NDUFS2: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
 
m (Bot: HTTP→HTTPS)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial''' also known as '''NADH-ubiquinone oxidoreductase 49 kDa subunit''' is an [[enzyme]] that in humans is encoded by the ''NDUFS2'' [[gene]].<ref name="pmid1832859">{{cite journal | vauthors = Fearnley IM, Finel M, Skehel JM, Walker JE | title = NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa subunits | journal = The Biochemical Journal | volume = 278 | issue =  3| pages = 821–9 | date = Sep 1991 | pmid = 1832859 | pmc = 1151420 | doi =  10.1042/bj2780821| series = 278 }}</ref><ref name="pmid9585441">{{cite journal | vauthors = Procaccio V, de Sury R, Martinez P, Depetris D, Rabilloud T, Soularue P, Lunardi J, Issartel J | title = Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory Complex I and immunodetection of the mature protein in mitochondria | journal = Mammalian Genome | volume = 9 | issue = 6 | pages = 482–4 | date = Jun 1998 | pmid = 9585441 | pmc = | doi = 10.1007/s003359900803 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: NDUFS2 NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4720| 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 2, 49kDa (NADH-coenzyme Q reductase)
| HGNCid = 7708
| Symbol = NDUFS2
| AltSymbols =;
| OMIM = 602985
| ECnumber = 
| Homologene = 56659
| MGIid = 2385112
| GeneAtlas_image1 = PBB_GE_NDUFS2_201966_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:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051287 |text = NAD 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 = 4720
    | Hs_Ensembl = ENSG00000158864
    | Hs_RefseqProtein = NP_004541
    | Hs_RefseqmRNA = NM_004550
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 159435729
    | Hs_GenLoc_end = 159450809
    | Hs_Uniprot = O75306
    | Mm_EntrezGene = 226646
    | Mm_Ensembl = ENSMUSG00000013593
    | Mm_RefseqmRNA = NM_153064
    | Mm_RefseqProtein = NP_694704
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 173071535
    | Mm_GenLoc_end = 173083787
    | Mm_Uniprot = Q3U5Y9
  }}
}}
'''NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase)''', also known as '''NDUFS2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NDUFS2 NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4720| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Mitochondrion|Mitochondrial]] [[NADH dehydrogenase|complex I]] is the first multimeric complex of the [[electron transport chain|respiratory chain]] that catalyzes the NADH oxidation with concomitant ubiquinone reduction and proton ejection out of the mitochondria. Mammalian mitochondrial complex I is an assembly of at least 43 different subunits. Seven of the subunits are encoded by the [[mitochondrial DNA|mitochondrial genome]]; the remainder are the products of nuclear genes. The [[iron-sulfur protein]] (IP) fraction of complex I is made up of 7 subunits, including NDUFS2.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Mitochondrial complex I (NADH-ubiquinone reductase; EC 1.6.5.3) is the first multimeric complex of the respiratory chain that catalyzes the NADH oxidation with concomitant ubiquinone reduction and proton ejection out of the mitochondria. Mammalian mitochondrial complex I is an assembly of at least 43 different subunits. Seven of the subunits are encoded by the mitochondrial genome; the remainder are the products of nuclear genes. The iron-sulfur protein (IP) fraction of complex I is made up of 7 subunits, including NDUFS2. See NDUFS1 (MIM 157655).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NDUFS2 NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4720| accessdate = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
Mutations in the NDUFS2 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>
 
