal-title":"J. Cell Sci."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/0022-2836(81)90430-7","article-title":"Three-dimensional structure of the vertebrate muscle A-band III: M-region structure and myosin filament symmetry","volume":"151","author":"Luther","year":"1981","journal-title":"J. Mol. Biol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/S0022-2836(67)80046-9","article-title":"The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor","volume":"30","author":"Huxley","year":"1967","journal-title":"J. Mol. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/S0006-3495(86)83447-6","article-title":"The \u2018crystalline\u2019 myosin cross-bridge array in relaxed bony fish muscles","volume":"50","author":"Harford","year":"1986","journal-title":"Biophys. J."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1073\/pnas.1212708110","article-title":"Atomic model of the human cardiac muscle myosin filament","volume":"110","author":"Kensler","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1385","DOI":"10.1083\/jcb.147.7.1385","article-title":"Visualization of head-head interactions in the inhibited state of smooth muscle myosin","volume":"147","author":"Wendt","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Knupp, C., Morris, E., and Squire, J.M. (2019). The Interacting Head Motif Structure Does Not Explain the X-Ray Diffraction Patterns in Relaxed Vertebrate (Bony Fish) Skeletal Muscle and Insect (Lethocerus) Flight Muscle. Biology, 8.","DOI":"10.20944\/preprints201907.0255.v1"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/0022-2836(78)90405-9","article-title":"Three-dimensional structure of the vertebrate muscle M-region","volume":"125","author":"Luther","year":"1978","journal-title":"J. Mol. Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1007\/BF00121071","article-title":"M-band Structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles","volume":"15","author":"Pask","year":"1994","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Lange, S., Pinotsis, N., Agarkova, I., and Ehler, E. (2019). The M-band: The underestimated part of the sarcomere. Biochim. Biophys. Acta Mol. Cell Res., in press.","DOI":"10.1016\/j.bbamcr.2019.02.003"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/0022-2836(80)90254-5","article-title":"Three-dimensional structure of the vertebrate muscle A-band. II. The myosin filament superlattice","volume":"141","author":"Luther","year":"1980","journal-title":"J. Mol. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"846","DOI":"10.3390\/biology3040846","article-title":"The intriguing dual lattices of the myosin filaments in vertebrate striated muscles: Evolution and advantage","volume":"3","author":"Luther","year":"2014","journal-title":"Biology"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.yjmcc.2019.05.026","article-title":"Fine mapping titin\u2019s C-zone: Matching cardiac myosin-binding protein C stripes with titin\u2019s super-repeats","volume":"133","author":"Tonino","year":"2019","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1038\/335824a0","article-title":"Why animals have different muscle fibre types","volume":"335","author":"Rome","year":"1988","journal-title":"Nature"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/S0022-2836(84)80007-8","article-title":"Purification and properties of native titin","volume":"180","author":"Trinick","year":"1984","journal-title":"J. Mol. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/978-1-4419-6366-6_6","article-title":"Role of titin in skeletal muscle function and disease","volume":"682","author":"Ottenheijm","year":"2010","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1016\/0022-2836(81)90517-9","article-title":"End-filaments: A new structural element of vertebrate skeletal muscle thick filaments","volume":"151","author":"Trinick","year":"1981","journal-title":"J. Mol. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/S0022-2836(02)00819-7","article-title":"Titin organisation and the 3D architecture of the vertebrate striated muscle I-Band","volume":"322","author":"Knupp","year":"2002","journal-title":"J. Mol. Biol."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1016\/0022-2836(73)90055-7","article-title":"A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization","volume":"74","author":"Offer","year":"1973","journal-title":"J. Mol. Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"11423","DOI":"10.1073\/pnas.1103216108","article-title":"Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle","volume":"108","author":"Luther","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1085\/jgp.201812200","article-title":"Regulation of myofilament force and loaded shortening by skeletal myosin binding protein C","volume":"151","author":"Robinett","year":"2019","journal-title":"J. Gen. Physiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/347037a0","article-title":"Atomic structure of the actin:DNase I complex","volume":"347","author":"Kabsch","year":"1990","journal-title":"Nature"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1038\/347044a0","article-title":"Atomic model of the actin filament","volume":"347","author":"Holmes","year":"1990","journal-title":"Nature"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.jsb.2017.01.004","article-title":"Relaxed and active thin filament structures; a new structural basis for the regulatory mechanism","volume":"197","author":"Paul","year":"2017","journal-title":"J. Struct. Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1007\/978-3-319-49674-0_9","article-title":"Tropomyosin Structure, Function, and Interactions: A Dynamic Regulator","volume":"82","author":"Barua","year":"2017","journal-title":"Subcell. Biochem."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"2275","DOI":"10.1016\/j.bpj.2019.05.009","article-title":"The Effect of Tropomyosin Mutations on Actin-Tropomyosin Binding: In Search of Lost Time","volume":"116","author":"Lehman","year":"2019","journal-title":"Biophys. J."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"68","DOI":"10.3389\/fmolb.2019.00068","article-title":"Computational Studies of Cardiac and Skeletal Troponin","volume":"6","author":"Bowman","year":"2019","journal-title":"Front. Mol. Biosci."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/s10974-019-09526-w","article-title":"Small molecule studies: The fourth wave of muscle research","volume":"40","author":"Marston","year":"2019","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/s10974-009-9189-6","article-title":"The vertebrate muscle Z-disc: Sarcomere anchor for structure and signalling","volume":"30","author":"Luther","year":"2009","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"15534","DOI":"10.1073\/pnas.1902235116","article-title":"Three-dimensional structure of the basketweave Z-band in midshipman fish sonic muscle","volume":"116","author":"Burgoyne","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1242\/jeb.124941","article-title":"The sarcomeric cytoskeleton: From molecules to motion","volume":"219","author":"Gautel","year":"2016","journal-title":"J. Exp. Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"9897","DOI":"10.1074\/jbc.R110.174268","article-title":"Cardiac Z-disc Signaling Network","volume":"286","author":"Frank","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"D313","DOI":"10.1093\/nar\/gkw1132","article-title":"The SWISS-MODEL Repository\u2014New features and functionality","volume":"45","author":"Bienert","year":"2017","journal-title":"Nucleic Acids Res."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1007\/s12551-014-0151-5","article-title":"The role of super-relaxed myosin in skeletal and cardiac muscle","volume":"7","author":"McNamara","year":"2015","journal-title":"Biophys. Rev."},{"key":"ref_50","first-page":"E1991","article-title":"Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals","volume":"115","author":"Lee","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1038\/nature03920","article-title":"Atomic model of a myosin filament in the relaxed state","volume":"436","author":"Woodhead","year":"2005","journal-title":"Nature"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"2386","DOI":"10.1073\/pnas.0708912105","article-title":"Three-dimensional structure of vertebrate cardiac muscle myosin filaments","volume":"105","author":"Zoghbi","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.jsb.2008.03.011","article-title":"Myosin filament 3D structure in mammalian cardiac muscle","volume":"163","author":"Morris","year":"2008","journal-title":"J. Struct. Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1007\/s12551-017-0295-1","article-title":"Lessons from a tarantula: New insights into muscle thick filament and myosin interacting-heads motif structure and function","volume":"9","author":"Alamo","year":"2017","journal-title":"Biophys. Rev."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"4617","DOI":"10.1021\/bi00801a004","article-title":"Mechanism of adenosine triphosphate hydrolysis by actomyosin","volume":"10","author":"Lymn","year":"1971","journal-title":"Biochemistry"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/S0006-3495(86)83509-3","article-title":"Stiffness of skinned rabbit psoas fibers in MgATP and MgPPi solution","volume":"50","author":"Brenner","year":"1986","journal-title":"Biophys. J."