[{"status":"public","has_accepted_license":"1","publication":"mBio","publisher":"American Society for Microbiology","publication_identifier":{"issn":["2150-7511"]},"intvolume":"        12","keyword":["Virology","Microbiology"],"month":"08","author":[{"first_name":"Dai","full_name":"Le, Dai","last_name":"Le"},{"id":"1F1EE44A-BF83-11EA-B3C1-BB9CC619BF3A","last_name":"Krasnopeeva","first_name":"Ekaterina","full_name":"Krasnopeeva, Ekaterina"},{"first_name":"Faris","full_name":"Sinjab, Faris","last_name":"Sinjab"},{"last_name":"Pilizota","first_name":"Teuta","full_name":"Pilizota, Teuta"},{"last_name":"Kim","first_name":"Minsu","full_name":"Kim, Minsu"}],"external_id":{"pmid":["34253054"]},"ddc":["570"],"article_number":"676","date_published":"2021-08-31T00:00:00Z","pmid":1,"oa_version":"Published Version","volume":12,"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","year":"2021","title":"Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria","article_processing_charge":"Yes","file_date_updated":"2024-04-10T09:05:49Z","language":[{"iso":"eng"}],"oa":1,"abstract":[{"lang":"eng","text":"Various toxic compounds disrupt bacterial physiology. While bacteria harbor defense mechanisms to mitigate the toxicity, these mechanisms are often coupled to the physiological state of the cells and become ineffective when the physiology is severely disrupted."}],"license":"https://creativecommons.org/licenses/by/4.0/","quality_controlled":"1","date_updated":"2024-04-10T09:13:59Z","citation":{"short":"D. Le, E. Krasnopeeva, F. Sinjab, T. Pilizota, M. Kim, MBio 12 (2021).","chicago":"Le, Dai, Ekaterina Krasnopeeva, Faris Sinjab, Teuta Pilizota, and Minsu Kim. “Active Efflux Leads to Heterogeneous Dissipation of Proton Motive Force by Protonophores in Bacteria.” <i>MBio</i>. American Society for Microbiology, 2021. <a href=\"https://doi.org/10.1128/mbio.00676-21\">https://doi.org/10.1128/mbio.00676-21</a>.","ieee":"D. Le, E. Krasnopeeva, F. Sinjab, T. Pilizota, and M. Kim, “Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria,” <i>mBio</i>, vol. 12, no. 4. American Society for Microbiology, 2021.","mla":"Le, Dai, et al. “Active Efflux Leads to Heterogeneous Dissipation of Proton Motive Force by Protonophores in Bacteria.” <i>MBio</i>, vol. 12, no. 4, 676, American Society for Microbiology, 2021, doi:<a href=\"https://doi.org/10.1128/mbio.00676-21\">10.1128/mbio.00676-21</a>.","ama":"Le D, Krasnopeeva E, Sinjab F, Pilizota T, Kim M. Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria. <i>mBio</i>. 2021;12(4). doi:<a href=\"https://doi.org/10.1128/mbio.00676-21\">10.1128/mbio.00676-21</a>","apa":"Le, D., Krasnopeeva, E., Sinjab, F., Pilizota, T., &#38; Kim, M. (2021). Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria. <i>MBio</i>. American Society for Microbiology. <a href=\"https://doi.org/10.1128/mbio.00676-21\">https://doi.org/10.1128/mbio.00676-21</a>","ista":"Le D, Krasnopeeva E, Sinjab F, Pilizota T, Kim M. 2021. Active efflux leads to heterogeneous dissipation of proton motive force by protonophores in bacteria. mBio. 12(4), 676."},"_id":"15270","issue":"4","type":"journal_article","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"publication_status":"published","date_created":"2024-04-03T07:51:57Z","file":[{"checksum":"529e3f97ae5c5f5cc743c4fc130c9440","access_level":"open_access","success":1,"date_updated":"2024-04-10T09:05:49Z","file_name":"2021_mBio_Le.pdf","content_type":"application/pdf","creator":"dernst","date_created":"2024-04-10T09:05:49Z","file_size":1344204,"file_id":"15309","relation":"main_file"}],"department":[{"_id":"CaGu"}],"doi":"10.1128/mbio.00676-21","article_type":"original","day":"31"},{"author":[{"first_name":"Bahia","full_name":"Khalfaoui-Hassani, Bahia","last_name":"Khalfaoui-Hassani"},{"id":"D560034C-10C4-11EA-ABF4-A4B43DDC885E","first_name":"Petru