{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,16]],"date-time":"2026-06-16T23:01:47Z","timestamp":1781650907487,"version":"3.54.5"},"reference-count":63,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2024,10,19]],"date-time":"2024-10-19T00:00:00Z","timestamp":1729296000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2024,10,19]],"date-time":"2024-10-19T00:00:00Z","timestamp":1729296000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"name":"Science and Engineering Research Board, Department of Science and Technology, Government of India","award":["EEQ\/2017\/000445"],"award-info":[{"award-number":["EEQ\/2017\/000445"]}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Mol Biol Rep"],"published-print":{"date-parts":[[2024,12]]},"DOI":"10.1007\/s11033-024-10022-9","type":"journal-article","created":{"date-parts":[[2024,10,19]],"date-time":"2024-10-19T07:03:20Z","timestamp":1729321400000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["Differential expression of nuclear-derived mitochondrial succinate dehydrogenase genes in metabolically active buffalo tissues"],"prefix":"10.1007","volume":"51","author":[{"given":"E. M.","family":"Sadeesh","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9442-3319","authenticated-orcid":false,"given":"Anuj","family":"Malik","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Madhuri S.","family":"Lahamge","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pratiksha","family":"Singh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2024,10,19]]},"reference":[{"key":"10022_CR1","doi-asserted-by":"publisher","first-page":"103","DOI":"10.3389\/fevo.2020.00103","volume":"8","author":"HI Ahmad","year":"2020","unstructured":"Ahmad HI, Ahmad MJ, Jabbir F, Ahmar S, Ahmad N, Elokil AA, Chen J (2020) The domestication makeup: evolution, survival, and challenges. Front EcolEvol 8:103. https:\/\/doi.org\/10.3389\/fevo.2020.00103","journal-title":"Front EcolEvol"},{"issue":"10","key":"10022_CR2","doi-asserted-by":"publisher","first-page":"2910","DOI":"10.3390\/ani11102910","volume":"11","author":"A Bertoni","year":"2021","unstructured":"Bertoni A, \u00c1lvarez-Mac\u00edas A, Mota-Rojas D, D\u00e1valos JL, Minervino AHH (2021) Dual-purpose water buffalo production systems in tropical latinamerica: bases for a sustainable model. Animals 11(10):2910. https:\/\/doi.org\/10.3390\/ani11102910","journal-title":"Animals"},{"issue":"10","key":"10022_CR3","doi-asserted-by":"publisher","first-page":"1274","DOI":"10.1016\/j.cub.2016.03.053","volume":"26","author":"A Karnkowska","year":"2016","unstructured":"Karnkowska A, Vacek V, Zub\u00e1\u010dov\u00e1 Z, Treitli SC, Petr\u017eelkov\u00e1 R, Eme L et al (2016) A Eukaryote without a mitochondrial organelle. Curr Biol 26(10):1274\u20131284. https:\/\/doi.org\/10.1016\/j.cub.2016.03.053","journal-title":"Curr Biol"},{"issue":"4","key":"10022_CR4","doi-asserted-by":"publisher","first-page":"312","DOI":"10.1016\/j.tibs.2017.01.003","volume":"42","author":"A Bezawork-Geleta","year":"2017","unstructured":"Bezawork-Geleta A, Rohlena J, Dong L, Pacak K, Neuzil J (2017) Mitochondrial complex II: at the crossroads. Trends Biochem Sci 42(4):312\u2013325. https:\/\/doi.org\/10.1016\/j.tibs.2017.01.003","journal-title":"Trends Biochem Sci"},{"key":"10022_CR5","doi-asserted-by":"publisher","first-page":"101674","DOI":"10.1016\/j.redox.2020.101674","volume":"37","author":"D Nolfi-Donegan","year":"2020","unstructured":"Nolfi-Donegan D, Braganza A, Shiva S (2020) Mitochondrial electron transport chain: oxidative phosphorylation, oxidant production, and methods of measurement. Redox Biol 37:101674. https:\/\/doi.org\/10.1016\/j.redox.2020.101674","journal-title":"Redox Biol"},{"issue":"13","key":"10022_CR6","doi-asserted-by":"publisher","first-page":"7487","DOI":"10.3390\/ijms23137487","volume":"23","author":"N