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Motion of myosin head domains during activation and force development in skeletal muscleInterference fine structure and sarcomere length dependence of the axial x-ray pattern from active single muscle fibers.X-ray diffraction studies of the contractile mechanism in single muscle fibres.Skeletal muscle resists stretch by rapid binding of the second motor domain of myosin to actinSize and speed of the working stroke of cardiac myosin in situ.RECENT IMPROVEMENTS IN SMALL ANGLE X-RAY DIFFRACTION FOR THE STUDY OF MUSCLE PHYSIOLOGY.Myosin filament activation in the heart is tuned to the mechanical task.Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog.The myosin motor in muscle generates a smaller and slower working stroke at higher load.Minimum number of myosin motors accounting for shortening velocity under zero load in skeletal muscle.The non-linear elasticity of the muscle sarcomere and the compliance of myosin motors.Force generation by skeletal muscle is controlled by mechanosensing in myosin filaments.There is no experimental evidence for non-linear myofilament elasticity in skeletal muscle.Thick Filament Mechano-Sensing in Skeletal and Cardiac Muscles: A Common Mechanism Able to Adapt the Energetic Cost of the Contraction to the Task.Mechanism of force generation by myosin heads in skeletal muscleThe structural basis of the increase in isometric force production with temperature in frog skeletal muscleConformation of the myosin motor during force generation in skeletal muscleInotropic interventions do not change the resting state of myosin motors during cardiac diastoleTemperature dependence of the force-generating process in single fibres from frog skeletal muscleA combined mechanical and X-ray diffraction study of stretch potentiation in single frog muscle fibresChanges in conformation of myosin heads during the development of isometric contraction and rapid shortening in single frog muscle fibresX-ray interference studies of crossbridge action in muscle contraction: evidence from quick releasesThe mechanism of the force response to stretch in human skinned muscle fibres with different myosin isoformsX-ray interference studies of crossbridge action in muscle contraction: evidence from muscles during steady shorteningStructural changes in the myosin filament and cross-bridges during active force development in single intact frog muscle fibres: stiffness and X-ray diffraction measurementsStructural changes in myosin motors and filaments during relaxation of skeletal muscleThe mechanism of the resistance to stretch of isometrically contracting single muscle fibresThe contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscleThe myofilament elasticity and its effect on kinetics of force generation by the myosin motorIs muscle powered by springs or motors?The force and stiffness of myosin motors in the isometric twitch of a cardiac trabecula and the effect of the extracellular calcium concentrationLow temperature traps myosin motors of mammalian muscle in a refractory state that prevents activationContracting striated muscle has a dynamic I-band spring with an undamped stiffness 100 times larger than the passive stiffnessA mechanical model of the half-sarcomere which includes the contribution of titin
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description
researcher ORCID ID = 0000-0001-5065-924X
@en
wetenschapper
@nl
name
Massimo Reconditi
@ast
Massimo Reconditi
@en
Massimo Reconditi
@es
Massimo Reconditi
@nl
type
label
Massimo Reconditi
@ast
Massimo Reconditi
@en
Massimo Reconditi
@es
Massimo Reconditi
@nl
prefLabel
Massimo Reconditi
@ast
Massimo Reconditi
@en
Massimo Reconditi
@es
Massimo Reconditi
@nl
P106
P1153
6603571169
P31
P496
0000-0001-5065-924X