{"isi":1,"file_date_updated":"2020-07-14T12:45:00Z","ddc":["572"],"volume":28,"publist_id":"7769","intvolume":" 28","year":"2018","citation":{"mla":"Fiedorczuk, Karol, and Leonid A. Sazanov. “Mammalian Mitochondrial Complex I Structure and Disease Causing Mutations.” Trends in Cell Biology, vol. 28, no. 10, Elsevier, 2018, pp. 835–67, doi:10.1016/j.tcb.2018.06.006.","ieee":"K. Fiedorczuk and L. A. Sazanov, “Mammalian mitochondrial complex I structure and disease causing mutations,” Trends in Cell Biology, vol. 28, no. 10. Elsevier, pp. 835–867, 2018.","apa":"Fiedorczuk, K., & Sazanov, L. A. (2018). Mammalian mitochondrial complex I structure and disease causing mutations. Trends in Cell Biology. Elsevier. https://doi.org/10.1016/j.tcb.2018.06.006","ista":"Fiedorczuk K, Sazanov LA. 2018. Mammalian mitochondrial complex I structure and disease causing mutations. Trends in Cell Biology. 28(10), 835–867.","chicago":"Fiedorczuk, Karol, and Leonid A Sazanov. “Mammalian Mitochondrial Complex I Structure and Disease Causing Mutations.” Trends in Cell Biology. Elsevier, 2018. https://doi.org/10.1016/j.tcb.2018.06.006.","ama":"Fiedorczuk K, Sazanov LA. Mammalian mitochondrial complex I structure and disease causing mutations. Trends in Cell Biology. 2018;28(10):835-867. doi:10.1016/j.tcb.2018.06.006","short":"K. Fiedorczuk, L.A. Sazanov, Trends in Cell Biology 28 (2018) 835–867."},"article_type":"original","_id":"152","language":[{"iso":"eng"}],"author":[{"id":"5BFF67CE-02D1-11E9-B11A-A5A4D7DFFFD0","full_name":"Fiedorczuk, Karol","first_name":"Karol","last_name":"Fiedorczuk"},{"full_name":"Sazanov, Leonid A","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","first_name":"Leonid A","last_name":"Sazanov","orcid":"0000-0002-0977-7989"}],"publication":"Trends in Cell Biology","has_accepted_license":"1","page":"835 - 867","doi":"10.1016/j.tcb.2018.06.006","external_id":{"isi":["000445118200007"]},"status":"public","title":"Mammalian mitochondrial complex I structure and disease causing mutations","quality_controlled":"1","date_created":"2018-12-11T11:44:54Z","user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","oa_version":"Submitted Version","oa":1,"scopus_import":"1","publisher":"Elsevier","issue":"10","date_published":"2018-07-26T00:00:00Z","publication_status":"published","abstract":[{"text":"Complex I has an essential role in ATP production by coupling electron transfer from NADH to quinone with translocation of protons across the inner mitochondrial membrane. Isolated complex I deficiency is a frequent cause of mitochondrial inherited diseases. Complex I has also been implicated in cancer, ageing, and neurodegenerative conditions. Until recently, the understanding of complex I deficiency on the molecular level was limited due to the lack of high-resolution structures of the enzyme. However, due to developments in single particle cryo-electron microscopy (cryo-EM), recent studies have reported nearly atomic resolution maps and models of mitochondrial complex I. These structures significantly add to our understanding of complex I mechanism and assembly. The disease-causing mutations are discussed here in their structural context.","lang":"eng"}],"department":[{"_id":"LeSa"}],"day":"26","type":"journal_article","file":[{"date_updated":"2020-07-14T12:45:00Z","file_size":2185385,"date_created":"2019-11-07T12:55:20Z","file_id":"6994","relation":"main_file","checksum":"ef6d2b4e1fd63948539639242610bfa6","file_name":"SasanovFinalMS+EdComments_LS_allacc_withFigs.pdf","creator":"lsazanov","access_level":"open_access","content_type":"application/pdf"}],"date_updated":"2023-09-13T08:51:56Z","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode","image":"/images/cc_by_nc_nd.png","name":"Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)","short":"CC BY-NC-ND (4.0)"},"article_processing_charge":"No","month":"07"}