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{{Infobox_gene}}
{{PBB_Controls
'''NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''NDUFS1'' [[gene]].<ref name="pmid1935949">{{cite journal | vauthors = Chow W, Ragan I, Robinson BH | title = Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase | journal = European Journal of Biochemistry / FEBS | volume = 201 | issue = 3 | pages = 547–50 | date = Nov 1991 | pmid = 1935949 | pmc =  | doi = 10.1111/j.1432-1033.1991.tb16313.x }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NDUFS1 NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4719| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)
| HGNCid = 7707
| Symbol = NDUFS1
| AltSymbols =; CI-75Kd; MGC26839; PRO1304
| OMIM = 157655
| ECnumber = 
| Homologene = 3670
| MGIid = 2443241
| GeneAtlas_image1 = PBB_GE_NDUFS1_203039_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003954 |text = NADH dehydrogenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0008137 |text = NADH dehydrogenase (ubiquinone) activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051537 |text = 2 iron, 2 sulfur cluster binding}} {{GNF_GO|id=GO:0051539 |text = 4 iron, 4 sulfur cluster binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0006120 |text = mitochondrial electron transport, NADH to ubiquinone}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4719
    | Hs_Ensembl = ENSG00000023228
    | Hs_RefseqProtein = NP_004997
    | Hs_RefseqmRNA = NM_005006
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 206695783
    | Hs_GenLoc_end = 206732392
    | Hs_Uniprot = P28331
    | Mm_EntrezGene = 227197
    | Mm_Ensembl = ENSMUSG00000025968
    | Mm_RefseqmRNA = NM_145518
    | Mm_RefseqProtein = NP_663493
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 63077861
    | Mm_GenLoc_end = 63110985
    | Mm_Uniprot = Q3TIU7
  }}
}}
'''NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)''', also known as '''NDUFS1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NDUFS1 NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4719| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The protein encoded by this gene belongs to the [[NADH dehydrogenase|complex I]] 75 kDa subunit family. Mammalian complex I is composed of 45 different subunits. It locates at the [[mitochondrion|mitochondrial]] inner membrane. This protein has [[NADH dehydrogenase]] activity and [[oxidoreductase]] activity. It transfers electrons from NADH to the [[respiratory chain]]. The immediate electron acceptor for the enzyme is believed to be [[ubiquinone]]. This protein is the largest subunit of complex I and it is a component of the [[iron-sulfur protein|iron-sulfur]] (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the complex I 75 kDa subunit family. Mammalian complex I is composed of 45 different subunits. It locates at the mitochondrial inner membrane. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This protein is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. Mutations in this gene are associated with complex I deficiency.<ref name="entrez">{{cite web | title = Entrez Gene: NDUFS1 NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4719| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
Mutations in the NDUFS1 gene are associated with Mitochondrial Complex I Deficiency, which is autosomal recessive. This deficiency is the most common enzymatic defect of the oxidative phosphorylation disorders.<ref>{{cite journal | vauthors = Kirby DM, Salemi R, Sugiana C, Ohtake A, Parry L, Bell KM, Kirk EP, Boneh A, Taylor RW, Dahl HH, Ryan MT, Thorburn DR | title = NDUFS6 mutations are a novel cause of lethal neonatal mitochondrial complex I deficiency | journal = The Journal of Clinical Investigation | volume = 114 | issue = 6 | pages = 837–45 | date = Sep 2004 | pmid = 15372108 | doi = 10.1172/JCI20683 | pmc=516258}}</ref><ref>{{cite journal | vauthors = McFarland R, Kirby DM, Fowler KJ, Ohtake A, Ryan MT, Amor DJ, Fletcher JM, Dixon JW, Collins FA, Turnbull DM, Taylor RW, Thorburn DR | title = De novo mutations in the mitochondrial ND3 gene as a cause of infantile mitochondrial encephalopathy and complex I deficiency | journal = Annals of Neurology | volume = 55 | issue = 1 | pages = 58–64 | date = Jan 2004 | pmid = 14705112 | doi = 10.1002/ana.10787 }}</ref> Mitochondrial complex I deficiency shows extreme genetic heterogeneity and can be caused by mutation in nuclear-encoded genes or in mitochondrial-encoded genes. There are no obvious genotype-phenotype correlations, and inference of the underlying basis from the clinical or biochemical presentation is difficult, if not impossible.