{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T05:01:29Z","timestamp":1790485289754,"version":"4.1.0"},"reference-count":40,"publisher":"National Academy of Sciences","issue":"38","license":[{"start":{"date-parts":[[2021,3,8]],"date-time":"2021-03-08T00:00:00Z","timestamp":1615161600000},"content-version":"vor","delay-in-days":181,"URL":"https:\/\/www.pnas.org\/site\/aboutpnas\/licenses.xhtml"}],"funder":[{"DOI":"10.13039\/100000011","name":"Howard Hughes Medical Institute","doi-asserted-by":"publisher","award":["N\/A"],"award-info":[{"award-number":["N\/A"]}],"id":[{"id":"10.13039\/100000011","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2020,9,22]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    The CydDC complex is involved in the assembly of cytochrome\n                    <jats:italic>bd<\/jats:italic>\n                    -I, a terminal oxidase of the respiratory chain required for growth under low oxygen conditions. It has been suggested that CydDC shuttles excessive\n                    <jats:sc>l<\/jats:sc>\n                    -cysteine from the cytoplasm to the periplasm, thereby maintaining bacterial redox homeostasis. Here, we demonstrate that the principle function of CydDC is in maintaining the reduced state of cytoplasmic\n                    <jats:sc>l<\/jats:sc>\n                    -cysteine, as opposed to exporting\n                    <jats:sc>l<\/jats:sc>\n                    -cysteine, thereby providing an important connection between sulfur metabolism, oxidative stress, and resistance to antibiotics. In particular, we establish the critical role of cytoplasmic\n                    <jats:sc>l<\/jats:sc>\n                    -cysteine in mediating the toxicity of aminoglycosides. Thus, understanding the mechanisms that control the bacterial redox state can lead to more effective strategies to counter bacterial resistance and tolerance.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2007817117","type":"journal-article","created":{"date-parts":[[2020,9,8]],"date-time":"2020-09-08T15:56:10Z","timestamp":1599580570000},"page":"23565-23570","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":37,"title":["CydDC functions as a cytoplasmic cystine reductase to sensitize\n                    <i>Escherichia coli<\/i>\n                    to oxidative stress and aminoglycosides"],"prefix":"10.1073","volume":"117","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3914-1380","authenticated-orcid":false,"given":"Alexander","family":"Mironov","sequence":"first","affiliation":[{"name":"Department of Molecular Biology, Engelhardt Institute of Molecular Biology, Russian Academy of Science, 119991 Moscow, Russia;"},{"name":"Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatyana","family":"Seregina","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology, Engelhardt Institute of Molecular Biology, Russian Academy of Science, 119991 Moscow, Russia;"},{"name":"Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8653-2355","authenticated-orcid":false,"given":"Konstantin","family":"Shatalin","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 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