DLST: Difference between revisions

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Latest revision as of 06:22, 10 January 2019

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial is an enzyme that in humans is encoded by the DLST gene.^[1]^[2]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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<imagemap> Image:TCACycle WP78.png

|{{{bSize}}}px|alt=TCA Cycle edit]]

TCA Cycle edit

↑ The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78".

References

↑ Ali G, Wasco W, Cai X, Szabo P, Sheu KF, Cooper AJ, Gaston SM, Gusella JF, Tanzi RE, Blass JP (Jul 1994). "Isolation, characterization, and mapping of gene encoding dihydrolipoyl succinyltransferase (E2k) of human alpha-ketoglutarate dehydrogenase complex". Somat Cell Mol Genet. 20 (2): 99–105. doi:10.1007/BF02290679. PMID 8009371.
↑ "Entrez Gene: DLST dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex)".

Chuang DT, Fisher CW, Lau KS, et al. (1991). "Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex". Mol. Biol. Med. 8 (1): 49–63. PMID 1943690.
Fregeau DR, Prindiville T, Coppel RL, et al. (1990). "Inhibition of alpha-ketoglutarate dehydrogenase activity by a distinct population of autoantibodies recognizing dihydrolipoamide succinyltransferase in primary biliary cirrhosis". Hepatology. 11 (6): 975–81. doi:10.1002/hep.1840110611. PMID 2365294.
Ono K, Hakozaki M, Kimura A, Kochi H (1987). "Purification, resolution, and reconstitution of rat liver branched-chain alpha-keto acid dehydrogenase complex". J. Biochem. 101 (1): 19–27. PMID 3571202.
Kochi H, Seino H, Ono K (1986). "Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate, and branched-chain alpha-keto acids in rat liver mitochondria: presence of interaction between the glycine cleavage system and alpha-keto acid dehydrogenase complexes". Arch. Biochem. Biophys. 249 (2): 263–72. doi:10.1016/0003-9861(86)90002-0. PMID 3753002.
Nakano K, Takase C, Sakamoto T, et al. (1994). "Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex". Eur. J. Biochem. 224 (1): 179–89. doi:10.1111/j.1432-1033.1994.tb20010.x. PMID 8076640.
Nakano K, Takase C, Sakamoto T, et al. (1993). "An unspliced cDNA for human dihydrolipoamide succinyltransferase: characterization and mapping of the gene to chromosome 14q24.2-q24.3". Biochem. Biophys. Res. Commun. 196 (2): 527–33. doi:10.1006/bbrc.1993.2282. PMID 8240324.
Nakano K, Matuda S, Sakamoto T, et al. (1994). "Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3". Biochim. Biophys. Acta. 1216 (3): 360–8. doi:10.1016/0167-4781(93)90002-u. PMID 8268217.
Cruts M, Backhovens H, Van Gassen G, et al. (1996). "Mutation analysis of the chromosome 14q24.3 dihydrolipoyl succinyltransferase (DLST) gene in patients with early-onset Alzheimer disease". Neurosci. Lett. 199 (1): 73–7. doi:10.1016/0304-3940(95)11982-3. PMID 8584231.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Matuda S, Kodama J, Goshi N, et al. (1998). "A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle". Biochem. Biophys. Res. Commun. 241 (1): 151–6. doi:10.1006/bbrc.1997.7784. PMID 9405249.
McCartney RG, Rice JE, Sanderson SJ, et al. (1998). "Subunit interactions in the mammalian alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components". J. Biol. Chem. 273 (37): 24158–64. doi:10.1074/jbc.273.37.24158. PMID 9727038.
Sheu KF, Brown AM, Haroutunian V, et al. (1999). "Modulation by DLST of the genetic risk of Alzheimer's disease in a very elderly population". Ann. Neurol. 45 (1): 48–53. doi:10.1002/1531-8249(199901)45:1<48::AID-ART9>3.0.CO;2-V. PMID 9894876.
Ma Q, Chan P, Yang J (2002). "[Association between DLST gene polymorphism and Alzheimer's disease]". Zhonghua Yi Xue Za Zhi. 81 (20): 1246–8. PMID 11825528.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Kanamori T, Nishimaki K, Asoh S, et al. (2003). "Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain". EMBO J. 22 (12): 2913–23. doi:10.1093/emboj/cdg299. PMC 162151. PMID 12805207.
Brown AM, Gordon D, Lee H, et al. (2004). "Substantial linkage disequilibrium across the dihydrolipoyl succinyltransferase gene region without Alzheimer's disease association". Neurochem. Res. 29 (3): 629–35. doi:10.1023/B:NERE.0000014833.54481.1d. PMID 15038610.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[WikiPathways-3] The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78".