<ref>{{cite journal | vauthors = Haack TB, Haberberger B, Frisch EM, Wieland T, Iuso A, Gorza M, Strecker V, Graf E, Mayr JA, Herberg U, Hennermann JB, Klopstock T, Kuhn KA, Ahting U, Sperl W, Wilichowski E, Hoffmann GF, Tesarova M, Hansikova H, Zeman J, Plecko B, Zeviani M, Wittig I, Strom TM, Schuelke M, Freisinger P, Meitinger T, Prokisch H | title = Molecular diagnosis in mitochondrial complex I deficiency using exome sequencing | journal = Journal of Medical Genetics | volume = 49 | issue = 4 | pages = 277–83 | date = Apr 2012 | pmid = 22499348 | doi = 10.1136/jmedgenet-2012-100846 }}</ref> However, the majority of cases are caused by mutations in nuclear-encoded genes.<ref>{{cite journal | vauthors = Loeffen JL, Smeitink JA, Trijbels JM, Janssen AJ, Triepels RH, Sengers RC, van den Heuvel LP | title = Isolated complex I deficiency in children: clinical, biochemical and genetic aspects | journal = Human Mutation | volume = 15 | issue = 2 | pages = 123–34 | date = 2000 | pmid = 10649489 | doi = 10.1002/(SICI)1098-1004(200002)15:2<123::AID-HUMU1>3.0.CO;2-P }}</ref><ref>{{cite journal | vauthors = Triepels RH, Van Den Heuvel LP, Trijbels JM, Smeitink JA | title = Respiratory chain complex I deficiency | journal = American Journal of Medical Genetics | volume = 106 | issue = 1 | pages = 37–45 | date = 2001 | pmid = 11579423 | doi = 10.1002/ajmg.1397 }}</ref> It causes a wide range of clinical disorders, ranging from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, nonspecific encephalopathy, hypertrophic cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease.<ref>{{cite journal | vauthors = Robinson BH | title = Human complex I deficiency: clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect | journal = Biochimica et Biophysica Acta | volume = 1364 | issue = 2 | pages = 271–86 | date = May 1998 | pmid = 9593934 | doi=10.1016/s0005-2728(98)00033-4}}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Duncan AM, Chow W, Robinson BH | title = Localization of the human 75-kDal Fe-S protein of NADH-coenzyme Q reductase gene (NDUFS1) to 2q33----q34 | journal = Cytogenetics and Cell Genetics | volume = 60 | issue = 3-4 | pages = 212–3 | year = 1992 | pmid = 1505218 | doi = 10.1159/000133340 }}
| citations =
* {{cite journal | vauthors = Sumegi B, Srere PA | title = Complex I binds several mitochondrial NAD-coupled dehydrogenases | journal = The Journal of Biological Chemistry | volume = 259 | issue = 24 | pages = 15040–5 | date = Dec 1984 | pmid = 6439716 | doi =  }}
*{{cite journal | author=Duncan AM, Chow W, Robinson BH |title=Localization of the human 75-kDal Fe-S protein of NADH-coenzyme Q reductase gene (NDUFS1) to 2q33----q34. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 3-4 |pages= 212-3 |year= 1992 |pmid= 1505218 |doi= }}
* {{cite journal | vauthors = Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA | title = cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed | journal = Biochemical and Biophysical Research Communications | volume = 253 | issue = 2 | pages = 415–22 | date = Dec 1998 | pmid = 9878551 | doi = 10.1006/bbrc.1998.9786 }}
*{{cite journal  | author=Chow W, Ragan I, Robinson BH |title=Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase. |journal=Eur. J. Biochem. |volume=201 |issue= 3 |pages= 547-50 |year= 1991 |pmid= 1935949 |doi=  }}
* {{cite journal | vauthors = Bénit P, Chretien D, Kadhom N, de Lonlay-Debeney P, Cormier-Daire V, Cabral A, Peudenier S, Rustin P, Munnich A, Rötig A | title = Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 genes in mitochondrial complex I deficiency | journal = American Journal of Human Genetics | volume = 68 | issue = 6 | pages = 1344–52 | date = Jun 2001 | pmid = 11349233 | pmc = 1226121 | doi = 10.1086/320603 }}
