{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:53:01Z","timestamp":1786978381151,"version":"build-2736575974"},"reference-count":23,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2018,5,6]],"date-time":"2018-05-06T00:00:00Z","timestamp":1525564800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100003825","name":"Magyar Tudom\u00e1nyos Akad\u00e9mia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003825","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Rapid Comm Mass Spectrometry"],"published-print":{"date-parts":[[2018,6,15]]},"abstract":"<jats:sec>\n                    <jats:title>Rationale<\/jats:title>\n                    <jats:p>Protein citrullination (deimination) is a post\u2010translational modification of proteins converting arginine(s) into citrulline(s). \u201cOvercitrullination\u201d could be associated with severe pathological conditions. Mass spectrometric analysis of modified proteins is hindered by several problems. A comprehensive study of the fragmentation of deiminated peptides is not yet available. In this paper we have made an attempt to describe the characteristics of these processes, based on the studies of epitope model oligopeptides derived from clinically relevant proteins.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>Solutions of purified model peptides containing either one or two citrulline residues as well as their native variants were injected directly into the electrospray source of a high accuracy and resolution quadrupole\u2010time\u2010of\u2010flight instrument and were analysed by tandem mass spectrometry using low\u2010energy collision\u2010induced dissociation.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      Loss of isocyanic acid from citrulline residues is a preferred fragmentation route for deiminated peptides, which yields ornithine residues in the sequence. However, simultaneous detection of both the isocyanic acid loss and sequence fragments is often compromised. A preferential cleavage site was observed between citrulline and any other following amino acids yielding intensive complementary b\u2010 and y\u2010type ions. Also, citrulline positioned at the\n                      <jats:italic>C<\/jats:italic>\n                      \u2010termini displays a preferential cleavage\n                      <jats:italic>N<\/jats:italic>\n                      \u2010terminal to this residue yielding characteristic y\n                      <jats:sub>1<\/jats:sub>\n                      ions. These phenomena are described here for the first time and are referred to as the \u201ccitrulline effect\u201d.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>We found that the citrulline effect is very pronounced and could be used as a complementary tool for the confirmation of modification sites in addition to losses of isocyanic acids from the protonated molecules or from fragment ions. Low collision energy applied to peptide ions having partially mobile protons reveals the site of modification by generating specific and intensive fragments of the sequence. On the other hand, fragmenting precursor ions with mobile protons usually allows full sequence coverage, although citrulline\u2010specific fragments may exhibit lower intensities compared to other fragments.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/rcm.8105","type":"journal-article","created":{"date-parts":[[2018,3,25]],"date-time":"2018-03-25T13:41:49Z","timestamp":1521985309000},"page":"844-850","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Mapping the tandem mass spectrometric characteristics of citrulline\u2010containing peptides"],"prefix":"10.1002","volume":"32","author":[{"given":"Arnold","family":"Steckel","sequence":"first","affiliation":[{"name":"Doctoral School of Chemistry ELTE E\u00f6tv\u00f6s Lor\u00e1nd University  Budapest Hungary"},{"name":"MTA\u2010ELTE Research Group of Peptide Chemistry, Hungarian Academy of Sciences ELTE E\u00f6tv\u00f6s Lor\u00e1nd University  Budapest Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katalin","family":"Uray","sequence":"additional","affiliation":[{"name":"MTA\u2010ELTE Research Group of Peptide Chemistry, Hungarian Academy of Sciences ELTE E\u00f6tv\u00f6s Lor\u00e1nd University  Budapest Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lilla","family":"Turi\u00e1k","sequence":"additional","affiliation":[{"name":"MS Proteomics Research Group, Research Centre for Natural Sciences Hungarian Academy of Sciences  Budapest Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"\u00c1gnes","family":"G\u00f6m\u00f6ry","sequence":"additional","affiliation":[{"name":"MS Proteomics Research Group, Research Centre for Natural Sciences Hungarian Academy of Sciences  Budapest Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L\u00e1szl\u00f3","family":"Drahos","sequence":"additional","affiliation":[{"name":"MS Proteomics Research Group, Research Centre for Natural Sciences Hungarian Academy of Sciences  Budapest Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ferenc","family":"Hudecz","sequence":"additional","affiliation":[{"name":"MTA\u2010ELTE Research Group of Peptide Chemistry, Hungarian Academy of Sciences ELTE E\u00f6tv\u00f6s Lor\u00e1nd University  Budapest Hungary"},{"name":"Department of Organic Chemistry ELTE E\u00f6tv\u00f6s Lor\u00e1nd University  Budapest Hungary"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7637-7133","authenticated-orcid":false,"given":"Gitta","family":"Schlosser","sequence":"additional","affiliation":[{"name":"MTA\u2010ELTE Research Group of Peptide Chemistry, Hungarian Academy of Sciences ELTE E\u00f6tv\u00f6s Lor\u00e1nd University  Budapest Hungary"},{"name":"Department of Analytical Chemistry ELTE E\u00f6tv\u00f6s Lor\u00e1nd University  Budapest 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