The widespread use of controlled molecular‐level motion in key natural processes suggests that great rewards could come from bridging the gap between the present generation of …
Do biological motors move with regular steps? To address this question, we constructed instrumentation with the spatial and temporal sensitivity to resolve movement on a molecular …
JT Finer, RM Simmons, JA Spudich - Nature, 1994 - nature.com
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 …
H Noji, R Yasuda, M Yoshida, K Kinosita Jr - Nature, 1997 - nature.com
Cells employ a variety of linear motors, such as myosin1–3, kinesin4 and RNA polymerase5, which move along and exert force on a filamentous structure. But only one rotary motor has …
AM Gordon, E Homsher, M Regnier - Physiological reviews, 2000 - journals.physiology.org
Ca2+ regulation of contraction in vertebrate striated muscle is exerted primarily through effects on the thin filament, which regulate strong cross-bridge binding to actin. Structural …
Myosin V is a dimeric molecular motor that moves processively on actin, with the center of mass moving∼ 37 nanometers for each adenosine triphosphate hydrolyzed. We have …
T Ha, P Tinnefeld - Annual review of physical chemistry, 2012 - annualreviews.org
Single-molecule fluorescence spectroscopy and super-resolution microscopy are important elements of the ongoing technical revolution to reveal biochemical and cellular processes in …
The application of single-molecule fluorescence techniques to complex biological systems places demands on the performance of single fluorophores. We present an enzymatic …
T Funatsu, Y Harada, M Tokunaga, K Saito, T Yanagida - Nature, 1995 - nature.com
VISUALIZATION of single actin filaments by fluorescence microscopy1led to the development of new in vitro assays for analysing actomyosin-based motility at the molecular …