Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaB-crystallin.
about
Recombinant deamidated mutants of Erwinia chrysanthemi L-asparaginase have similar or increased activity compared to wild-type enzyme.Vitamin C-mediated Maillard reaction in the lens probed in a transgenic-mouse model.Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin.Identification of crystallin modifications in the human lens cortex and nucleus using laser capture microdissection and CyDye labeling.Dynamic subunit exchange and the regulation of microtubule assembly by the stress response protein human alphaB crystallin.Structural and functional roles of deamidation of N146 and/or truncation of NH2- or COOH-termini in human αB-crystallin.Racemization of two proteins over our lifespan: deamidation of asparagine 76 in γS crystallin is greater in cataract than in normal lenses across the age range.Molecular mechanism of formation of cortical opacity in CRYAAN101D transgenic mice.The common modification in alphaA-crystallin in the lens, N101D, is associated with increased opacity in a mouse model.Determination of dideoxyosone precursors of AGEs in human lens proteins.A novel alphaB-crystallin mutation associated with autosomal dominant congenital lamellar cataract.UV-A-induced structural and functional changes in human lens deamidated alphaB-crystallin.Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activitySmall heat shock protein activity is regulated by variable oligomeric substructure.Protein-protein interactions and lens transparency.Lens aging: effects of crystallins.Structural and functional properties of NH(2)-terminal domain, core domain, and COOH-terminal extension of αA- and αB-crystallins.Deamidation of Human γS-Crystallin Increases Attractive Protein Interactions: Implications for Cataract.Post-translationally modified human lens crystallin fragments show aggregation in vitro.Insights into the domains required for dimerization and assembly of human alphaB crystallin.Age-dependent deamidation of glutamine residues in human γS crystallin: deamidation and unstructured regions.Camelid VH H affinity ligands enable separation of closely related biopharmaceuticalsEngineering deamidation-susceptible asparagines leads to improved stability to thermal cycling in a lipase.Interaction of βA3-Crystallin with Deamidated Mutants of αA- and αB-Crystallins.Protein deamidation in biopharmaceutical manufacture: understanding, control and impact
P2860
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P2860
Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaB-crystallin.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Effect of deamidation of aspar ...... human lens alphaB-crystallin.
@ast
Effect of deamidation of aspar ...... human lens alphaB-crystallin.
@en
type
label
Effect of deamidation of aspar ...... human lens alphaB-crystallin.
@ast
Effect of deamidation of aspar ...... human lens alphaB-crystallin.
@en
prefLabel
Effect of deamidation of aspar ...... human lens alphaB-crystallin.
@ast
Effect of deamidation of aspar ...... human lens alphaB-crystallin.
@en
P356
P1476
Effect of deamidation of aspar ...... human lens alphaB-crystallin.
@en
P2093
Om P Srivastava
Ratna Gupta
P304
P356
10.1167/IOVS.03-0720
P407
P577
2004-01-01T00:00:00Z