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A."},{"key":"10.1016\/S0005-2728(03)00059-8_BIB107","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1002\/j.1460-2075.1989.tb03424.x","article-title":"A homologue of the nuclear coded 49 kd subunit of bovine mitochondrial NADH\u2013ubiquinone reductase is coded in chloroplast DNA","volume":"8","author":"Fearnley","year":"1989","journal-title":"EMBO J."},{"key":"10.1016\/S0005-2728(03)00059-8_BIB108","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1021\/bi00221a024","article-title":"The 30-kilodalton subunit of bovine mitochondrial complex I is homologous to a protein coded in chloroplast DNA","volume":"30","author":"Pilkington","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/S0005-2728(03)00059-8_BIB109","doi-asserted-by":"crossref","first-page":"3257","DOI":"10.1021\/bi00434a021","article-title":"Mitochondrial NADH\u2013ubiquinone reductase: complementary DNA sequences of import precursors of the bovine and human 24-kDa subunit","volume":"28","author":"Pilkington","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/S0005-2728(03)00059-8_BIB110","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1007\/BF00393404","article-title":"cDNA of the 24 kDa subunit of the bovine respiratory chain NADH dehydrogenase: high sequence conservation in mammals and tissue-specific and growth-dependent expression","volume":"16","author":"Chomyn","year":"1989","journal-title":"Curr. 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