Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
about
Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitusβA3/A1-crystallin: more than a lens proteinStructure-based prediction of asparagine and aspartate degradation sites in antibody variable regionsLens β-crystallins: the role of deamidation and related modifications in aging and cataract.Recombinant deamidated mutants of Erwinia chrysanthemi L-asparaginase have similar or increased activity compared to wild-type enzyme.Deamidation alters interactions of beta-crystallins in hetero-oligomersAggregation of deamidated human betaB2-crystallin and incomplete rescue by alpha-crystallin chaperone.Top-down study of β2-microglobulin deamidationRacemization 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.Protein determinants of phage T4 lysis inhibition.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.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.Mass spectrometric analysis of asparagine deamidation and aspartate isomerization in polypeptides.The βγ-crystallins: native state stability and pathways to aggregation.Dementia-linked amyloidosis is associated with brain protein deamidation as revealed by proteomic profiling of human brain tissues.Protein misfolding and aggregation in cataract disease and prospects for prevention.Brain proteomics supports the role of glutamate metabolism and suggests other metabolic alterations in protein l-isoaspartyl methyltransferase (PIMT)-knockout miceTryptophan cluster protects human γD-crystallin from ultraviolet radiation-induced photoaggregation in vitro.Toward proteome-scale identification and quantification of isoaspartyl residues in biological samples.Truncated human betaB1-crystallin shows altered structural properties and interaction with human betaA3-crystallinTyrosine/cysteine cluster sensitizing human γD-crystallin to ultraviolet radiation-induced photoaggregation in vitro.Dissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins.Proteomic analysis of protein deamidation.Overview of the Lens.Detection, evaluation and minimization of nonenzymatic deamidation in proteomic sample preparation.An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin.Deamidation of Human γS-Crystallin Increases Attractive Protein Interactions: Implications for Cataract.Changes in solvent accessibility of wild-type and deamidated βB2-crystallin following complex formation with αA-crystallin.Deamidation accelerates amyloid formation and alters amylin fiber structureAggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.Inhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate.Structural analysis of the mutant protein D26G of human γS-crystallin, associated with Coppock cataract.Age-dependent deamidation of glutamine residues in human γS crystallin: deamidation and unstructured regions.Engineering deamidation-susceptible asparagines leads to improved stability to thermal cycling in a lipase.Enzymatic attributes of an l-isoaspartyl methyltransferase from Candida utilis and its role in cell survival.Sequence and Solution Effects on the Prevalence of d-Isomers Produced by Deamidation.Factors affecting the physical stability (aggregation) of peptide therapeutics.Racemization at the Asp 58 residue in αA-crystallin from the lens of high myopic cataract patients.
P2860
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P2860
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
@en
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
@nl
type
label
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
@en
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
@nl
prefLabel
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
@en
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.
@nl
P2860
P356
P1433
P1476
Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin
@en
P2093
Borries Demeler
Kirsten J Lampi
P2860
P304
P356
10.1110/PS.035410.108
P577
2008-06-20T00:00:00Z