Investigation of the early stages of human γD-crystallin aggregation process.

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A γA-Crystallin Mouse Mutant Secc with Small Eye, Cataract and Closed Eyelid.Sodium louroyl sarcosinate (sarkosyl) modulate amyloid fibril formation in hen egg white lysozyme (HEWL) at alkaline pH: a molecular insight study.

P2860

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P2860

Investigation of the early stages of human γD-crystallin aggregation process.

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http://www.wikidata.org/entity/Q51408747

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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Investigation of the early stages of human γD-crystallin aggregation process.

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Investigation of the early stages of human γD-crystallin aggregation process.

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Item

label

Investigation of the early stages of human γD-crystallin aggregation process.

@en

Investigation of the early stages of human γD-crystallin aggregation process.

@nl

prefLabel

Investigation of the early stages of human γD-crystallin aggregation process.

@en

Investigation of the early stages of human γD-crystallin aggregation process.

@nl

P1476

Investigation of the early stages of human γD-crystallin aggregation process.

@en

P2093

Chih-Kai Chang

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

Chun-Hsien Lo

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

Hsiang-Chun Hsiao

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

Josephine W Wu

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

Steven S-S Wang

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

P2860

The RosettaDock server for local protein-protein docking

VMD: visual molecular dynamics

GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation

Protein folding and misfolding

PIC: Protein Interactions Calculator

The influence of cholesterol on membrane protein structure, function, and dynamics studied by molecular dynamics simulations.

Integrating atomistic molecular dynamics simulations, experiments, and network analysis to study protein dynamics: strength in unity.

Molecular dynamics of a protein surface: ion-residues interactions

Optical trapping with high forces reveals unexpected behaviors of prion fibrils.

beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin

P304

1042-1054

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P31

scholarly article

P356

10.1080/07391102.2016.1170632

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P433

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

P478

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

P577

2016-03-30T00:00:00Z

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P698

27025196

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Investigation of the early stages of human γD-crystallin aggregation process.

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P2860

P2860

Investigation of the early stages of human γD-crystallin aggregation process.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698