*{{cite journal | author=Sumegi B, Srere PA |title=Complex I binds several mitochondrial NAD-coupled dehydrogenases. |journal=J. Biol. Chem. |volume=259 |issue= 24 |pages= 15040-5 |year= 1985 |pmid= 6439716 |doi=  }}
* {{cite journal | vauthors = Ricci JE, Muñoz-Pinedo C, Fitzgerald P, Bailly-Maitre B, Perkins GA, Yadava N, Scheffler IE, Ellisman MH, Green DR | title = Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain | journal = Cell | volume = 117 | issue = 6 | pages = 773–86 | date = Jun 2004 | pmid = 15186778 | doi = 10.1016/j.cell.2004.05.008 }}
*{{cite journal | author=Loeffen JL, Triepels RH, van den Heuvel LP, ''et al.'' |title=cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed. |journal=Biochem. Biophys. Res. Commun. |volume=253 |issue= 2 |pages= 415-22 |year= 1999 |pmid= 9878551 |doi= 10.1006/bbrc.1998.9786 }}
* {{cite journal | vauthors = Martín MA, Blázquez A, Gutierrez-Solana LG, Fernández-Moreira D, Briones P, Andreu AL, Garesse R, Campos Y, Arenas J | title = Leigh syndrome associated with mitochondrial complex I deficiency due to a novel mutation in the NDUFS1 gene | journal = Archives of Neurology | volume = 62 | issue = 4 | pages = 659–61 | date = Apr 2005 | pmid = 15824269 | doi = 10.1001/archneur.62.4.659 }}
*{{cite journal | author=Bénit P, Chretien D, Kadhom N, ''et al.'' |title=Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 genes in mitochondrial complex I deficiency. |journal=Am. J. Hum. Genet. |volume=68 |issue= 6 |pages= 1344-52 |year= 2001 |pmid= 11349233 |doi=  }}
* {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Iuso A, Scacco S, Piccoli C, Bellomo F, Petruzzella V, Trentadue R, Minuto M, Ripoli M, Capitanio N, Zeviani M, Papa S | title = Dysfunctions of cellular oxidative metabolism in patients with mutations in the NDUFS1 and NDUFS4 genes of complex I | journal = The Journal of Biological Chemistry | volume = 281 | issue = 15 | pages = 10374–80 | date = Apr 2006 | pmid = 16478720 | doi = 10.1074/jbc.M513387200 }}
*{{cite journal | author=Ricci JE, Muñoz-Pinedo C, Fitzgerald P, ''et al.'' |title=Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain. |journal=Cell |volume=117 |issue= 6 |pages= 773-86 |year= 2004 |pmid= 15186778 |doi= 10.1016/j.cell.2004.05.008 }}
* {{cite journal | vauthors = Piccoli C, Scacco S, Bellomo F, Signorile A, Iuso A, Boffoli D, Scrima R, Capitanio N, Papa S | title = cAMP controls oxygen metabolism in mammalian cells | journal = FEBS Letters | volume = 580 | issue = 18 | pages = 4539–43 | date = Aug 2006 | pmid = 16870178 | doi = 10.1016/j.febslet.2006.06.085 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Hillier LW, Graves TA, Fulton RS, ''et al.'' |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724-31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 }}
*{{cite journal  | author=Martín MA, Blázquez A, Gutierrez-Solana LG, ''et al.'' |title=Leigh syndrome associated with mitochondrial complex I deficiency due to a novel mutation in the NDUFS1 gene. |journal=Arch. Neurol. |volume=62 |issue= 4 |pages= 659-61 |year= 2005 |pmid= 15824269 |doi= 10.1001/archneur.62.4.659 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal | author=Iuso A, Scacco S, Piccoli C, ''et al.'' |title=Dysfunctions of cellular oxidative metabolism in patients with mutations in the NDUFS1 and NDUFS4 genes of complex I. |journal=J. Biol. Chem. |volume=281 |issue= 15 |pages= 10374-80 |year= 2006 |pmid= 16478720 |doi= 10.1074/jbc.M513387200 }}
*{{cite journal | author=Piccoli C, Scacco S, Bellomo F, ''et al.'' |title=cAMP controls oxygen metabolism in mammalian cells. |journal=FEBS Lett. |volume=580 |issue= 18 |pages= 4539-43 |year= 2006 |pmid= 16870178 |doi= 10.1016/j.febslet.2006.06.085 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{NADH or NADPH oxidoreductases}}
{{WikiDoc Sources}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
[[Category:Human proteins]]
[[Category:EC 1.6.5]]
 