Turton","year":"2022","unstructured":"Turton N, Cufflin N, Dewsbury M, Fitzpatrick O, Islam R, Watler LL et al (2022) The biochemical assessment of mitochondrial respiratory chain disorders. Int J Mol Sci 23(13):7487. https:\/\/doi.org\/10.3390\/ijms23137487","journal-title":"Int J Mol Sci"},{"key":"10022_CR7","doi-asserted-by":"publisher","first-page":"563","DOI":"10.3390\/genes11050563","volume":"11","author":"P Jadiya","year":"2020","unstructured":"Jadiya P, Tamar D (2020) Mitochondrial protein quality control mechanisms. Genes 11:563. https:\/\/doi.org\/10.3390\/genes11050563","journal-title":"Genes"},{"issue":"5","key":"10022_CR8","doi-asserted-by":"publisher","first-page":"528","DOI":"10.1111\/cen.14289","volume":"93","author":"J MacFarlane","year":"2020","unstructured":"MacFarlane J, Seong KC, Bisambar C, Madhu B, Allinson K, Marker A et al (2020) A review of the tumour spectrum of germline succinate dehydrogenase gene mutations: beyond phaeochromocytoma and paraganglioma. Clin Endocrinol (Oxf) 93(5):528\u2013538. https:\/\/doi.org\/10.1111\/cen.14289","journal-title":"Clin Endocrinol (Oxf)"},{"issue":"5","key":"10022_CR9","doi-asserted-by":"publisher","first-page":"267","DOI":"10.1038\/s41580-018-0092-0","volume":"20","author":"N Pfanner","year":"2021","unstructured":"Pfanner N, Warscheid B, Wiedemann N (2021) Mitochondrial proteins: from biogenesis to functional networks. Nat Rev Mol Cell Biol 20(5):267\u2013284. https:\/\/doi.org\/10.1038\/s41580-018-0092-0","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"20","key":"10022_CR10","doi-asserted-by":"publisher","first-page":"4023","DOI":"10.1007\/s00018-019-03200-7","volume":"76","author":"B Moosavi","year":"2019","unstructured":"Moosavi B, Berry EA, Zhu XL, Yang WC, Yang GF (2019) The assembly of succinate dehydrogenase: a key enzyme in bioenergetics. Cell Mol Life Sci 76(20):4023\u20134042. https:\/\/doi.org\/10.1007\/s00018-019-03200-7","journal-title":"Cell Mol Life Sci"},{"issue":"6572","key":"10022_CR11","doi-asserted-by":"publisher","first-page":"1227","DOI":"10.1126\/science.abi7495","volume":"374","author":"JB Spinelli","year":"2021","unstructured":"Spinelli JB, Rosen PC, Sprenger HG, Puszynska AM, Mann JL, Roessler JM et al (2021) Fumarate is a terminal electron acceptor in the mammalian electron transport chain. Science 374(6572):1227\u20131237. https:\/\/doi.org\/10.1126\/science.abi7495","journal-title":"Science"},{"issue":"6","key":"10022_CR12","doi-asserted-by":"publisher","first-page":"384","DOI":"10.1136\/jmedgenet-2017-105127","volume":"55","author":"KA Andrews","year":"2018","unstructured":"Andrews KA, Ascher DB, Pires DEV, Barnes DR, Vialard L, Casey RT et al (2018) Tumour risks and genotype\u2013phenotype correlations associated with germline variants in succinate dehydrogenase subunit genes SDHB, SDHC and SDHD. J Med Genet 55(6):384\u2013394. https:\/\/doi.org\/10.1136\/jmedgenet-2017-105127","journal-title":"J Med Genet"},{"key":"10022_CR13","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1016\/j.mito.2017.12.002","volume":"42","author":"M JodeiriFarshbaf","year":"2018","unstructured":"JodeiriFarshbaf M, Kiani-Esfahani A (2018) Succinate dehydrogenase: Prospect for neurodegenerative diseases. Mitochondrion 42:77\u201383. https:\/\/doi.org\/10.1016\/j.mito.2017.12.002","journal-title":"Mitochondrion"},{"issue":"1\u20132","key":"10022_CR14","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1016\/j.ymgme.2020.09.009","volume":"131","author":"M Fullerton","year":"2020","unstructured":"Fullerton M, McFarland R, Taylor RW, Alston CL (2020) The genetic basis of isolated mitochondrial complex II deficiency. Mol Genet Metab 131(1\u20132):53\u201365. https:\/\/doi.org\/10.1016\/j.ymgme.2020.09.009","journal-title":"Mol Genet Metab"},{"issue":"1","key":"10022_CR15","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1111\/j.1365-2796.2009.02111.x","volume":"266","author":"B