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the X-ray crystal structure of human selenocysteine lyase and the key residue that provides the selenocysteine specificity
Results confirm that HCV core protein is associated with specific changes in mRNA expression, including the gene for selenocysteine lyase, which may be involved in the pathophysiology of hepatocellular carcinoma.
PMID:10692412 concerns mostly mouse selenocysteine lyase, however, refers to the sequence of the N-terminal region of putative human protein.
This study showed that Male mice lacking two key genes involved in Se metabolism (Scly(-/-)Sepp1 (show SEPP1 Proteins)(-/-) mice), selenoprotein P (Sepp1 (show SEPP1 Proteins)) and Sec lyase (Scly), develop severe neurological dysfunction, neurodegeneration, and audiogenic seizures.
our findings unveil a new metabolic role for Reg3beta in protein nitration and a new biosynthesis control of GPX1 (show GPX1 Proteins) by a completely "unrelated" regenerating protein, Reg3beta, via transcriptional activation of Scly
These findings provide the first in vivo evidence that Scly and Sepp1 (show SEPP1 Proteins) work cooperatively to maintain selenoprotein function in the mammalian brain.
The results suggested a dependence of glucose and lipid homeostasis on selenocysteine lyase activity. These findings connect Se and energy metabolism and demonstrate for the first time a unique physiological role of selenocysteine lyase.
Scly knockout mice do not display neurological dysfunction comparable to Sepp1 (show SEPP1 Proteins) knockout mice.
Selenocysteine lyase (SCLY\; EC 184.108.40.206) catalyzes the pyridoxal 5-prime phosphate-dependent conversion of L-selenocysteine to L-alanine and elemental selenium (Mihara et al., 2000
, selenocysteine lyase; Selenocysteine reductase
, selenocysteine reductase
, selenocysteine lyase
, Selenocysteine lyase