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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.

Biochimica et biophysica acta

Ambrus A, Wang J, Mizsei R, Zambo Z, Torocsik B, Jordan F, Adam-Vizi V.
PMID: 27544700
Biochim Biophys Acta. 2016 Nov;1862(11):2098-2109. doi: 10.1016/j.bbadis.2016.08.013. Epub 2016 Aug 18.

Pathogenic amino acid substitutions of the common E3 component (hE3) of the human alpha-ketoglutarate dehydrogenase and the pyruvate dehydrogenase complexes lead to severe metabolic diseases (E3 deficiency), which usually manifest themselves in cardiological and/or neurological symptoms and often cause...

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Ambrus A, Wang J, Mizsei R, et al. 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. Biochim Biophys Acta. 2016;1862(11):2098-2109doi: 10.1016/j.bbadis.2016.08.013.
Ambrus, A., Wang, J., Mizsei, R., Zambo, Z., Torocsik, B., Jordan, F., & Adam-Vizi, V. (2016). 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. Biochimica et biophysica acta, 1862(11), 2098-2109. https://doi.org/10.1016/j.bbadis.2016.08.013
Ambrus, Attila, et al. "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." Biochimica et biophysica acta vol. 1862,11 (2016): 2098-2109. doi: https://doi.org/10.1016/j.bbadis.2016.08.013
Ambrus A, Wang J, Mizsei R, Zambo Z, Torocsik B, Jordan F, Adam-Vizi V. 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. Biochim Biophys Acta. 2016 Nov;1862(11):2098-2109. doi: 10.1016/j.bbadis.2016.08.013. Epub 2016 Aug 18. PMID: 27544700; PMCID: PMC5035230.
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Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase.

Plant physiology

Ji L, Becana M, Sarath G, Shearman L, Klucas RV.
PMID: 12232320
Plant Physiol. 1994 Sep;106(1):203-209. doi: 10.1104/pp.106.1.203.

We previously cloned and sequenced a cDNA encoding soybean ferric leghemoglobin reductase (FLbR), an enzyme postulated to play an important role in maintaining leghemoglobin in a functional ferrous state in nitrogen-fixing root nodules. This cDNA was sub-cloned into an...

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Ji L, Becana M, Sarath G, et al. Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase. Plant Physiol. 1994;106(1):203-209doi: 10.1104/pp.106.1.203.
Ji, L., Becana, M., Sarath, G., Shearman, L., & Klucas, R. V. (1994). Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase. Plant physiology, 106(1), 203-209. https://doi.org/10.1104/pp.106.1.203
Ji, L., et al. "Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase." Plant physiology vol. 106,1 (1994): 203-209. doi: https://doi.org/10.1104/pp.106.1.203
Ji L, Becana M, Sarath G, Shearman L, Klucas RV. Overproduction in Escherichia coli and Characterization of a Soybean Ferric Leghemoglobin Reductase. Plant Physiol. 1994 Sep;106(1):203-209. doi: 10.1104/pp.106.1.203. PMID: 12232320; PMCID: PMC159517.
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Reexploring 5-methoxyindole-2-carboxylic acid (MICA) as a potential antidiabetic agent.

Diabetes, metabolic syndrome and obesity : targets and therapy

Yan LJ.
PMID: 29765243
Diabetes Metab Syndr Obes. 2018 May 04;11:183-186. doi: 10.2147/DMSO.S166485. eCollection 2018.

5-Methoxyindole-2-carboxylic acid (MICA) is a potent hypoglycemic agent that inhibits gluconeogenesis in the liver. It is also a well-known inhibitor of mitochondrial dihydrolipoamide dehydrogenase. MICA was extensively studied in the 1960s and 1970s and was once tested for its...

