Characterization of a Human Dihydrolipoamide Dehydrogenase Mutant Showing Significantly Decreased Catalytic Efficiency toward NAD⁺

• Kim, Hakjung
• • Journal of the Korean Chemical Society
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  • v.64 no.3
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  • pp.141-144
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  • 2020
• https://doi.org/10.5012/jkcs.2020.64.3.141 인용 PDF KSCI

Characterization of a Naturally Occurring Mutation (Arg-447 to Gly) in Human Dihydrolipoamide Dehydrogenase of Patients with Neurological Deterioration

• Kim, Hakjung
• • Journal of the Korean Chemical Society
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  • v.60 no.1
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  • pp.88-92
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  • 2016
• https://doi.org/10.5012/jkcs.2016.60.1.88 인용 PDF KSCI KPUBS HTML

Characterization of Site-Specific Mutations Affecting the Catalytic Efficiency of Human Dihydrolipoamide Dehydrogenase toward NAD⁺

• Kim, Hakjung
• • Journal of the Korean Chemical Society
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  • v.59 no.2
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  • pp.183-187
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  • 2015
• https://doi.org/10.5012/jkcs.2015.59.2.183 인용 PDF KSCI KPUBS HTML

Characterization of Two Site-Specific Mutations in Human Dihydrolipoamide Dehydrogenase Deteriorating the Apparent Enzyme Binding Affinities to Both Dihydrolipoamide and NAD⁺

• Kim, Hakjung
• • Journal of the Korean Chemical Society
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  • v.62 no.3
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  • pp.253-256
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  • 2018
• https://doi.org/10.5012/jkcs.2018.62.3.253 인용 PDF KSCI

Characterization of Site-specific Mutations in Human Dihydrolipoamide Dehydrogenase Significantly Destabilizing the Transition State of the Enzyme Catalysis

• Kim, Hakjung
• • Journal of the Korean Chemical Society
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  • v.59 no.4
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  • pp.344-348
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  • 2015
• https://doi.org/10.5012/jkcs.2015.59.4.344 인용 PDF KSCI KPUBS

Site-Specific Modifications of the Cys-45 Residue in Human Dihydrolipoamide Dehydrogenase to Ser and Tyr

• Kim, Hak-Jung
• • Bulletin of the Korean Chemical Society
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  • v.28 no.6
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  • pp.907-908
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  • 2007
• https://doi.org/10.5012/bkcs.2007.28.6.907 인용 PDF KSCI

Characterization of a Site-specifically Modified Human Dihydrolipoamide Dehydrogenase Mutant Showing Significantly Changed Kinetic Properties

• Kim, Hakjung
• • Journal of the Korean Chemical Society
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  • v.65 no.2
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  • pp.83-87
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  • 2021
• https://doi.org/10.5012/jkcs.2021.65.2.83 인용 PDF KSCI

Characterization of a Naturally Occurring Mutation (Ile-358 to Thr) in Human Dihydrolipoamide Dehydrogenase of a Patient with Leigh Syndrome

• Yuan, Lin;Kim, Hak-Jung
• • Bulletin of the Korean Chemical Society
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  • v.33 no.5
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  • pp.1445-1446
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  • 2012
• https://doi.org/10.5012/bkcs.2012.33.5.1445 인용 PDF KSCI

Characterization of Two Naturally Occurring Mutations (Gly-101 Deletion and Glu-340 to Lys Substitution) in Human Dihydrolipoamide Dehydrogenase of a Patient with Metabolic Acidosis

• Kim, Hak-Jung
• • Bulletin of the Korean Chemical Society
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  • v.33 no.8
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  • pp.2477-2478
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  • 2012
• https://doi.org/10.5012/bkcs.2012.33.8.2477 인용 PDF KSCI

Characterization of Two Site-specifically Mutated Human Dihydrolipoamide Dehydrogenase (Leu-46 to Ala and Pro-52 to Val)

• Yuan, Lin;Cho, Young-Joon;Kim, Hak-Jung
• • Bulletin of the Korean Chemical Society
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  • v.30 no.9
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  • pp.2121-2124
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  • 2009
• https://doi.org/10.5012/bkcs.2009.30.9.2121 인용 PDF KSCI

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