HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.

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Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau Terminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3

P2860

Q58569487-301C5DE3-4A20-4D3D-87D0-EE512FE6A4A3 Q58741923-E4EAA22D-99A2-4380-BEF3-E733DD319B54

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HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.

Item

http://www.wikidata.org/entity/Q47234323

description

2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

@zh-cn

2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

@yue

2018年學術文章

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name

HspB1 and Hsc70 chaperones eng ...... effects on amyloid formation.

@en

HspB1 and Hsc70 chaperones eng ...... effects on amyloid formation.

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type

Item

label

HspB1 and Hsc70 chaperones eng ...... effects on amyloid formation.

@en

HspB1 and Hsc70 chaperones eng ...... effects on amyloid formation.

@nl

prefLabel

HspB1 and Hsc70 chaperones eng ...... effects on amyloid formation.

@en

HspB1 and Hsc70 chaperones eng ...... effects on amyloid formation.

@nl

P1476

HspB1 and Hsc70 chaperones eng ...... effects on amyloid formation.

@en

P2093

Amanda F Clouser

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

Hannah E R Baughman

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

Rachel E Klevit

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

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Frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17)

Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif

Hsp90-Tau complex reveals molecular basis for specificity in chaperone action

The structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicity

Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation

Molecular mechanism of Thioflavin-T binding to amyloid fibrils

Structural polymorphism of 441-residue tau at single residue resolution

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

Molecular chaperones in protein folding and proteostasis

Tau suppression in a neurodegenerative mouse model improves memory function

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scholarly article

P356

10.1074/JBC.M117.803411

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P407

English

P50

Abhinav Nath

P577

2018-01-03T00:00:00Z

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P698

29298892

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P921

molecular chaperones

P932

5827454

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

HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.

about

P2860

P2860

HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P31

P356

P407

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P31

P356

P407

P50

P577

P698

P921

P932