{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,14]],"date-time":"2026-03-14T09:45:04Z","timestamp":1773481504187,"version":"3.50.1"},"reference-count":22,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2016,10,2]],"date-time":"2016-10-02T00:00:00Z","timestamp":1475366400000},"content-version":"vor","delay-in-days":2511,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/2.5\/uk\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2010,1,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Using sensitive sequence profile analysis, we identify a hitherto uncharacterized cysteine-rich, transmembrane (TM) module, CYSTM, found in a wide range of tail-anchored membrane proteins across eukaryotes. This superfamily includes Schizosaccharomyces Uvi15, Arabidopsis PCC1, Digtaria CDT1 and Saccharomyces proteins YDL012C and YDR210W, which have all been implicated in resistance\/response to stress or pathogens. Based on the pattern of conserved cysteines and data from different chemical genetics studies, we suggest that CYSTM proteins might have critical role in responding to deleterious compounds at the plasma membrane via chelation or redox-based mechanisms. Thus, CYSTM proteins are likely to be part of a novel cellular protective mechanism that is widely active in eukaryotes, including humans.<\/jats:p>\n               <jats:p>Contact: \u00a0aravind@ncbi.nih.gov<\/jats:p>\n               <jats:p>Supplementary Information: \u00a0Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btp647","type":"journal-article","created":{"date-parts":[[2009,11,19]],"date-time":"2009-11-19T01:13:16Z","timestamp":1258593196000},"page":"149-152","source":"Crossref","is-referenced-by-count":52,"title":["CYSTM, a novel cysteine-rich transmembrane module with a role in stress tolerance across eukaryotes"],"prefix":"10.1093","volume":"26","author":[{"given":"Thiago M.","family":"Venancio","sequence":"first","affiliation":[{"name":"National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA"}]},{"given":"L.","family":"Aravind","sequence":"additional","affiliation":[{"name":"National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA"}]}],"member":"286","published-online":{"date-parts":[[2009,11,17]]},"reference":[{"key":"2023012508171246900_B1","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: a new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"2023012508171246900_B2","doi-asserted-by":"crossref","first-page":"8219","DOI":"10.1074\/jbc.M212725200","article-title":"Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae","volume":"278","author":"Beilharz","year":"2003","journal-title":"J. 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