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Yan LJ. Reexploring 5-methoxyindole-2-carboxylic acid (MICA) as a potential antidiabetic agent. Diabetes Metab Syndr Obes. 2018;11:183-186doi: 10.2147/DMSO.S166485.
Yan, L. J. (2018). Reexploring 5-methoxyindole-2-carboxylic acid (MICA) as a potential antidiabetic agent. Diabetes, metabolic syndrome and obesity : targets and therapy, 11183-186. https://doi.org/10.2147/DMSO.S166485
Yan, Liang-Jun. "Reexploring 5-methoxyindole-2-carboxylic acid (MICA) as a potential antidiabetic agent." Diabetes, metabolic syndrome and obesity : targets and therapy vol. 11 (2018): 183-186. doi: https://doi.org/10.2147/DMSO.S166485
Yan LJ. Reexploring 5-methoxyindole-2-carboxylic acid (MICA) as a potential antidiabetic agent. Diabetes Metab Syndr Obes. 2018 May 04;11:183-186. doi: 10.2147/DMSO.S166485. eCollection 2018. PMID: 29765243; PMCID: PMC5942165.
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The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia.

Molecular genetics and metabolism reports

Alfarsi A, Alfadhel M, Alameer S, Alhashem A, Tabarki B, Ababneh F, Al Fares A, Al Mutairi F.
PMID: 34745891
Mol Genet Metab Rep. 2021 Oct 23;29:100817. doi: 10.1016/j.ymgmr.2021.100817. eCollection 2021 Dec.

BACKGROUND: Dihydrolipoamide dehydrogenase deficiency (DLDD) is a rare metabolic disorder inherited in an autosomal recessive manner. This heterogeneous disease has a variable clinical presentation, onset, and biochemical markers.MATERIALS AND METHODS: We retrospectively reviewed the clinical and molecular diagnosis of...

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Alfarsi A, Alfadhel M, Alameer S, et al. The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia. Mol Genet Metab Rep. 2021;29:100817doi: 10.1016/j.ymgmr.2021.100817.
Alfarsi, A., Alfadhel, M., Alameer, S., Alhashem, A., Tabarki, B., Ababneh, F., Al Fares, A., & Al Mutairi, F. (2021). The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia. Molecular genetics and metabolism reports, 29100817. https://doi.org/10.1016/j.ymgmr.2021.100817
Alfarsi, Anar, et al. "The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia." Molecular genetics and metabolism reports vol. 29 (2021): 100817. doi: https://doi.org/10.1016/j.ymgmr.2021.100817
Alfarsi A, Alfadhel M, Alameer S, Alhashem A, Tabarki B, Ababneh F, Al Fares A, Al Mutairi F. The phenotypic spectrum of dihydrolipoamide dehydrogenase deficiency in Saudi Arabia. Mol Genet Metab Rep. 2021 Oct 23;29:100817. doi: 10.1016/j.ymgmr.2021.100817. eCollection 2021 Dec. PMID: 34745891; PMCID: PMC8554626.
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Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent.

Proteins

Dayan A, Yeheskel A, Lamed R, Fleminger G, Ashur-Fabian O.
PMID: 32761961
Proteins. 2020 Aug 06; doi: 10.1002/prot.25991. Epub 2020 Aug 06.

Dihydrolipoamide dehydrogenase (DLDH) is a mitochondrial enzyme that comprises an essential component of the pyruvate dehydrogenase complex. Lines of evidence have shown that many dehydrogenases possess unrelated actions known as moonlightings in addition to their oxidoreductase activity. As part...

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Dayan A, Yeheskel A, Lamed R, et al. Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent. Proteins. 2020;doi: 10.1002/prot.25991.
Dayan, A., Yeheskel, A., Lamed, R., Fleminger, G., & Ashur-Fabian, O. (2020). Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent. Proteins, . https://doi.org/10.1002/prot.25991
Dayan, Avraham, et al. "Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent." Proteins vol. (2020). doi: https://doi.org/10.1002/prot.25991
Dayan A, Yeheskel A, Lamed R, Fleminger G, Ashur-Fabian O. Dihydrolipoamide dehydrogenase moonlighting activity as a DNA chelating agent. Proteins. 2020 Aug 06; doi: 10.1002/prot.25991. Epub 2020 Aug 06. PMID: 32761961.
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Mycoplasma synoviae dihydrolipoamide dehydrogenase is an immunogenic fibronectin/plasminogen binding protein and a putative adhesin.

