Robustness in jasmonate signaling: mechanisms of concerted regulation and implications for crop improvement. [PDF]
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Cryo-EM structure of bacterial nitrilase reveals insight into oligomerization, substrate recognition, and catalysis. [PDF]
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SIRT5-mediated desuccinylation of MTHFD2 enhances chemoresistance in breast cancer cells by reducing therapy-induced senescence. [PDF]
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HIV-1 vif mediates ubiquitination of the proximal protomer in the APOBEC3H dimer to induce degradation. [PDF]
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Selectivity analysis of diaminopyrimidine-based inhibitors of MTHFD1, MTHFD2 and MTHFD2L. [PDF]
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Genomic Insights into Cyanide Biodegradation in the Pseudomonas Genus. [PDF]
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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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