Effect of silybin on the fibrillation of hen egg-white lysozyme.

about

Effect of silybin on the fibrillation of hen egg-white lysozyme.

Item

http://www.wikidata.org/entity/Q50228170

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh-hant

name

Effect of silybin on the fibrillation of hen egg-white lysozyme.

@en

Effect of silybin on the fibrillation of hen egg-white lysozyme.

@nl

type

Item

label

Effect of silybin on the fibrillation of hen egg-white lysozyme.

@en

Effect of silybin on the fibrillation of hen egg-white lysozyme.

@nl

prefLabel

Effect of silybin on the fibrillation of hen egg-white lysozyme.

@en

Effect of silybin on the fibrillation of hen egg-white lysozyme.

@nl

P1476

Effect of silybin on the fibrillation of hen egg-white lysozyme.

@en

P2093

Hua-Jin Zeng

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

Ling-Bo Qu

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

Min Miao

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

Ran Yang

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

P2860

Amyloid fibrils from the viewpoint of protein folding

Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission.

Lysozyme amyloidogenesis is accelerated by specific nicking and fragmentation but decelerated by intact protein binding and conversion.

A highly amyloidogenic region of hen lysozyme.

Human lysozyme gene mutations cause hereditary systemic amyloidosis.

Protein aggregation: folding aggregates, inclusion bodies and amyloid.

Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease.

Inhibition of amyloid fibril formation and cytotoxicity by a chemical analog of Curcumin as a stable inhibitor.

Conformational constraints for amyloid fibrillation: the importance of being unfolded.

P31

scholarly article

P356

10.1002/JMR.2566

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

P433

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

P478

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

P577

2016-09-27T00:00:00Z

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

P698

27670268

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