Veterinary microbiology

Qi J, Wang Y, Li H, Shang Y, Gao S, Ding C, Liu X, Wang S, Li T, Tian M, Yu S.
PMID: 35032790
Vet Microbiol. 2021 Dec 31;265:109328. doi: 10.1016/j.vetmic.2021.109328. Epub 2021 Dec 31.

Mycoplasma synoviae (M. synoviae) is an important avian pathogen that causes arthritis and airsacculitis in young chickens and turkeys. Infection by M. synoviae results in considerable economic losses to the poultry industry worldwide. Cytoadherence is a crucial stage during...

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Qi J, Wang Y, Li H, et al. Mycoplasma synoviae dihydrolipoamide dehydrogenase is an immunogenic fibronectin/plasminogen binding protein and a putative adhesin. Vet Microbiol. 2021;265:109328doi: 10.1016/j.vetmic.2021.109328.
Qi, J., Wang, Y., Li, H., Shang, Y., Gao, S., Ding, C., Liu, X., Wang, S., Li, T., Tian, M., & Yu, S. (2021). Mycoplasma synoviae dihydrolipoamide dehydrogenase is an immunogenic fibronectin/plasminogen binding protein and a putative adhesin. Veterinary microbiology, 265109328. https://doi.org/10.1016/j.vetmic.2021.109328
Qi, Jingjing, et al. "Mycoplasma synoviae dihydrolipoamide dehydrogenase is an immunogenic fibronectin/plasminogen binding protein and a putative adhesin." Veterinary microbiology vol. 265 (2021): 109328. doi: https://doi.org/10.1016/j.vetmic.2021.109328
Qi J, Wang Y, Li H, Shang Y, Gao S, Ding C, Liu X, Wang S, Li T, Tian M, Yu S. Mycoplasma synoviae dihydrolipoamide dehydrogenase is an immunogenic fibronectin/plasminogen binding protein and a putative adhesin. Vet Microbiol. 2021 Dec 31;265:109328. doi: 10.1016/j.vetmic.2021.109328. Epub 2021 Dec 31. PMID: 35032790.
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Identification of Multiple Soluble Fe(III) Reductases in Gram-Positive Thermophilic Bacterium Thermoanaerobacter indiensis BSB-33.

International journal of genomics

Pal S.
PMID: 25180173
Int J Genomics. 2014;2014:850607. doi: 10.1155/2014/850607. Epub 2014 Aug 07.

Thermoanaerobacter indiensis BSB-33 has been earlier shown to reduce Fe(III) and Cr(VI) anaerobically at 60°C optimally. Further, the Gram-positive thermophilic bacterium contains Cr(VI) reduction activity in both the membrane and cytoplasm. The soluble fraction prepared from T. indiensis cells...

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Pal S. Identification of Multiple Soluble Fe(III) Reductases in Gram-Positive Thermophilic Bacterium Thermoanaerobacter indiensis BSB-33. Int J Genomics. 2014;2014:850607doi: 10.1155/2014/850607.
Pal, S. (2014). Identification of Multiple Soluble Fe(III) Reductases in Gram-Positive Thermophilic Bacterium Thermoanaerobacter indiensis BSB-33. International journal of genomics, 2014850607. https://doi.org/10.1155/2014/850607
Pal, Subrata. "Identification of Multiple Soluble Fe(III) Reductases in Gram-Positive Thermophilic Bacterium Thermoanaerobacter indiensis BSB-33." International journal of genomics vol. 2014 (2014): 850607. doi: https://doi.org/10.1155/2014/850607
Pal S. Identification of Multiple Soluble Fe(III) Reductases in Gram-Positive Thermophilic Bacterium Thermoanaerobacter indiensis BSB-33. Int J Genomics. 2014;2014:850607. doi: 10.1155/2014/850607. Epub 2014 Aug 07. PMID: 25180173; PMCID: PMC4142287.
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Potassium Iodide-Induced Changes in Pyruvate Dehydrogenase Complex from Bacillus stearothermophilus.

