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New techniques in linear and non-linear laser optics in muscle research.Probing myosin structural conformation in vivo by second-harmonic generation microscopy.Ca-activation and stretch-activation in insect flight muscle.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.Stiffness and fraction of Myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoasSkeletal 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.Effect of inorganic phosphate on the force and number of myosin cross-bridges during the isometric contraction of permeabilized muscle fibers from rabbit psoas.The effect of myofilament compliance on kinetics of force generation by myosin motors in muscle.Myosin filament activation in the heart is tuned to the mechanical task.Low-force transitions in single titin molecules reflect a memory of contractile history.Sarcomere-length dependence of myosin filament structure in skeletal muscle fibres of the frog.Energy storage during stretch of active single fibres from frog skeletal muscle.Muscle Thixotropy: More than Just Cross-Bridges? Response to Comment by Campbell and Lakie.The myosin motor in muscle generates a smaller and slower working stroke at higher load.Force generation by skeletal muscle is controlled by mechanosensing in myosin filaments.Effects of myosin heavy chain (MHC) plasticity induced by HMGCoA-reductase inhibition on skeletal muscle functionsMechanism of force generation by myosin heads in skeletal muscleThe structural basis of the increase in isometric force production with temperature in frog 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 muscleTension transients during steady lengthening of tetanized muscle fibres of the frogComparison of energy output during ramp and staircase shortening in frog muscle fibresThe effect of hypertonicity on force generation in tetanized single fibres from frog skeletal muscleCross-bridge kinetics studied with staircase shortening in single fibres from frog skeletal muscleMechanical and energy characteristics during shortening in isolated type-1 muscle fibres from Xenopus laevis studied at maximal and submaximal activationChanges in conformation of myosin heads during the development of isometric contraction and rapid shortening in single frog muscle fibresThe mechanism of the force response to stretch in human skinned muscle fibres with different myosin isoformsStructural 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 fibresForce and number of myosin motors during muscle shortening and the coupling with the release of the ATP hydrolysis productsThe 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 motorThe 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 activation
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P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0001-6512-4897
@en
name
Marco Linari
@ast
Marco Linari
@en
Marco Linari
@es
Marco Linari
@nl
type
label
Marco Linari
@ast
Marco Linari
@en
Marco Linari
@es
Marco Linari
@nl
prefLabel
Marco Linari
@ast
Marco Linari
@en
Marco Linari
@es
Marco Linari
@nl
P106
P1153
6701813686
P21
P31
P496
0000-0001-6512-4897