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Biochemical and biological studies of irradiated and non-irradiated extracts of Solanum aculeastrum Dunal fruit. [PDF]
Sci RepAmer AA +4 more
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Sortase-mediated surface display of a chimeric immunogen on Bacillus subtilis: a chicken necrotic enteritis vaccine candidate. [PDF]
Microb Cell FactAl-Aneed B +8 more
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Utilizing a Proximity Dependent Labeling Strategy to Study Cancer-Immune Intercellular Interactions In Vitro and In Vivo. [PDF]
J Pharmacol Exp TherMaffuid K, Cao Y.
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When Paul Berg meets Donald Crothers: an achiral connection through protein biosynthesis. [PDF]
Nucleic Acids ResKumar P, Sankaranarayanan R.
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Determination of Potential Lead Compound from Magnolia officinalis for Alzheimer's Disease through Pharmacokinetic Prediction, Molecular Docking, Dynamic Simulation, and Experimental Validation. [PDF]
Int J Mol SciYoun K, Jun M.
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Discrimination by rat liver aminoacyltransferase I against met-tRNAF∗
Biochemical and Biophysical Research Communications, 1970The two species of methionine-accepting tRNA from rat liver have been separated and their enzymatic binding to ribosomes studied. At a Mg++ concentration of 0.006 M, rat liver aminoacyltransferase I promotes the binding of the non-formylatable species of Met-tRNA to 80 S ribosomes in the presence of poly AUG.
H M, Moon, J F, Collins, E S, Maxwell
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Biochemical and Biophysical Research Communications, 2007
SyrC, a component of the multienzyme system of syringomycin biosynthesis, has been shown to shuttle Thr/4-Cl-Thr between the thiolation domains SyrB1-T1 and SyrE-T8,9 by transiently linking it to Cys224 in the enzyme active site. We present data on the structure-function relationship in vivo of this protein and an in silico model of its three ...
FULLONE, Maria Rosaria +5 more
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SyrC, a component of the multienzyme system of syringomycin biosynthesis, has been shown to shuttle Thr/4-Cl-Thr between the thiolation domains SyrB1-T1 and SyrE-T8,9 by transiently linking it to Cys224 in the enzyme active site. We present data on the structure-function relationship in vivo of this protein and an in silico model of its three ...
FULLONE, Maria Rosaria +5 more
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Acta Diabetologica Latina, 1970
Aminoacyltransferase II catalyzed the hydrolysis of GTP in the presence of unwashed skeletal muscle ribosomes; however, there was also hydrolysis of the nucleoside triphosphate in the absence of the enzyme. Hydrolysis of GTP in the absence of aminoacyltransferase II was reduced, though not eliminated, by washing the ribosomes in 0.5 M NH4Cl.
D P, Leader, I G, Wool, J E, Leader
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Aminoacyltransferase II catalyzed the hydrolysis of GTP in the presence of unwashed skeletal muscle ribosomes; however, there was also hydrolysis of the nucleoside triphosphate in the absence of the enzyme. Hydrolysis of GTP in the absence of aminoacyltransferase II was reduced, though not eliminated, by washing the ribosomes in 0.5 M NH4Cl.
D P, Leader, I G, Wool, J E, Leader
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Journal of Biochemistry, 2002
A unique enzyme with some properties favorable for the synthesis of D-amino acid-containing peptides has been purified from the culture broth of Saccharothrix sp. AS-2. The purification steps included ammonium sulfate fractionation, chromatographies on CM-Toyopearl 650M and ProtEx Butyl, and sucrose density-gradient isoelectric focusing.
Akio, Sugihara +7 more
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A unique enzyme with some properties favorable for the synthesis of D-amino acid-containing peptides has been purified from the culture broth of Saccharothrix sp. AS-2. The purification steps included ammonium sulfate fractionation, chromatographies on CM-Toyopearl 650M and ProtEx Butyl, and sucrose density-gradient isoelectric focusing.
Akio, Sugihara +7 more
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Current Computer-Aided Drug Design
Background: Drug-resistant Staphylococcus aureus represents a substantial healthcare challenge worldwide, and its range of available therapeutic options continues to diminish progressively. Thus, this study aimed to identify potential inhibitors against FemA, a crucial protein involved in the cell wall biosynthesis of S. aureus.
Narjes Noori, Goodarzi +5 more
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Background: Drug-resistant Staphylococcus aureus represents a substantial healthcare challenge worldwide, and its range of available therapeutic options continues to diminish progressively. Thus, this study aimed to identify potential inhibitors against FemA, a crucial protein involved in the cell wall biosynthesis of S. aureus.
Narjes Noori, Goodarzi +5 more
openaire +2 more sources