Bioscience, biotechnology, and biochemistry

Aso Y, Hiromasa Y, Aikawa Y, Meno K, Ishiguro M.
PMID: 27393359
Biosci Biotechnol Biochem. 1998;62(1):108-16. doi: 10.1271/bbb.62.108.

Treatment with KI and its subsequent removal induced disassembly of Bacillus stearothermophilus pyruvate dehydrogenase complex (PDC) and association of disassembly products, respectively. The disassembly yielded neither completely dissociated components nor aggregate, but did yield a few molecular forms smaller...

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Aso Y, Hiromasa Y, Aikawa Y, et al. Potassium Iodide-Induced Changes in Pyruvate Dehydrogenase Complex from Bacillus stearothermophilus. Biosci Biotechnol Biochem. 1998;62(1):108-16doi: 10.1271/bbb.62.108.
Aso, Y., Hiromasa, Y., Aikawa, Y., Meno, K., & Ishiguro, M. (1998). Potassium Iodide-Induced Changes in Pyruvate Dehydrogenase Complex from Bacillus stearothermophilus. Bioscience, biotechnology, and biochemistry, 62(1), 108-16. https://doi.org/10.1271/bbb.62.108
Aso, Y, et al. "Potassium Iodide-Induced Changes in Pyruvate Dehydrogenase Complex from Bacillus stearothermophilus." Bioscience, biotechnology, and biochemistry vol. 62,1 (1998): 108-16. doi: https://doi.org/10.1271/bbb.62.108
Aso Y, Hiromasa Y, Aikawa Y, Meno K, Ishiguro M. Potassium Iodide-Induced Changes in Pyruvate Dehydrogenase Complex from Bacillus stearothermophilus. Biosci Biotechnol Biochem. 1998;62(1):108-16. doi: 10.1271/bbb.62.108. PMID: 27393359.
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Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme.

Journal of biochemical and pharmacological research

Yan LJ, Thangthaeng N, Sumien N, Forster MJ.
PMID: 23646291
J Biochem Pharmacol Res. 2013 Mar;1(1):30-42.

Dihydrolipoamide dehydrogenase (DLDH) is a multifunctional oxidoreductase and is well known as an essential component of four mammalian mitochondrial multienzyme complexes: pyruvate dehydrogenase, α-ketoglutarate dehydrogenase, branched chain α-keto acid dehydrogenase, and the glycine cleavage system. However, existence of extracellular...

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Yan LJ, Thangthaeng N, Sumien N, et al. Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme. J Biochem Pharmacol Res. 2013;1(1):30-42
Yan, L. J., Thangthaeng, N., Sumien, N., & Forster, M. J. (2013). Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme. Journal of biochemical and pharmacological research, 1(1), 30-42.
Yan, Liang-Jun, et al. "Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme." Journal of biochemical and pharmacological research vol. 1,1 (2013): 30-42.
Yan LJ, Thangthaeng N, Sumien N, Forster MJ. Serum Dihydrolipoamide Dehydrogenase Is a Labile Enzyme. J Biochem Pharmacol Res. 2013 Mar;1(1):30-42. PMID: 23646291; PMCID: PMC3641859.
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Suppression of a core metabolic enzyme dihydrolipoamide dehydrogenase (.

Genes & diseases

Ahmad W, Ebert PR.
PMID: 34522713
Genes Dis. 2020 Aug 20;8(6):849-866. doi: 10.1016/j.gendis.2020.08.004. eCollection 2021 Nov.

A decrease in energy metabolism is associated with Alzheimer's disease (AD), but it is not known whether the observed decrease exacerbates or protects against the disease. The importance of energy metabolism in AD is reinforced by the observation that...

