The Structural Basis of Muscular Contraction

Squire, John M.

doi:10.1007/978-1-4613-3183-4

Cited by 317 publications

(249 citation statements)

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“…Is should be important to compare it with the existing models for the filament structure (review [21]). In particular, it should be confirmed that, in natural filaments, 1 head/crossbridge can be inserted in the backbone and can interact with the opposite head.…”

Section: Discussionmentioning

confidence: 99%

“…In particular, it should be confirmed that, in natural filaments, 1 head/crossbridge can be inserted in the backbone and can interact with the opposite head. This seems to be structurally possible since, according to [21], the most probable case is that corresponding to a hollow center of the core -5O-1OOA in diameter: this is sufficient to insert two adjacent heads, with their long axis approximately parallel ( fig. 2A).…”

Section: Discussionmentioning

confidence: 99%

“…This proposal would be supported by the fact that extremely active muscles (e.g., insect flightmuscles), have a considerable number of myosin molecules in excess. Moreover, the reported values of NM are variable (254 I NM I 432; table 7.2 in [21]). Such a variability may be related to the age of the animal, owing to the age-dependent metabolism: the young animals would have more myosin molecules/filament than the old animals.…”

Section: Discussionmentioning

confidence: 99%

“…Now, according to Squire [21], there are -100 levels of crossbridges (crowns; 143 A repeats). Since each crown contains at least 2 crossbridges [21] …”

Section: Native Filamentsmentioning

confidence: 99%

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The possible roles of the myosin heads

Morel

Garrigos

1982

FEBS Letters

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It is suggested that, in the conditions which exist in vivo, one head of a myosin molecule interacts with another head of the opposite molecule, inside the backbone of the thick filament. The other head lies outside and can interact with actin. This model is based on the fact that a dimer of the myosin heads exists and that there is a close correlation between the properties of the dimer and those of the thick filament diameter. In natural filaments, there are myosin molecules in excess and it is suggested that these molecules have their two heads outside the backbone.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…Now, according to Squire [21], there are -100 levels of crossbridges (crowns; 143 A repeats). Since each crown contains at least 2 crossbridges [21] …”

Section: Native Filamentsmentioning

confidence: 99%

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The possible roles of the myosin heads

Morel

Garrigos

1982

FEBS Letters

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“…These include titin or connectin (6,7), MyBP-C (C-protein) (8), MyBP-H (H-protein) (9,10), myomesin (11), M protein (12,13), skelemin (14), MM-creatine kinase (15,16), AMP-deaminase (17), and X-protein (the slow-type isoform of MyBP-C) (18 -20). The MyBPs, first isolated in crude myosin preparations by Offer and colleagues (21) in the early 1970s are a group of proteins distributed in the central two-thirds of the cross-bridge bearing region (C-zone) of the A-band (22). This zone contains a set of 11 transverse repeats of 43 nm axial spacing, distributed along the constant diameter region of the thick filaments.…”

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confidence: 99%

Isoform-specific Interaction of the Myosin-binding Proteins (MyBPs) with Skeletal and Cardiac Myosin Is a Property of the C-terminal Immunoglobulin Domain

Alyonycheva¹,

Matsukawa²,

Reinach³

et al. 1997

Journal of Biological Chemistry

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Evolution of myosin filament arrangements in vertebrate skeletal muscle

1996

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A survey of skeletal muscles throughout craniates shows basic kinds of myosin filament arrangement, simple‐lattice and superlattice, within the A‐band of each sarcomere. Distribution of simple‐ and superlattice arrangements across a phylogeny of craniates suggests that the superlattice arrangement is primitive and that Amia and teleosts are derived in showing simple‐lattice arrangements. Two taxa examined (Scyliorhinus and Acipenser) show both lattice types within the same organism implying that there is not a simple evolutionary transformation of one to the other fiber arrangement. We discuss the possible functional significance of the different lattice types. We believe that the crossbridges may have greater competition for actin binding sites in simple‐lattice muscles compared to the superlattice types. © 1996 Wiley‐Liss, Inc.

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The Structural Basis of Muscular Contraction

Cited by 317 publications

References 0 publications

The possible roles of the myosin heads

The possible roles of the myosin heads

Isoform-specific Interaction of the Myosin-binding Proteins (MyBPs) with Skeletal and Cardiac Myosin Is a Property of the C-terminal Immunoglobulin Domain

Evolution of myosin filament arrangements in vertebrate skeletal muscle

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