 
{{gene-2-stub}}

Revision as of 12:46, 5 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial is an enzyme that in humans is encoded by the NDUFS1 gene.[1][2]

Function

The protein encoded by this gene belongs to the complex I 75 kDa subunit family. Mammalian complex I is composed of 45 different subunits. It locates at the mitochondrial inner membrane. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This protein is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.[2]

Clinical significance

Mutations in the NDUFS1 gene are associated with Mitochondrial Complex I Deficiency, which is autosomal recessive. This deficiency is the most common enzymatic defect of the oxidative phosphorylation disorders.[3][4] Mitochondrial complex I deficiency shows extreme genetic heterogeneity and can be caused by mutation in nuclear-encoded genes or in mitochondrial-encoded genes. There are no obvious genotype-phenotype correlations, and inference of the underlying basis from the clinical or biochemical presentation is difficult, if not impossible.[5] However, the majority of cases are caused by mutations in nuclear-encoded genes.[6][7] It causes a wide range of clinical disorders, ranging from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, nonspecific encephalopathy, hypertrophic cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease.[8]

References

  1. ↑ Chow W, Ragan I, Robinson BH (Nov 1991). "Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase". European Journal of Biochemistry / FEBS. 201 (3): 547–50. doi:10.1111/j.1432-1033.1991.tb16313.x. PMID 1935949.
  2. ↑ 2.0 2.1 "Entrez Gene: NDUFS1 NADH dehydrogenase (ubiquinone) Fe-S protein 1, 75kDa (NADH-coenzyme Q reductase)".
  3. ↑ Kirby DM, Salemi R, Sugiana C, Ohtake A, Parry L, Bell KM, Kirk EP, Boneh A, Taylor RW, Dahl HH, Ryan MT, Thorburn DR (Sep 2004). "NDUFS6 mutations are a novel cause of lethal neonatal mitochondrial complex I deficiency". The Journal of Clinical Investigation. 114 (6): 837–45. doi:10.1172/JCI20683. PMC 516258. PMID 15372108.
  4. ↑ McFarland R, Kirby DM, Fowler KJ, Ohtake A, Ryan MT, Amor DJ, Fletcher JM, Dixon JW, Collins FA, Turnbull DM, Taylor RW, Thorburn DR (Jan 2004). "De novo mutations in the mitochondrial ND3 gene as a cause of infantile mitochondrial encephalopathy and complex I deficiency". Annals of Neurology. 55 (1): 58–64. doi:10.1002/ana.10787. PMID 14705112.
  5. ↑ Haack TB, Haberberger B, Frisch EM, Wieland T, Iuso A, Gorza M, Strecker V, Graf E, Mayr JA, Herberg U, Hennermann JB, Klopstock T, Kuhn KA, Ahting U, Sperl W, Wilichowski E, Hoffmann GF, Tesarova M, Hansikova H, Zeman J, Plecko B, Zeviani M, Wittig I, Strom TM, Schuelke M, Freisinger P, Meitinger T, Prokisch H (Apr 2012). "Molecular diagnosis in mitochondrial complex I deficiency using exome sequencing". Journal of Medical Genetics. 49 (4): 277–83. doi:10.1136/jmedgenet-2012-100846. PMID 22499348.
  6. ↑ Loeffen JL, Smeitink JA, Trijbels JM, Janssen AJ, Triepels RH, Sengers RC, van den Heuvel LP (2000). "Isolated complex I deficiency in children: clinical, biochemical and genetic aspects". Human Mutation. 15 (2): 123–34. doi:10.1002/(SICI)1098-1004(200002)15:2<123::AID-HUMU1>3.0.CO;2-P. PMID 10649489.
  7. ↑ Triepels RH, Van Den Heuvel LP, Trijbels JM, Smeitink JA (2001). "Respiratory chain complex I deficiency". American Journal of Medical Genetics. 106 (1): 37–45. doi:10.1002/ajmg.1397. PMID 11579423.
  8. ↑ Robinson BH (May 1998). "Human complex I deficiency: clinical spectrum and involvement of oxygen free radicals in the pathogenicity of the defect". Biochimica et Biophysica Acta. 1364 (2): 271–86. doi:10.1016/s0005-2728(98)00033-4. PMID 9593934.

