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==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
*{{cite journal  |vauthors=Ross MT, Grafham DV, Coffey AJ |title=The DNA sequence of the human X chromosome. |journal=Nature |volume=434 |issue= 7031 |pages= 325–37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 |pmc=2665286|display-authors=etal}}
*{{cite journal  |vauthors=Ross MT, Grafham DV, Coffey AJ |title=The DNA sequence of the human X chromosome |journal=Nature |volume=434 |issue= 7031 |pages= 325–37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 |pmc=2665286|display-authors=etal}}
*{{cite journal  |vauthors=Need AC, Keefe RS, Ge D |title=Pharmacogenetics of antipsychotic response in the CATIE trial: a candidate gene analysis. |journal=Eur. J. Hum. Genet. |volume=17 |issue= 7 |pages= 946–57 |year= 2009 |pmid= 19156168 |doi= 10.1038/ejhg.2008.264 |pmc=2986499|display-authors=etal}}
*{{cite journal  |vauthors=Need AC, Keefe RS, Ge D |title=Pharmacogenetics of antipsychotic response in the CATIE trial: a candidate gene analysis |journal=Eur. J. Hum. Genet. |volume=17 |issue= 7 |pages= 946–57 |year= 2009 |pmid= 19156168 |doi= 10.1038/ejhg.2008.264 |pmc=2986499|display-authors=etal}}
*{{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  |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  |vauthors=Burki F, Kaessmann H |title=Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux. |journal=Nat. Genet. |volume=36 |issue= 10 |pages= 1061–3 |year= 2004 |pmid= 15378063 |doi= 10.1038/ng1431 }}
*{{cite journal  |vauthors=Burki F, Kaessmann H |title=Birth and adaptive evolution of a hominoid gene that supports high neurotransmitter flux |journal=Nat. Genet. |volume=36 |issue= 10 |pages= 1061–3 |year= 2004 |pmid= 15378063 |doi= 10.1038/ng1431 }}
*{{cite journal  |vauthors=Plaitakis A, Latsoudis H, Kanavouras K |title=Gain-of-function variant in GLUD2 glutamate dehydrogenase modifies Parkinson's disease onset. |journal=Eur. J. Hum. Genet. |volume=18 |issue= 3 |pages= 336–41 |year= 2010 |pmid= 19826450 |doi= 10.1038/ejhg.2009.179 |pmc=2987208|display-authors=etal}}
*{{cite journal  |vauthors=Plaitakis A, Latsoudis H, Kanavouras K |title=Gain-of-function variant in GLUD2 glutamate dehydrogenase modifies Parkinson's disease onset |journal=Eur. J. Hum. Genet. |volume=18 |issue= 3 |pages= 336–41 |year= 2010 |pmid= 19826450 |doi= 10.1038/ejhg.2009.179 |pmc=2987208|display-authors=etal}}
*{{cite journal  |vauthors=Yang SJ, Cho EH, Choi MM |title=Critical role of the cysteine 323 residue in the catalytic activity of human glutamate dehydrogenase isozymes. |journal=Mol. Cells |volume=19 |issue= 1 |pages= 97–103 |year= 2005 |pmid= 15750346 |doi=  |display-authors=etal}}
*{{cite journal  |vauthors=Yang SJ, Cho EH, Choi MM |title=Critical role of the cysteine 323 residue in the catalytic activity of human glutamate dehydrogenase isozymes |journal=Mol. Cells |volume=19 |issue= 1 |pages= 97–103 |year= 2005 |pmid= 15750346 |doi=  |display-authors=etal}}
*{{cite journal  |vauthors=Yang SJ, Huh JW, Hong HN |title=Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes. |journal=FEBS Lett. |volume=562 |issue= 1-3 |pages= 59–64 |year= 2004 |pmid= 15044002 |doi= 10.1016/S0014-5793(04)00183-8 |display-authors=etal}}
*{{cite journal  |vauthors=Yang SJ, Huh JW, Hong HN |title=Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes |journal=FEBS Lett. |volume=562 |issue= 1–3 |pages= 59–64 |year= 2004 |pmid= 15044002 |doi= 10.1016/S0014-5793(04)00183-8 |display-authors=etal}}
*{{cite journal  |vauthors=Kanavouras K, Borompokas N, Latsoudis H |title=Mutations in human GLUD2 glutamate dehydrogenase affecting basal activity and regulation. |journal=J. Neurochem. |volume=109 Suppl 1 |issue=  |pages= 167–73 |year= 2009 |pmid= 19393024 |doi= 10.1111/j.1471-4159.2009.05914.x |display-authors=etal}}
