Swimming against the tide
NaturePublished 14 December 2000
David Cyranoski
Citations95
SJR quartileQ1
SJR score18.29
SNIP10.16
Generate an AI Snapshot to get a quick, structured summary of this paper.
Study Snapshot
ObjectiveStudy objective
MethodsResearch methodology
PopulationPopulation studied
Sample sizeSample sizes
OutcomesStudy outcomes here
ResultsStudy results comes here
LimitationsResearch study limitations comes here
A concise AI-generated summary of the paper will appear here once you click Generate AI Snapshot.
Abstract
Toshio Yanagida rejects the conventional biophysical explanation of muscle contraction. No one doubts his technical genius, but could the debate he started ultimately hold back the field? David Cyranoski investigates.
Keywords
MedicineBiochemistry, Genetics and Molecular Biology
NatureSingle myosin molecule mechanics: piconewton forces and nanometre steps
1,925 Citations1994Jeffrey T. Finer, Robert Simmons +1 more
A new in vitro assay using a feedback enhanced laser trap system allows direct measurement of force and displacement that results from the interaction of a single myosin molecule with a single suspended actin filament.
ScienceStructure of the actin-myosin complex and its implications for muscle contraction
1,797 Citations1993Ivan Rayment, Hazel M. Holden +5 more
The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.
NatureImaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
1,051 Citations1995Takashi Funatsu, Yoshie Harada +3 more
This approach can be used directly to image single fluorescently labelled myosin molecules and detect individual ATP turnover reactions and can be applied to the study of many types of enzymes and biomolecules.
CellCrystal Structure of a Vertebrate Smooth Muscle Myosin Motor Domain and Its Complex with the Essential Light Chain
639 Citations1998Roberto Domínguez, Yelena Freyzon +2 more
A comparison of the lever arm positions in MDE-AIF4- and in nucleotide-free skeletal S1 shows that a potential displacement of approximately 10 nm can be achieved during the power stroke, consistent with the fact that they both bind weakly to actin.
NatureMovement and force produced by a single myosin head
619 Citations1995Justin E. Molloy, Julie E. Burns +3 more
It is shown, using an optical-tweezers transducer, that a single myosin subfragment-1 (S1), which is a singleMyosin head, can act as an independent generator of force and movement.
NatureA single myosin head moves along an actin filament with regular steps of 5.3 nanometres
534 Citations1999K. Kitamura, Makio Tokunaga +2 more
A new instrument is developed with which individual myosin subfragment-1 molecules are captured and directly manipulated using a scanning probe to resolve the individual mechanical events of force generation by actomyosin.
CellSimultaneous Observation of Individual ATPase and Mechanical Events by a Single Myosin Molecule during Interaction with Actin
480 Citations1998Akihiko Ishijima, Hiroaki Kojima +5 more
The results show that the force generation does not always coincide with the release of bound nucleotide, presumably ADP, and suggests that myosin has a hysteresis or memory state, which stores chemical energy from ATP hydrolysis.
NatureDirect observation of motion of single F-actin filaments in the presence of myosin
477 Citations1984Toshio Yanagida, Michiyuki Nakase +2 more
Direct observation by fluorescence microscopy of the movements of single F-actin filaments interacting with soluble myosin fragments energized by Mg2+-ATP is reported.
NatureSliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle
260 Citations1985Toshio Yanagida, Toshiaki Arata +1 more
Measurements of the sliding distance of an actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle in an unloaded condition show that the average sliding distance is ≥600 Å, much longer than the length of power stroke of myOSin crossbridges deduced from mechanical studies of muscle, which is of the order of 80 Å.
NatureDynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction
222 Citations1999John E. T. Corrie, Birgit Brandmeier +10 more
The results reveal the structural basis for the lever-arm action of the light-chain domain of the myosin motor during force generation in muscle.
Proceedings of the National Academy of SciencesDetection of single-molecule interactions using correlated thermal diffusion
129 Citations1997Amit Mehta, J.T. Finer +1 more
Thermal diffusion is exploited by using correlation between motion of optically trapped beads attached to both ends of a single actin filament to track binding events of individual myosin molecules and estimate its thermal fluctuation in a poststroke state as comparable in amplitude to the measured stroke distance.
Nature Structural BiologyConformation of the myosin motor during force generation in skeletal muscle
107 Citations2000Malcolm Irving, Gabriella Piazzesi +7 more
X-ray fiber diffraction is used to test the crystallographic model and measure the interdomain bending during force generation in an intact single muscle fiber and shows the average bend of the force-generating myosin heads in a muscle fiber is intermediate between those in crystal structures with different bound nucleotides.
Journal of Biological ChemistryThe Light Chain Binding Domain of Expressed Smooth Muscle Heavy Meromyosin Acts as a Mechanical Lever
100 Citations2000David M. Warshaw, William H. Guilford +6 more
The single molecule displacement and force data support the hypothesis that the neck functions as a rigid lever, with the fulcrum for movement and force located at a point within the motor domain.