kinesin


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kinesin

[kī′nēs·ən]
(cell and molecular biology)
An enzyme that hydrolyzes adenosine triphosphate to provide energy to power anterograde [from (-) to (+)] movement along microtubules.
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For their research, the scientists extracted microtubules from the brain tissue of cows, and mixed them kinesin - a protein that attaches to the microtubules - and adenosine triphosphate (ATP) - often called the "molecular unit of currency" of intracellular energy transfer.
The report provides comprehensive information on the Kinesin Spindle Protein (KSP or Eg5), targeted therapeutics, complete with analysis by indications, stage of development, mechanism of action (MoA), route of administration (RoA) and molecule type.
Louis, MO); MKLP1/KRP-110, a rabbit polyclonal anti-sea urchin kinesin (gift of Dr.
Turning natures' machinery on its head, the researchers used known techniques to glue the "shoulders" of kinesin motors to a glass substrate.
CENP-E is a mitotic kinesin directly involved in coupling the mechanics of mitosis with the mitotic checkpoint signaling machinery, regulating cell-cycle transition from metaphase to anaphase.
Since it had been already observed that in stable microtubules there is no possibility for tubulin bound nucleotide cycling, we propose that tubulin tail energase action releases the energy accumulated in metastable conformational states of kinesin, dynein, or phosphorylated MAPs.
Instead of having kinesin move around, the scientists anchored the molecules so that their heads would propel free microtubules through the channels, explains biophysicist Cees Dekker.
Tokyo, Japan, Jan 11, 2006 - (JCN) - Kyowa Hakko Kogyo announced on January 10 that it has signed a licensing agreement with US pharmaceutical company Eli Lilly on mitotic kinesin Eg5 inhibitor, Kyowa Hakko's proprietary compound for anti-tumor agents.
A kinesin like calmodulin binding protein (KCBP) is a unique microtubule motor protein originally discovered in flowering plants that contains two microtubule-binding sites, myosin tail homology, and a regulatory calcium/ calmodulin-binding domain.
These examples set the stage for a discussion of the motor protein kinesin, which moves along protein tracks called microtubules.
A physicist at the Georgia Institute of Technology, Atlanta, argues that what appears to be a walk along a microtubule for kinesin proteins is really random motion cleverly constrained by chemical switching carried out by adenosine triphosphate.
Several members of the kinesin motor family are selectively moving into axons, presumably guided by the specific organisation of the neuronal microtubule cytoskeleton.