Cytoplasmic dynein binding, run length, and velocity are guided by long-range electrostatic interactions
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Forces and Disease: Electrostatic force differences caused by mutations in kinesin motor domains can distinguish between disease-causing and non-disease-causing mutations.Allosteric conformational change cascade in cytoplasmic dynein revealed by structure-based molecular simulations.DelPhiForce, a tool for electrostatic force calculations: Applications to macromolecular binding.E-hooks provide guidance and a soft landing for the microtubule binding domain of dynein
P2860
Cytoplasmic dynein binding, run length, and velocity are guided by long-range electrostatic interactions
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2016 nî lūn-bûn
@nan
2016 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2016年の論文
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年学术文章
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2016年學術文章
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name
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@ast
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@en
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@nl
type
label
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@ast
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@en
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@nl
prefLabel
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@ast
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@en
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@nl
P2860
P3181
P356
P1433
P1476
Cytoplasmic dynein binding, ru ...... nge electrostatic interactions
@en
P2093
P2860
P2888
P3181
P356
10.1038/SREP31523
P407
P50
P577
2016-08-17T00:00:00Z
P6179
1005545113