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Cited by 8 publications
(14 citation statements)
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References 35 publications
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“…Temperature-sensitive mutations of NIMA reversibly arrest cells in late G2 (Brzywczy et al, 2011), despite the presence of activated p34 cdc2 kinase activity, indicating that NIMA function, plays an essential role downstream or parallel to p34 cdc2 for progression through mitosis (Osmani et al, 1991). Although phosphorylation of NIMA by p34 cdc2 /cyclin B is not required for basal level NIMA kinase activity, it appears to be required for mitotic entry (Ye et al, 1995).…”
Section: Nima-related Kinase2mentioning
confidence: 99%
“…Temperature-sensitive mutations of NIMA reversibly arrest cells in late G2 (Brzywczy et al, 2011), despite the presence of activated p34 cdc2 kinase activity, indicating that NIMA function, plays an essential role downstream or parallel to p34 cdc2 for progression through mitosis (Osmani et al, 1991). Although phosphorylation of NIMA by p34 cdc2 /cyclin B is not required for basal level NIMA kinase activity, it appears to be required for mitotic entry (Ye et al, 1995).…”
Section: Nima-related Kinase2mentioning
confidence: 99%
“…In filamentous fungi, sulfur containing amino acids, methionine and cysteine, as well as inorganic sulfur are the most metabolized sulfur sources via the methionine-cysteine cycle [ 14 ]. Sulfur uptake, a key step in sulfur assimilation, is mediated by plasma membrane sulfate permease [ 15 ].…”
Section: Introductionmentioning
confidence: 99%
“…Transcription of the sulfate permease gene of fungi is strongly regulated by sulfur levels and is repressed by methionine supplementation in the medium [ 20 ]. Transcriptional regulation of sulfur metabolism is dependent on the Sulfur Metabolite Repression (SMR) system that consists of the metR gene encoding a bZIP transcriptional factor, which controls the expression of all sulfur metabolizing enzymes [ 14 , 21 , 22 ]. In A .…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…Enzyme-catalyzed S-methylation reactions using SAM yield SAH, which in A. nidulans and other organisms is subsequently hydrolyzed to homocysteine (Hcy) and adenosine via the action of S-adenosylhomocysteinase. The resultant Hcy is then reconverted to Met via the action of methionine synthase, with methylenetetrahydrofolate (from the methyl cycle) as the methyl source (23,24). Notably, SAH is a competitive inhibitor of selected methyltransferases, and Hcy is cytotoxic, in A. nidulans (25,26).…”
mentioning
confidence: 99%