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zeige Details Hall, Kirsten, Cole, Douglas G., ... Force–velocity relationships in kinesin-driven motility
in: Nature . - London [u.a.] : Nature Publising Group, ISSN 1476-4687, Vol. 364, No. 6436 (1993), p. 457-459
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1993
KINESIN is a microtubule-based motor protein that uses energy released from Mg–ATP hydrolysis to generate force for the movement of intracellular membranes towards the fast-growing (plus) ends of microtubule tracks in cells1. Kinesin-driven microtubule movement can be visualized and quantified using light microscope motility assays2–5 but our understanding of how kinesin generates force and motion is incomplete6. Here we report the use of a centrifuge microscope7,8 to obtain force–velocity curves for kinesin-driven motility and to estimate that the maximal isometric force generated per kinesin is 0.12 ± 0.03 pN per molecule.
beteiligte Personen: Hall, Kirsten , Cole, Douglas G. , Yeh, Yin , Scholey, Jonathan M. , Baskin, Ronald J.
Format: Elektronisch
Erschienen: 1993.
Serie: Nature Archives 1869 - 2007 [Dig. Serial]
Schlagwörter:
URL: http://dx.doi.org/10.1038/364457a0

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zeige Details Cohn, Stanley A., Ingold, Amie L., ... Correlation between the ATPase and microtubule translocating activities of sea urchin egg kinesin
in: Nature . - London [u.a.] : Nature Publising Group, ISSN 1476-4687, Vol. 328, No. 6126 (1987), p. 160-163
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zeige Details Scholey, J. M., Porter, M. E., ... Identification of kinesin in sea urchin eggs, and evidence for its localization in the mitotic spindle
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zeige Details Petrofsky, J. S., Phillips, C. A. The influence of recruitment order and fibre composition on the force-velocity relationship and fatiguability of skeletal muscles in the cat
in: Medical & biological engineering & computing , ISSN 1741-0444, Vol. 18 (4. 1980), p. 381-390
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