[pmid8009371-1] Ali G, Wasco W, Cai X, Szabo P, Sheu KF, Cooper AJ, Gaston SM, Gusella JF, Tanzi RE, Blass JP (Jul 1994). "Isolation, characterization, and mapping of gene encoding dihydrolipoyl succinyltransferase (E2k) of human alpha-ketoglutarate dehydrogenase complex". Somat Cell Mol Genet. 20 (2): 99–105. doi:10.1007/BF02290679. PMID 8009371.

[entrez-2] "Entrez Gene: DLST dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex)".

[1]

[2]

[§ 1]

@@ Line 1: / Line 1: @@
-<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
+{{Underlinked|date=May 2016}}
-{{PBB_Controls
+{{Infobox_gene}}
-| update_page = yes
+'''Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''DLST'' [[gene]].<ref name="pmid8009371">{{cite journal | vauthors = Ali G, Wasco W, Cai X, Szabo P, Sheu KF, Cooper AJ, Gaston SM, Gusella JF, Tanzi RE, Blass JP | title = Isolation, characterization, and mapping of gene encoding dihydrolipoyl succinyltransferase (E2k) of human alpha-ketoglutarate dehydrogenase complex | journal = Somat Cell Mol Genet | volume = 20 | issue = 2 | pages = 99–105 |date=Jul 1994 | pmid = 8009371 | pmc =  | doi =10.1007/BF02290679  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DLST dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1743| accessdate = }}</ref>
-| 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. -->
+== Interactive pathway map ==
-{{GNF_Protein_box
+{{TCACycle_WP78|highlight=DLST}}
- | image =
- | image_source =
- | PDB =
- | Name = Dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex)
- | HGNCid = 2911
- | Symbol = DLST
- | AltSymbols =; DLTS
- | OMIM = 126063
- | ECnumber =
- | Homologene = 1456
- | MGIid = 1926170
- | GeneAtlas_image1 = PBB_GE_DLST_215210_s_at_tn.png
- | Function = {{GNF_GO|id=GO:0004149 |text = dihydrolipoyllysine-residue succinyltransferase activity}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0031405 |text = lipoic acid binding}}
- | Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0045252 |text = oxoglutarate dehydrogenase complex}}
- | Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006099 |text = tricarboxylic acid cycle}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 1743
-    | Hs_Ensembl = ENSG00000119689
-    | Hs_RefseqProtein = NP_001924
-    | Hs_RefseqmRNA = NM_001933
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 14
-    | Hs_GenLoc_start = 74418372
-    | Hs_GenLoc_end = 74440196
-    | Hs_Uniprot = P36957
-    | Mm_EntrezGene = 78920
-    | Mm_Ensembl = ENSMUSG00000004789
-    | Mm_RefseqmRNA = NM_030225
-    | Mm_RefseqProtein = NP_084501
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 12
-    | Mm_GenLoc_start = 85999940
-    | Mm_GenLoc_end = 86023948
-    | Mm_Uniprot = Q3UEA0
-  }}
-}}
-'''Dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex)''', also known as '''DLST''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DLST dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1743| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
@@ Line 55: / Line 13: @@
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Chuang DT, Fisher CW, Lau KS, ''et al.'' |title=Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex. |journal=Mol. Biol. Med. |volume=8 |issue= 1 |pages= 49-63 |year= 1991 |pmid= 1943690 |doi=  }}
+*{{cite journal  | vauthors=Chuang DT, Fisher CW, Lau KS |title=Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex. |journal=Mol. Biol. Med. |volume=8 |issue= 1 |pages= 49–63 |year= 1991 |pmid= 1943690 |doi=  |display-authors=etal}}
