Tau mutants bind tubulin heterodimers with enhanced affinity.
about
Folding of the Tau Protein on MicrotubulesTau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeatsTau Aggregation Propensity Engrained in Its Solution State.Tau Binds to Multiple Tubulin Dimers with Helical Structure.Katanin Severing and Binding Microtubules Are Inhibited by Tubulin Carboxy TailsA functional role for intrinsic disorder in the tau-tubulin complex.Inferring Mechanistic Parameters from Amyloid Formation Kinetics by Approximate Bayesian Computation.The Distance between N and C Termini of Tau and of FTDP-17 Mutants Is Modulated by Microtubule Interactions in Living Cells.Oligomerization of the microtubule-associated protein tau is mediated by its N-terminal sequences: implications for normal and pathological tau action.IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies.Distinct differences in prion-like seeding and aggregation between tau protein variants provide mechanistic insights into tauopathies.Revealing Conformational Variants of Solution-Phase Intrinsically Disordered Tau Protein at the Single-Molecule Level.Conformational Heterogeneity and FRET Data Interpretation for Dimensions of Unfolded Proteins.HDAC6 and RhoA are novel players in Abeta-driven disruption of neuronal polarity.Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles.Heterogeneous Tau-Tubulin Complexes Accelerate Microtubule Polymerization.Quarterly intrinsic disorder digest (April-May-June, 2014).Structural evaluations of tau protein conformation: methodologies and approaches.Imbalanced Expression of Tau and Tubulin Induces Neuronal Dysfunction in C. elegans Models of Tauopathy.
P2860
Q27701048-713A65D5-092D-4966-8CAF-C703E7AB453FQ34203739-04B2F0D9-A9EB-42BF-95FE-41D6AF77E5A5Q36282762-16ACD989-E485-4CDC-8395-139A489C3795Q36420845-C8BC6F30-7988-4DFF-8943-3810C17E4207Q36426507-02C62917-858B-4E59-9EE6-77DFA0417CE2Q37514847-62C7FDBF-A205-4DEA-B659-369C17CA3CE9Q38905586-FE53D441-4F53-4073-8BB7-69A5BDABA1F6Q40990185-A99340FE-5CEE-40E6-9704-B5E925F50F6BQ42575598-2AB9B1B2-C3D6-4FBE-8241-C335325863A5Q47227239-410C993F-4942-4356-BAB8-6C5A6AF77B21Q47273210-93613ACE-BE08-4FD8-B089-CE36358662FCQ47611682-2FA7F959-5A19-4DAA-B63C-5DD04556B3F4Q47698068-34D22582-1212-455A-B859-DBD3A68C3443Q48769009-620014D7-F66F-485F-928E-C12DF2A184D8Q49787664-254744E4-2AA5-4D9C-B085-F4AE9CCA9DD5Q50573557-837F88FC-B032-424E-AE25-6458DEBB7C46Q50787059-65514F2E-0098-4731-8C25-66CAF052B2F1Q51104104-43F7EA4D-685E-4B7E-B88A-002E2D44E7B4Q55401909-F7173757-C875-4D69-B628-5E6941C673AE
P2860
Tau mutants bind tubulin heterodimers with enhanced affinity.
description
2014 nî lūn-bûn
@nan
2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Tau mutants bind tubulin heterodimers with enhanced affinity.
@ast
Tau mutants bind tubulin heterodimers with enhanced affinity.
@en
type
label
Tau mutants bind tubulin heterodimers with enhanced affinity.
@ast
Tau mutants bind tubulin heterodimers with enhanced affinity.
@en
prefLabel
Tau mutants bind tubulin heterodimers with enhanced affinity.
@ast
Tau mutants bind tubulin heterodimers with enhanced affinity.
@en
P2093
P2860
P356
P1476
Tau mutants bind tubulin heterodimers with enhanced affinity.
@en
P2093
Elizabeth Rhoades
Garrett Cobb
Shana Elbaum-Garfinkle
P2860
P304
P356
10.1073/PNAS.1315983111
P407
P577
2014-04-14T00:00:00Z