Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments - Wikidata - wikimedia - TriplyDB

Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments

Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments

http://www.wikidata.org/entity/Q33983175

about

The Opitz syndrome gene product, MID1, associates with microtubules Vitamin C and Vitamin E for Alzheimer's Disease C-terminal region of MAP7 domain containing protein 3 (MAP7D3) promotes microtubule polymerization by binding at the C-terminal tail of tubulin Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments Curcumin and its derivatives: their application in neuropharmacology and neuroscience in the 21st century NMR Meets Tau: Insights into Its Function and Pathology The Metamorphic Nature of the Tau Protein: Dynamic Flexibility Comes at a Cost Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation Tau physiology and pathomechanisms in frontotemporal lobar degeneration Phosphorylation by neuronal cdc2-like protein kinase promotes dimerization of Tau protein in vitro Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics Staging of neurofibrillary degeneration caused by human tau overexpression in a unique cellular model of human tauopathy Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation The neuronal microtubule-associated protein tau is a substrate for caspase-3 and an effector of apoptosis Altered tubulin assembly dynamics with N-homocysteinylated human 4R/1N tau in vitro.Mutations in mitochondrial cytochrome c oxidase genes segregate with late-onset Alzheimer disease Nucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constants Three repeat isoforms of tau inhibit assembly of four repeat tau filaments A nucleated assembly mechanism of Alzheimer paired helical filaments.Quantitative characterization of heparin binding to Tau protein: implication for inducer-mediated Tau filament formation.TOC1: a valuable tool in assessing disease progression in the rTg4510 mouse model of tauopathy.Fibrillogenesis of tau: insights from tau missense mutations in FTDP-17.Tau aggregation into fibrillar polymers: taupathies.Fibrillization of human tau is accelerated by exposure to lead via interaction with His-330 and His-362.The role of dimerization in prion replication Oligomer formation of tau protein hyperphosphorylated in cells.RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments.Antioxidants as treatment for neurodegenerative disorders.Zinc binding directly regulates tau toxicity independent of tau hyperphosphorylation.Characterization of prefibrillar Tau oligomers in vitro and in Alzheimer disease.Inhibition of tau aggregation by a rosamine derivative that blocks tau intermolecular disulfide cross-linking.Understanding the kinetic roles of the inducer heparin and of rod-like protofibrils during amyloid fibril formation by Tau protein Secondary nucleating sequences affect kinetics and thermodynamics of tau aggregation.Tau assembly in inducible transfectants expressing wild-type or FTDP-17 tau.Free fatty acids stimulate the polymerization of tau and amyloid beta peptides. In vitro evidence for a common effector of pathogenesis in Alzheimer's disease.Using intramolecular disulfide bonds in tau protein to deduce structural features of aggregation-resistant conformations.An evolutionary roadmap to the microtubule-associated protein MAP Tau Small misfolded Tau species are internalized via bulk endocytosis and anterogradely and retrogradely transported in neurons.Complementary dimerization of microtubule-associated tau protein: Implications for microtubule bundling and tau-mediated pathogenesis.

P2860

Q22009027-7B3F21D3-16B9-4F99-8075-6FD0E04C1291 Q22241556-40C4A1DD-DC3E-43CA-BA62-F91DE26BCB8B Q24299178-631E1D61-4CE5-4A69-A529-1D8AC334DBF8 Q24598853-83EE6CC1-6D2B-4411-9B24-4D0457E36DBB Q24599152-53238ADB-71AC-4262-AAE3-65A06FE6DE49 Q24630927-E491D727-0D93-4E66-9B93-5CE3501B3A41 Q26747418-542C0D2D-2D53-401B-A403-278EF0540308 Q26772846-9AB9BE84-5ED4-451E-8E61-DB63B4E3CAAD Q27670453-C3382621-2282-4EA9-8DE3-E8C39D3E8A8F Q28070250-9F3E054D-2B1C-4179-A4EC-E33ED42605ED Q28253196-CB44A663-E991-47BA-8EC0-7401CD5379A5 Q28278995-6BD16631-586E-4CED-A95B-91EBE0C0B277 Q28345670-9D51F4DF-1F6D-4071-860B-87DD100D6CE8 Q28367378-D4F6C447-68D4-4041-A6DA-D06BF1216734 Q28610657-45705C32-0554-4A54-8C3E-FA4A8142F29B Q30422002-A875FDC2-8102-4F59-B6D2-944D06208E7D Q30454431-7CCCD325-FB20-43F1-99A8-B896658D9F9E Q30481896-DDFEDE9D-BDC8-4435-AF02-4F1F6F4337CF Q33593147-8F012EF0-B27A-4B65-A155-D8FF2ABBC9B8 Q33608410-50741B78-CB71-453A-826B-923B1ABDDB7F Q33666468-CAAF656F-9CF4-4C98-A745-6F18BFB04F36 Q33749435-50C8B252-B346-4A96-9B14-8F18B86BBB1D Q33750059-DB1447CC-373D-4C93-A944-77E8933B0AEF Q33957159-3F8CE387-347C-46E1-9CD7-E231D328F49A Q34037901-DCC393D2-5FBC-4648-8DAB-C029A3A0D799 Q34177517-D446EDBD-35F7-4723-9143-7C4BE4D958CD Q34634346-30913A23-695E-414B-9EFC-2DA54AF7A21F Q34737245-C675C85A-CC40-4001-9D14-CB2518C9B21B Q34974866-7432CC30-2D58-4E43-8D3E-BE6B971D5369 Q35012356-F7F3F457-C33F-4154-A071-7E49C48CECE3 Q35067755-CB9127F3-C9C6-4DDE-942D-AFADCCBD5EAE Q35185595-2ECAE746-B026-465A-8BDE-968321AE72EC Q35604223-23440F84-F00A-4126-ACF7-156EADE1863D Q35613197-0173C695-4D62-47F0-9F02-B52FABC8A501 Q35747827-8E494062-435D-4C11-B2DC-5F5A4D506214 Q35764771-D6828426-B6DB-417C-A601-170FEE024769 Q35842029-782650E4-32CA-45E2-ACDA-57FDD3C4720B Q35974613-F5A33AFC-A23E-4814-97F4-7A65CD6C57B9 Q36543778-B7B4DA62-6529-4E78-964A-B20C204514C7 Q36677242-405F6A1C-0A13-43AC-BFD3-67ABF6806378