-*{{cite journal  | author=Fregeau DR, Prindiville T, Coppel RL, ''et al.'' |title=Inhibition of alpha-ketoglutarate dehydrogenase activity by a distinct population of autoantibodies recognizing dihydrolipoamide succinyltransferase in primary biliary cirrhosis. |journal=Hepatology |volume=11 |issue= 6 |pages= 975-81 |year= 1990 |pmid= 2365294 |doi=  }}
+*{{cite journal  | vauthors=Fregeau DR, Prindiville T, Coppel RL |title=Inhibition of alpha-ketoglutarate dehydrogenase activity by a distinct population of autoantibodies recognizing dihydrolipoamide succinyltransferase in primary biliary cirrhosis. |journal=Hepatology |volume=11 |issue= 6 |pages= 975–81 |year= 1990 |pmid= 2365294 |doi=10.1002/hep.1840110611  |display-authors=etal}}
-*{{cite journal  | author=Ono K, Hakozaki M, Kimura A, Kochi H |title=Purification, resolution, and reconstitution of rat liver branched-chain alpha-keto acid dehydrogenase complex. |journal=J. Biochem. |volume=101 |issue= 1 |pages= 19-27 |year= 1987 |pmid= 3571202 |doi=  }}
+*{{cite journal  | vauthors=Ono K, Hakozaki M, Kimura A, Kochi H |title=Purification, resolution, and reconstitution of rat liver branched-chain alpha-keto acid dehydrogenase complex. |journal=J. Biochem. |volume=101 |issue= 1 |pages= 19–27 |year= 1987 |pmid= 3571202 |doi=  }}
-*{{cite journal  | author=Kochi H, Seino H, Ono K |title=Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate, and branched-chain alpha-keto acids in rat liver mitochondria: presence of interaction between the glycine cleavage system and alpha-keto acid dehydrogenase complexes. |journal=Arch. Biochem. Biophys. |volume=249 |issue= 2 |pages= 263-72 |year= 1986 |pmid= 3753002 |doi=  }}
+*{{cite journal  | vauthors=Kochi H, Seino H, Ono K |title=Inhibition of glycine oxidation by pyruvate, alpha-ketoglutarate, and branched-chain alpha-keto acids in rat liver mitochondria: presence of interaction between the glycine cleavage system and alpha-keto acid dehydrogenase complexes. |journal=Arch. Biochem. Biophys. |volume=249 |issue= 2 |pages= 263–72 |year= 1986 |pmid= 3753002 |doi=10.1016/0003-9861(86)90002-0  }}
-*{{cite journal  | author=Ali G, Wasco W, Cai X, ''et al.'' |title=Isolation, characterization, and mapping of gene encoding dihydrolipoyl succinyltransferase (E2k) of human alpha-ketoglutarate dehydrogenase complex. |journal=Somat. Cell Mol. Genet. |volume=20 |issue= 2 |pages= 99-105 |year= 1994 |pmid= 8009371 |doi=  }}
+*{{cite journal  | vauthors=Nakano K, Takase C, Sakamoto T |title=Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. |journal=Eur. J. Biochem. |volume=224 |issue= 1 |pages= 179–89 |year= 1994 |pmid= 8076640 |doi=10.1111/j.1432-1033.1994.tb20010.x  |display-authors=etal}}
-*{{cite journal  | author=Nakano K, Takase C, Sakamoto T, ''et al.'' |title=Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. |journal=Eur. J. Biochem. |volume=224 |issue= 1 |pages= 179-89 |year= 1994 |pmid= 8076640 |doi=  }}
+*{{cite journal  | vauthors=Nakano K, Takase C, Sakamoto T |title=An unspliced cDNA for human dihydrolipoamide succinyltransferase: characterization and mapping of the gene to chromosome 14q24.2-q24.3. |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 527–33 |year= 1993 |pmid= 8240324 |doi= 10.1006/bbrc.1993.2282 |display-authors=etal}}
-*{{cite journal  | author=Nakano K, Takase C, Sakamoto T, ''et al.'' |title=An unspliced cDNA for human dihydrolipoamide succinyltransferase: characterization and mapping of the gene to chromosome 14q24.2-q24.3. |journal=Biochem. Biophys. Res. Commun. |volume=196 |issue= 2 |pages= 527-33 |year= 1993 |pmid= 8240324 |doi= 10.1006/bbrc.1993.2282 }}
