Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins

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Identification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/ACS.JPROTEOME.7B00073
P932PMC publication ID5387677
P698PubMed publication ID28234481

P50authorRyan R JulianQ57069223
P2093author name stringYana A Lyon
Georgette M Sabbah
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Domain swapping in human alpha A and alpha B crystallins affects oligomerization and enhances chaperone-like activityQ74008662
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Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens functionQ27661297
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Succinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotrioseQ27756794
Crystal structure of a small heat-shock proteinQ27765131
The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavageQ28142819
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AlphaB-crystallin in lens development and muscle integrity: a gene knockout approachQ28512665
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Racemisation and human cataract. D-Ser, D-Asp/Asn and D-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lensesQ28743054
Side chain chemistry mediates backbone fragmentation in hydrogen deficient peptide radicalsQ33396334
Aspartic acid racemization in heavy molecular weight crystallins and water insoluble protein from normal human lenses and cataractsQ33966380
Identification of amino acid epimerization and isomerization in crystallin proteins by tandem LC-MSQ34300357
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New experimental evidence for in-chain amino acid racemization of serine in a model peptideQ34739262
Deamidation: Differentiation of aspartyl from isoaspartyl products in peptides by electron capture dissociationQ36476874
Evolution of crystallins for a role in the vertebrate eye lens.Q36722216
Importance of eye lens α‐crystallin heteropolymer with 3:1 αA to αB ratio: Stability, aggregation, and modificationsQ36738905
Identification of long-lived proteins reveals exceptional stability of essential cellular structuresQ37210826
Site-specific characterization of (D)-amino acid containing peptide epimers by ion mobility spectrometryQ37724249
Isomerization of aspartyl residues in crystallins and its influence upon cataractQ38566934
Isomerization of a single aspartyl residue of anti-epidermal growth factor receptor immunoglobulin gamma2 antibody highlights the role avidity plays in antibody activityQ40018957
Primary sequence contribution to the optical function of the eye lens.Q40375255
Recognition of D-aspartyl residues in polypeptides by the erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis.Q41114791
Structural elements affecting the recognition of L-isoaspartyl residues by the L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesisQ41153015
Racemization of the Succinimide Intermediate Formed in Proteins and Peptides: A Computational Study of the Mechanism Catalyzed by Dihydrogen Phosphate IonQ41613730
Lens alpha-crystallin: function and structureQ41632199
Alpha B- and βA3-crystallins containing d-aspartic acids exist in a monomeric state.Q41754957
Protein carboxyl methyltransferase from cow eye lensQ42260224
Accelerated aging of Asp 58 in αA crystallin and human cataract formationQ43451658
Structure-dependent nonenzymatic deamidation of glutaminyl and asparaginyl pentapeptidesQ44893900
Differentiation of aspartic and isoaspartic acids using electron transfer dissociationQ46843070
P433issue4
P304page(s)1797-1805
P577publication date2017-02-24
P1433published inJournal of Proteome ResearchQ3186939
P1476titleIdentification of Sequence Similarities among Isomerization Hotspots in Crystallin Proteins
P478volume16