Selectivity analysis of diaminopyrimidine-based inhibitors of MTHFD1, MTHFD2 and MTHFD2L. [PDF]
Jha V, Eriksson LA.
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Enhanced Analysis of Low-Abundance Proteins in Soybean Seeds Using Advanced Mass Spectrometry. [PDF]
Meng B +10 more
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Genomic Insights into Cyanide Biodegradation in the Pseudomonas Genus. [PDF]
Sáez LP +6 more
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The one-carbon metabolic enzyme MTHFD2 promotes resection and homologous recombination after ionizing radiation. [PDF]
Marttila P +14 more
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Development of Potent and Selective Inhibitors of Methylenetetrahydrofolate Dehydrogenase 2 for Targeting Acute Myeloid Leukemia: SAR, Structural Insights, and Biological Characterization. [PDF]
Chang HH +19 more
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AMP and adenosine aminohydrolases in rat tissues.
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Characterization of purified guanine aminohydrolase
Archives of Biochemistry and Biophysics, 1979Abstract Guanine aminohydrolase (GAH) (E.C. 3.5.4.3) was purified by affinity chromatography on 9-( p -β-aminoethoxyphenyl)guanine-Sepharose to a specific activity of 35.5 units/mg. The molecular weight of the enzyme was estimated to be 110,000 by gel filtration.
J D, Bergstrom, A L, Bieber
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On the regulatory properties of deoxycytidylate aminohydrolase
Biochemical and Biophysical Research Communications, 1964Abstract In a previous paper we suggested the occurrence of at least one regulatory site ( Scarano et al., 1962 , Scarano et al., 1963 ) on dCMP aminohydrolase. The present paper reports further experiments that support this hypothesis.
E, Scarano, G, Geraci, M, Rossi
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Characterization of bovine liver guanine aminohydrolase
International Journal of Biochemistry, 1981Abstract 1. 1. The isoelectric points of bovine liver guanine aminohydrolase and xanthine oxidase are 4.90 and 6.25, respectively. 2. 2. The molecular weight of the guanine aminohydrolase is 95,000. 3. 3. The guanine aminohydrolase is formed from two subunits of identical molecular weight.
J M, Galilea, E I, Canela, J, Bozal
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A fluorimetric assay for guanine aminohydrolase
Analytical Biochemistry, 1974Abstract A rapid, sensitive, and versatile assay for guanine aminohydrolase is described. It is based on the difference in native fluorescence of guanine, the substrate, and xanthine, the reaction product when excitation and emission wavelengths are 285 nm and 345 nm, respectively.
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