The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner. - Wikidata - wikimedia - TriplyDB

The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner.

The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner.

http://www.wikidata.org/entity/Q34600755

about

Frontotemporal lobar degeneration: old knowledge and new insight into the pathogenetic mechanisms of tau mutations Physiological and pathological phosphorylation of tau by Cdk5 Tau mutant A152T, a risk factor for FTD/PSP, induces neuronal dysfunction and reduced lifespan independently of aggregation in a C. elegans Tauopathy model Tau physiology and pathomechanisms in frontotemporal lobar degeneration Tau Biology and Tau-Directed Therapies for Alzheimer's Disease Rapid changes in phospho-MAP/tau epitopes during neuronal stress: cofilin-actin rods primarily recruit microtubule binding domain epitopes mTOR and neuronal cell cycle reentry: How impaired brain insulin signaling promotes Alzheimer's disease.Single-molecule tracking of tau reveals fast kiss-and-hop interaction with microtubules in living neurons Hirano bodies differentially modulate cell death induced by tau and the amyloid precursor protein intracellular domain.Roles of tau protein in health and disease.RNA protein granules modulate tau isoform expression and induce neuronal sprouting Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats Interplay between phosphorylation and palmitoylation mediates plasma membrane targeting and sorting of GAP43.Extracellular α-synuclein leads to microtubule destabilization via GSK-3β-dependent Tau phosphorylation in PC12 cells Pseudohyperphosphorylation has differential effects on polymerization and function of tau isoforms.Optical highlighter molecules in neurobiology.An evolutionary roadmap to the microtubule-associated protein MAP Tau Region-specific dendritic simplification induced by Aβ, mediated by tau via dysregulation of microtubule dynamics: a mechanistic distinct event from other neurodegenerative processes.NMDA receptor subunit composition determines beta-amyloid-induced neurodegeneration and synaptic loss.Identification of Novel Tau Interactions with Endoplasmic Reticulum Proteins in Alzheimer's Disease Brain.Mobility and subcellular localization of endogenous, gene-edited Tau differs from that of over-expressed human wild-type and P301L mutant Tau Annexin A2 system in human biology: cell surface and beyond.Presence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau's interaction with microtubules in axon-like processes.Astrocyte pathology in a human neural stem cell model of frontotemporal dementia caused by mutant TAU protein.Biochemistry and cell biology of tau protein in neurofibrillary degeneration Microglia: an active player in the regulation of synaptic activity.Protein phosphorylation in neurodegeneration: friend or foe?Is membrane homeostasis the missing link between inflammation and neurodegenerative diseases?Chronic consumption of Annona muricata juice triggers and aggravates cerebral tau phosphorylation in wild-type and MAPT transgenic mice.Microtubule dynamics and the neurodegenerative triad of Alzheimer's disease: The hidden connection.Signaling pathways and posttranslational modifications of tau in Alzheimer's disease: the humanization of yeast cells.Quantitative and combinatory determination of in situ phosphorylation of tau and its FTDP-17 mutants.A refined reaction-diffusion model of tau-microtubule dynamics and its application in FDAP analysis.Structural transitions in tau k18 on micelle binding suggest a hierarchy in the efficacy of individual microtubule-binding repeats in filament nucleation.Tau phosphorylation affects its axonal transport and degradation.FTDP-17 tau mutations induce distinct effects on aggregation and microtubule interactions.Derailed intraneuronal signalling drives pathogenesis in sporadic and familial Alzheimer's disease.Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes.Can numerical modeling help understand the fate of tau protein in the axon terminal?Extracellular Tau and Its Potential Role in the Propagation of Tau Pathology.

P2860

e0caa8c89d8a527290d7d428550b211d4ddc334c

P248

Q26777247-D514B1FA-0208-468B-93E6-C083E299DDA2 Q26860395-2442A6A9-0DF9-42FB-B993-11043ED7CCD9 Q27301090-9CE9536A-77A4-424A-8520-2CEF9CC84DD4 Q28070250-BADDC877-F185-4487-B5FB-3ACC365638FF Q28071398-666DC1D7-B3EA-4FC9-84E0-EFBD0E8F0427 Q28478846-C32E6073-AA30-4CE0-AA28-0CCEE4E6E317 Q30275585-70E3A11B-F880-412D-B7A1-DDFD96540FB1 Q30597670-2545E11B-FF9A-4098-9547-E83479A7C8D1 Q31165645-865C6C14-8B67-47D3-BE55-E15CAC932D6C Q33559303-B87BEF50-2881-4128-9BE4-EB532EAC87EA Q33761207-0052C76D-C9E3-4127-A590-36EED2780D80 Q34203739-6D7257E0-7992-4EE4-B453-94874997FAE4 Q34428642-D9B98E89-83E5-4699-AB5D-0A2B07FCE766 Q35144986-5479DA8D-F4F9-4B6B-9B37-3D4879DF2726 Q35575041-12A74F3C-EC88-4157-9DC2-2A67E1125AA2 Q35803285-EB94F359-1B20-4225-8EE5-A7FD4EE4B896 Q35974613-5DE11F30-4100-4629-9FAD-92A5DF0BD12E Q36252602-28181456-D214-4641-B8D2-52DAADC9AA87 Q36809558-E8E41EED-24BB-42EF-BA34-67D8FB210857 Q36939900-9A865BA8-976A-4FE3-89B3-07FAAB3CCDA0 Q37064222-AD6EC565-51FF-4020-AE14-116FB93694ED Q37406212-4B3C2E33-67E3-4D33-9DFA-4F43EC96FBBA Q37573270-AD5BB868-2F9C-48F9-B7D4-1CB815043F11 Q37678874-4FABAEB7-AD71-47D8-B1E5-65DEA768A2C7 Q38023859-8D12365C-EFF0-4200-9CCB-ABA582DE5AE0 Q38168519-63D23397-E32C-4D47-BE48-0E8E3838DD9A Q38214594-3EFDC7C6-3ACC-4D72-84A3-5558481AA008 Q38592446-0467D9B6-1953-49FF-BF97-3C701E074493 Q38749513-C402DEA4-AB8E-4091-BDA2-D708F2C61D3F Q39165865-F49D6423-5E7E-4BBA-9CB7-91B00F7E460E Q39208164-9CE6157A-3594-458A-8420-35079C00EEFD Q41117848-80DC91D3-1E75-4DA4-BC71-3873B76D7C33 Q41734408-F51C8167-2626-471D-8BFA-078F6A45FC9F Q42157648-C567B771-A229-4632-A89B-82A83E7C6F28 Q42160128-2E85C113-C8B1-4D40-BD72-A8393AF40ED6 Q42836387-7A83A059-220C-470C-947D-3E614DC94D44 Q42872730-F15D855E-3358-4F5B-B460-672BEE431956 Q44441688-C479AF7B-B7B9-4E48-AE09-6C4CD3BC2E0B Q44877131-ECE59CE7-2616-4366-B5DA-B1890818107B Q47139411-79B2C6FD-779F-4C7F-B4EA-2955E2C2446F