Pasini","year":"2009","unstructured":"Pasini B, Stratakis CA (2009) SDH mutations in tumorigenesis and inherited endocrine tumours: lesson from the phaeochromocytoma-paraganglioma syndromes. J Intern Med 266(1):19\u201342. https:\/\/doi.org\/10.1111\/j.1365-2796.2009.02111.x","journal-title":"J Intern Med"},{"issue":"7","key":"10022_CR16","doi-asserted-by":"publisher","first-page":"1043","DOI":"10.1016\/j.cell.2005.05.025","volume":"121","author":"F Sun","year":"2005","unstructured":"Sun F, Huo X, Zhai Y, Wang A, Xu J, Su D, Bartlam M, Rao Z (2005) Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121(7):1043\u20131057. https:\/\/doi.org\/10.1016\/j.cell.2005.05.025","journal-title":"Cell"},{"issue":"18","key":"10022_CR17","doi-asserted-by":"publisher","first-page":"e2216713120","DOI":"10.1073\/pnas.2216713120","volume":"120","author":"Z Du","year":"2023","unstructured":"Du Z, Zhou X, Lai Y, Xu J, Zhang Y, Zhou S et al (2023) Structure of the human respiratory complex II. Proc Natl Acad Sci U S A 120(18):e2216713120. https:\/\/doi.org\/10.1073\/pnas.2216713120","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"2","key":"10022_CR18","doi-asserted-by":"publisher","first-page":"168","DOI":"10.3109\/10409238.2014.990556","volume":"50","author":"JG Van Vranken","year":"2015","unstructured":"Van Vranken JG, Na U, Winge DR, Rutter J (2015) Protein-mediated assembly of succinate dehydrogenase and its cofactors. Crit Rev Biochem Mol Biol 50(2):168\u2013180. https:\/\/doi.org\/10.3109\/10409238.2014.990556","journal-title":"Crit Rev Biochem Mol Biol"},{"issue":"2","key":"10022_CR19","doi-asserted-by":"publisher","first-page":"292","DOI":"10.1016\/j.cmet.2015.12.005","volume":"23","author":"N Maio","year":"2016","unstructured":"Maio N, Ghezzi D, Verrigni D, Rizza T, Bertini E, Martinelli D et al (2016) Disease-causing SDHAF1 mutations impair transfer of Fe-S clusters to SDHB. Cell Metab 23(2):292\u2013302. https:\/\/doi.org\/10.1016\/j.cmet.2015.12.005","journal-title":"Cell Metab"},{"key":"10022_CR20","doi-asserted-by":"publisher","first-page":"38","DOI":"10.1016\/j.sbi.2019.01.027","volume":"59","author":"P Sharma","year":"2019","unstructured":"Sharma P, Maklashina E, Cecchini G, Iverson TM (2019) Maturation of the respiratory complex II flavoprotein. Curr Opin Struct Biol 59:38\u201346. https:\/\/doi.org\/10.1016\/j.sbi.2019.01.027","journal-title":"Curr Opin Struct Biol"},{"issue":"2","key":"10022_CR21","doi-asserted-by":"publisher","first-page":"144","DOI":"10.1038\/ng1095-144","volume":"11","author":"T Bourgeron","year":"1995","unstructured":"Bourgeron T, Rustin P, Chretien D, Birch-Machin M, Bourgeois M, Viegas-P\u00e9quignot E, Munnich A, R\u00f6tig A (1995) Mutation of a nuclear succinate dehydrogenase gene results in mitochondrial respiratory chain deficiency. Nat Genet 11(2):144\u2013149. https:\/\/doi.org\/10.1038\/ng1095-144","journal-title":"Nat Genet"},{"issue":"10","key":"10022_CR22","doi-asserted-by":"publisher","first-page":"1160","DOI":"10.1038\/ejhg.2010.83","volume":"18","author":"A Levitas","year":"2010","unstructured":"Levitas A, Muhammad E, Harel G, Saada A, Caspi VC, Manor E, Beck JC, Sheffield V, Parvari R (2010) Familial neonatal isolated cardiomyopathy caused by a mutation in the flavoprotein subunit of succinate dehydrogenase. Eur J Hum Genet 18(10):1160\u20131165. https:\/\/doi.org\/10.1038\/ejhg.2010.83","journal-title":"Eur J Hum Genet"},{"issue":"9","key":"10022_CR23","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1136\/jmedgenet-2012-101146","volume":"49","author":"CL Alston","year":"2012","unstructured":"Alston CL, Davison JE, Meloni F, van der Westhuizen FH, He L, Hornig-Do HT et al (2012) Recessive germline SDHA and SDHB mutations causing leukodystrophy and isolated mitochondrial complex II deficiency. J