Differences in α-Crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses.

scientific article published on 20 March 2018

Differences in α-Crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.EXER.2018.03.018
P932PMC publication ID5964019
P698PubMed publication ID29571628

P2093author name stringRyan R Julian
Yana A Lyon
Georgette M Sabbah
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Age-dependent racemization of serine residues in a human chaperone proteinQ41857228
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Sequence and Solution Effects on the Prevalence of d-Isomers Produced by Deamidation.Q45969140
Isomerization of Asp-Asp motif in model peptides and a monoclonal antibody Fab fragmentQ46135976
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Age-related changes in human lens crystallins identified by HPLC and mass spectrometryQ47694043
P304page(s)131-141
P577publication date2018-03-20
P1433published inExperimental Eye ResearchQ15754753
P1476titleDifferences in α-Crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses.
P478volume171

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cites work (P2860)
Q64058284Isomerization as the secret Achilles' heel of long-lived proteins
Q83225749Long-lived metabolic enzymes in the crystalline lens identified by pulse-labeling of mice and mass spectrometry
Q91609310Molecular Processes Implicated in Human Age-Related Nuclear Cataract
Q93089168Spontaneous Isomerization of Long-Lived Proteins Provides a Molecular Mechanism for the Lysosomal Failure Observed in Alzheimer's Disease
Q57801154Spontaneous cross-linking of proteins at aspartate and asparagine residues is mediated via a succinimide intermediate
Q64105433Structural and functional consequences of age-related isomerization in α-crystallins

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