P2860

Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments

http://www.wikidata.org/entity/Q33983175

description

1995 nî lūn-bûn

@nan

1995 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

name

Oxidation of cysteine-322 in t ...... ly of paired helical filaments

@ast

Oxidation of cysteine-322 in t ...... ly of paired helical filaments

@en

type

label

Oxidation of cysteine-322 in t ...... ly of paired helical filaments

@ast

Oxidation of cysteine-322 in t ...... ly of paired helical filaments

@en

prefLabel

Oxidation of cysteine-322 in t ...... ly of paired helical filaments

@ast

Oxidation of cysteine-322 in t ...... ly of paired helical filaments

@en

P1433

Q33983175-602D552C-642B-4BD9-A99C-C363DC20921E

P1476

Q33983175-2180D9A2-0282-44E2-9D31-18BD338FE39F

P2093

Q33983175-4BEA1ECF-87D0-4008-A0C8-514024D57B90

Q33983175-9838ADA0-4AE5-4D67-8B1B-004480ED8D65

Q33983175-A5E34C0E-0AEC-4DB6-852C-00F5DB051235

P2860

Q33983175-0759741B-EF7C-497B-8815-70235ACE357C

Q33983175-0DE10759-94B0-4731-BBEA-ABA5E305F0E5

Q33983175-1923BE7F-6C13-47CA-95B0-9206A10C051A

Q33983175-19583712-09FC-4ED1-900F-205AB688645D

Q33983175-1D55B6F1-7050-4E6D-807C-B96361E6DB89

Q33983175-1F630969-31B4-4E1B-A458-56687CFEE89C

Q33983175-20FB3428-AC68-45B9-8F59-639747D5A367

Q33983175-213409E1-CF5B-4B2A-9CD7-F47953BE85F7

Q33983175-2790EEE9-824F-40DA-9960-C0490F277985

Q33983175-4FD8872C-2F48-4CE8-8585-0260856A6B8B

P304

Q33983175-9C161CC3-2054-49A0-971C-4C9A9B5A1AC6

P31

Q33983175-51E417BD-CD21-421A-9909-A9EB49C2B15C

P356

Q33983175-50371FFD-7B55-461B-9E28-5DC5943EEF1C

P407

Q33983175-104B7F56-E472-42B6-990A-10D44F05AD8D

P433

Q33983175-B070D832-EDF0-4820-B9D6-39B50406F0D2

P478

Q33983175-A764A847-7EC9-4A0A-A1BD-2300E79CA16D

P50

Q33983175-71E8DD10-38DA-4C2E-A201-17DE830942DD

P577

Q33983175-760A52D9-CC93-4E8E-8C3F-7409420D12A4

P5875

Q33983175-771A2A59-43A7-4FB5-9ABB-74FF3747E261

P698

Q33983175-800B5179-CFD0-4E64-9557-B8FEA89D7B0C

P932

Q33983175-E0756A03-4E1C-4A6D-B524-96BD864A965E

P356

PNAS.92.18.8463

P1433

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

P1476

Oxidation of cysteine-322 in t ...... ly of paired helical filaments

@en

P2093

Biernat J

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

Mandelkow E

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

Schweers O

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

P2860

Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262

Tissue sulfhydryl groups

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis.

The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region

Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction.

Oxidative damage and mitochondrial decay in aging.

Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of beta-amyloid-mediated cell death

P304

8463-8467

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

P31

scholarly article

P356

10.1073/PNAS.92.18.8463

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

P407

P433

18

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

P478

92

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

P50

Eva-Maria Mandelkow

P577

1995-08-01T00:00:00Z

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

P5875

15532470

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

P698

7667312

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

P932

41177

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