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Deamidation alters the structure and decreases the stability of human lens betaA3-crystallinDifferential analysis of D-beta-Asp-containing proteins found in normal and infrared irradiated rabbit lens.Solvent accessibility of betaB2-crystallin and local structural changes due to deamidation at the dimer interface.New insight into the dynamical system of αB-crystallin oligomers.Quantitative analysis of isomeric (l-α-, l-β-, D-α-, D-β-) aspartyl residues in proteins from elderly donors.Isomerization of aspartyl residues in crystallins and its influence upon cataract.Effect of Asp 96 isomerization on the properties of a lens αB-crystallin-derived short peptide.Rapid survey of four Asp isomers in disease-related proteins by LC-MS combined with commercial enzymes.Alpha B- and βA3-crystallins containing d-aspartic acids exist in a monomeric state.Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.Ferulic Acid Suppresses Amyloid β Production in the Human Lens Epithelial Cell Stimulated with Hydrogen PeroxideDeamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin.The presence of D-beta-aspartic acid-containing peptides in elastic fibers of sun-damaged skin: a potent marker for ultraviolet-induced skin aging.Identification of ᴅ-amino acid-containing peptides in human serum.D-Amino acids in protein: The mirror of life as a molecular index of aging.Localization of D-beta-aspartic acid-containing proteins in human eyesIsomerization of Asp residues plays an important role in αA-crystallin dissociationIdentification of Isomeric Aspartate residues in βB2-crystallin from Aged Human LensAsp 58 modulates lens αA-crystallin oligomer formation and chaperone functionNegative charge at aspartate 151 is important for human lens αA-crystallin stability and chaperone functionSite-specific rapid deamidation and isomerization in human lens αA-crystallin in vitroIsomeric Replacement of a Single Aspartic Acid Induces a Marked Change in Protein Function: The Example of Ribonuclease A
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P50
description
researcher
@en
wetenschapper
@nl
name
Takumi Takata
@en
Takumi Takata
@nl
type
label
Takumi Takata
@en
Takumi Takata
@nl
prefLabel
Takumi Takata
@en
Takumi Takata
@nl
P106
P31
P496
0000-0003-3208-3704