Further reading

  • Duncan AM, Chow W, Robinson BH (1992). "Localization of the human 75-kDal Fe-S protein of NADH-coenzyme Q reductase gene (NDUFS1) to 2q33----q34". Cytogenetics and Cell Genetics. 60 (3–4): 212–3. doi:10.1159/000133340. PMID 1505218.
  • Sumegi B, Srere PA (Dec 1984). "Complex I binds several mitochondrial NAD-coupled dehydrogenases". The Journal of Biological Chemistry. 259 (24): 15040–5. PMID 6439716.
  • Loeffen JL, Triepels RH, van den Heuvel LP, Schuelke M, Buskens CA, Smeets RJ, Trijbels JM, Smeitink JA (Dec 1998). "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochemical and Biophysical Research Communications. 253 (2): 415–22. doi:10.1006/bbrc.1998.9786. PMID 9878551.
  • Bénit P, Chretien D, Kadhom N, de Lonlay-Debeney P, Cormier-Daire V, Cabral A, Peudenier S, Rustin P, Munnich A, Rötig A (Jun 2001). "Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 genes in mitochondrial complex I deficiency". American Journal of Human Genetics. 68 (6): 1344–52. doi:10.1086/320603. PMC 1226121. PMID 11349233.
  • Ricci JE, Muñoz-Pinedo C, Fitzgerald P, Bailly-Maitre B, Perkins GA, Yadava N, Scheffler IE, Ellisman MH, Green DR (Jun 2004). "Disruption of mitochondrial function during apoptosis is mediated by caspase cleavage of the p75 subunit of complex I of the electron transport chain". Cell. 117 (6): 773–86. doi:10.1016/j.cell.2004.05.008. PMID 15186778.
  • Martín MA, Blázquez A, Gutierrez-Solana LG, Fernández-Moreira D, Briones P, Andreu AL, Garesse R, Campos Y, Arenas J (Apr 2005). "Leigh syndrome associated with mitochondrial complex I deficiency due to a novel mutation in the NDUFS1 gene". Archives of Neurology. 62 (4): 659–61. doi:10.1001/archneur.62.4.659. PMID 15824269.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  • Iuso A, Scacco S, Piccoli C, Bellomo F, Petruzzella V, Trentadue R, Minuto M, Ripoli M, Capitanio N, Zeviani M, Papa S (Apr 2006). "Dysfunctions of cellular oxidative metabolism in patients with mutations in the NDUFS1 and NDUFS4 genes of complex I". The Journal of Biological Chemistry. 281 (15): 10374–80. doi:10.1074/jbc.M513387200. PMID 16478720.
  • Piccoli C, Scacco S, Bellomo F, Signorile A, Iuso A, Boffoli D, Scrima R, Capitanio N, Papa S (Aug 2006). "cAMP controls oxygen metabolism in mammalian cells". FEBS Letters. 580 (18): 4539–43. doi:10.1016/j.febslet.2006.06.085. PMID 16870178.


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