{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T20:42:58Z","timestamp":1791405778145,"version":"4.3.3"},"reference-count":34,"publisher":"Wiley","issue":"11","license":[{"start":{"date-parts":[[2019,5,14]],"date-time":"2019-05-14T00:00:00Z","timestamp":1557792000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["U54 GM074807"],"award-info":[{"award-number":["U54 GM074807"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 GM103725"],"award-info":[{"award-number":["R01 GM103725"]}],"id":[{"id":"10.13039\/100000002","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":[[2019,6,15]]},"abstract":"<jats:sec>\n                    <jats:title>Rationale<\/jats:title>\n                    <jats:p>Proteins undergo post\u2010translational modifications and proteolytic processing that can affect their biological function. Processing often involves the loss of single residues. Cleavage of signal peptides from the N\u2010terminus is commonly associated with translocation. Recent reports have suggested that other processing sites also exist.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>\n                      The secreted proteins from\n                      <jats:styled-content style=\"fixed-case\">\n                        <jats:italic>S. aureus<\/jats:italic>\n                      <\/jats:styled-content>\n                      N315 were precipitated with trichloroacetic acid (TCA) and amidinated with\n                      <jats:italic>S<\/jats:italic>\n                      \u2010methyl thioacetimidate (SMTA). Amidinated proteins were digested with trypsin and analyzed with a high\u2010resolution orbitrap mass spectrometer.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>\n                      Sixteen examples of\n                      <jats:styled-content style=\"fixed-case\">\n                        <jats:italic>Staphylococcus aureus<\/jats:italic>\n                      <\/jats:styled-content>\n                      secretory proteins that lose an N\u2010terminal signal peptide during their export were identified using this amidination approach. The N\u2010termini of proteins with and without methionine were identified. Unanticipated protein cleavages due to sortase and an unknown protease were also uncovered.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions<\/jats:title>\n                    <jats:p>A simple N\u2010terminal amidination based mass spectrometry approach is described that facilitates identification of the N\u2010terminus of a mature protein and the discovery of unexpected processing sites.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1002\/rcm.8435","type":"journal-article","created":{"date-parts":[[2019,3,18]],"date-time":"2019-03-18T21:22:40Z","timestamp":1552944160000},"page":"1015-1023","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["Identification of N\u2010terminal protein processing sites by chemical labeling mass spectrometry"],"prefix":"10.1002","volume":"33","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8835-0130","authenticated-orcid":false,"given":"Santosh A.","family":"Misal","sequence":"first","affiliation":[{"name":"Department of Chemistry Indiana University  Bloomington Indiana USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sujun","family":"Li","sequence":"additional","affiliation":[{"name":"School of Informatics, Computing, and Engineering Indiana University  Bloomington Indiana USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haixu","family":"Tang","sequence":"additional","affiliation":[{"name":"School of Informatics, Computing, and Engineering Indiana University  Bloomington Indiana USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Predrag","family":"Radivojac","sequence":"additional","affiliation":[{"name":"School of Informatics, Computing, and Engineering Indiana University  Bloomington Indiana USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9784-1804","authenticated-orcid":false,"given":"James P.","family":"Reilly","sequence":"additional","affiliation":[{"name":"Department of Chemistry Indiana University  Bloomington Indiana USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2019,5,14]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.201400157"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1021\/acs.jproteome.8b00373"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1021\/ac401000q"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1042\/BJ20070775"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1007\/978-1-4939-6850-3_6"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1007\/s13361-012-0379-x"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/ac0348625"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.O113.032854"},{"issue":"8","key":"e_1_2_6_10_1","doi-asserted-by":"crossref","first-page":"5060","DOI":"10.1016\/S0021-9258(18)42730-5","article-title":"The occurrence of O\u2010acylation during biotinylation of gonadotropin\u2010releasing hormone and analogs. 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