{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T23:57:10Z","timestamp":1761609430709,"version":"build-2065373602"},"reference-count":40,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,11,1]],"date-time":"2020-11-01T00:00:00Z","timestamp":1604188800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP19K07031","JP16K08207"],"award-info":[{"award-number":["JP19K07031","JP16K08207"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2020,11]]},"DOI":"10.1016\/j.bbapap.2020.140496","type":"journal-article","created":{"date-parts":[[2020,7,13]],"date-time":"2020-07-13T22:11:13Z","timestamp":1594678273000},"page":"140496","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":2,"title":["Effect of amino acids present at the carboxyl end of succinimidyl residue on the rate constants for succinimidyl hydrolysis in small peptides"],"prefix":"10.1016","volume":"1868","author":[{"given":"Yutaka","family":"Sadakane","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sayumi","family":"Senda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Taku","family":"Deguchi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Atsuki","family":"Tanaka","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hiromasa","family":"Tsuruta","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shota","family":"Morimoto","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2020.140496_bb0005","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.exger.2007.12.001","article-title":"Nonenzymatic posttranslational protein modifications in ageing","volume":"43","author":"Soski\u0107","year":"2008","journal-title":"Exp. Gerontol."},{"key":"10.1016\/j.bbapap.2020.140496_bb0010","doi-asserted-by":"crossref","DOI":"10.3390\/ijms19082449","article-title":"Implications of metal binding and asparagine deamidation for amyloid formation","volume":"19","author":"Sadakane","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbapap.2020.140496_bb0015","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1016\/S0021-9258(19)75855-4","article-title":"Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation","volume":"262","author":"Geiger","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0020","doi-asserted-by":"crossref","first-page":"12283","DOI":"10.1016\/S0021-9258(18)45348-3","article-title":"Partial repair of deamidation-damaged calmodulin by protein carboxyl methyltransferase","volume":"262","author":"Johnson","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0025","doi-asserted-by":"crossref","first-page":"24586","DOI":"10.1016\/S0021-9258(17)31432-1","article-title":"Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L-isoaspartate-(D-aspartate) O-methyltransferase","volume":"269","author":"Brennan","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0030","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1006\/prep.1995.1041","article-title":"Cloning, expression, and purification of rat brain protein L-isoaspartyl methyltransferase","volume":"6","author":"David","year":"1995","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bbapap.2020.140496_bb0035","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/S0965-1748(96)00071-9","article-title":"Structural organization and developmental expression of the protein isoaspartyl methyltransferase gene from Drosophila melanogaster","volume":"27","author":"O'Connor","year":"1997","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.bbapap.2020.140496_bb0040","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1007\/BF00019007","article-title":"A distinctly regulated protein repair L-isoaspartyl methyltransferase from Arabidopsis thaliana","volume":"30","author":"Mudgett","year":"1996","journal-title":"Plant Mol. Biol."},{"key":"10.1016\/j.bbapap.2020.140496_bb0045","doi-asserted-by":"crossref","first-page":"11100","DOI":"10.1021\/bi00092a020","article-title":"Characterization of plant L-isoaspartyl methyltransferases that may be involved in seed survival: purification, cloning, and sequence analysis of the wheat germ enzyme","volume":"32","author":"Mudgett","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2020.140496_bb0050","doi-asserted-by":"crossref","first-page":"14562","DOI":"10.1016\/S0021-9258(18)98723-5","article-title":"Purification, gene cloning, and sequence analysis of an L-isoaspartyl protein carboxyl methyltransferase from Escherichia coli","volume":"266","author":"Fu","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0055","doi-asserted-by":"crossref","first-page":"10794","DOI":"10.1021\/bi00034a012","article-title":"Protein L-isoaspartyl methyltransferase from the nematode Caenorhabditis elegans: genomic structure and substrate specificity","volume":"34","author":"Kagan","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2020.140496_bb0060","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/S0305-0491(96)00333-1","article-title":"Molecular phylogenetics of a protein repair methyltransferase","volume":"117","author":"Kagan","year":"1997","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"10.1016\/j.bbapap.2020.140496_bb0065","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/S1568-1637(03)00011-4","article-title":"Aging as war between chemical and biochemical processes: protein methylation and the recognition of age-damaged proteins for repair","volume":"2","author":"Clarke","year":"2003","journal-title":"Ageing Res. Rev."