Single-molecule analysis of the actomyosin motor using nano-manipulation

A Ishijima, Y Harada, H Kojima, T Funatsu… - Biochemical and …, 1994 - Elsevier
The elementary events in energy transduction by the actomyosin motor, driven by ATP
hydrolysis, were directly recorded from multiple and single molecules using a recently …

Harmonic force spectroscopy measures load-dependent kinetics of individual human β-cardiac myosin molecules

J Sung, S Nag, KI Mortensen, CL Vestergaard… - Nature …, 2015 - nature.com
Molecular motors are responsible for numerous cellular processes from cargo transport to
heart contraction. Their interactions with other cellular components are often transient and …

Right-handed rotation of an actin filament in an in vitro motile system

T Nishizaka, T Yagi, Y Tanaka, S Ishiwata - Nature, 1993 - nature.com
MUSCLE contraction occurs by mutual sliding between thick (myosin) and thin (actin)
filaments1, 2. But the physical and chemical properties of the sliding force are not clear; …

Biophysical properties of human β-cardiac myosin with converter mutations that cause hypertrophic cardiomyopathy

M Kawana, SS Sarkar, S Sutton, KM Ruppel… - Science …, 2017 - science.org
Hypertrophic cardiomyopathy (HCM) affects 1 in 500 individuals and is an important cause
of arrhythmias and heart failure. Clinically, HCM is characterized as causing …

The in vitro motility activity of β-cardiac myosin depends on the nature of the β-myosin heavy chain gene mutation in hypertrophic cardiomyopathy

G Cuda, L Fananapazir, ND Epstein… - Journal of Muscle …, 1997 - Springer
Several mutations in the β-myosin heavy chain gene cause hypertrophic cardiomyopathy.
This study investigates (1) the in vitro velocities of translocation of fluorescently-labelled …

Evidence that the head of kinesin is sufficient for force generation and motility in vitro

JT Yang, WM Saxton, RJ Stewart, EC Raff… - Science, 1990 - science.org
Kinesin is a mechanochemical protein that converts the chemical energy in adenosine
triphosphate into mechanical force for movement of cellular components along microtubules …

Quantized velocities at low myosin densities in an in vitro motility

TQP Uyeda, HM Warrick, SJ Kron, JA Spudich - Nature, 1991 - nature.com
An in vitro motility assay has been developed in which single actin filaments move on one or
a few heavy meromyosin (HMM) molecules. This movement is slower than when many HMM …

Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro.

K Collins, JR Sellers, P Matsudaira - The Journal of cell biology, 1990 - ncbi.nlm.nih.gov
kD-calmodulin, when immobilized on nitrocellulose-coated coverslips, translocates actin
filaments at a maximal rate of 0.07-0.1 micron/s at 37 degrees C. Actin activates MgATPase …

The three-dimensional structure of a molecular motor

I Rayment, HM Holden - Trends in biochemical sciences, 1994 - cell.com
Myosin is one of only three proteins known to convert chemica! energy into mechanical
work. Although the chemical, kinetic and physiological characteristics of this protein have …

Chemo-mechanical energy transduction in relation to myosin isoform composition in skeletal muscle fibres of the rat.

C Reggiani, EJ Potma, R Bottinelli… - The Journal of …, 1997 - ncbi.nlm.nih.gov
ATP consumption and force development were determined in single skinned muscle fibres
of the rat at 12 degrees C. Myofibrillar ATPase consumption was measured photometrically …