Med Genet 49(9):569\u2013577.","journal-title":"J Med Genet"},{"issue":"1","key":"10022_CR24","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1002\/ajmg.a.37986","volume":"173","author":"C Courage","year":"2017","unstructured":"Courage C, Jackson CB, Hahn D, Euro L, Nuoffer JM, Gallati S, Schaller A (2017) SDHA mutation with dominant transmission results in complex II deficiency with ocular, cardiac, and neurologic involvement. Am J Med Genet A 173(1):225\u2013230. https:\/\/doi.org\/10.1002\/ajmg.a.37986","journal-title":"Am J Med Genet A"},{"key":"10022_CR25","doi-asserted-by":"publisher","unstructured":"Ardissone A, Invernizzi F, Nasca A, Moroni I, Farina L, Ghezzi D (2015) Mitochondrial leukoencephalopathy and complex II deficiency associated with a recessive SDHB mutation with reduced penetrance. Mol Genet Metab Rep 51\u201354. https:\/\/doi.org\/10.1016\/j.ymgmr.2015.10.006","DOI":"10.1016\/j.ymgmr.2015.10.006"},{"issue":"3","key":"10022_CR26","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1002\/ana.24572","volume":"79","author":"G Helman","year":"2016","unstructured":"Helman G, Caldovic L, Whitehead MT, Simons C, Brockmann K, Edvardson S et al (2016) Magnetic resonance imaging spectrum of succinate dehydrogenase-related infantile leukoencephalopathy. Ann Neurol 79(3):379\u2013386. https:\/\/doi.org\/10.1002\/ana.24572","journal-title":"Ann Neurol"},{"issue":"6","key":"10022_CR27","doi-asserted-by":"publisher","first-page":"1031","DOI":"10.1002\/ana.24650","volume":"79","author":"A Vanderver","year":"2016","unstructured":"Vanderver A, Simons C, Helman G, Crawford J, Wolf NI, Bernard G et al (2016) Whole exome sequencing in patients with white matter abnormalities. Ann Neurol 79(6):1031\u20131037. https:\/\/doi.org\/10.1002\/ana.24650","journal-title":"Ann Neurol"},{"key":"10022_CR28","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1007\/8904_2016_582","volume":"33","author":"S Gr\u00f8nborg","year":"2017","unstructured":"Gr\u00f8nborg S, Darin N, Miranda MJ, Damgaard B, Cayuela JA, Oldfors A et al (2017) Leukoencephalopathy due to complex II deficiency and bi-allelic SDHB mutations: further cases and implications for genetic counselling. JIMD Rep 33:69\u201377. https:\/\/doi.org\/10.1007\/8904_2016_582","journal-title":"JIMD Rep"},{"issue":"4","key":"10022_CR29","doi-asserted-by":"publisher","first-page":"345","DOI":"10.1111\/ahg.12377","volume":"84","author":"P Kaur","year":"2020","unstructured":"Kaur P, Sharma S, Kadavigere R, Girisha KM, Shukla A (2020) Novel variant p.(Ala102Thr) in SDHB causes mitochondrial complex II deficiency: case report and review of the literature. Ann Hum Genet 84(4):345\u2013351. https:\/\/doi.org\/10.1111\/ahg.12377","journal-title":"Ann Hum Genet"},{"issue":"3","key":"10022_CR30","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1136\/jmedgenet-2013-101932","volume":"51","author":"CB Jackson","year":"2014","unstructured":"Jackson CB, Nuoffer JM, Hahn D, Prokisch H, Haberberger B, Gautschi M et al (2014) Mutations in SDHD lead to autosomal recessive encephalomyopathy and isolated mitochondrial complex II deficiency. J Med Genet 51(3):170\u2013175. https:\/\/doi.org\/10.1136\/jmedgenet-2013-101932","journal-title":"J Med Genet"},{"issue":"8","key":"10022_CR31","doi-asserted-by":"publisher","first-page":"869","DOI":"10.1007\/s00439-015-1568-z","volume":"134","author":"CL Alston","year":"2015","unstructured":"Alston CL, CeccatelliBerti C, Blakely EL, Ol\u00e1hov\u00e1 M, He L, McMahon CJ et al (2015) A recessive homozygous p.Asp92Gly SDHD mutation causes prenatal cardiomyopathy and a severe mitochondrial complex II deficiency. Hum Genet 134(8):869\u2013879. https:\/\/doi.org\/10.1007\/s00439-015-1568-z","journal-title":"Hum Genet"},{"issue":"6","key":"10022_CR32","doi-asserted-by":"publisher","first-page":"654","DOI":"10.1038\/ng.378","volume":"41","author":"D