Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin. - Wikidata - awgldk - TriplyDB

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

http://www.wikidata.org/entity/Q34579872

about

Interaction of ATP with a small heat shock protein from Mycobacterium leprae: effect on its structure and function Biophysical Characterization of Essential Phosphorylation at the Flexible C-Terminal Region of C-Raf with 14-3-3ζ Protein.Protective Effects of Acetylation on the Pathological Reactions of the Lens Crystallins with Homocysteine Thiolactone.Increased hydrophobic surface exposure in the cataract-related G18V variant of human γS-crystallin.Importance of the positively charged residue at position 54 to the chaperoning function, conformational stability and amyloidogenic nature of human αA-crystallin.Deciphering the role of the AT-rich interaction domain and the HMG-box domain of ARID-HMG proteins of Arabidopsis thaliana.

P2860

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P2860

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

http://www.wikidata.org/entity/Q34579872

description

2014 nî lūn-bûn

@nan

2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի նոյեմբերին 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

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@ast

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@en

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@nl

type

label

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@ast

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@en

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@nl

prefLabel

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@ast

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@en

Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin.

@nl

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Acetylation of Gly1 and Lys2 promotes aggregation of human γD-crystallin

@en

P2093

Anirban Bhunia

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

Ashis Biswas

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

Benlian Wang

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

Cibin T Raghavan

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

Michael A DiMauro

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

Rajiv Kumar Kar

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

Ram H Nagaraj

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

P2860

Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens

Primary structure of beta s-crystallin from human lens

Methylation and carbamylation of human gamma-crystallins

Molecular basis of a progressive juvenile-onset hereditary cataract

High-resolution X-ray crystal structures of human gammaD crystallin (1.25 A) and the R58H mutant (1.15 A) associated with aculeiform cataract

PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations

N-terminal acetyltransferases and sequence requirements for N-terminal acetylation of eukaryotic proteins.

The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage

Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics

Alpha-crystallin can function as a molecular chaperone

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scholarly article

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10.1021/BI501004Y

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46

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53

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Sandip Kumar Nandi

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2014-11-13T00:00:00Z

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268228694

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25393041

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4245984

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