*{{cite journal  |vauthors=Kanavouras K, Borompokas N, Latsoudis H |title=Mutations in human GLUD2 glutamate dehydrogenase affecting basal activity and regulation |journal=J. Neurochem. |volume=109 Suppl 1 |issue=  |pages= 167–73 |year= 2009 |pmid= 19393024 |doi= 10.1111/j.1471-4159.2009.05914.x |display-authors=etal}}
*{{cite journal  |vauthors=Mastorodemos V, Zaganas I, Spanaki C |title=Molecular basis of human glutamate dehydrogenase regulation under changing energy demands. |journal=J. Neurosci. Res. |volume=79 |issue= 1-2 |pages= 65–73 |year=  2005|pmid= 15578726 |doi= 10.1002/jnr.20353 |display-authors=etal}}
*{{cite journal  |vauthors=Mastorodemos V, Zaganas I, Spanaki C |title=Molecular basis of human glutamate dehydrogenase regulation under changing energy demands |journal=J. Neurosci. Res. |volume=79 |issue= 1–2 |pages= 65–73 |year=  2005|pmid= 15578726 |doi= 10.1002/jnr.20353 |display-authors=etal}}
*{{cite journal  |vauthors=Smith TJ, Schmidt T, Fang J |title=The structure of apo human glutamate dehydrogenase details subunit communication and allostery. |journal=J. Mol. Biol. |volume=318 |issue= 3 |pages= 765–77 |year= 2002 |pmid= 12054821 |doi= 10.1016/S0022-2836(02)00161-4 |display-authors=etal}}
*{{cite journal  |vauthors=Smith TJ, Schmidt T, Fang J |title=The structure of apo human glutamate dehydrogenase details subunit communication and allostery |journal=J. Mol. Biol. |volume=318 |issue= 3 |pages= 765–77 |year= 2002 |pmid= 12054821 |doi= 10.1016/S0022-2836(02)00161-4 |display-authors=etal}}
*{{cite journal  |vauthors=Plaitakis A, Spanaki C, Mastorodemos V, Zaganas I |title=Study of structure-function relationships in human glutamate dehydrogenases reveals novel molecular mechanisms for the regulation of the nerve tissue-specific (GLUD2) isoenzyme. |journal=Neurochem. Int. |volume=43 |issue= 4-5 |pages= 401–10 |year=  2003|pmid= 12742085 |doi=  10.1016/S0197-0186(03)00028-7}}
*{{cite journal  |vauthors=Plaitakis A, Spanaki C, Mastorodemos V, Zaganas I |title=Study of structure-function relationships in human glutamate dehydrogenases reveals novel molecular mechanisms for the regulation of the nerve tissue-specific (GLUD2) isoenzyme |journal=Neurochem. Int. |volume=43 |issue= 4–5 |pages= 401–10 |year=  2003|pmid= 12742085 |doi=  10.1016/S0197-0186(03)00028-7}}
*{{cite journal  |vauthors=Mastorodemos V, Kotzamani D, Zaganas I |title=Human GLUD1 and GLUD2 glutamate dehydrogenase localize to mitochondria and endoplasmic reticulum. |journal=Biochem. Cell Biol. |volume=87 |issue= 3 |pages= 505–16 |year= 2009 |pmid= 19448744 |doi= 10.1139/o09-008 |display-authors=etal}}
*{{cite journal  |vauthors=Mastorodemos V, Kotzamani D, Zaganas I |title=Human GLUD1 and GLUD2 glutamate dehydrogenase localize to mitochondria and endoplasmic reticulum |journal=Biochem. Cell Biol. |volume=87 |issue= 3 |pages= 505–16 |year= 2009 |pmid= 19448744 |doi= 10.1139/o09-008 |display-authors=etal}}
*{{cite journal  |vauthors=Spanaki C, Zaganas I, Kleopa KA, Plaitakis A |title=Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells. |journal=J. Biol. Chem. |volume=285 |issue= 22 |pages= 16748–56 |year= 2010 |pmid= 20194501 |doi= 10.1074/jbc.M109.092999 |pmc=2878061}}
*{{cite journal  |vauthors=Spanaki C, Zaganas I, Kleopa KA, Plaitakis A |title=Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells |journal=J. Biol. Chem. |volume=285 |issue= 22 |pages= 16748–56 |year= 2010 |pmid= 20194501 |doi= 10.1074/jbc.M109.092999 |pmc=2878061}}
*{{cite journal  |vauthors=Ahmed M, Forsberg J, Bergsten P |title=Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry. |journal=J. Proteome Res. |volume=4 |issue= 3 |pages= 931–40 |year=  2005|pmid= 15952740 |doi= 10.1021/pr050024a }}
