Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
about
The low density lipoprotein receptor-related protein 6 interacts with glycogen synthase kinase 3 and attenuates activityUntangling tau imagingTau and tauopathiesMaintenance of synaptic stability requires calcium-independent phospholipase A₂ activityAcetylated tau destabilizes the cytoskeleton in the axon initial segment and is mislocalized to the somatodendritic compartment.Differential and regulated binding of cAMP-dependent protein kinase and protein kinase C isoenzymes to gravin in human model neurons: Evidence that gravin provides a dynamic platform for the localization for kinases during neuronal developmentPhosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau proteinTau-mediated neurodegeneration in Alzheimer's disease and related disordersTau phosphorylation regulates the interaction between BIN1's SH3 domain and Tau's proline-rich domainTyrosine phosphorylation of tau regulates its interactions with Fyn SH2 domains, but not SH3 domains, altering the cellular localization of tau.Hirano bodies differentially modulate cell death induced by tau and the amyloid precursor protein intracellular domain.Roles of tau protein in health and disease.The role of the lipid bilayer in tau aggregationStructure and pathology of tau protein in Alzheimer disease.Interplay between phosphorylation and palmitoylation mediates plasma membrane targeting and sorting of GAP43.Increased tau phosphorylation and impaired presynaptic function in hypertriglyceridemic ApoB-100 transgenic miceStrategies for diminishing katanin-based loss of microtubules in tauopathic neurodegenerative diseases.The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes.The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner.Roles of cholesterol and lipids in the etiopathogenesis of Alzheimer's disease.Expression of Tau40 induces activation of cultured rat microglial cells.Profiling murine tau with 0N, 1N and 2N isoform-specific antibodies in brain and peripheral organs reveals distinct subcellular localization, with the 1N isoform being enriched in the nucleus.Ectosomes: a new mechanism for non-exosomal secretion of tau protein.The Co-chaperone BAG2 Mediates Cold-Induced Accumulation of Phosphorylated Tau in SH-SY5Y Cells.The many faces of tauAnalysis of a membrane-enriched proteome from postmortem human brain tissue in Alzheimer's disease.Tau Hyperphosphorylation and Oxidative Stress, a Critical Vicious Circle in Neurodegenerative Tauopathies?Region-specific dendritic simplification induced by Aβ, mediated by tau via dysregulation of microtubule dynamics: a mechanistic distinct event from other neurodegenerative processes.Transgenic models of Alzheimer's disease: better utilization of existing models through viral transgenesis.The importance of tau phosphorylation for neurodegenerative diseasesAnesthesia-induced hyperphosphorylation detaches 3-repeat tau from microtubules without affecting their stability in vivo.The role of tau in neurodegenerationLeucine carboxyl methyltransferase 1 (LCMT1)-dependent methylation regulates the association of protein phosphatase 2A and Tau protein with plasma membrane microdomains in neuroblastoma cellsImmunotherapy targeting pathological tau protein in Alzheimer's disease and related tauopathies.Two novel Tau antibodies targeting the 396/404 region are primarily taken up by neurons and reduce Tau protein pathologyPresence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau's interaction with microtubules in axon-like processes.The mitotic tensegrity guardian tau protects mammary epithelia from katanin-like1-induced aneuploidy.Biochemical Distribution of Tau Protein in Synaptosomal Fraction of Transgenic Mice Expressing Human P301L Tau.The role of extracellular Tau in the spreading of neurofibrillary pathology.Membrane association and release of wild-type and pathological tau from organotypic brain slice cultures.