Ghezzi","year":"2009","unstructured":"Ghezzi D, Goffrini P, Uziel G, Horvath R, Klopstock T, Lochm\u00fcller H et al (2009) SDHAF1, encoding a LYR complex-II specific assembly factor, is mutated in SDH-defective infantile leukoencephalopathy. Nat Genet 41(6):654\u2013656. https:\/\/doi.org\/10.1038\/ng.378","journal-title":"Nat Genet"},{"key":"10022_CR33","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1016\/S1470-2045(10)70007-3","volume":"11","author":"JP Bayley","year":"2010","unstructured":"Bayley JP, Kunst HP, Cascon A, Sampietro ML, Gaal J, Korpershoek E et al (2010) SDHAF2 mutations in familial and sporadic paraganglioma and phaeochromocytoma. Lancet Oncol 11:366\u2013372. https:\/\/doi.org\/10.1016\/S1470-2045(10)70007-3","journal-title":"Lancet Oncol"},{"issue":"8","key":"10022_CR34","doi-asserted-by":"publisher","first-page":"1107","DOI":"10.1002\/1873-3468.14022","volume":"595","author":"CS Palmer","year":"2021","unstructured":"Palmer CS, Anderson AJ, Stojanovski D (2021) Mitochondrial protein import dysfunction: mitochondrial disease, neurodegenerative disease and cancer. FEBS Lett 595(8):1107\u20131131. https:\/\/doi.org\/10.1002\/1873-3468.14022","journal-title":"FEBS Lett"},{"key":"10022_CR35","doi-asserted-by":"publisher","first-page":"D1541","DOI":"10.1093\/nar\/gkaa1011","volume":"49","author":"S Rath","year":"2021","unstructured":"Rath S, Sharma R, Gupta R, Ast T, Chan C, Durham TJ et al (2021) MitoCarta3.0: an updated mitochondrial proteome now with sub-organelle localization and pathway annotations. Nucleic Acids Res 49:D1541\u2013D1547. https:\/\/doi.org\/10.1093\/nar\/gkaa1011","journal-title":"Nucleic Acids Res"},{"key":"10022_CR36","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1016\/j.cell.2008.06.016","volume":"134","author":"DJ Pagliarini","year":"2008","unstructured":"Pagliarini DJ, Calvo SE, Chang B, Sheth SA, Vafai SB, Ong SE et al (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell 134:112\u2013123. https:\/\/doi.org\/10.1016\/j.cell.2008.06.016","journal-title":"Cell"},{"issue":"1","key":"10022_CR37","doi-asserted-by":"publisher","first-page":"1","DOI":"10.22175\/mmb.11705","volume":"5","author":"R Ramanathan","year":"2021","unstructured":"Ramanathan R, Nair MN, Wang Y, Li S, Beach CM, Mancini R et al (2021) Differential abundance of mitochondrial proteome influences the color stability of beef longissimus lumborum and psoas major muscles. Meat Muscle Biol 5(1):1\u201316. https:\/\/doi.org\/10.22175\/mmb.11705","journal-title":"Meat Muscle Biol"},{"key":"10022_CR38","doi-asserted-by":"publisher","unstructured":"Zhai C, Li Puma LC, Chicco AJ, Omar A, Delmore RJ, Geornaras I et al (2022) Pulmonary arterial pressure in fattened Angus steers at moderate altitude influences early postmortem mitochondria functionality and meat color during retail display. J Ani Sci 100(2). https:\/\/doi.org\/10.1093\/jas\/skac002","DOI":"10.1093\/jas\/skac002"},{"issue":"6","key":"10022_CR39","doi-asserted-by":"publisher","first-page":"5255","DOI":"10.1007\/s11033-023-08416-2","volume":"50","author":"EM Sadeesh","year":"2023","unstructured":"Sadeesh EM, Singla N, Lahamge MS, Kumari S, Ampadi AN, Anuj M (2023) Tissue heterogeneity of mitochondrial activity, biogenesis and mitochondrial protein gene expression in buffalo. Mol Bio Rep 50(6):5255\u20135266. https:\/\/doi.org\/10.1007\/s11033-023-08416-2","journal-title":"Mol Bio Rep"},{"key":"10022_CR40","doi-asserted-by":"publisher","DOI":"10.1007\/s12033-024-01206-6","author":"EM Sadeesh","year":"2024","unstructured":"Sadeesh EM, Lahamge MS, Malik A, Ampadi AN (2024) Nuclear genome-encoded mitochondrial OXPHOS complex I genes in female buffalo show tissue-specific differences. Mol Biotechnol Https:\/doi. https:\/\/doi.org\/10.1007\/s12033-024-01206-6","journal-title":"Mol Biotechnol