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in press. Shows that the nucleotide hydrolysis cycle of kinesin can be uncoupled from motility by mutating conserved residues at the neck-core interface of kinesin. On the basis of extensive mutagenesis analyses, the paper proposes that the neck-core interface acts as a critical mechanical transducer for kinesin motility.
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Case R.B., Rice S., Hart C.L., Vale R.D. Role of the kinesin neck linker and catalytic core in microtubule based motility. Curr Biol. 2000;. in press. Shows that the nucleotide hydrolysis cycle of kinesin can be uncoupled from motility by mutating conserved residues at the neck-core interface of kinesin. On the basis of extensive mutagenesis analyses, the paper proposes that the neck-core interface acts as a critical mechanical transducer for kinesin motility.
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(2000)
Curr Biol
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Case, R.B.1
Rice, S.2
Hart, C.L.3
Vale, R.D.4
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50
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0033576727
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A structural change in the kinesin motor that drives motility
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The authors used four independent methods to visualize large conformational changes of the neck linker in kinesin. Using electron paramagnetic resonance, fluoresence resonance energy transfer, pre-steady state kinetics, and cryo-electron microscopy, the authors demonstrate that the neck linker becomes immobilized and extended towards the microtubule plus end when kinesin binds to the microtubule and ATP. The neck linker reverts to a more mobile conformation when γ-phosphate is released after nucleotide hydrolysis. This conformational change explains the direction of kinesin motion as well as processive movement by the kinesin dimer.
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Rice S., Lin A.W., Safer D., Hart C.H., Naber N., Carragher B.O., Cain S.M., Pechatnikowa E., Wilson-Kubalek E.M., Pate E.et al. A structural change in the kinesin motor that drives motility. Nature. 402:1999;778-784. The authors used four independent methods to visualize large conformational changes of the neck linker in kinesin. Using electron paramagnetic resonance, fluoresence resonance energy transfer, pre-steady state kinetics, and cryo-electron microscopy, the authors demonstrate that the neck linker becomes immobilized and extended towards the microtubule plus end when kinesin binds to the microtubule and ATP. The neck linker reverts to a more mobile conformation when γ-phosphate is released after nucleotide hydrolysis. This conformational change explains the direction of kinesin motion as well as processive movement by the kinesin dimer.
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(1999)
Nature
, vol.402
, pp. 778-784
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Rice, S.1
Lin, A.W.2
Safer, D.3
Hart, C.H.4
Naber, N.5
Carragher, B.O.6
Cain, S.M.7
Pechatnikowa, E.8
Wilson-Kubalek, E.M.9
Pate, E.10
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51
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0032550175
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Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: Comparison with X-ray structure and implications for motility
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Hoenger A., Sack S., Thormahlen M., Marx A., Muller J., Gross H., Mandelkow E. Image reconstructions of microtubules decorated with monomeric and dimeric kinesins: comparison with X-ray structure and implications for motility. J Cell Biol. 141:1998;419-430.
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(1998)
J Cell Biol
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Hoenger, A.1
Sack, S.2
Thormahlen, M.3
Marx, A.4
Muller, J.5
Gross, H.6
Mandelkow, E.7
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52
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0344867017
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Congruent docking of dimeric kinesin and ncd into three-dimensional electron cryomicroscopy maps of microtubule-motor ADP complexes
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All atomic resolution structures of kinesin motors are available only with ADP (the product of ATP hydrolysis) bound in their active sites. However, most electron microscopy studies of motor-microtubule complexes have been performed in the presence of a non-hydrolyzable analog of ATP (AMPPNP) that induces strong binding of motors to microtubules. The authors of this paper present maps of microtubules decorated by dimeric kinesin and ncd in the presence of ADP. Although the proposed alternative docking of the crystal structures of kinesin and ncd dimers into the new maps disagrees with the results presented in this review, the discrepancy reflects objective challenges of the docking procedure.
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Hirose K., Lowe J., Alonso M., Cross R., Amos L.A. Congruent docking of dimeric kinesin and ncd into three-dimensional electron cryomicroscopy maps of microtubule-motor ADP complexes. Mol Biol Cell. 10:1999;2063-2074. All atomic resolution structures of kinesin motors are available only with ADP (the product of ATP hydrolysis) bound in their active sites. However, most electron microscopy studies of motor-microtubule complexes have been performed in the presence of a non-hydrolyzable analog of ATP (AMPPNP) that induces strong binding of motors to microtubules. The authors of this paper present maps of microtubules decorated by dimeric kinesin and ncd in the presence of ADP. Although the proposed alternative docking of the crystal structures of kinesin and ncd dimers into the new maps disagrees with the results presented in this review, the discrepancy reflects objective challenges of the docking procedure.
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(1999)
Mol Biol Cell
, vol.10
, pp. 2063-2074
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Hirose, K.1
Lowe, J.2
Alonso, M.3
Cross, R.4
Amos, L.A.5
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53
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0032780181
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Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
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Wriggers W., Milligan R.A., McCammon J.A. Situs: A package for docking crystal structures into low-resolution maps from electron microscopy. J Struct Biol. 125:1999;185-195.