*{{cite journal  |vauthors=Ahmed M, Forsberg J, Bergsten P |title=Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry |journal=J. Proteome Res. |volume=4 |issue= 3 |pages= 931–40 |year=  2005|pmid= 15952740 |doi= 10.1021/pr050024a }}
*{{cite journal  |vauthors=Rosso L, Marques AC, Reichert AS, Kaessmann H |title=Mitochondrial targeting adaptation of the hominoid-specific glutamate dehydrogenase driven by positive Darwinian selection. |journal=PLoS Genet. |volume=4 |issue= 8 |pages= e1000150 |year= 2008 |pmid= 18688271 |doi= 10.1371/journal.pgen.1000150 |pmc=2478720}}
*{{cite journal  |vauthors=Rosso L, Marques AC, Reichert AS, Kaessmann H |title=Mitochondrial targeting adaptation of the hominoid-specific glutamate dehydrogenase driven by positive Darwinian selection |journal=PLoS Genet. |volume=4 |issue= 8 |pages= e1000150 |year= 2008 |pmid= 18688271 |doi= 10.1371/journal.pgen.1000150 |pmc=2478720}}
*{{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  |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  |vauthors=Zaganas I, Kanavouras K, Mastorodemos V |title=The human GLUD2 glutamate dehydrogenase: localization and functional aspects. |journal=Neurochem. Int. |volume=55 |issue= 1-3 |pages= 52–63 |year=  2009|pmid= 19428807 |doi= 10.1016/j.neuint.2009.03.001 |display-authors=etal}}
*{{cite journal  |vauthors=Zaganas I, Kanavouras K, Mastorodemos V |title=The human GLUD2 glutamate dehydrogenase: localization and functional aspects |journal=Neurochem. Int. |volume=55 |issue= 1–3 |pages= 52–63 |year=  2009|pmid= 19428807 |doi= 10.1016/j.neuint.2009.03.001 |display-authors=etal}}
*{{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= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 |pmc=139241|display-authors=etal}}
*{{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= 2002 |pmid= 12477932 |doi= 10.1073/pnas.242603899 |pmc=139241|display-authors=etal}}
*{{cite journal  |vauthors=Kanavouras K, Mastorodemos V, Borompokas N |title=Properties and molecular evolution of human GLUD2 (neural and testicular tissue-specific) glutamate dehydrogenase. |journal=J. Neurosci. Res. |volume=85 |issue= 15 |pages= 3398–406 |year= 2007 |pmid= 17924438 |doi= 10.1002/jnr.21576 |display-authors=etal}}
*{{cite journal  |vauthors=Kanavouras K, Mastorodemos V, Borompokas N |title=Properties and molecular evolution of human GLUD2 (neural and testicular tissue-specific) glutamate dehydrogenase |journal=J. Neurosci. Res. |volume=85 |issue= 15 |pages= 3398–406 |year= 2007 |pmid= 17924438 |doi= 10.1002/jnr.21576 |display-authors=etal}}
{{refend}}
{{refend}}



Latest revision as of 22:33, 5 September 2018

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

Glutamate dehydrogenase 2, mitochondrial, also known as GDH 2, is an enzyme that in humans is encoded by the GLUD2 gene.[1][2][3] This dehydrogenase is one of the family of glutamate dehydrogenases that are ubiquitous in life.

Function

Glutamate dehydrogenase 2 is localized to the mitochondrion and acts as a homohexamer to recycle glutamate during neurotransmission. The encoded enzyme catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate.[1]

References

  1. 1.0 1.1 "Entrez Gene: glutamate dehydrogenase 2".
  2. Shashidharan P, Michaelidis TM, Robakis NK, Kresovali A, Papamatheakis J, Plaitakis A (June 1994). "Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene". J. Biol. Chem. 269 (24): 16971–6. PMID 8207021.
  3. Shashidharan P, Clarke DD, Ahmed N, Moschonas N, Plaitakis A (May 1997). "Nerve tissue-specific human glutamate dehydrogenase that is thermolabile and highly regulated by ADP". J. Neurochem. 68 (5): 1804–11. doi:10.1046/j.1471-4159.1997.68051804.x. PMID 9109504.

Further reading