+*{{cite journal  | vauthors=Nakano K, Matuda S, Sakamoto T |title=Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3. |journal=Biochim. Biophys. Acta |volume=1216 |issue= 3 |pages= 360–8 |year= 1994 |pmid= 8268217 |doi=  10.1016/0167-4781(93)90002-u|display-authors=etal}}
-*{{cite journal  | author=Nakano K, Matuda S, Sakamoto T, ''et al.'' |title=Human dihydrolipoamide succinyltransferase: cDNA cloning and localization on chromosome 14q24.2-q24.3. |journal=Biochim. Biophys. Acta |volume=1216 |issue= 3 |pages= 360-8 |year= 1994 |pmid= 8268217 |doi=  }}
+*{{cite journal  | vauthors=Cruts M, Backhovens H, Van Gassen G |title=Mutation analysis of the chromosome 14q24.3 dihydrolipoyl succinyltransferase (DLST) gene in patients with early-onset Alzheimer disease. |journal=Neurosci. Lett. |volume=199 |issue= 1 |pages= 73–7 |year= 1996 |pmid= 8584231 |doi=10.1016/0304-3940(95)11982-3  |display-authors=etal}}
-*{{cite journal  | author=Cruts M, Backhovens H, Van Gassen G, ''et al.'' |title=Mutation analysis of the chromosome 14q24.3 dihydrolipoyl succinyltransferase (DLST) gene in patients with early-onset Alzheimer disease. |journal=Neurosci. Lett. |volume=199 |issue= 1 |pages= 73-7 |year= 1996 |pmid= 8584231 |doi=  }}
+*{{cite journal  | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791  }}
-*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
+*{{cite journal  | vauthors=Matuda S, Kodama J, Goshi N |title=A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle. |journal=Biochem. Biophys. Res. Commun. |volume=241 |issue= 1 |pages= 151–6 |year= 1998 |pmid= 9405249 |doi= 10.1006/bbrc.1997.7784 |display-authors=etal}}
-*{{cite journal  | author=Matuda S, Kodama J, Goshi N, ''et al.'' |title=A polypeptide derived from mitochondrial dihydrolipoamide succinyltransferase is located on the plasma membrane in skeletal muscle. |journal=Biochem. Biophys. Res. Commun. |volume=241 |issue= 1 |pages= 151-6 |year= 1998 |pmid= 9405249 |doi= 10.1006/bbrc.1997.7784 }}
+*{{cite journal  | vauthors=McCartney RG, Rice JE, Sanderson SJ |title=Subunit interactions in the mammalian alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components. |journal=J. Biol. Chem. |volume=273 |issue= 37 |pages= 24158–64 |year= 1998 |pmid= 9727038 |doi=10.1074/jbc.273.37.24158  |display-authors=etal}}
-*{{cite journal  | author=McCartney RG, Rice JE, Sanderson SJ, ''et al.'' |title=Subunit interactions in the mammalian alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components. |journal=J. Biol. Chem. |volume=273 |issue= 37 |pages= 24158-64 |year= 1998 |pmid= 9727038 |doi=  }}
+*{{cite journal  | vauthors=Sheu KF, Brown AM, Haroutunian V |title=Modulation by DLST of the genetic risk of Alzheimer's disease in a very elderly population. |journal=Ann. Neurol. |volume=45 |issue= 1 |pages= 48–53 |year= 1999 |pmid= 9894876 |doi=10.1002/1531-8249(199901)45:1<48::AID-ART9>3.0.CO;2-V  |display-authors=etal}}
-*{{cite journal  | author=Sheu KF, Brown AM, Haroutunian V, ''et al.'' |title=Modulation by DLST of the genetic risk of Alzheimer's disease in a very elderly population. |journal=Ann. Neurol. |volume=45 |issue= 1 |pages= 48-53 |year= 1999 |pmid= 9894876 |doi=  }}
+*{{cite journal  | vauthors=Ma Q, Chan P, Yang J |title=[Association between DLST gene polymorphism and Alzheimer's disease] |journal=Zhonghua Yi Xue Za Zhi |volume=81 |issue= 20 |pages= 1246–8 |year= 2002 |pmid= 11825528 |doi=  }}