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Ahmad W, Ebert PR. Suppression of a core metabolic enzyme dihydrolipoamide dehydrogenase (. Genes Dis. 2020;8(6):849-866doi: 10.1016/j.gendis.2020.08.004.
Ahmad, W., & Ebert, P. R. (2021). Suppression of a core metabolic enzyme dihydrolipoamide dehydrogenase (. Genes & diseases, 8(6), 849-866. https://doi.org/10.1016/j.gendis.2020.08.004
Ahmad, Waqar, and Ebert, Paul R. "Suppression of a core metabolic enzyme dihydrolipoamide dehydrogenase (." Genes & diseases vol. 8,6 (2021): 849-866. doi: https://doi.org/10.1016/j.gendis.2020.08.004
Ahmad W, Ebert PR. Suppression of a core metabolic enzyme dihydrolipoamide dehydrogenase (. Genes Dis. 2020 Aug 20;8(6):849-866. doi: 10.1016/j.gendis.2020.08.004. eCollection 2021 Nov. PMID: 34522713; PMCID: PMC8427249.
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5-Methoxyindole-2-Carboylic Acid (MICA) Fails to Retard Development and Progression of Type II Diabetes in ZSF1 Diabetic Rats.

Reactive oxygen species (Apex, N.C.)

Li CY, Ma WX, Yan LJ.
PMID: 32551363
React Oxyg Species (Apex). 2020 May 01;9(27):144-147.

5-Methoxyindole-2-carboxylic acid (MICA) is a well-established reversible inhibitor of mitochondrial dihydrolipoamide dehydrogenase (DLDH). This chemical, as an indole derivative, has been shown to be neuroprotective against ischemic stroke injury when administered either before or after ischemic stroke in animal...

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Li CY, Ma WX, Yan LJ. 5-Methoxyindole-2-Carboylic Acid (MICA) Fails to Retard Development and Progression of Type II Diabetes in ZSF1 Diabetic Rats. React Oxyg Species (Apex). 2020;9(27):144-147
Li, C. Y., Ma, W. X., & Yan, L. J. (2020). 5-Methoxyindole-2-Carboylic Acid (MICA) Fails to Retard Development and Progression of Type II Diabetes in ZSF1 Diabetic Rats. Reactive oxygen species (Apex, N.C.), 9(27), 144-147.
Li, Chun-Yan, et al. "5-Methoxyindole-2-Carboylic Acid (MICA) Fails to Retard Development and Progression of Type II Diabetes in ZSF1 Diabetic Rats." Reactive oxygen species (Apex, N.C.) vol. 9,27 (2020): 144-147.
Li CY, Ma WX, Yan LJ. 5-Methoxyindole-2-Carboylic Acid (MICA) Fails to Retard Development and Progression of Type II Diabetes in ZSF1 Diabetic Rats. React Oxyg Species (Apex). 2020 May 01;9(27):144-147. PMID: 32551363; PMCID: PMC7301685.
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Analysis of Secreted Proteins and Potential Virulence .

Frontiers in microbiology

He Y, Wang S, Wang K, Zhou J, Han Z, Sun F.
PMID: 33763038
Front Microbiol. 2021 Mar 02;12:612166. doi: 10.3389/fmicb.2021.612166. eCollection 2021.

No abstract available.

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He Y, Wang S, Wang K, et al. Analysis of Secreted Proteins and Potential Virulence . Front Microbiol. 2021;12:612166doi: 10.3389/fmicb.2021.612166.
He, Y., Wang, S., Wang, K., Zhou, J., Han, Z., & Sun, F. (2021). Analysis of Secreted Proteins and Potential Virulence . Frontiers in microbiology, 12612166. https://doi.org/10.3389/fmicb.2021.612166
He, Yu, et al. "Analysis of Secreted Proteins and Potential Virulence ." Frontiers in microbiology vol. 12 (2021): 612166. doi: https://doi.org/10.3389/fmicb.2021.612166
He Y, Wang S, Wang K, Zhou J, Han Z, Sun F. Analysis of Secreted Proteins and Potential Virulence . Front Microbiol. 2021 Mar 02;12:612166. doi: 10.3389/fmicb.2021.612166. eCollection 2021. PMID: 33763038; PMCID: PMC7982893.
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Showing 1 to 12 of 34 entries