Https:\/doi"},{"key":"10022_CR41","doi-asserted-by":"publisher","unstructured":"Sadeesh EM, Lahamge MS, Malik A, Ampadi AN (2024) Differential expression of nuclear-encoded mitochondrial protein genes of ATP synthase across different tissues of female buffalo.Mol Biotechnol. https:\/\/doi.org\/10.1007\/s12033-024-01085-x","DOI":"10.1007\/s12033-024-01085-x"},{"key":"10022_CR42","doi-asserted-by":"publisher","first-page":"i884","DOI":"10.1093\/bioinformatics\/bty560","volume":"34","author":"S Chen","year":"2018","unstructured":"Chen S, Zhou Y, Chen Y, Gu J (2018) FASTP: an ultra-fast all-in-one FASTQ preprocessor. Bioinformatics 34:i884\u2013i890","journal-title":"Bioinformatics"},{"key":"10022_CR43","doi-asserted-by":"crossref","unstructured":"Kim D, Paggi JM, Park C, Bennett C, Salzberg SL (2019) Graph-based genome alignment and genotyping with HISAT2 and HISAT- genotype.Nature biotechnology 37. 8:907\u2013915","DOI":"10.1038\/s41587-019-0201-4"},{"issue":"1","key":"10022_CR44","doi-asserted-by":"publisher","first-page":"139","DOI":"10.1093\/bioinformatics\/btp616","volume":"26","author":"MD Robinson","year":"2010","unstructured":"Robinson MD, McCarthy DJ, Smyth GK (2010) edgeR: a Bioconductor package for differential expression analysis of digital gene expression data. Bioinformatics 26(1):139\u2013140. https:\/\/doi.org\/10.1093\/bioinformatics\/btp616","journal-title":"Bioinformatics"},{"issue":"1","key":"10022_CR45","doi-asserted-by":"publisher","first-page":"289","DOI":"10.1111\/j.2517-6161.1995.tb02031.x","volume":"57","author":"Y Benjamini","year":"1995","unstructured":"Benjamini Y, Hochberg Y (1995) Controlling the false discovery rate: a practical and powerful approach to multiple testing. J Roy Stat Soc: Ser B (Methodol) 57(1):289\u2013300","journal-title":"J Roy Stat Soc: Ser B (Methodol)"},{"issue":"2","key":"10022_CR46","doi-asserted-by":"publisher","first-page":"E287","DOI":"10.1210\/jc.2014-1870","volume":"100","author":"M Menara","year":"2015","unstructured":"Menara M, Oudijk L, Badoual C, Bertherat J, Lepoutre-Lussey C, Amar L et al (2015) SDHD immunohistochemistry: a new tool to validate SDHx mutations in pheochromocytoma\/paraganglioma. J Clin Endocrinol Metab 100(2):E287\u2013291. https:\/\/doi.org\/10.1210\/jc.2014-1870","journal-title":"J Clin Endocrinol Metab"},{"issue":"6","key":"10022_CR47","doi-asserted-by":"publisher","first-page":"807","DOI":"10.1038\/modpathol.2015.41","volume":"28","author":"TG Papathomas","year":"2015","unstructured":"Papathomas TG, Oudijk L, Persu A, Gill AJ, van Nederveen F, Tischler AS et al (2015) SDHB\/SDHA immunohistochemistry in pheochromocytomas and paragangliomas:amulticenter interobserver variation analysis using virtual microscopy: a multinational study of the European Network for the study ofAdrenalTumors (ENS@T). Mod Pathol 28(6):807\u2013821. https:\/\/doi.org\/10.1038\/modpathol.2015.41","journal-title":"Mod Pathol"},{"key":"10022_CR48","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1186\/2049-3002-2-21","volume":"2","author":"PP Aspuria","year":"2014","unstructured":"Aspuria PP, Lunt SY, Varemo L, Vergnes L, Gozo M, Beach JA et al (2014) Succinate dehydrogenase inhibition leads to epithelial-mesenchymal transition and reprogrammed carbon metabolism. Cancer Metab 2:21. https:\/\/doi.org\/10.1186\/2049-3002-2-21","journal-title":"Cancer Metab"},{"key":"10022_CR49","doi-asserted-by":"publisher","first-page":"769196","DOI":"10.3389\/fonc.2021.769196","volume":"11","author":"L Xia","year":"2021","unstructured":"Xia L, Zhang H, Wang X, Zhang X, Nie K (2021) The role of succinic acid metabolism in ovarian cancer. Front Oncol 11:769196. https:\/\/doi.org\/10.3389\/fonc.2021.769196","journal-title":"Front Oncol"},{"key":"10022_CR50","doi-asserted-by":"publisher","first-page":"567","DOI":"10.1016\/j.bbabio.2006.05.015","volume":"1757","author":"MA