-*{{cite journal  | author=Ma Q, Chan P, Yang J |title=[Association between DLST gene polymorphism and Alzheimer's disease] |journal=Zhonghua Yi Xue Za Zhi |volume=81 |issue= 20 |pages= 1246-8 |year= 2002 |pmid= 11825528 |doi=  }}
+*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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  | pmc=139241 |display-authors=etal}}
-*{{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=Kanamori T, Nishimaki K, Asoh S |title=Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain |journal=EMBO J. |volume=22 |issue= 12 |pages= 2913–23 |year= 2003 |pmid= 12805207 |doi= 10.1093/emboj/cdg299  | pmc=162151 |display-authors=etal}}
-*{{cite journal  | author=Kanamori T, Nishimaki K, Asoh S, ''et al.'' |title=Truncated product of the bifunctional DLST gene involved in biogenesis of the respiratory chain. |journal=EMBO J. |volume=22 |issue= 12 |pages= 2913-23 |year= 2003 |pmid= 12805207 |doi= 10.1093/emboj/cdg299 }}
+*{{cite journal  | vauthors=Brown AM, Gordon D, Lee H |title=Substantial linkage disequilibrium across the dihydrolipoyl succinyltransferase gene region without Alzheimer's disease association |journal=Neurochem. Res. |volume=29 |issue= 3 |pages= 629–35 |year= 2004 |pmid= 15038610 |doi=10.1023/B:NERE.0000014833.54481.1d  |display-authors=etal}}
-*{{cite journal  | author=Brown AM, Gordon D, Lee H, ''et al.'' |title=Substantial linkage disequilibrium across the dihydrolipoyl succinyltransferase gene region without Alzheimer's disease association. |journal=Neurochem. Res. |volume=29 |issue= 3 |pages= 629-35 |year= 2004 |pmid= 15038610 |doi=  }}
+*{{cite journal  | vauthors=Gerhard DS, Wagner L, Feingold EA |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  | pmc=528928 |display-authors=etal}}
-*{{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  | vauthors=Stelzl U, Worm U, Lalowski M |title=A human protein-protein interaction network: a resource for annotating the proteome |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 |display-authors=etal}}
-*{{cite journal  | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
+*{{cite journal  | vauthors=Rual JF, Venkatesan K, Hao T |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 |display-authors=etal}}
-*{{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 }}
 }}
 {{refend}}
-{{protein-stub}}
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+{{Multienzyme complexes}}
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+[[Category:Mitochondrial proteins]]

v t e Enzymes: multienzyme complexes
Photosynthesis	Photosynthetic reaction center complex proteins Photosystem I II
Dehydrogenase	Pyruvate dehydrogenase complex E1 E2 E3 Oxoglutarate dehydrogenase OGDH DLST DLD Branched-chain alpha-keto acid dehydrogenase complex BCKDHA BCKDHB DBT DLD
Other	CAD Carbamoyl phosphate synthase II Aspartate carbamoyltransferase Dihydroorotase Cholesterol side-chain cleavage enzyme Cytochrome b6f complex Electron transport chain Fatty acid synthetase complex Glycine decarboxylase complex Mitochondrial trifunctional protein HADHA HADHB Phosphoenolpyruvate sugar phosphotransferase system Polyketide synthase Sucrase-isomaltase complex Tryptophan synthase

DLST: Difference between revisions

Latest revision as of 06:22, 10 January 2019

Interactive pathway map

References

Further reading

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