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1007\/BF00713057","article-title":"Cross-bridge behaviour during muscle contraction","volume":"6","author":"Huxley","year":"1985","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1126\/science.6979780","article-title":"Muscular contraction: Kinetics of crossbridge attachment studied by high-frequency stiffness measurements","volume":"217","author":"Cecchi","year":"1982","journal-title":"Science"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1023\/A:1005582324129","article-title":"Sarcomere tension-stiffness relation during the tetanus rise in single frog muscle fibres","volume":"20","author":"Bagni","year":"1999","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Squire, J.M. (2011). Muscle Contraction. eLS, John Wiley and Sons, Ltd.","DOI":"10.1002\/9780470015902.a0001256.pub3"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/0079-6107(68)90023-0","article-title":"Calcium ion and muscle contraction","volume":"18","author":"Ebashi","year":"1968","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1101\/SQB.1973.037.01.046","article-title":"Structural changes in actin- and myosin-containing filaments during contraction","volume":"37","author":"Huxley","year":"1972","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1101\/SQB.1973.037.01.044","article-title":"X-ray evidence for conformational change in actin filaments of vertebrate skeletal muscle","volume":"37","author":"Haselgrove","year":"1972","journal-title":"Cold Spring Harb. Symp. Quant. Biol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0022-2836(73)90527-5","article-title":"Structural role of tropomyosin in muscle regulation: Analysis of the X-ray diffraction patterns from relaxed and contracting muscles","volume":"75","author":"Parry","year":"1973","journal-title":"J. Mol. Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1006\/jmbi.1996.0800","article-title":"Steric-model for activation of muscle thin filaments","volume":"266","author":"Vibert","year":"1997","journal-title":"J. Mol. Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1096\/fasebj.12.10.761","article-title":"A new look at thin filament regulation in vertebrate skeletal muscle","volume":"12","author":"Squire","year":"1998","journal-title":"FASEB J."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"4","DOI":"10.2174\/1871529X18666180326120638","article-title":"Regulation of Smooth Muscle Myosin Light Chain Phosphatase by Multisite Phosphorylation of the Myosin Targeting Subunit, MYPT1","volume":"18","author":"MacDonald","year":"2018","journal-title":"Cardiovasc. Hematol. Disord. Drug Targets"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1007\/978-4-431-38453-3_21","article-title":"Regulation by myosin: How calcium regulates some myosins, past and present","volume":"592","year":"2007","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1042\/bj1510099","article-title":"Phosphorylation of the light-chain components of myosin from cardiac and red skeletal muscles","volume":"151","author":"Frearson","year":"1975","journal-title":"Biochem. J."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"jeb167718","DOI":"10.1242\/jeb.167718","article-title":"Myosin phosphorylation improves contractile economy of mouse fast skeletal muscle during staircase potentiation","volume":"221","author":"Bunda","year":"2018","journal-title":"J. Exp. Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"15485","DOI":"10.1073\/pnas.1903033116","article-title":"Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle","volume":"116","author":"Ponnam","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.abb.2018.10.007","article-title":"Skeletal myosin binding protein-C: An increasingly important regulator of striated muscle physiology","volume":"660","author":"McNamara","year":"2018","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/S0006-3495(93)81110-X","article-title":"Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament","volume":"65","author":"McKillop","year":"1993","journal-title":"Biophys. J."},{"key":"ref_74","first-page":"194S","article-title":"The role of three-state docking of myosin S1 with actin in force generation","volume":"68","author":"Geeves","year":"1995","journal-title":"Biophys. J."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Heilmeyer, L.M.C., Ruegg, J.C., and Wicland, T.L. (1976). Molecular Basis of Motility, Springer.","DOI":"10.1007\/978-3-642-81013-8"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1038\/233533a0","article-title":"Proposed Mechanism of Force Generation in Striated Muscle","volume":"233","author":"Huxley","year":"1971","journal-title":"Nature"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1113\/jphysiol.1977.sp011911","article-title":"Tension responses to sudden length change in stimulated frog muscle fibres near slack length","volume":"269","author":"Ford","year":"1977","journal-title":"J. Physiol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1113\/jphysiol.1981.sp013582","article-title":"The relation between stiffness and filament overlap in stimulated frog muscle fibres","volume":"311","author":"Ford","year":"1981","journal-title":"J. Physiol."