P2860

The frontotemporal dementia mutation R406W blocks tau's interaction with the membrane in an annexin A2-dependent manner.

http://www.wikidata.org/entity/Q34600755

description

2011 nî lūn-bûn

@nan

2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի փետրվարին 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

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@ast

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@en

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@nl

type

label

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@ast

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@en

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@nl

prefLabel

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@ast

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@en

The frontotemporal dementia mu ...... n annexin A2-dependent manner.

@nl

P1433

Q34600755-5CFA7E3A-826B-475A-8C3D-88B526EAD270

P1476

Q34600755-AF712646-D6AF-4522-9282-8D260217658F

P2093

Q34600755-181A394E-6577-4013-9526-1C54FEF498B9

Q34600755-5F5D032C-16B6-4236-802F-8D12AC1E1F7A

Q34600755-6901D056-3305-4985-B218-C6A9192B7BE6

Q34600755-9B3B4951-A0FA-420E-ADB0-8C2796282469

Q34600755-B3342EAF-ED41-48C1-BF5C-27575A6D40F8

Q34600755-BC8009B5-2BDF-4D75-AA04-A52632D69F97

Q34600755-D3867E78-E7C6-45DE-9EE7-4904283763ED

P2860

Q34600755-06F0B3DB-9B48-493E-AF43-D870800051AD

Q34600755-0BA6C48C-A511-4A93-90A0-C6A43885A785

Q34600755-0CEEB6AC-E083-4929-BEEF-44386275CCFC

Q34600755-0EA750F0-49EE-41C6-83E3-B98D114D5EA9

Q34600755-27C06F97-6F8F-495F-B2D2-ABC780AC7FEB

Q34600755-27E718D7-0AF1-4A33-A59F-899BA50D61B8

Q34600755-28ECF686-EDBB-4046-833A-EA255C47BFFE

Q34600755-2D8883A4-08FE-48FB-BFFC-32EF9194AF9F

Q34600755-33539C7B-7B63-4365-88BA-63754A35F37C

Q34600755-3942618B-1987-4B07-99B6-664641065FE4

P304

Q34600755-EC0B029A-7A1A-4BC4-B97C-088380C8CD45

P31

Q34600755-D070F168-2FE3-4420-95E8-D4DF2DE1708C

P356

Q34600755-B26D9651-F42E-46D0-A957-F82770C1915B

P407

Q34600755-CDC378D2-9CBD-4A53-AFCF-4696B20E4B7D

P433

Q34600755-DB87CE62-FB87-4288-B3D3-F48344CF3941

P478

Q34600755-2EBBA3DE-B84A-431A-92EB-04F5A6811073

P50

Q34600755-FB9FA735-F564-4C60-888A-D868E3711D61

P577

Q34600755-6D0734A8-1530-4C66-8A51-65E1A8508A1C

P5875

Q34600755-771EDA2D-D618-4921-92C6-15111B7362E7

P698

Q34600755-081DD412-DCE7-414A-B479-9CCC26F5E12E

P932

Q34600755-5C4CA8C7-7EF8-448F-B8B3-085202144542

P356

P1433

Journal of Cell Biology

P1476

The frontotemporal dementia mu ...... an annexin A2-dependent manner

@en

P2093

Anne Gauthier-Kemper

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

Carina Weissmann

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

Jürgen J Heinisch

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

Nataliya Golovyashkina

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

Roland Brandt

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

Volker Gerke

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

Zsofia Sebö-Lemke

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

P2860

Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments

Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network

Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain

Analysis of binding reactions by fluorescence recovery after photobleaching

Phosphorylation-mimicking glutamate clusters in the proline-rich region are sufficient to simulate the functional deficiencies of hyperphosphorylated tau protein

Annexins: from structure to function

Annexins: linking Ca2+ signalling to membrane dynamics

A photoactivatable GFP for selective photolabeling of proteins and cells

Alterations of annexin expression in pathological neuronal and glial reactions. Immunohistochemical localization of annexins I, II (p36 and p11 subunits), IV, and VI in the human hippocampus.

Lentivirus-based genetic manipulations of cortical neurons and their optical and electrophysiological monitoring in vivo.

P304

647-661

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

P31

scholarly article

P356

10.1083/JCB.201007161

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

P407

P433

4

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

P478

192

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

P50

P577

2011-02-01T00:00:00Z

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

P5875

49853410

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

P698

21339331

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

P932

3044115

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