Tau stabilizes microtubules by binding at the interface between tubulin heterodimers. - Wikidata - wikimedia - TriplyDB

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

http://www.wikidata.org/entity/Q35764234

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NMR Meets Tau: Insights into Its Function and Pathology The Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a Cost Misframed ubiquitin and impaired protein quality control: an early event in Alzheimer's disease Direct force measurements reveal that protein Tau confers short-range attractions and isoform-dependent steric stabilization to microtubules.Stabilizer-Guided Inhibition of Protein-Protein Interactions The Dark Matter of Biology Conserved Lysine Acetylation within the Microtubule-Binding Domain Regulates MAP2/Tau Family Members Rabies Virus Infection Induces Microtubule Depolymerization to Facilitate Viral RNA Synthesis by Upregulating HDAC6.Human cyclophilin 40 unravels neurotoxic amyloids.Targeting intrinsically disordered proteins in rational drug discovery.Tau-ism: The Yin and Yang of Microtubule Sliding, Detachment, and Rupture.Recent Advances in the Study of Bipolar/Rod-Shaped Microglia and their Roles in Neurodegeneration.Tau secretion is correlated to an increase of Golgi dynamics.Tau Binds to Multiple Tubulin Dimers with Helical Structure.Knockdown of Tubulin Polymerization Promoting Protein Family Member 3 Suppresses Proliferation and Induces Apoptosis in Non-Small-Cell Lung Cancer.Collapsin Response Mediator Protein-2 (CRMP2) is a Plausible Etiological Factor and Potential Therapeutic Target in Alzheimer's Disease: Comparison and Contrast with Microtubule-Associated Protein Tau Role of tau in the spatial organization of axonal microtubules: keeping parallel microtubules evenly distributed despite macromolecular crowding.A conceptual view at microtubule plus end dynamics in neuronal axons.A functional role for intrinsic disorder in the tau-tubulin complex.Presence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau's interaction with microtubules in axon-like processes.The Elephant in the Room: The Role of Microtubules in Cancer.Stability properties of neuronal microtubules.Protein phosphatase 2A inhibition and subsequent cytoskeleton reorganization contributes to cell migration caused by microcystin-LR in human laryngeal epithelial cells (Hep-2).Monoaminergic neuropathology in Alzheimer's disease.The Role of the Carboxyl-Terminal Sequence of Tau and MAP2 in the Pathogenesis of Dementia Signaling pathways and posttranslational modifications of tau in Alzheimer's disease: the humanization of yeast cells.Cerebrospinal Fluid Biomarkers in Alzheimer's Disease-From Brain Starch to Bench and Bedside.The Distance between N and C Termini of Tau and of FTDP-17 Mutants Is Modulated by Microtubule Interactions in Living Cells.Dysregulation of Microtubule Stability Impairs Morphofunctional Connectivity in Primary Neuronal Networks.Microtubules in health and degenerative disease of the nervous system.Oligomerization of the microtubule-associated protein tau is mediated by its N-terminal sequences: implications for normal and pathological tau action.Motifs in the tau protein that control binding to microtubules and aggregation determine pathological effects A validated antibody panel for the characterization of tau post-translational modifications.Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau.Probing the interaction of silver nanoparticles with tau protein and neuroblastoma cell line as nervous system models.Probing Conformational Dynamics of Tau Protein by Hydrogen/Deuterium Exchange Mass Spectrometry.Amyloidogenesis of Tau protein.Stabilization of dynamic microtubules by mDia1 drives Tau-dependent Aβ1-42 synaptotoxicity.Local Nucleation of Microtubule Bundles through Tubulin Concentration into a Condensed Tau Phase.Microtubule organization, dynamics and functions in differentiated cells.

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P2860

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

http://www.wikidata.org/entity/Q35764234

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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name

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

@ast

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

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type

label

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

@ast

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

@en

prefLabel

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

@ast

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

@en

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PNAS.1504081112

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers.

@en

P2093

Harindranath Kadavath

http://www.w3.org/2001/XMLSchema#string

Henning Urlaub

http://www.w3.org/2001/XMLSchema#string

Jacek Biernat

http://www.w3.org/2001/XMLSchema#string

Katharina Tepper

http://www.w3.org/2001/XMLSchema#string

Romina V Hofele

http://www.w3.org/2001/XMLSchema#string

Satish Kumar

http://www.w3.org/2001/XMLSchema#string

P2860

A protein factor essential for microtubule assembly

Tau protein binds to microtubules through a flexible array of distributed weak sites

Repeat motifs of tau bind to the insides of microtubules in the absence of taxol

Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

MAP2 and tau bind longitudinally along the outer ridges of microtubule protofilaments

Refined structure of alpha beta-tubulin at 3.5 A resolution

Structural insight into the inhibition of tubulin by vinca domain peptide ligands

High-Resolution Microtubule Structures Reveal the Structural Transitions in αβ-Tubulin upon GTP Hydrolysis

Structure of the alpha beta tubulin dimer by electron crystallography

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7501-7506

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scholarly article

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10.1073/PNAS.1504081112

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24

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112

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Eckhard Mandelkow

Markus Zweckstetter

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2015-06-01T00:00:00Z

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26034266

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4475932

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