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Knupp, C., and Squire, J.M. (2019). Myosin Cross-Bridge Behaviour in Contracting Muscle\u2014The T1 Curve of Huxley and Simmons (1971) Revisited. Int. J. Mol. Sci., 20.","DOI":"10.20944\/preprints201903.0147.v1"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1016\/S0006-3495(94)80728-3","article-title":"X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle","volume":"67","author":"Huxley","year":"1994","journal-title":"Biophys. J."},{"key":"ref_81","first-page":"1196","article-title":"X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction","volume":"68","author":"Wakabayashi","year":"1994","journal-title":"Biophys. J."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1007\/s10974-010-9232-7","article-title":"Cross-bridge and filament compliance in muscle: Implications for tension generation and lever arm swing","volume":"31","author":"Offer","year":"2010","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/0022-2836(68)90437-3","article-title":"Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor cross-bridge lattice","volume":"31","author":"Reedy","year":"1968","journal-title":"J. Mol. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1007\/BF01773878","article-title":"Actin filament organisation and myosin head labelling patterns in vertebrate skeletal muscles in the rigor and weak-binding states","volume":"9","author":"Squire","year":"1988","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"14949","DOI":"10.1073\/pnas.261560698","article-title":"Mapping the actin filament with myosin","volume":"98","author":"Steffen","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1742-4658.2007.06178.x","article-title":"Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures","volume":"275","author":"Wlodawer","year":"2008","journal-title":"FEBS J."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1107\/S2059798317016709","article-title":"Where is crystallography going?","volume":"74","author":"Grimes","year":"2018","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1111\/boc.201600042","article-title":"The integrative role of cryo-electron microscopy in molecular and cellular structural biology","volume":"109","author":"Orlov","year":"2017","journal-title":"Biol. Cell."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"10804","DOI":"10.1002\/anie.201802731","article-title":"From Electron Crystallography to Single Particle CryoEM (Nobel Lecture)","volume":"57","author":"Henderson","year":"2018","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/j.sbi.2019.05.021","article-title":"Advances in cryo-electron tomography and sub-tomogram averaging and classification","volume":"58","author":"Zhang","year":"2019","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Taylor, K.A., Rahmani, H., Edwards, R.J., and Reedy, M.K. (2019). Insights into Actin-Myosin Interactions within Muscle from 3D Electron Microscopy. Int. J. Mol. Sci., 20.","DOI":"10.20944\/preprints201903.0095.v1"},{"key":"ref_92","doi-asserted-by":"crossref","unstructured":"Dietz, M.S., and Heilemann, M. (2019). Optical super-resolution microscopy unravels the molecular composition of functional protein complexes. Nanoscale.","DOI":"10.1039\/C9NR06364A"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.abb.2015.06.006","article-title":"3D reconstruction of two-dimensional crystals","volume":"581","author":"Stahlberg","year":"2015","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"e13","DOI":"10.1017\/S0033583516000068","article-title":"Single particle electron cryo-microscopy: Trends, issues and future perspective","volume":"49","author":"Vinothkumar","year":"2016","journal-title":"Q. Rev. Biophys."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"5181","DOI":"10.1074\/jbc.REV118.005602","article-title":"Challenges and opportunities in cryo-EM single-particle analysis","volume":"294","author":"Lyumkis","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Nwanochie, E., and Uversky, V.N. (2019). Structure Determination by Single-Particle Cryo-Electron Microscopy: Only the Sky (and Intrinsic Disorder) is the Limit. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20174186"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/j.cell.2015.03.050","article-title":"A primer to single-particle cryo-electron microscopy","volume":"161","author":"Cheng","year":"2015","journal-title":"Cell"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1007\/s10974-004-5333-5","article-title":"Single Particle Analysis: A new approach to solving the 3D structure of Myosin Filaments","volume":"25","author":"Morris","year":"2004","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/j.jsb.2009.12.010","article-title":"A novel approach to the structural analysis of partially decorated actin based filaments","volume":"170","author":"Paul","year":"2010","journal-title":"J. Struct. Biol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1042\/bj0750335","article-title":"Fluorescence-polarization spectrum and electronic-energy transfer in tyrosine, tryptophan and related compounds","volume":"75","author":"Weber","year":"1960","journal-title":"Biochem. J."