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Properties and subunit composition of the pig heart 2-oxoglutarate dehydrogenase.

作者信息

Koike K, Hamada M, Tanaka N, Otsuka K I, Ogasahara K, Koike M

出版信息

J Biol Chem. 1974 Jun 25;249(12):3836-42.

PMID:4857981
Abstract
摘要

相似文献

1
Properties and subunit composition of the pig heart 2-oxoglutarate dehydrogenase.猪心脏2-氧代戊二酸脱氢酶的性质和亚基组成。
J Biol Chem. 1974 Jun 25;249(12):3836-42.
2
Mammalian alpha-keto acid dehydrogenase complexes. 8. Properties and subunit composition of the pig heart lipoate succinyltransferase.哺乳动物α-酮酸脱氢酶复合体。8. 猪心硫辛酸琥珀酰转移酶的性质和亚基组成。
J Biol Chem. 1974 Jan 10;249(1):191-8.
3
Alpha-keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex.α-酮酸脱氢酶复合体。第十九部分：大肠杆菌α-酮戊二酸脱氢酶复合体的亚基结构。
J Biol Chem. 1973 Aug 10;248(15):5282-90.
4
Properties and subunit structure of pig heart pyruvate dehydrogenase.
J Biochem. 1976 Jun;79(6):1273-85. doi: 10.1093/oxfordjournals.jbchem.a131181.
5
Structure, assembly and function of mammalian alpha-keto acid dehydrogenase complexes.哺乳动物α-酮酸脱氢酶复合体的结构、组装及功能
Adv Biophys. 1976:187-227.
6
Stabilization of mammalian liver branched-chain alpha-ketoacid dehydrogenase by thiamin pyrophosphate.硫胺素焦磷酸对哺乳动物肝脏支链α-酮酸脱氢酶的稳定作用。
Arch Biochem Biophys. 1980 Jun;202(1):23-8. doi: 10.1016/0003-9861(80)90401-4.
7
The subunit structure of the pyruvate-dehydrogenase complex from Escherichia coli K-12. The core complex.
Eur J Biochem. 1972 Oct;30(2):354-60. doi: 10.1111/j.1432-1033.1972.tb02105.x.
8
The subunit structure of the Escherichia coli K12 pyruvate-dehydrogenase complex. Dihydrolipoamide-dehydrogenase component.大肠杆菌K12丙酮酸脱氢酶复合体的亚基结构。二氢硫辛酰胺脱氢酶组分。
Eur J Biochem. 1973 Jun;35(2):307-10. doi: 10.1111/j.1432-1033.1973.tb02839.x.
9
[Studies on pig heart 2-oxoglutarate dehydrogenase (author's transl)].猪心脏2-氧代戊二酸脱氢酶的研究（作者译）
Seikagaku. 1974 Jul 25;46(7):325-35.
10
Dehydrogenases of alpha-keto acids: essential groups of the active centers.
Adv Enzyme Regul. 1986;25:347-75. doi: 10.1016/0065-2571(86)90023-3.

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Microgliosis, neuronal death, minor behavioral abnormalities and reduced endurance performance in alpha-ketoglutarate dehydrogenase complex deficient mice.α-酮戊二酸脱氢酶复合体缺陷小鼠中的小胶质细胞增生、神经元死亡、轻微行为异常及耐力表现下降。
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The α-Ketoglutarate Dehydrogenase Complex as a Hub of Plasticity in Neurodegeneration and Regeneration.α-酮戊二酸脱氢酶复合物作为神经变性和再生可塑性的枢纽。
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Reverse and Forward Electron Flow-Induced HO Formation Is Decreased in α-Ketoglutarate Dehydrogenase (α-KGDH) Subunit (E2 or E3) Heterozygote Knock Out Animals.
在α-酮戊二酸脱氢酶（α-KGDH）亚基（E2或E3）杂合子敲除动物中，反向和正向电子流诱导的羟基自由基（HO）形成减少。
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Structural alterations induced by ten disease-causing mutations of human dihydrolipoamide dehydrogenase analyzed by hydrogen/deuterium-exchange mass spectrometry: Implications for the structural basis of E3 deficiency.通过氢/氘交换质谱分析人类二氢硫辛酰胺脱氢酶的十种致病突变所诱导的结构改变：对E3缺乏症结构基础的启示
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Glutathionylation of α-ketoglutarate dehydrogenase: the chemical nature and relative susceptibility of the cofactor lipoic acid to modification.α-酮戊二酸脱氢酶的谷胱甘肽化：辅因子硫辛酸修饰的化学性质及相对敏感性。
Free Radic Biol Med. 2013 Aug;61:161-9. doi: 10.1016/j.freeradbiomed.2013.03.020. Epub 2013 Apr 6.
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An update on the role of mitochondrial α-ketoglutarate dehydrogenase in oxidative stress.线粒体 α-酮戊二酸脱氢酶在氧化应激中的作用最新进展。
Mol Cell Neurosci. 2013 Jul;55:13-6. doi: 10.1016/j.mcn.2012.07.005. Epub 2012 Jul 20.
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Effects of long-term oxygen treatment on alpha-ketoglutarate dehydrogenase activity and oxidative modifications in mitochondria of the guinea pig heart.长期氧疗对豚鼠心脏α-酮戊二酸脱氢酶活性及线粒体氧化修饰的影响。
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Cause and consequence: mitochondrial dysfunction initiates and propagates neuronal dysfunction, neuronal death and behavioral abnormalities in age-associated neurodegenerative diseases.原因与后果：线粒体功能障碍在与年龄相关的神经退行性疾病中引发并加剧神经元功能障碍、神经元死亡及行为异常。
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Alpha-ketoglutarate dehydrogenase: a target and generator of oxidative stress.α-酮戊二酸脱氢酶：氧化应激的靶点与产生源
Philos Trans R Soc Lond B Biol Sci. 2005 Dec 29;360(1464):2335-45. doi: 10.1098/rstb.2005.1764.
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Mitochondrial alpha-ketoglutarate dehydrogenase complex generates reactive oxygen species.线粒体α-酮戊二酸脱氢酶复合物产生活性氧。
J Neurosci. 2004 Sep 8;24(36):7779-88. doi: 10.1523/JNEUROSCI.1899-04.2004.