Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins. - Wikidata - awgldk - TriplyDB

Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins.

Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins.

http://www.wikidata.org/entity/Q30399065

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Sequence and Solution Effects on the Prevalence of d-Isomers Produced by Deamidation.Strategies for analysis of isomeric peptides.Differences in α-Crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses.

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P2860

Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins.

http://www.wikidata.org/entity/Q30399065

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2017 nî lūn-bûn

@nan

2017 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2017 թվականի փետրվարին հրատարակված գիտական հոդված

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2017年の論文

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2017年論文

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2017年論文

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2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

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2017年论文

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name

Identification of Sequence Sim ...... tspots in Crystallin Proteins.

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Identification of Sequence Sim ...... tspots in Crystallin Proteins.

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Identification of Sequence Sim ...... tspots in Crystallin Proteins.

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Identification of Sequence Sim ...... tspots in Crystallin Proteins.

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Identification of Sequence Sim ...... tspots in Crystallin Proteins.

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Identification of Sequence Sim ...... tspots in Crystallin Proteins.

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P356

ACS.JPROTEOME.7B00073

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Journal of Proteome Research

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Identification of Sequence Sim ...... tspots in Crystallin Proteins.

@en

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Georgette M Sabbah

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Yana A Lyon

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P2860

Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20

Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function

Structural changes induced by the deamidation and isomerization of asparagine revealed by the crystal structure of Ustilago sphaerogena ribonuclease U2B

Succinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotriose

Crystal structure of a small heat-shock protein

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

Protein homeostasis: live long, won't prosper

Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein alpha B-crystallin

AlphaB-crystallin in lens development and muscle integrity: a gene knockout approach

Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins

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1797-1805

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scholarly article

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10.1021/ACS.JPROTEOME.7B00073

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4

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16

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2017-02-24T00:00:00Z

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28234481

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5387677

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