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1093\/oxfordjournals.jbchem.a128518","article-title":"Effects of pH and some agents on the fluorescence of myosin A","volume":"61","author":"Kasuya","year":"1967","journal-title":"J. Biochem."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"4517","DOI":"10.1021\/bi00839a044","article-title":"Polarization of tryptophan fluorescence in muscle","volume":"8","author":"Aronson","year":"1969","journal-title":"Biochemistry"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/S0006-3495(74)85911-4","article-title":"Use of fluorescence polarization to observe changes in attitude of S-1 moieties in muscle fibers","volume":"14","author":"Nihei","year":"1974","journal-title":"Biophys. J."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/22704","article-title":"Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction","volume":"400","author":"Corrie","year":"1999","journal-title":"Nature"},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Bajar, B.T., Wang, E.S., Zhang, S., Lin, M.Z., and Chu, J. (2016). A Guide to Fluorescent Protein FRET Pairs. Sensors, 16.","DOI":"10.3390\/s16091488"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1007\/s12551-017-0252-z","article-title":"FRET from single to multiplexed signaling events","volume":"9","author":"Bunt","year":"2017","journal-title":"Biophys. Rev."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"2836","DOI":"10.1016\/S0006-3495(97)78312-7","article-title":"Mapping fluorophore distributions in three dimensions by quantitative multiple angle-total internal reflection fluorescence microscopy","volume":"73","author":"Olveczky","year":"1997","journal-title":"Biophys. J."},{"key":"ref_108","doi-asserted-by":"crossref","unstructured":"Guhathakurta, P., Prochniewicz, E., and Thomas, D.D. (2018). Actin-Myosin Interaction: Structure, Function and Drug Discovery. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19092628"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1146\/annurev.biophys.35.040405.102118","article-title":"Site-directed spectroscopic probes of actomyosin structural dynamics","volume":"38","author":"Thomas","year":"2009","journal-title":"Annu. Rev. Biophys."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1002\/jss.400030410","article-title":"The quantitative measurement of rotational motion of the subfragment-1 region of myosin by saturation transfer epr spectroscopy","volume":"3","author":"Thomas","year":"1975","journal-title":"J. Supramol. Struct."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1085\/jgp.201812210","article-title":"Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels","volume":"151","author":"Savich","year":"2019","journal-title":"J. Gen. Physiol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/0079-6107(73)90007-2","article-title":"The kinetics of muscle contraction","volume":"27","author":"White","year":"1973","journal-title":"Prog. Biophys."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1007\/s10741-005-5248-2","article-title":"Kinetics and energetics of the crossbridge cycle","volume":"10","author":"Maughan","year":"2005","journal-title":"Heart Fail. Rev."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1146\/annurev.bb.18.060189.001323","article-title":"Properties and uses of photoreactive caged compounds","volume":"18","author":"McCray","year":"1989","journal-title":"Annu. Rev. Biophys. Biophys. Chem."},{"key":"ref_115","first-page":"191S","article-title":"A new method for the time-resolved measurement of phosphate release in permeabilized muscle fibers","volume":"68","author":"Ferenczi","year":"1995","journal-title":"Biophys. J."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1111\/j.1469-7793.1999.0839s.x","article-title":"The efficiency of contraction in rabbit skeletal muscle fibres determined from the rate of release of inorganic phosphate","volume":"517","author":"He","year":"1999","journal-title":"J Physiol."},{"key":"ref_117","first-page":"319","article-title":"Time-resolved X-ray diffraction studies of myosin head movements in live frog sartorius muscle during isometric and isotonic contractions","volume":"15","author":"Bordas","year":"1994","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S0006-3495(92)81613-2","article-title":"Evidence for structurally different attached states of myosin cross-bridges on actin during contraction of fish muscle","volume":"63","author":"Harford","year":"1992","journal-title":"Biophys. J."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.jmb.2009.04.047","article-title":"Probing Muscle Myosin Motor Action: X-Ray (M3 and M6) Interference Measurements Report Motor Domain Not Lever Arm Movement","volume":"390","author":"Knupp","year":"2009","journal-title":"J. Mol. Boil."