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Results 1 - 10 of 11 > >>
EC Number
Amino acid exchange
mutation eliminates prolyl hydroxylase activity of HPH-1
substitution of the Fe(II)-binding aspartate for a glutamate residue manifests significantly reduced Fe(II) binding, yet maintains catalytic activity with a 5fold faster reaction with O2
mutation eliminates prolyl hydroxylase activity of HPH-1
mutation eliminates prolyl hydroxylase activity of HPH-1
PDH2 knockout in NP cells lentiviral expression of shPHD2, phenotype, overview. TNF-alpha-dependent induction in expression of PHD3, SDC4, MMP13, and ADAMTS5, catabolic marker genes that are hallmark of disc degeneration, is significantly reduced in PHD2 silenced cells. Silencing of PHD2 significantly restores the TNF-alpha-mediated reduction in aggrecan sand collagen II
siRNA against PHD2 causes sufficient PHD2 knockdown in glioblastoma cell lines U-87MG, U-138MG, and U-343MG
the expression of PHD2 gene is silenced via specific siRNA (siPHD2) in the erythropoietin (EPO)-producing human HCC cell line HepG2. PHD2 knockdown causes a marked reduction of erythropoietin (EPO) production. HIF seems not to be involved in this process
inactive mutant of HIF-P4H-1
disruption of 2OG binding in this variant does not accelerate O2 activation
the mutant shows 15fold increased turnover at limiting O2 concentrations compared to the wild type enzyme
Results 1 - 10 of 11 > >>