},{"key":"10.1016\/j.bbapap.2020.140496_bb0070","doi-asserted-by":"crossref","first-page":"6132","DOI":"10.1073\/pnas.94.12.6132","article-title":"Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth, and fatal seizures in mice","volume":"94","author":"Kim","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2020.140496_bb0075","doi-asserted-by":"crossref","first-page":"14814","DOI":"10.1073\/pnas.251446498","article-title":"Extension of the Drosophila lifespan by overexpression of a protein repair methyltransferase","volume":"98","author":"Chavous","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2020.140496_bb0080","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1073\/pnas.98.3.944","article-title":"Molecular clocks","volume":"98","author":"Robinson","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2020.140496_bb0085","doi-asserted-by":"crossref","first-page":"22549","DOI":"10.1016\/S0021-9258(18)54607-X","article-title":"Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides","volume":"266","author":"Tyler-Cross","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0090","doi-asserted-by":"crossref","first-page":"6164","DOI":"10.1016\/S0021-9258(18)83327-0","article-title":"Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins","volume":"264","author":"Stephenson","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0095","doi-asserted-by":"crossref","first-page":"3240","DOI":"10.1016\/j.jchromb.2011.03.020","article-title":"Determination of rate constants for \u03b2-linkage isomerization of three specific aspartyl residues in recombinant human \u03b1A-crystallin protein by reversed-phase HPLC","volume":"879","author":"Sadakane","year":"2011","journal-title":"J. Chromatogr. B"},{"key":"10.1016\/j.bbapap.2020.140496_bb0100","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1126\/science.3353715","article-title":"Tertiary structure is a principal determinant to protein deamidation","volume":"240","author":"Kossiakoff","year":"1988","journal-title":"Science"},{"key":"10.1016\/j.bbapap.2020.140496_bb0105","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1111\/j.1399-3011.1987.tb03390.x","article-title":"Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins","volume":"30","author":"Clarke","year":"1987","journal-title":"Int. J. Pept. Protein Res."},{"key":"10.1016\/j.bbapap.2020.140496_bb0110","doi-asserted-by":"crossref","first-page":"12409","DOI":"10.1073\/pnas.221463198","article-title":"Deamidation of human proteins","volume":"98","author":"Robinson","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2020.140496_bb0115","doi-asserted-by":"crossref","first-page":"1825","DOI":"10.1016\/S0731-7085(02)00525-3","article-title":"Quantification of the isomerization of Asp residue in recombinant human \u03b1A crystallin by reversed-phase HPLC","volume":"30","author":"Sadakane","year":"2003","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.bbapap.2020.140496_bb0120","doi-asserted-by":"crossref","first-page":"1371","DOI":"10.1002\/cbdv.200900330","article-title":"Quantification of structural alterations of l-Asp and l-Asn residues in peptides related to neuronal diseases by reversed-phase high-performance liquid chromatography","volume":"7","author":"Sadakane","year":"2010","journal-title":"Chem. Biodivers."},{"key":"10.1016\/j.bbapap.2020.140496_bb0125","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1006\/abio.2000.4601","article-title":"Analysis of isoaspartate in peptides and proteins without the use of radioisotopes","volume":"282","author":"Schurter","year":"2000","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0130","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0058515","article-title":"Kinetics of isomerization and inversion of aspartate 58 of \u03b1A-crystallin peptide mimics under physiological conditions","volume":"8","author":"Aki","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bbapap.2020.140496_bb0135","doi-asserted-by":"crossref","first-page":"19396","DOI":"10.1016\/S0021-9258(18)55010-9","article-title":"Structural elements affecting the recognition of L-isoaspartyl residues by the L-isoaspartyl\/D-aspartyl protein methyltransferase. Implications for the repair hypothesis","volume":"266","author":"Lowenson","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0140","doi-asserted-by":"crossref","first-page":"5985","DOI":"10.1016\/S0021-9258(18)42652-X","article-title":"Recognition of D-aspartyl residues in polypeptides by the