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| Home > Publications database > Structures of kinesin and kinesin–microtubule interactions > print |
| 001 | 390701 | ||
| 005 | 20250804155648.0 | ||
| 024 | 7 | _ | |a 10.1016/S0955-0674(99)80005-2 |2 doi |
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| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Mandelkow, Eckhard |0 P:(DE-H253)PIP1002054 |b 0 |e Corresponding author |
| 245 | _ | _ | |a Structures of kinesin and kinesin–microtubule interactions |
| 260 | _ | _ | |a Amsterdam [u.a.] |c 1999 |b Elsevier |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 500 | _ | _ | |a F-Bereich; Max-Planck-Gesellschaft |
| 520 | _ | _ | |a Several X-ray crystal structures of kinesin motor domains have recently been solved at high resolution (∼0.2–0.3 nm), in both their monomeric and dimeric states. They show the folding of the polypeptide chain and different arrangements of subunits in the dimer. In addition, cryo-electron microscopy and image reconstruction have revealed microtubules decorated with kinesin at intermediate resolution (∼2 nm), showing the distribution and orientation of kinesin heads on the microtubule surface. The comparison of the X-ray and electron microscopy results yields a model of how monomeric motor domains bind to the microtubule but the binding of dimeric motors, their stoichiometry, or the influence of nucleotides remains a matter of debate. |
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| 700 | 1 | _ | |a Hoenger, Andreas |0 P:(DE-HGF)0 |b 1 |e Corresponding author |
| 773 | _ | _ | |a 10.1016/S0955-0674(99)80005-2 |g Vol. 11, no. 1, p. 34 - 44 |0 PERI:(DE-600)2013029-6 |n 1 |p 34 - 44 |t Current opinion in cell biology |v 11 |y 1999 |x 0955-0674 |
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