Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation - Wikidata - thesis-toulmin - TriplyDB

Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation

Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation

http://www.wikidata.org/entity/Q24644484

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PMeS: prediction of methylation sites based on enhanced feature encoding scheme Anti-chaperone betaA3/A1(102-117) peptide interacting sites in human alphaB-crystallin Isolation and characterization of betaA3-crystallin associated proteinase from alpha-crystallin fraction of human lenses.Protein post-translational modifications: In silico prediction tools and molecular modeling.Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidation MeMo: a web tool for prediction of protein methylation modifications.Degradation of an old human protein: age-dependent cleavage of γS-crystallin generates a peptide that binds to cell membranes Shotgun proteomic analysis of S-thiolation sites of guinea pig lens nuclear crystallins following oxidative stress in vivo Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility?Is protein methylation in the human lens a result of non-enzymatic methylation by S-adenosylmethionine?Quantitative proteomics analysis with iTRAQ in human lenses with nuclear cataracts of different axial lengths Lens aging: effects of crystallins.Mass spectrometry-based proteomics approaches applied in cataract research.Orphan PTMs: Rare, yet functionally important modifications of cysteine.Computational prediction of methylation types of covalently modified lysine and arginine residues in proteins.Analysis of proteomic differences between liquefied after-cataracts and normal lenses using two-dimensional gel electrophoresis and mass spectrometry.Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.Age-dependent modification of proteins: N-terminal racemization.Protein Disulfide Levels and Lens Elasticity Modulation: Applications for Presbyopia.

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P2860

Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation

http://www.wikidata.org/entity/Q24644484

description

2005 nî lūn-bûn

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2005 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2005 թվականի հունվարին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Modifications of human betaA1/ ...... lutathiolation, and truncation

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Modifications of human betaA1/ ...... lutathiolation, and truncation

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Modifications of human betaA1/ ...... lutathiolation, and truncation

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label

Modifications of human betaA1/ ...... lutathiolation, and truncation

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Modifications of human betaA1/ ...... lutathiolation, and truncation

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Modifications of human betaA1/ ...... lutathiolation, and truncation

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Modifications of human betaA1/ ...... lutathiolation, and truncation

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Modifications of human betaA1/ ...... lutathiolation, and truncation

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Modifications of human betaA1/ ...... lutathiolation, and truncation

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Protein Science

P1476

Modifications of human betaA1/ ...... lutathiolation, and truncation

@en

P2093

David L Smith

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

Jean B Smith

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Ronald L Cerny

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Veniamin N Lapko

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P2860

Progressive juvenile-onset punctate cataracts caused by mutation of the gammaD-crystallin gene

The sequence of human betaB1-crystallin cDNA allows mass spectrometric detection of betaB1 protein missing portions of its N-terminal extension

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

Shotgun identification of protein modifications from protein complexes and lens tissue

Methylation and carbamylation of human gamma-crystallins

Molecular basis of a progressive juvenile-onset hereditary cataract

Structure of the crystallins

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

Deamidation in human gamma S-crystallin from cataractous lenses is influenced by surface exposure

S-methylated cysteines in human lens gamma S-crystallins

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45-54

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scholarly article

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10.1110/PS.04738505

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1

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14

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8150257

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15576560

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2253330

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