Existence of molten globule state in homocysteine-induced protein covalent modifications

about

Existence of molten globule state in homocysteine-induced protein covalent modifications

Item

http://www.wikidata.org/entity/Q28545034

description

2014 nî lūn-bûn

@nan

2014 թուականին հրատարակուած գիտական յօդուած

@hyw

2014 թվականին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Existence of molten globule state in homocysteine-induced protein covalent modifications

@ast

Existence of molten globule state in homocysteine-induced protein covalent modifications

@en

Existence of molten globule state in homocysteine-induced protein covalent modifications

@nl

type

Item

label

Existence of molten globule state in homocysteine-induced protein covalent modifications

@ast

Existence of molten globule state in homocysteine-induced protein covalent modifications

@en

Existence of molten globule state in homocysteine-induced protein covalent modifications

@nl

prefLabel

Existence of molten globule state in homocysteine-induced protein covalent modifications

@ast

Existence of molten globule state in homocysteine-induced protein covalent modifications

@en

Existence of molten globule state in homocysteine-induced protein covalent modifications

@nl

P1476

Existence of molten globule state in homocysteine-induced protein covalent modifications

@en

P2093

Gurumayum Suraj Sharma

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

Laishram Rajendrakumar Singh

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

Tarun Kumar

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

P2860

Tissue sulfhydryl groups

Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4'-dithiodipyridine

The sulfur-containing amino acids: an overview

Homocysteine and cardiovascular disease

Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels

Modification by homocysteine thiolactone affects redox status of cytochrome C.

The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

Molten globule of hemoglobin proceeds into aggregates and advanced glycated end products.

Homocysteine potentiates copper- and amyloid beta peptide-mediated toxicity in primary neuronal cultures: possible risk factors in the Alzheimer's-type neurodegenerative pathways.

Amyloid fibrillogenesis: themes and variations.

P304

e113566

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

P31

scholarly article

P356

10.1371/JOURNAL.PONE.0113566

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

P407

English

P433

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

P478

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

P577

2014-01-01T00:00:00Z

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

P5875

268793267

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

P698

25405350

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

P932

4236184

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