== See also ==
* [[NDUFS1]]
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
| citations =
* {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1-2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
*{{cite journal | author=Fearnley IM, Finel M, Skehel JM, Walker JE |title=NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa subunits. |journal=Biochem. J. |volume=278 ( Pt 3) |issue=  |pages= 821-9 |year= 1991 |pmid= 1832859 |doi=  }}
* {{cite journal | vauthors = Loeffen J, van den Heuvel L, Smeets R, Triepels R, Sengers R, Trijbels F, Smeitink J | title = cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed | journal = Biochemical and Biophysical Research Communications | volume = 247 | issue = 3 | pages = 751–8 | date = Jun 1998 | pmid = 9647766 | doi = 10.1006/bbrc.1998.8882 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |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=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
* {{cite journal | vauthors = Triepels RH, Hanson BJ, van den Heuvel LP, Sundell L, Marusich MF, Smeitink JA, Capaldi RA | title = Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns | journal = The Journal of Biological Chemistry | volume = 276 | issue = 12 | pages = 8892–7 | date = Mar 2001 | pmid = 11112787 | doi = 10.1074/jbc.M009903200 }}
*{{cite journal  | author=Procaccio V, de Sury R, Martinez P, ''et al.'' |title=Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory Complex I and immunodetection of the mature protein in mitochondria. |journal=Mamm. Genome |volume=9 |issue= 6 |pages= 482-4 |year= 1998 |pmid= 9585441 |doi=  }}
* {{cite journal | vauthors = Loeffen J, Elpeleg O, Smeitink J, Smeets R, Stöckler-Ipsiroglu S, Mandel H, Sengers R, Trijbels F, van den Heuvel L | title = Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy | journal = Annals of Neurology | volume = 49 | issue = 2 | pages = 195–201 | date = Feb 2001 | pmid = 11220739 | doi = 10.1002/1531-8249(20010201)49:2<195::AID-ANA39>3.0.CO;2-M }}
*{{cite journal | author=Loeffen J, van den Heuvel L, Smeets R, ''et al.'' |title=cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed. |journal=Biochem. Biophys. Res. Commun. |volume=247 |issue= 3 |pages= 751-8 |year= 1998 |pmid= 9647766 |doi= 10.1006/bbrc.1998.8882 }}
* {{cite journal | vauthors = Murray J, Taylor SW, Zhang B, Ghosh SS, Capaldi RA | title = Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry | journal = The Journal of Biological Chemistry | volume = 278 | issue = 39 | pages = 37223–30 | date = Sep 2003 | pmid = 12857734 | doi = 10.1074/jbc.M305694200 }}
*{{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 = Ugalde C, Janssen RJ, van den Heuvel LP, Smeitink JA, Nijtmans LG | title = Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency | journal = Human Molecular Genetics | volume = 13 | issue = 6 | pages = 659–67 | date = Mar 2004 | pmid = 14749350 | doi = 10.1093/hmg/ddh071 }}
*{{cite journal | author=Triepels RH, Hanson BJ, van den Heuvel LP, ''et al.'' |title=Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns. |journal=J. Biol. Chem. |volume=276 |issue= 12 |pages= 8892-7 |year= 2001 |pmid= 11112787 |doi= 10.1074/jbc.M009903200 }}
* {{cite journal | vauthors = Bourges I, Ramus C, Mousson de Camaret B, Beugnot R, Remacle C, Cardol P, Hofhaus G, Issartel JP | title = Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin | journal = The Biochemical Journal | volume = 383 | issue = Pt. 3 | pages = 491–9 | date = Nov 2004 | pmid = 15250827 | pmc = 1133742 | doi = 10.1042/BJ20040256 }}
*{{cite journal | author=Loeffen J, Elpeleg O, Smeitink J, ''et al.'' |title=Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy. |journal=Ann. Neurol. |volume=49 |issue= 2 |pages= 195-201 |year= 2001 |pmid= 11220739 |doi= }}
* {{cite journal | vauthors = Ma J, Dempsey AA, Stamatiou D, Marshall KW, Liew CC | title = Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects | journal = Atherosclerosis | volume = 191 | issue = 1 | pages = 63–72 | date = Mar 2007 | pmid = 16806233 | doi = 10.1016/j.atherosclerosis.2006.05.032 }}
*{{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 = Vogel RO, Dieteren CE, van den Heuvel LP, Willems PH, Smeitink JA, Koopman WJ, Nijtmans LG | title = Identification of mitochondrial complex I assembly intermediates by tracing tagged NDUFS3 demonstrates the entry point of mitochondrial subunits | journal = The Journal of Biological Chemistry | volume = 282 | issue = 10 | pages = 7582–90 | date = Mar 2007 | pmid = 17209039 | doi = 10.1074/jbc.M609410200 }}
*{{cite journal | author=Murray J, Taylor SW, Zhang B, ''et al.'' |title=Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry. |journal=J. Biol. Chem. |volume=278 |issue= 39 |pages= 37223-30 |year= 2003 |pmid= 12857734 |doi= 10.1074/jbc.M305694200 }}
*{{cite journal | author=Ugalde C, Janssen RJ, van den Heuvel LP, ''et al.'' |title=Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency. |journal=Hum. Mol. Genet. |volume=13 |issue= 6 |pages= 659-67 |year= 2004 |pmid= 14749350 |doi= 10.1093/hmg/ddh071 }}
*{{cite journal | author=Bourges I, Ramus C, Mousson de Camaret B, ''et al.'' |title=Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin. |journal=Biochem. J. |volume=383 |issue= Pt. 3 |pages= 491-9 |year= 2005 |pmid= 15250827 |doi= 10.1042/BJ20040256 }}
*{{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=Ma J, Dempsey AA, Stamatiou D, ''et al.'' |title=Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects. |journal=Atherosclerosis |volume=191 |issue= 1 |pages= 63-72 |year= 2007 |pmid= 16806233 |doi= 10.1016/j.atherosclerosis.2006.05.032 }}
*{{cite journal | author=Vogel RO, Dieteren CE, van den Heuvel LP, ''et al.'' |title=Identification of mitochondrial complex I assembly intermediates by tracing tagged NDUFS3 demonstrates the entry point of mitochondrial subunits. |journal=J. Biol. Chem. |volume=282 |issue= 10 |pages= 7582-90 |year= 2007 |pmid= 17209039 |doi= 10.1074/jbc.M609410200 }}
}}
{{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]]
[[Category:EC 1.6.99]]
 
