In the last two decades, considerable progress has been made in the field of molecular
biology, which has enabled a molecular-level understanding of a number of interesting …

Various molecular cell biology and molecular genetic approaches have indicated significant
roles for kinesin superfamily proteins (KIFs) in intracellular transport and have shown that …

Allosteric modulation of protein function, wherein the binding of an effector to a protein
triggers conformational changes at distant functional sites, plays a central part in the control …

Motor proteins such as kinesin, myosin and polymerase convert chemical energy into work
through a cycle that involves nucleotide hydrolysis. Kinetic rates in the cycle that depend …

Kinesin-1 is a dimeric motor that transports cargo along microtubules, taking 8.2-nm steps in
a hand-over-hand fashion. The ATP hydrolysis cycles of its two heads are maintained out of …

This critical review was motivated by the 10th Biophysical Discussions meeting,''Molecular
Motors: Point Counterpoint'', held in Asilomar, CA, during October 19–22, 2006. Biophysical …

Kinesin advances 8 nm along a microtubule per ATP hydrolyzed, but the mechanism
responsible for coordinating the enzymatic cycles of kinesin's two identical motor domains …

The majority of active transport in the cell is driven by three classes of molecular motors: the
kinesin and dynein families that move toward the plus-end and minus-end of microtubules …

The dimeric motor protein kinesin-1 walks along microtubules by alternatingly hydrolyzing
ATP and moving two motor domains ('heads'). Nanometer-precision single-molecule studies …

Tubulin dimers assemble into dynamic microtubules, which are used by molecular motors as
tracks for intracellular transport. Organization and dynamics of the microtubule network are …