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Structural changes in muscle during contraction: interference
microscopy of living muscle fibres
Huxley, A. F. & Niedergerke, R.
Nature 173, 971-973 (22 May 1954)
Interference microscopy shows that the width of 'A bands'
in muscle fibres remains constant during contraction
(see
picture), suggesting a 'sliding filament' model in which
myosin filaments run the length of the A band and actin filaments
slide into the A band.
Changes in the cross-striations of muscle during contraction
and stretch and their structural interpretation
Huxley, H. E., Hanson, J.
Nature 173, 973-976 (22 May 1954)
Light microscopy of isolated myofibrils independently
establishes the sliding filament mechanism and constancy of
the A-band width. Myosin is extracted from the A bands and the
role of ATP hydrolysis in the contraction cycle demonstrated.
| After the sliding filament model became
accepted, the focus shifted to the molecular mechanism
of contraction: what makes the filaments slide? Early
electron micrographs had shown 'crossbridges' linking
the myosin and actin filaments in the overlap region.
Here, key papers from Nature's archive reveal each
decade of progress since the first reports of filament
sliding. |
1960s
Induced changes in orientation of the cross-bridges of glycerinated insect flight muscle
Reedy M. K., Holmes K. C. & Tregear R. T.
Nature 207(3), 1276-80-976 (18 Sep 1965)
X-ray diffraction and electron microscopy
demonstrate that the transition from relaxed to 'rigor' (high
tension) insect flight muscle is accompanied by a re-orientation
of the crossbridges between actin and myosin filaments.
1970s
Proposed mechanism of force generation in striated muscle
Huxley, A. F. & Simmons, R. M.
Nature 233, 533-538 (22 Sep 1971)
After a small rapid shortening is imposed on intact muscle fibres, the fibres quickly recover but only over a range of sliding of 10 nanometres between the myosin and actin filaments, leading to the concept of a 'working stroke' of 10 nm.
1980s
Myosin subfragment-1 is sufficient to move actin filaments in
vitro
Toyoshima, Y. Y. et al.
Nature 328, 536-539 (6 Aug 1987)
Single myosin heads cause sliding of isolated
actin filaments in the presence of ATP—the first direct
demonstration that the 'head' of the myosin filament is the
functional motor.
1990s
Single myosin molecule mechanics: piconewton force and nanometre steps
Finer, J. T., Simmons, R. M. & Spudich, J. A.
Nature 368, 113-119 (10 March 1994)
The first direct measurement of the working stroke produced by a single myosin molecule shows excellent agreement with the 1971 measurements by Huxley and Simmons in intact muscle.
2000s
The myosin motor in muscle generates a smaller and slower working stroke at higher load
M. Reconditi et al.
Nature 428, 578-581 (1 Apr 2004)
X-ray interference shows that the working stroke of the myosin head depends on the load of the motor.
Sliding across a cytoskeletal milestone
Tskhovrebova, L. & Trinick, J.
Nature Cell Biology 6, 375 (May 2004)
Single-molecule visualization in cell biology
Sako, Y. & Yanagida, T.
Nature Reviews Molecular Cell Biology 4, SS1-SS5 (2003)
Mechanism of force generation by myosin heads in skeletal muscle
Piazzesi, G. et al.
Nature 415, 659-662 (7 Feb 2002)
A crossbridge too far
Spudich, J. A. & Rock, R. S.
Nature Cell Biology 4 (1), E8-E10 (Jan 2002)
The myosin swinging cross-bridge model
Spudich, J. A.
Nature Reviews Molecular Cell Biology 2, 387-392
(1 May 2001)
Motor protiens: Another step ahead for myosin
Irving, M. and Goldman, Y. E.
Nature 398, 464-465 (8 April 1999) N&V
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