erythrocyte L-isoaspartyl\/D-aspartyl protein methyltransferase, implications for the repair hypothesis","volume":"267","author":"Lowenson","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2020.140496_bb0145","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/BF00966926","article-title":"Kinetic properties of bovine brain protein L-isoaspartyl methyltransferase determined using a synthetic isoaspartyl peptide substrate","volume":"18","author":"Johnson","year":"1993","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.bbapap.2020.140496_bb0150","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1002\/pro.5560020305","article-title":"Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues: effects of the solvent dielectric","volume":"2","author":"Brennan","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbapap.2020.140496_bb0155","doi-asserted-by":"crossref","first-page":"7757","DOI":"10.1073\/pnas.81.24.7757","article-title":"Mammalian brain and erythrocyte carboxyl methyltransferases are similar enzymes that recognize both D-aspartyl and L-isoaspartyl residues in structurally altered protein substrates","volume":"81","author":"O\u2019Connor","year":"1984","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2020.140496_bb0160","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1006\/prep.1995.1041","article-title":"Cloning, expression, and purification of rat brain protein L-isoaspartyl methyltransferase","volume":"6","author":"David","year":"1995","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bbapap.2020.140496_bb0165","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1023\/A:1015807303766","article-title":"Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide","volume":"7","author":"Patel","year":"1990","journal-title":"Pharm. Res."},{"key":"10.1016\/j.bbapap.2020.140496_bb0170","doi-asserted-by":"crossref","first-page":"4069","DOI":"10.1021\/bi00851a040","article-title":"Side reactions in the synthesis of peptides containing the aspartyglycyl sequence","volume":"7","author":"Ondetti","year":"1968","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2020.140496_bb0175","doi-asserted-by":"crossref","first-page":"2421","DOI":"10.1021\/ja00871a030","article-title":"Co-operative effects of functional groups in peptides. I. Aspartyl-serine derivatives","volume":"84","author":"Bernhard","year":"1962","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2020.140496_bb0180","doi-asserted-by":"crossref","first-page":"11440","DOI":"10.3390\/molecules190811440","article-title":"Roles of intramolecular and intermolecular hydrogen bonding in a three-water-assisted mechanism of succinimide formation from aspartic acid residues","volume":"19","author":"Takahashi","year":"2014","journal-title":"Molecules"},{"key":"10.1016\/j.bbapap.2020.140496_bb0185","doi-asserted-by":"crossref","DOI":"10.3390\/ijms19020637","article-title":"Phosphate-catalyzed succinimide formation from asp residues: a computational study of the mechanism","volume":"19","author":"Kirikoshi","year":"2018","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbapap.2020.140496_bb0190","doi-asserted-by":"crossref","first-page":"5283","DOI":"10.1073\/pnas.082102799","article-title":"Protein deamidation","volume":"99","author":"Robinson","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2020.140496_bb0195","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/S0378-4347(00)00548-X","article-title":"Identification of multiple sources of charge heterogeneity in a recombinant antibody","volume":"752","author":"Harris","year":"2001","journal-title":"J. Chromatogr. B Biomed. Sci. Appl."},{"key":"10.1016\/j.bbapap.2020.140496_bb0200","doi-asserted-by":"crossref","first-page":"468","DOI":"10.2174\/138920108786786402","article-title":"Heterogeneity of monoclonal antibodies revealed by charge-sensitive methods","volume":"9","author":"Vlasak","year":"2008","journal-title":"Curr. Pharm. Biotechnol."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963920301436?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963920301436?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T23:52:58Z","timestamp":1761609178000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963920301436"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,11]]},"references-count":40,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2020,11]]}},"alternative-id":["S1570963920301436"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2020.140496","relation":{},"ISSN":["1570-9639"],"issn-type":[{"type":"print","value":"1570-9639"}],"subject":[],"published":{"date-parts":[[2020,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Effect of amino acids present at the carboxyl end of succinimidyl residue on the rate constants for succinimidyl hydrolysis in small peptides","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbapap.2020.140496","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"140496"}}