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We
are moving!
The Cross lab is
moving, together with the McAinsh and Straube labs, to Warwick
medical school, to found a new Centre for Mechanochemical
Cell Biology. We will move into temporary space at Warwick
at the start of February 2010, and subsequently move into a new
building, which we are currently designing. Our new centre will
address problems in the cell biology and biophysics of motorized
self-organization in cells. More soon! |
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> Article in 'Chart News', Oct 2009 |
Kinesins are nanometer-scale protein machines that move stepwise
along microtubules.
Some kinesins haul molecular cargo along microtubules, others crosslink
and slide microtubules and still others depolymerize microtubules.
These activities allow cells to self-organize, for example at cell division.
My colleagues and I believe in the power of basic scientific discovery
to advance medicine. By elucidating basic biological mechanisms, we aim
to engender and inform the development of new therapeutics.
Robert
Cross Group Leader
CV
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Eg-regious
Kase's review of the many faces of the Eg5
spindle motor.
Eprint
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EinMal
ist keinMal
Miho shows definitively that Mal3 inhibits
shrinkage and accelerates rescue - but does not affect catastrophe.
Eprint |
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Bundleworker
Marcus Braun (McAinsh
lab) showed that kinesin-14 actively sorts microtubules into
parallel bundles.
Eprint |
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Du
mal
Amedee des Georges discovered that Mal3,
a tip-tracking protein, changes microtubule
structure.
Eprint
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Eg
hop Kuniyoshi Kaseda found that Eg5, an essential
mitotic motor, can move by a hopping mechanism.
Eprint
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Kinesin's
ATP gate Maria Alonso showed that ATP binding triggers
kinesin steps by unmasking the leading head.
Eprint
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Kinesin
backsteps Nick Carter
used
single molecule optical trapping to show that kinesin can walk backwards.
Eprint |
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Twister
Jun Yajima showed that
microtubules moving over single-headed kinesins
spin around their long axis.
Eprint |
Last
edit 18 Oct 2009 |
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