Study of structure-function relationships in human glutamate dehydrogenases reveals novel molecular mechanisms for the regulation of the nerve tissue-specific (GLUD2) isoenzyme.

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作者： Andreas,Plaitakis ^[1] ; Cleanthe,Spanaki ; Vasilis,Mastorodemos ; Ioannis,Zaganas

作者单位： Department of Neurology, Section of Medicine, School of Health Sciences, University of Crete, Heraklion, Crete, Greece. plaitak@med.uoc.gr ^[1]

主题词动物(Animals);细胞系(Cell Line);谷氨酸脱氢酶(Glutamate Dehydrogenase);人类(Humans);诱变, 定点(Mutagenesis, Site-Directed);重组蛋白质类(Recombinant Proteins);斜纹夜蛾属(Spodoptera);构效关系(Structure-Activity Relationship)

DOI 10.1016/s0197-0186(03)00028-7

PMID 12742085

发布时间 2019-09-01

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Neurochemistry international

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Study of structure-function relationships in human glutamate dehydrogenases reveals novel molecular mechanisms for the regulation of the nerve tissue-specific (GLUD2) isoenzyme.

Neurochemistry international

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Neurochemistry international

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Study of structure-function relationships in human glutamate dehydrogenases reveals novel molecular mechanisms for the regulation of the nerve tissue-specific (GLUD2) isoenzyme.

Neurochemistry international

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Neurochemistry international

相关期刊

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