Selak","year":"2006","unstructured":"Selak MA, Duran RV, Gottlieb E (2006) Redox stress is not essential for the pseudo-hypoxic phenotype of succinate dehydrogenase deficient cells. BiochimBiophys Acta 1757:567\u2013572. https:\/\/doi.org\/10.1016\/j.bbabio.2006.05.015","journal-title":"BiochimBiophys Acta"},{"key":"10022_CR51","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.ceb.2014.09.004","volume":"33","author":"DG Hardie","year":"2015","unstructured":"Hardie DG (2015) AMPK: positive and negative regulation, and its role in whole-body energy homeostasis. Curr Opin Cell Biol 33:1\u20137. https:\/\/doi.org\/10.1016\/j.ceb.2014.09.004","journal-title":"Curr Opin Cell Biol"},{"issue":"15","key":"10022_CR52","doi-asserted-by":"publisher","first-page":"3011","DOI":"10.1093\/hmg\/ddq206","volume":"19","author":"N Burnichon","year":"2010","unstructured":"Burnichon N, Bri\u00e8re JJ, Lib\u00e9 R, Vescovo L, Rivi\u00e8re J, Tissier F et al (2010) SDHA is a tumor suppressor gene causing paraganglioma. Hum Mol Genet 19(15):3011\u20133020. https:\/\/doi.org\/10.1093\/hmg\/ddq206","journal-title":"Hum Mol Genet"},{"key":"10022_CR53","doi-asserted-by":"publisher","first-page":"115","DOI":"10.1186\/s13048-014-0115-1","volume":"7","author":"L Chen","year":"2014","unstructured":"Chen L, Liu T, Zhang S, Zhou J, Wang Y, Di W (2014) Succinate dehydrogenase subunit B inhibits the AMPK-HIF-1alpha pathway in human ovarian cancer in vitro. J Ovarian Res 7:115. https:\/\/doi.org\/10.1186\/s13048-014-0115-1","journal-title":"J Ovarian Res"},{"issue":"3","key":"10022_CR54","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1530\/ERC-11-0324","volume":"19","author":"A Malinoc","year":"2012","unstructured":"Malinoc A, Sullivan M, Wiech T, Schmid KW, Jilg C, Straeter J et al (2012) Biallelic inactivation of the SDHC gene in renal carcinoma associated with paraganglioma syndrome type 3. EndocrRelat Cancer 19(3):283\u2013290. https:\/\/doi.org\/10.1530\/ERC-11-0324","journal-title":"EndocrRelat Cancer"},{"key":"10022_CR55","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.mito.2020.04.002","volume":"53","author":"S Mukherjee","year":"2020","unstructured":"Mukherjee S, Ghosh A (2020) Molecular mechanism of mitochondrial respiratory chain assembly and its relation to mitochondrial diseases. Mitochondrion 53:1\u201320. https:\/\/doi.org\/10.1016\/j.mito.2020.04.002","journal-title":"Mitochondrion"},{"key":"10022_CR56","doi-asserted-by":"publisher","first-page":"69","DOI":"10.1186\/1750-1172-7-69","volume":"7","author":"A Ohlenbusch","year":"2012","unstructured":"Ohlenbusch A, Edvardson S, Skorpen J, Bjornstad A, Saada A, Elpeleg O et al (2012) Leukoencephalopathy with accumulated succinate is indicative of SDHAF1-related complex II deficiency. Orphanet J Rare Dis 7:69. https:\/\/doi.org\/10.1186\/1750-1172-7-69","journal-title":"Orphanet J Rare Dis"},{"issue":"2","key":"10022_CR57","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1002\/ajmg.a.35714","volume":"161A","author":"S Jain-Ghai","year":"2013","unstructured":"Jain-Ghai S, Cameron JM, Al Maawali A, Blaser S, MacKay N, Robinson B et al (2013) Complex II deficiency-a case report and review of the literature. Am J Med Genet A 161A(2):285\u2013294. https:\/\/doi.org\/10.1002\/ajmg.a.35714","journal-title":"Am J Med Genet A"},{"key":"10022_CR58","doi-asserted-by":"publisher","first-page":"23548","DOI":"10.1073\/pnas.2007391117","volume":"117","author":"P Sharma","year":"2020","unstructured":"Sharma P, Maklashina E, Cecchini G, Iverson TM (2020) The roles of SDHAF2 and dicarboxylate in covalent flavinylation of SDHA, the human complex II flavoprotein. Proc Natl Acad Sci 117:23548\u201323556. https:\/\/doi.org\/10.1073\/pnas.2007391117","journal-title":"Proc Natl Acad Sci"},{"issue":"2","key":"10022_CR59","doi-asserted-by":"publisher","first-page":"253","DOI":"10.1016\/j.cmet.2014.05.014","volume":"20","author":"U