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microphthalmia, syndrome
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NAA10
Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotes.
Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-����-acetylation features.
The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways.
An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricus.
Expression, crystallization and preliminary X-ray crystallographic analyses of two N-terminal acetyltransferase-related proteins from Thermoplasma acidophilum.
Structure of Thermoplasma volcanium Ard1 belongs to N-acetyltransferase family member suggesting multiple ligand binding modes with acetyl coenzyme A and coenzyme A.
Genetic manipulation indicates that ARD1 is an essential N(alpha)-acetyltransferase in Trypanosoma brucei.
N-terminal processing of proteins exported by malaria parasites.
Ribosomal protein modification in Escherichia coli. II. Studies of a mutant lacking the N-terminal acetylation of protein S18.
Ribosomal protein modification in Escherichia coli. I. A mutant lacking the N-terminal acetylation of protein S5 exhibits thermosensitivity.
Ribosomal protein modification in Escherichia coli. III. Studies of mutants lacking an acetylase activity specific for protein L12.
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