 
{{gene-1-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 dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial also known as NADH-ubiquinone oxidoreductase 49 kDa subunit is an enzyme that in humans is encoded by the NDUFS2 gene.[1][2][3]

Function

Mitochondrial complex I is the first multimeric complex of the respiratory chain that catalyzes the NADH oxidation with concomitant ubiquinone reduction and proton ejection out of the mitochondria. Mammalian mitochondrial complex I is an assembly of at least 43 different subunits. Seven of the subunits are encoded by the mitochondrial genome; the remainder are the products of nuclear genes. The iron-sulfur protein (IP) fraction of complex I is made up of 7 subunits, including NDUFS2.[3]

Clinical significance

Mutations in the NDUFS2 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.[4][5] 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.[6] However, the majority of cases are caused by mutations in nuclear-encoded genes.[7][8] 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.[9]

See also

References

  1. ↑ Fearnley IM, Finel M, Skehel JM, Walker JE (Sep 1991). "NADH:ubiquinone oxidoreductase from bovine heart mitochondria. cDNA sequences of the import precursors of the nuclear-encoded 39 kDa and 42 kDa subunits". The Biochemical Journal. 278. 278 (3): 821–9. doi:10.1042/bj2780821. PMC 1151420. PMID 1832859.
  2. ↑ Procaccio V, de Sury R, Martinez P, Depetris D, Rabilloud T, Soularue P, Lunardi J, Issartel J (Jun 1998). "Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory Complex I and immunodetection of the mature protein in mitochondria". Mammalian Genome. 9 (6): 482–4. doi:10.1007/s003359900803. PMID 9585441.
  3. ↑ 3.0 3.1 "Entrez Gene: NDUFS2 NADH dehydrogenase (ubiquinone) Fe-S protein 2, 49kDa (NADH-coenzyme Q reductase)".
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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

  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Loeffen J, van den Heuvel L, Smeets R, Triepels R, Sengers R, Trijbels F, Smeitink J (Jun 1998). "cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed". Biochemical and Biophysical Research Communications. 247 (3): 751–8. doi:10.1006/bbrc.1998.8882. PMID 9647766.
  • 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.
  • Triepels RH, Hanson BJ, van den Heuvel LP, Sundell L, Marusich MF, Smeitink JA, Capaldi RA (Mar 2001). "Human complex I defects can be resolved by monoclonal antibody analysis into distinct subunit assembly patterns". The Journal of Biological Chemistry. 276 (12): 8892–7. doi:10.1074/jbc.M009903200. PMID 11112787.
  • Loeffen J, Elpeleg O, Smeitink J, Smeets R, Stöckler-Ipsiroglu S, Mandel H, Sengers R, Trijbels F, van den Heuvel L (Feb 2001). "Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy". Annals of Neurology. 49 (2): 195–201. doi:10.1002/1531-8249(20010201)49:2<195::AID-ANA39>3.0.CO;2-M. PMID 11220739.
  • Murray J, Taylor SW, Zhang B, Ghosh SS, Capaldi RA (Sep 2003). "Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry". The Journal of Biological Chemistry. 278 (39): 37223–30. doi:10.1074/jbc.M305694200. PMID 12857734.
  • Ugalde C, Janssen RJ, van den Heuvel LP, Smeitink JA, Nijtmans LG (Mar 2004). "Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency". Human Molecular Genetics. 13 (6): 659–67. doi:10.1093/hmg/ddh071. PMID 14749350.
  • Bourges I, Ramus C, Mousson de Camaret B, Beugnot R, Remacle C, Cardol P, Hofhaus G, Issartel JP (Nov 2004). "Structural organization of mitochondrial human complex I: role of the ND4 and ND5 mitochondria-encoded subunits and interaction with prohibitin". The Biochemical Journal. 383 (Pt. 3): 491–9. doi:10.1042/BJ20040256. PMC 1133742. PMID 15250827.
  • Ma J, Dempsey AA, Stamatiou D, Marshall KW, Liew CC (Mar 2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis. 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.
  • Vogel RO, Dieteren CE, van den Heuvel LP, Willems PH, Smeitink JA, Koopman WJ, Nijtmans LG (Mar 2007). "Identification of mitochondrial complex I assembly intermediates by tracing tagged NDUFS3 demonstrates the entry point of mitochondrial subunits". The Journal of Biological Chemistry. 282 (10): 7582–90. doi:10.1074/jbc.M609410200. PMID 17209039.


Retrieved from "https://www.wikidoc.org/index.php?title=NDUFS2&oldid=1411262"