Na","year":"2014","unstructured":"Na U, Yu W, Cox J, Bricker DK, Brockmann K, Rutter J et al (2014) The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase. Cell Metab 20(2):253\u2013266. https:\/\/doi.org\/10.1016\/j.cmet.2014.05.014","journal-title":"Cell Metab"},{"issue":"1","key":"10022_CR60","doi-asserted-by":"publisher","first-page":"497","DOI":"10.1186\/s12885-017-3486-z","volume":"17","author":"T Dwight","year":"2017","unstructured":"Dwight T, Na U, Kim E, Zhu Y, Richardson AL, Robinson BG et al (2017) Analysis of SDHAF3 in familial and sporadic pheochromocytoma and paraganglioma. BMC Cancer 17(1):497. https:\/\/doi.org\/10.1186\/s12885-017-3486-z","journal-title":"BMC Cancer"},{"issue":"2","key":"10022_CR61","doi-asserted-by":"publisher","first-page":"168","DOI":"10.3109\/10409238.2014.990556","volume":"50","author":"JG Van Vranken","year":"2015","unstructured":"Van Vranken JG, Na U, Winge DR, Rutter J (2015) Protein-mediated assembly of succinate dehydrogenase and its cofactors. Crit Rev Biochem Mol Biol 50(2):168\u2013180","journal-title":"Crit Rev Biochem Mol Biol"},{"issue":"1","key":"10022_CR62","doi-asserted-by":"publisher","first-page":"3947","DOI":"10.1038\/s41467-022-31548-1","volume":"213","author":"X Wang","year":"2022","unstructured":"Wang X, Zhang X, Cao K, Zeng M, Fu X, Zheng A et al (2022) Cardiac disruption of SDHAF4-mediated mitochondrial complex II assembly promotes dilated cardiomyopathy. Nat Commun 213(1):3947. https:\/\/doi.org\/10.1038\/s41467-022-31548-1","journal-title":"Nat Commun"},{"key":"10022_CR63","doi-asserted-by":"publisher","first-page":"247","DOI":"10.1016\/j.freeradbiomed.2023.07.023","volume":"207","author":"K Cao","year":"2023","unstructured":"Cao K, Xu J, Cao W, Wang X, Lv W, Zeng M et al (2023) Assembly of mitochondrial succinate dehydrogenase in human health and disease. Free RadicBiol Med 207:247\u2013259. https:\/\/doi.org\/10.1016\/j.freeradbiomed.2023.07.023","journal-title":"Free RadicBiol Med"}],"container-title":["Molecular Biology Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11033-024-10022-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s11033-024-10022-9\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s11033-024-10022-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,2,5]],"date-time":"2025-02-05T04:34:17Z","timestamp":1738730057000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s11033-024-10022-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,10,19]]},"references-count":63,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2024,12]]}},"alternative-id":["10022"],"URL":"https:\/\/doi.org\/10.1007\/s11033-024-10022-9","relation":{},"ISSN":["0301-4851","1573-4978"],"issn-type":[{"value":"0301-4851","type":"print"},{"value":"1573-4978","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,10,19]]},"assertion":[{"value":"22 August 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"14 October 2024","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 October 2024","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Our study employed tissue specimens collected post-slaughter. As there was no direct interaction with live animals, ethical approval was not required for this research.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Ethical approval"}},{"value":"This article does not involve personal data or require consent, as no individual participation was involved.","order":3,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent to participate"}},{"value":"All authors have consented to the publication of this research in this journal.","order":4,"name":"Ethics","group":{"name":"EthicsHeading","label":"Consent for publication"}},{"value":"The authors declare no competing interests.","order":5,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"1071"}}