Iulian","full_name":"Trasnea, Petru Iulian","last_name":"Trasnea"},{"last_name":"Steimle","full_name":"Steimle, Stefan","first_name":"Stefan"},{"full_name":"Koch, Hans-Georg","first_name":"Hans-Georg","last_name":"Koch"},{"last_name":"Daldal","first_name":"Fevzi","full_name":"Daldal, Fevzi"}],"article_number":"e01567","ddc":["570"],"external_id":{"pmid":["34281385"]},"oa_version":"Published Version","date_published":"2021-08-31T00:00:00Z","volume":12,"pmid":1,"year":"2021","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import","article_processing_charge":"No","has_accepted_license":"1","status":"public","publication":"mBio","publisher":"American Society for Microbiology","publication_identifier":{"issn":["2150-7511"]},"intvolume":"        12","month":"08","keyword":["Virology","Microbiology"],"date_created":"2024-04-03T07:59:04Z","publication_status":"published","tmp":{"short":"CC BY (4.0)","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png"},"type":"journal_article","doi":"10.1128/mbio.01567-21","department":[{"_id":"LeSa"}],"file":[{"content_type":"application/pdf","checksum":"2f6a57637cb3162eaeeb155a5b031e76","access_level":"open_access","success":1,"date_updated":"2024-04-09T10:45:11Z","file_name":"2021_mBio_KhalfaouiHassani.pdf","relation":"main_file","file_id":"15306","creator":"dernst","date_created":"2024-04-09T10:45:11Z","file_size":3383398}],"article_type":"original","day":"31","abstract":[{"text":"Copper (Cu) is a redox-active micronutrient that is both essential and toxic. Its cellular homeostasis is critical for supporting cuproprotein maturation while avoiding excessive oxidative stress. The Cu importer CcoA is the prototype of the widespread CalT subfamily of the MFS-type transporters. Hence, understanding its molecular mechanism of function is significant. Here, we show that CcoA undergoes a thiol:disulfide oxidoreduction cycle, which is important for its Cu import activity.","lang":"eng"}],"language":[{"iso":"eng"}],"oa":1,"file_date_updated":"2024-04-09T10:45:11Z","citation":{"mla":"Khalfaoui-Hassani, Bahia, et al. “Cysteine Mutants of the Major Facilitator Superfamily-Type Transporter CcoA Provide Insight into Copper Import.” <i>MBio</i>, vol. 12, no. 4, e01567, American Society for Microbiology, 2021, doi:<a href=\"https://doi.org/10.1128/mbio.01567-21\">10.1128/mbio.01567-21</a>.","ieee":"B. Khalfaoui-Hassani, P. I. Trasnea, S. Steimle, H.-G. Koch, and F. Daldal, “Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import,” <i>mBio</i>, vol. 12, no. 4. American Society for Microbiology, 2021.","chicago":"Khalfaoui-Hassani, Bahia, Petru Iulian Trasnea, Stefan Steimle, Hans-Georg Koch, and Fevzi Daldal. “Cysteine Mutants of the Major Facilitator Superfamily-Type Transporter CcoA Provide Insight into Copper Import.” <i>MBio</i>. American Society for Microbiology, 2021. <a href=\"https://doi.org/10.1128/mbio.01567-21\">https://doi.org/10.1128/mbio.01567-21</a>.","short":"B. Khalfaoui-Hassani, P.I. Trasnea, S. Steimle, H.-G. Koch, F. Daldal, MBio 12 (2021).","ista":"Khalfaoui-Hassani B, Trasnea PI, Steimle S, Koch H-G, Daldal F. 2021. Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import. mBio. 12(4), e01567.","apa":"Khalfaoui-Hassani, B., Trasnea, P. I., Steimle, S., Koch, H.-G., &#38; Daldal, F. (2021). Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import. <i>MBio</i>. American Society for Microbiology. <a href=\"https://doi.org/10.1128/mbio.01567-21\">https://doi.org/10.1128/mbio.01567-21</a>","ama":"Khalfaoui-Hassani B, Trasnea PI, Steimle S, Koch H-G, Daldal F. Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide insight into copper import. <i>mBio</i>. 2021;12(4). doi:<a href=\"https://doi.org/10.1128/mbio.01567-21\">10.1128/mbio.01567-21</a>"},"date_updated":"2024-04-09T10:47:16Z","quality_controlled":"1","issue":"4","_id":"15274"}]