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|標題:||Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance||作者:||Lai, Shu-Jung
Luk, Louis Y P
|關鍵字:||Aspartate phosphorylation;Drug resistance;Histidine phosphorylation;Pathogenic bacteria;Post-translational modification;Proteomics;Acinetobacter baumannii;Amino Acids;Aspartic Acid;Bacteria;Bacterial Proteins;Binding Sites;Helicobacter pylori;Histidine;Klebsiella pneumoniae;Phosphorylation;Prokaryotic Cells;Protein Processing, Post-Translational;Proteomics;Sequence Analysis, Protein;Vibrio vulnificus;Zinc;Drug Resistance||出版社:||BMC MICROBIOLOGY||Project:||BMC microbiology, Volume 17, Issue 1, Page(s) 123.||摘要:||
Phosphorylation of amino acid residues on proteins is an important and common post-translational modification in both eukaryotes and prokaryotes. Most research work has been focused on phosphorylation of serine, threonine or tyrosine residues, whereas phosphorylation of other amino acids are significantly less clear due to the controversy on their stability under standard bioanalytical conditions.
|Appears in Collections:||生命科學系所|
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