Electrostatically biased binding of kinesin to microtubules
about
Modeling protein association mechanisms and kineticsA second tubulin binding site on the kinesin-13 motor head domain is important during mitosisAltered nucleotide-microtubule coupling and increased mechanical output by a kinesin mutantCytoplasmic dynein binding, run length, and velocity are guided by long-range electrostatic interactionsStructure-based molecular simulations reveal the enhancement of biased Brownian motions in single-headed kinesinMultiscale method for modeling binding phenomena involving large objects: application to kinesin motor domains motion along microtubules.Reversal of axonal growth defects in an extraocular fibrosis model by engineering the kinesin-microtubule interface.AvrBsT acetylates Arabidopsis ACIP1, a protein that associates with microtubules and is required for immunityDNA Polymerase Conformational Dynamics and the Role of Fidelity-Conferring Residues: Insights from Computational SimulationsThe family-specific K-loop influences the microtubule on-rate but not the superprocessivity of kinesin-3 motors.Distinct mechanisms of a phosphotyrosyl peptide binding to two SH2 domainsMapping the structural and dynamical features of multiple p53 DNA binding domains: insights into loop 1 intrinsic dynamics.Rab6 regulation of the kinesin family KIF1C motor domain contributes to Golgi tethering.Theory of active transport in filopodia and stereocilia.Mapping the Processivity Determinants of the Kinesin-3 Motor Domain.Displacement-weighted velocity analysis of gliding assays reveals that Chlamydomonas axonemal dynein preferentially moves conspecific microtubulesMapping the structural and dynamical features of kinesin motor domainsKinesin-1 motors can circumvent permanent roadblocks by side-shifting to neighboring protofilaments.Forces and Disease: Electrostatic force differences caused by mutations in kinesin motor domains can distinguish between disease-causing and non-disease-causing mutations.Maximum power operation of interacting molecular motors.Suspended microtubules demonstrate high sensitivity and low experimental variability in kinesin bead assay.Kinesin rotates unidirectionally and generates torque while walking on microtubules.Protein-protein association rates captured in a single geometric parameter.Biosensing MAPs as "roadblocks": kinesin-based functional analysis of tau protein isoforms and mutants using suspended microtubules (sMTs).Precision knockdown of EGFR gene expression using radio frequency electromagnetic energy.Parsing the roles of neck-linker docking and tethered head diffusion in the stepping dynamics of kinesin.
P2860
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P2860
Electrostatically biased binding of kinesin to microtubules
description
2011 nî lūn-bûn
@nan
2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Electrostatically biased binding of kinesin to microtubules
@ast
Electrostatically biased binding of kinesin to microtubules
@en
Electrostatically biased binding of kinesin to microtubules
@nl
type
label
Electrostatically biased binding of kinesin to microtubules
@ast
Electrostatically biased binding of kinesin to microtubules
@en
Electrostatically biased binding of kinesin to microtubules
@nl
prefLabel
Electrostatically biased binding of kinesin to microtubules
@ast
Electrostatically biased binding of kinesin to microtubules
@en
Electrostatically biased binding of kinesin to microtubules
@nl
P2093
P2860
P50
P3181
P1433
P1476
Electrostatically biased binding of kinesin to microtubules
@en
P2093
Dana M Gheorghe
Gary Huber
J Andrew McCammon
Maciej Dlugosz
Maria Alonso
P2860
P304
P3181
P356
10.1371/JOURNAL.PBIO.1001207
P407
P577
2011-11-29T00:00:00Z