Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/95828
標題: Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance
作者: Lai, Shu-Jung
Tu, I-Fan
Wu, Wan-Ling
Yang, Jhih-Tian
Luk, Louis Y P
賴美津
Lai, Mei-Chin
Tsai, Yu-Hsuan
Wu, Shih-Hsiung
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
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.
URI: http://hdl.handle.net/11455/95828
文章連結: https://www.ncbi.nlm.nih.gov/pubmed/28545444
Appears in Collections:生命科學系所

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