Myosin

Harrington, William F.; Rodgers, Michael E.

doi:10.1146/annurev.bi.53.070184.000343

Cited by 314 publications

(205 citation statements)

References 125 publications

(179 reference statements)

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“…Further digestion of the heavy meromyosin with papain, another proteolytic enzyme, removes the rest of the coiled coil rod portion (fragment S2) and leaves a globular protein, which includes the paired head of the MHCs and four light chains (fragment S1). This head region of the molecule contains ATPase activity and hence acts as a site of chemico-mechanical transduction [11].…”

Section: Structural Organization and Developmental Regulation Of Myosmentioning

confidence: 99%

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Factors controlling cardiac myosin-isoform shift during hypertrophy and heart failure

Gupta

2007

Journal of Molecular and Cellular Cardiology

190

171

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Section: Structural Organization and Developmental Regulation Of Myosmentioning

confidence: 99%

“…1). The atria contain a separate myosin isoform (Va) that is made up of two αMHCs and a separate set of light chains (LC-1a and LC-2a) [11,13].…”

Section: Structural Organization and Developmental Regulation Of Myosmentioning

confidence: 99%

Factors controlling cardiac myosin-isoform shift during hypertrophy and heart failure

Gupta

2007

Journal of Molecular and Cellular Cardiology

190

171

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“…Describing invertebrate thick filament structure has therefore been an enormous undertaking, and even today detailed understanding of their structure is available for only a few types of thick filament. Reviews with data on invertebrate thick filament structure include Harrington and Roger (1984), Warrick and Spudich (1987), Barral and Epstein (1999), Squire et al (2005a) and Craig and Woodhead (2006).…”

Section: Thick Filamentmentioning

confidence: 99%

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

131

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This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

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“…Both myosin head (St) and neck (hinge&) regions would fulfil this criterion [9]. Indeed, the majority of myosin antibodies react with the Si and SZ fragments [13].…”

Section: Resultsmentioning

confidence: 99%

Dissociation of actomyosin complex by monovalent fragments of polyclonal antibodies to myosin

Mazander

Gröschel‐Stewart

1985

FEBS Letters

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Myosin

Cited by 314 publications

References 125 publications

Factors controlling cardiac myosin-isoform shift during hypertrophy and heart failure

Factors controlling cardiac myosin-isoform shift during hypertrophy and heart failure

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Dissociation of actomyosin complex by monovalent fragments of polyclonal antibodies to myosin

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