Human cyclophilin 40 unravels neurotoxic amyloids. - Wikidata - awgldk - TriplyDB

Human cyclophilin 40 unravels neurotoxic amyloids.

Human cyclophilin 40 unravels neurotoxic amyloids.

http://www.wikidata.org/entity/Q33842022

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Imbalances in the Hsp90 Chaperone Machinery: Implications for Tauopathies.Molecular dynamics simulations of site point mutations in the TPR domain of cyclophilin 40 identify conformational states with distinct dynamic and enzymatic properties.

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Human cyclophilin 40 unravels neurotoxic amyloids.

http://www.wikidata.org/entity/Q33842022

description

2017 nî lūn-bûn

@nan

2017 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2017 թվականի հունիսին հրատարակված գիտական հոդված

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2017年の論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年論文

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2017年论文

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name

Human cyclophilin 40 unravels neurotoxic amyloids.

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Human cyclophilin 40 unravels neurotoxic amyloids.

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type

label

Human cyclophilin 40 unravels neurotoxic amyloids.

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Human cyclophilin 40 unravels neurotoxic amyloids.

@en

prefLabel

Human cyclophilin 40 unravels neurotoxic amyloids.

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Human cyclophilin 40 unravels neurotoxic amyloids.

@en

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JOURNAL.PBIO.2001336

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Human cyclophilin 40 unravels neurotoxic amyloids.

@en

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Amirthaa Suntharalingam

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April Darling

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Bryce A Nordhues

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Chad A Dickey

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Filippo Favretto

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Jeremy D Baker

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Jonathan J Sabbagh

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Laura J Blair

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Leia E Sullivan

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Lindsey B Shelton

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

P2860

The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions

The cyclophilins

Features of alpha-synuclein that could explain the progression and irreversibility of Parkinson's disease

Two structures of cyclophilin 40: folding and fidelity in the TPR domains

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Neuropathological stageing of Alzheimer-related changes

Engineering enhanced protein disaggregases for neurodegenerative disease

The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease

IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content

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e2001336

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scholarly article

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10.1371/JOURNAL.PBIO.2001336

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6

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15

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Eckhard Mandelkow

Markus Zweckstetter

Vladimir Uversky

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2017-06-27T00:00:00Z

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28654636

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5486962

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