{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:18:03Z","timestamp":1791292683050,"version":"4.1.0"},"reference-count":19,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2008,12,31]],"date-time":"2008-12-31T00:00:00Z","timestamp":1230681600000},"content-version":"vor","delay-in-days":5478,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[1994,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Under favorable conditions, Asp or Asn residues can undergo rearrangement to a succinimide (cyclic imide), which may also serve as an intermediate for deamidation and\/or isoaspartate formation. Direct identification of such succinimides by peptide mapping is hampered by their lability at neutral and alkaline pH. We determined that incubation in 2 M hydroxylamine, 0.2 M Tris buffer, pH 9, for 2 h at 45 \u00b0C will specifically cleave on the C\u2010terminal side of succinimides without cleavage at Asn\u2010Gly bonds; yields are typically \u223c 50%. N\u2010terminal sequence analysis can then be used to identify an internal sequence generated by cleavage of the succinimide, hence identifying the succinimide site.<\/jats:p>","DOI":"10.1002\/pro.5560030119","type":"journal-article","created":{"date-parts":[[2010,7,12]],"date-time":"2010-07-12T05:51:19Z","timestamp":1278913879000},"page":"147-149","source":"Crossref","is-referenced-by-count":48,"title":["Identification of succinimide sites in proteins by N\u2010terminal sequence analysis after alkaline hydroxylamine cleavage"],"prefix":"10.1002","volume":"3","author":[{"given":"May Y.","family":"Kwong","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Reed J.","family":"Harris","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,12,31]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00053a042"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja00300a039"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0076-6879(77)47016-2"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.10.4285"},{"key":"e_1_2_1_6_1","first-page":"4745","article-title":"Selective deamidation of ribonuclease A","volume":"268","author":"DiDonato A","year":"1993","journal-title":"J Biol Chem"},{"key":"e_1_2_1_7_1","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 proteins","volume":"262","author":"Geiger T","year":"1987","journal-title":"J Biol Chern"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00493a012"},{"key":"e_1_2_1_9_1","doi-asserted-by":"crossref","first-page":"14262","DOI":"10.1016\/S0021-9258(18)71672-4","article-title":"Formation of isoaspartate at two distinct sites during in vitro aging of human growth hormone","volume":"264","author":"Johnson BA","year":"1989","journal-title":"J Biol Chern"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.3353715"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0165-022X(92)90051-B"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560021011"},{"key":"e_1_2_1_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/B978-0-12-058757-5.50053-6"},{"key":"e_1_2_1_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)83327-0"},{"key":"e_1_2_1_15_1","doi-asserted-by":"crossref","first-page":"13544","DOI":"10.1016\/S0021-9258(18)92732-8","article-title":"Isolation and characterization of a succinimide variant of methionyl human growth hormone","volume":"266","author":"Teshima GT","year":"1991","journal-title":"J Biol Chem"},{"key":"e_1_2_1_16_1","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\u2010Cross R","year":"1991","journal-title":"J Biol Chem"},{"key":"e_1_2_1_17_1","doi-asserted-by":"publisher","DOI":"10.1002\/pro.5560011211"},{"key":"e_1_2_1_18_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF01024992"},{"key":"e_1_2_1_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(18)37383-6"},{"key":"e_1_2_1_20_1","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/4.3.283"}],"container-title":["Protein Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fpro.5560030119","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fpro.5560030119","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/pro.5560030119","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,10,24]],"date-time":"2023-10-24T07:42:34Z","timestamp":1698133354000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/pro.5560030119"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1994,1]]},"references-count":19,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1994,1]]}},"alternative-id":["10.1002\/pro.5560030119"],"URL":"https:\/\/doi.org\/10.1002\/pro.5560030119","archive":["Portico"],"relation":{},"ISSN":["0961-8368","1469-896X"],"issn-type":[{"value":"0961-8368","type":"print"},{"value":"1469-896X","type":"electronic"}],"subject":[],"published":{"date-parts":[[1994,1]]}}}