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1088\/0034-4885\/60\/12\/005","article-title":"Time-resolved studies of muscle using synchrotron radiation","volume":"60","author":"Harford","year":"1997","journal-title":"Rep. Prog. Phys."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1006\/jmbi.1997.1321","article-title":"Myosin head configuration in relaxed fish muscle: Resting myosin heads must swing axially by up to 150 Angstroms or turn upside down to reach rigor","volume":"273","author":"Hudson","year":"1997","journal-title":"J. Mol. Biol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1016\/S0006-3495(03)74545-7","article-title":"Myosin head configuration in relaxed insect flight muscle: X-ray modelled resting cross-bridges in a pre-powerstroke state are poised for actin binding","volume":"85","author":"Hudson","year":"2003","journal-title":"Biophys. J."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/S0168-9002(97)00211-8","article-title":"The \u201crapid\u201d high rate large area X-ray detector system","volume":"92","author":"Lewis","year":"1997","journal-title":"Nucl. Instrum. Methods Phys. Res. Sect. A"},{"key":"ref_124","doi-asserted-by":"crossref","unstructured":"Eakins, F., Pinali, C., Gleeson, A., Knupp, C., and Squire, J.M. (2016). X-ray Diffraction Evidence for Low Force Actin-Attached and Rigor-Like Cross-Bridges in the Contractile Cycle. Biology, 5.","DOI":"10.3390\/biology5040041"},{"key":"ref_125","doi-asserted-by":"crossref","unstructured":"M\u00e5nsson, A., Usaj, M., Moretto, L., and Rassier, D.E. (2018). Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19071863"},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Sugi, H., Chaen, S., and Akimoto, T. (2018). Electron Microscopic Recording of the Power and Recovery Strokes of Individual Myosin Heads Coupled with ATP Hydrolysis: Facts and Implications. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19051368"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1016\/j.tibs.2016.09.006","article-title":"How Myosin Generates Force on Actin Filaments","volume":"41","author":"Houdusse","year":"2016","journal-title":"Trends Biochem. Sci."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.cell.2012.05.037","article-title":"Structure of the rigor actin-tropomyosin-myosin complex","volume":"150","author":"Behrmann","year":"2012","journal-title":"Cell"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1038\/nature18295","article-title":"Cryo-EM structure of a human cytoplasmic actomyosin complex at near-atomic resolution","volume":"534","author":"Heissler","year":"2016","journal-title":"Nature"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/j.devcel.2015.03.025","article-title":"How actin initiates the motor activity of Myosin","volume":"33","author":"Llinas","year":"2015","journal-title":"Dev. Cell."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"14593","DOI":"10.1073\/pnas.1517566112","article-title":"Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V","volume":"112","author":"Trivedi","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1007\/s12551-017-0272-8","article-title":"The Frank-Starling Law: A jigsaw of titin proportions","volume":"9","author":"Sequeira","year":"2017","journal-title":"Biophys. Rev."},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Eakins, F., Harford, J.J., Knupp, C., Roessle, M., and Squire, J.M. (2018). Different Myosin Head Conformations in Bony Fish Muscles Put into Rigor at Different Sarcomere Lengths. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19072091"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1016\/j.bpj.2014.05.044","article-title":"In situ time-resolved FRET reveals effects of sarcomere length on cardiac thin-filament activation","volume":"107","author":"Li","year":"2014","journal-title":"Biophys. J."},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Iwamoto, H. (2018). Synchrotron Radiation X-ray Diffraction Techniques Applied to Insect Flight Muscle. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19061748"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1038\/nature03230","article-title":"Molecular dynamics of cyclically contracting insect flight muscle in vivo","volume":"433","author":"Dickinson","year":"2005","journal-title":"Nature"},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Ranatunga, K.W. (2018). Temperature Effects on Force and Actin\u2013Myosin Interaction in Muscle: A Look Back on Some Experimental Findings. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19051538"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Katayama, E., and Kodera, N. (2018). Unconventional Imaging Methods to Capture Transient Structures during Actomyosin Interaction. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19051402"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"3273","DOI":"10.1091\/mbc.e14-05-1016","article-title":"Some personal and historical notes on the utility of \u201cdeep-etch\u201d electron microscopy for making cell structure\/function correlations","volume":"25","author":"Heuser","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.bbrc.2011.01.087","article-title":"Electron microscopic evidence for the myosin head lever arm mechanism in hydrated myosin filaments using the gas environmental chamber","volume":"405","author":"Minoda","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Ma, W., Gong, H., and Irving, T. (2018). Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19092643"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/s10974-019-09543-9","article-title":"Monitoring the myosin crossbridge cycle in contracting muscle: Steps towards \u2018Muscle-the Movie\u2019","volume":"40","author":"Eakins","year":"2019","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"578","DOI":"10.1038\/nature02380","article-title":"Fischetti, R.F.; Irving, T.; Piazzesi, G. The myosin motor in muscle generates a smaller and slower working stroke at higher load","volume":"428","author":"Reconditi","year":"2004","journal-title":"Nature"},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Marston, S. (2018). The Molecular Mechanisms of Mutations in Actin and Myosin that Cause Inherited Myopathy. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19072020"},{"key":"ref_145","doi-asserted-by":"crossref","unstructured":"Vikhorev, P.G., and Vikhoreva, N.N. (2018). Cardiomyopathies and Related Changes in Contractility of Human Heart Muscle. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19082234"},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Borovikov, Y.S., Karpicheva, O.E., Simonyan, A.O., Avrova, S.V., Rogozovets, E.A., Sirenko, V.V., and Redwood, C.S. (2018). The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies. Int. J. Mol. Sci., 19.","DOI":"10.3390\/ijms19123975"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1126\/science.aad3456","article-title":"A small-molecule inhibitor of sarcomere contractility suppresses hypertrophic cardiomyopathy in mice","volume":"351","author":"Green","year":"2016","journal-title":"Science"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"e009627","DOI":"10.1161\/JAHA.118.009627","article-title":"Impact of the Myosin Modulator Mavacamten on Force Generation and Cross-Bridge Behavior in a Murine Model of Hypercontractility","volume":"7","author":"Mamidi","year":"2018","journal-title":"J. Am. Heart Assoc."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"E7486","DOI":"10.1073\/pnas.1720342115","article-title":"Mavacamten stabilizes an autoinhibited state of two-headed cardiac myosin","volume":"115","author":"Rohde","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1113\/jphysiol.1969.sp008723","article-title":"Force measurements in skinned muscle fibres","volume":"200","author":"Hellam","year":"1969","journal-title":"J. Physiol."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1016\/S0021-9258(18)81304-7","article-title":"The binding of calcium to actomyosin systems in relation to their biological activity","volume":"238","author":"Weber","year":"1963","journal-title":"J. Biol. Chem."},{"key":"ref_152","unstructured":"Squire, J.M. (1986). Muscle: Design, Diversity and Disease, Benjamin\/Cummings Publishing Co."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.bbadis.2006.05.010","article-title":"Dystrophin, its interactions with other proteins, and implications for muscular dystrophy","volume":"1772","author":"Ervasti","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Meyers, T.A., and Townsend, D. (2019). Cardiac Pathophysiology and the Future of Cardiac Therapies in Duchenne Muscular Dystrophy. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20174098"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1007\/s10974-019-09535-9","article-title":"What is the level of dystrophin expression required for effective therapy of Duchenne muscular dystrophy?","volume":"40","author":"Wells","year":"2019","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_156","first-page":"165","article-title":"Congenital myopathies: An update","volume":"12","author":"Claeys","year":"2019","journal-title":"Dev. Med. Child. Neurol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/20\/22\/5715\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T13:34:30Z","timestamp":1760189670000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/20\/22\/5715"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,11,14]]},"references-count":156,"journal-issue":{"issue":"22","published-online":{"date-parts":[[2019,11]]}},"alternative-id":["ijms20225715"],"URL":"https:\/\/doi.org\/10.3390\/ijms20225715","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,11,14]]}}}