P2860
Q24299312-60235A03-7915-41DA-B7F2-4B0C72A41BE1Q26739091-61B7F847-FC1F-483D-856A-7E6AC161449AQ27027415-EC0DA72D-3881-4077-A303-646C61AA13D1Q27027705-9D684AB8-FD22-4C76-941B-33C564F5216BQ27301070-F4606946-28DB-4C79-A2EF-FA42445CEEC2Q28186760-0E90BE90-3F5D-4C88-BADC-130560BF1AE3Q28344418-FDA79D2C-F98C-41A8-9B31-6ACEDC8D1B88Q29618148-58BFDCC1-9403-4AB4-9157-B497A818C053Q30009097-EA822CF4-5E65-483C-AD12-FA46AF004BC9Q30010481-94EE57B0-C397-404E-8D7F-041E66D1D7C3Q31165645-B4E15ACC-4505-4144-9121-A205108B49E7Q33559303-7C4424C1-6194-405F-9769-16E95FFE361EQ33880243-8D50044A-0EE6-45AC-935E-65B95B7A08D9Q34280787-66552B20-A752-4AA4-A32E-4C45897A5F0FQ34428642-536DE5E6-906F-403D-AF3C-01570B06DC3AQ34430592-C1673C50-69B9-4624-A2CF-2875B027C569Q34505647-05A865A7-B37D-49FE-BB39-E7A145A19818Q34506434-8A671A9F-2811-4E24-9969-8C2BB2BEF5F6Q34600755-A3F34CE9-4260-412A-8723-D1A05AC2A5CCQ35016920-A25A96E7-732F-4C00-AD9E-00210A14D8D0Q35022620-2DAC06A0-8AC7-414C-BE89-099DBD2BFF52Q35081058-47DC843B-3503-4D66-B41D-BA13F6764D26Q35196319-1064A150-748B-48B1-B34A-D97611C194E8Q35712546-5C9BC589-1E6F-455C-AF45-86E267EE2F41Q35870359-F216A74B-493C-4116-96D2-196C1AA0D8B4Q35917235-386F050C-8AC7-47DE-980E-D56CB777E9EAQ36241505-6BD593CC-D20C-42FA-A9C5-9DB790D1E31FQ36252602-59C7050C-326B-4A31-91E9-F1646326FBD9Q36950042-E0691FAC-3D09-4002-9617-7C5892F96510Q36968220-533CF3F3-D251-4FF6-AACD-A57366838B36Q37029878-E095B254-9258-48CF-9098-C61000257B6FQ37145919-CBD85C4D-EF46-440F-96FA-23F6EF72D8FFQ37189534-F4116274-6F59-4DC0-A4F3-F043D3597309Q37308949-0DB6E330-C0EF-446B-97D0-0797521EFC89Q37311364-4483A636-E571-4751-91A2-92FF59A0F896Q37573270-09ED29C5-E09C-491E-B70C-7DA87D6EC0B2Q37619817-369AE5EE-E044-4EE0-A2CD-D8DFDB7BCADEQ37629345-D163003A-D137-42F0-8163-2184EE8C31D3Q37734856-403408BB-F8A2-4002-96BC-A2711F6BDE17Q37745627-E396D349-9C72-4542-852A-ECC6D26A8EF6
P2860
Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
description
2000 nî lūn-bûn
@nan
2000 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Interaction of tau with the ne ...... ed in paired helical filaments
@ast
Interaction of tau with the ne ...... ed in paired helical filaments
@en
Interaction of tau with the ne ...... ed in paired helical filaments
@en-gb
Interaction of tau with the ne ...... ed in paired helical filaments
@nl
type
label
Interaction of tau with the ne ...... ed in paired helical filaments
@ast
Interaction of tau with the ne ...... ed in paired helical filaments
@en
Interaction of tau with the ne ...... ed in paired helical filaments
@en-gb
Interaction of tau with the ne ...... ed in paired helical filaments
@nl
prefLabel
Interaction of tau with the ne ...... ed in paired helical filaments
@ast
Interaction of tau with the ne ...... ed in paired helical filaments
@en
Interaction of tau with the ne ...... ed in paired helical filaments
@en-gb
Interaction of tau with the ne ...... ed in paired helical filaments
@nl
P2093
P3181
P356
P1476
Interaction of tau with the ne ...... ed in paired helical filaments
@en
P2093
P304
P3181
P356
10.1074/JBC.M000389200
P407
P577
2000-05-26T00:00:00Z