Literature DB >> 620080

Myosin subfragment-1 attachment to actin. Expected effect on equatorial reflections.

R W Lymn.   

Abstract

The characteristic equatorial X-ray pattern from a relaxed vertebrate skeletal muscle changes when the muscle is activated. In particular, there is a simultaneous decrease in the intensity of the first reflection (I10) and increase in the intensity of the second (I11). This observed change is almost reciprocal. When compared with the predictions of computer modeling, it produces a strong argument that the intensity change is due to a redistribution of myosin heads (myosin subfragment-1 or S-1), which results from the formation and configuration changes of actin-myosin links. Computer modeling shows that different actin-S-1 configurations will give different numerical values for I10 and I11, assuming the same number of attachments. For a given configuration, the intensity changes are a nonlinear function of attachment number, so that direct scaling of force to reflection intensity may be difficult. Data from active muscle are consistent with the notion that in different states of active muscle, i.e. shortening or isometric, there are different average configurations of actin-myosin attachment and different numbers of actin-myosin links.

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Year:  1978        PMID: 620080      PMCID: PMC1473376          DOI: 10.1016/S0006-3495(78)85510-6

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  14 in total

Review 1.  Muscle filament structure and muscle contraction.

Authors:  J M Squire
Journal:  Annu Rev Biophys Bioeng       Date:  1975

2.  Equatorial X-ray reflections and cross arm movement in skeletal muscle.

Authors:  R W Lymn
Journal:  Nature       Date:  1975-12-25       Impact factor: 49.962

3.  Muscle structure and theories of contraction.

Authors:  A F HUXLEY
Journal:  Prog Biophys Biophys Chem       Date:  1957

4.  X-ray diffraction of actively shortening muscle.

Authors:  R J Podolsky; H St Onge; L Yu; R W Lymn
Journal:  Proc Natl Acad Sci U S A       Date:  1976-03       Impact factor: 11.205

5.  Low-angle x-ray diagrams from skeletal muscle: the effect of AMP-PNP, a non-hydrolyzed analogue of ATP.

Authors:  R W Lymn
Journal:  J Mol Biol       Date:  1975-12-25       Impact factor: 5.469

6.  Cross-bridge movement during muscle contraction.

Authors:  J C Haselgrove; M Stewart; H E Huxley
Journal:  Nature       Date:  1976-06-17       Impact factor: 49.962

7.  Proposed mechanism of force generation in striated muscle.

Authors:  A F Huxley; R M Simmons
Journal:  Nature       Date:  1971-10-22       Impact factor: 49.962

8.  Structural difference between resting and rigor muscle; evidence from intensity changes in the lowangle equatorial x-ray diagram.

Authors:  H E Huxley
Journal:  J Mol Biol       Date:  1968-11-14       Impact factor: 5.469

9.  Three-dimensional reconstruction of F-actin, thin filaments and decorated thin filaments.

Authors:  P B Moore; H E Huxley; D J DeRosier
Journal:  J Mol Biol       Date:  1970-06-14       Impact factor: 5.469

10.  The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor.

Authors:  H E Huxley; W Brown
Journal:  J Mol Biol       Date:  1967-12-14       Impact factor: 5.469

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  21 in total

1.  Evidence for structurally different attached states of myosin cross-bridges on actin during contraction of fish muscle.

Authors:  J J Harford; J M Squire
Journal:  Biophys J       Date:  1992-08       Impact factor: 4.033

2.  Second harmonic generation microscopy probes different states of motor protein interaction in myofibrils.

Authors:  Sebastian Schürmann; Frederic von Wegner; Rainer H A Fink; Oliver Friedrich; Martin Vogel
Journal:  Biophys J       Date:  2010-09-22       Impact factor: 4.033

3.  State-dependent radial elasticity of attached cross-bridges in single skinned fibres of rabbit psoas muscle.

Authors:  S Xu; B Brenner; L C Yu
Journal:  J Physiol       Date:  1993-02       Impact factor: 5.182

4.  Characterizations of cross-bridges in the presence of saturating concentrations of MgAMP-PNP in rabbit permeabilized psoas muscle.

Authors:  S M Frisbie; S Xu; J M Chalovich; L C Yu
Journal:  Biophys J       Date:  1998-06       Impact factor: 4.033

5.  Modulation of cross-bridge affinity for MgGTP by Ca2+ in skinned fibers of rabbit psoas muscle.

Authors:  S M Frisbie; J M Chalovich; B Brenner; L C Yu
Journal:  Biophys J       Date:  1997-05       Impact factor: 4.033

6.  Analysis of equatorial x-ray diffraction patterns from skeletal muscle.

Authors:  L C Yu
Journal:  Biophys J       Date:  1989-03       Impact factor: 4.033

7.  Movements of cross-bridges during and after slow length changes in active frog skeletal muscle.

Authors:  I Matsubara; N Yagi
Journal:  J Physiol       Date:  1985-04       Impact factor: 5.182

8.  Tension transients during steady shortening of frog muscle fibres.

Authors:  L E Ford; A F Huxley; R M Simmons
Journal:  J Physiol       Date:  1985-04       Impact factor: 5.182

9.  State-dependent radial elasticity of attached cross-bridges in single skinned fibres of rabbit psoas muscle.

Authors:  S Xu; B Brenner; L C Yu
Journal:  J Physiol       Date:  1993-06       Impact factor: 5.182

10.  Effects of 2,3-butanedione monoxime on contraction of frog skeletal muscles: an X-ray diffraction study.

Authors:  N Yagi; S Takemori; M Watanabe; K Horiuti; Y Amemiya
Journal:  J Muscle Res Cell Motil       Date:  1992-04       Impact factor: 2.698

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