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J Struct Biol
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Wriggers, W.1
Milligan, R.A.2
McCammon, J.A.3
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54
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Role of the kinesin neck region in processive microtubule-based motility
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Romberg L., Pierce D.W., Vale R.D. Role of the kinesin neck region in processive microtubule-based motility. J Cell Biol. 140:1998;1407-1416.
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(1998)
J Cell Biol
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Romberg, L.1
Pierce, D.W.2
Vale, R.D.3
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55
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0031041380
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Monomeric kinesin head domains hydrolyze multiple ATP molecules before release from a microtubule
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Jiang W., Hackney D.D. Monomeric kinesin head domains hydrolyze multiple ATP molecules before release from a microtubule. J Biol Chem. 272:1997;5616-5621.
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Jiang, W.1
Hackney, D.D.2
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56
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One-headed kinesin derivatives move by a nonprocessive, low-duty ratio mechanism unlike that of two-headed kinesin
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Young E.C., Mahtani H.K., Gelles J. One-headed kinesin derivatives move by a nonprocessive, low-duty ratio mechanism unlike that of two-headed kinesin. Biochemistry. 37:1998;3467-3479.
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Biochemistry
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Young, E.C.1
Mahtani, H.K.2
Gelles, J.3
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57
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Processivity of the motor protein kinesin requires two heads
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Hancock W.O., Howard J. Processivity of the motor protein kinesin requires two heads. J Cell Biol. 140:1998;1395-1405.
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J Cell Biol
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Hancock, W.O.1
Howard, J.2
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Engineering a lever arm into kinesin neck
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Mazumdar M., Cross R.A. Engineering a lever arm into kinesin neck. J Biol Chem. 273:1998;29352-29359.
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J Biol Chem
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The structural and mechanical cycle of kinesin
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Mandelkow E., Johnson K.A. The structural and mechanical cycle of kinesin. Trends Biol Sci. 23:1998;429-434.
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Trends Biol Sci
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Johnson, K.A.2
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Structure of kinesin and kinesin-microtubule complexes
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Mandelkow E., Hoenger A. Structure of kinesin and kinesin-microtubule complexes. Curr Opin Cell Biol. 11:1999;34-44.
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Structure of the αβ tubulin dimer by electron crystallography
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Nogales E., Wolf S.G., Downing K.H. Structure of the αβ tubulin dimer by electron crystallography. Nature. 391:1998;199-203.
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(1998)
Nature
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Nogales, E.1
Wolf, S.G.2
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Tubulin structure: Insights into microtubule properties and functions
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Downing K.H., Nogales E. Tubulin structure: insights into microtubule properties and functions. Curr Opin Struct Biol. 8:1998;785-791.
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Curr Opin Struct Biol
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Downing, K.H.1
Nogales, E.2
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65
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0033534629
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High-resolution model of the microtubule
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Describes a high-resolution model of the microtubule that has been obtained by docking the crystal structure of a tubulin protofilament into a 20 Å map of the microtubule. The model establishes the position of the different structural elements of tubulin with respect to the inside, outside, and plus and minus ends of the microtubule. It also provides a structural rationalization for a variety of the microtubules properties, in particular, as cellular tracks for motor proteins.
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Nogales E., Whittaker M., Milligan R.A., Downing K.H. High-resolution model of the microtubule. Cell. 96:1999;79-88. Describes a high-resolution model of the microtubule that has been obtained by docking the crystal structure of a tubulin protofilament into a 20 Å map of the microtubule. The model establishes the position of the different structural elements of tubulin with respect to the inside, outside, and plus and minus ends of the microtubule. It also provides a structural rationalization for a variety of the microtubules properties, in particular, as cellular tracks for motor proteins.
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(1999)
Cell
, vol.96
, pp. 79-88
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Nogales, E.1
Whittaker, M.2
Milligan, R.A.3
Downing, K.H.4
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66
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0033582814
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A processive single-headed motor: Kinesin superfamily protein KIF1A
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This is the first and only report in which the processivity of a single-headed kinesin construct has been demonstrated. A recombinant chimeric construct of the motor domain of KIF1A, a member of the unc104/KIF1A family of monomeric kinesins, is shown to move processively along the microtubule for more than one micrometer. The movement was stochastic and fitted a biased Brownian movement model.
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Okada Y., Hirokawa N. A processive single-headed motor: kinesin superfamily protein KIF1A. Science. 283:1999;152-157. This is the first and only report in which the processivity of a single-headed kinesin construct has been demonstrated. A recombinant chimeric construct of the motor domain of KIF1A, a member of the unc104/KIF1A family of monomeric kinesins, is shown to move processively along the microtubule for more than one micrometer. The movement was stochastic and fitted a biased Brownian movement model.
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(1999)
Science
, vol.283
, pp. 152-157
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Okada, Y.1
Hirokawa, N.2
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