aminoadipate-semialdehyde synthase ; Homo sapiens






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1 3110158 The bifunctional aminoadipic semialdehyde synthase in lysine degradation. Separation of reductase and dehydrogenase domains by limited proteolysis and column chromatography. J Biol Chem 1987 Jul 5 3
2 4774398 Lysine metabolism in mammals. Biochem J 1973 Oct 1
3 10775527 Identification of the alpha-aminoadipic semialdehyde synthase gene, which is defective in familial hyperlysinemia. Am J Hum Genet 2000 Jun 2
4 11286508 Identification of the alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LYS5 gene. Mol Genet Metab 2001 Apr 2
5 16525756 Lysine catabolism, an effective versatile regulator of lysine level in plants. Amino Acids 2006 Mar 1
6 19774086 LKR/SDH plays important roles throughout the tick life cycle including a long starvation period. PLoS One 2009 Sep 23 7
7 23890588 Clinical, biochemical, molecular and therapeutic aspects of 2 new cases of 2-aminoadipic semialdehyde synthase deficiency. Mol Genet Metab 2013 Nov 1
8 32567100 Deletion of 2-aminoadipic semialdehyde synthase limits metabolite accumulation in cell and mouse models for glutaric aciduria type 1. J Inherit Metab Dis 2020 Nov 1
9 33100873 Next generation sequencing reveals novel homozygous frameshift in <i>PUS7</i> and splice acceptor variants in <i>AASS</i> gene leading to intellectual disability, developmental delay, dysmorphic feature and microcephaly. Saudi J Biol Sci 2020 Nov 2