Please use this identifier to cite or link to this item:
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
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
Project: BMC microbiology, Volume 17, Issue 1, Page(s) 123.
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.
DOI: 10.1186/s12866-017-1034-2
Appears in Collections:生命科學系所

Files in This Item:
File Description SizeFormat Existing users please Login
12866_2017_Article_1034.pdf期刊論文1.32 MBAdobe PDFThis file is only available in the university internal network   
Show full item record

Google ScholarTM




Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.