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Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/95828
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dc.contributor.authorLai, Shu-Jungzh_TW
dc.contributor.authorTu, I-Fanzh_TW
dc.contributor.authorWu, Wan-Lingzh_TW
dc.contributor.authorYang, Jhih-Tianzh_TW
dc.contributor.authorLuk, Louis Y Pzh_TW
dc.contributor.author賴美津zh_TW
dc.contributor.authorLai, Mei-Chinzh_TW
dc.contributor.authorTsai, Yu-Hsuanzh_TW
dc.contributor.authorWu, Shih-Hsiungzh_TW
dc.date2017-
dc.date.accessioned2018-10-26T03:49:08Z-
dc.date.available2018-10-26T03:49:08Z-
dc.identifier.urihttp://hdl.handle.net/11455/95828-
dc.description.abstractPhosphorylation 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.zh_TW
dc.language.isoen_USzh_TW
dc.publisherBMC MICROBIOLOGYzh_TW
dc.relationBMC microbiology, Volume 17, Issue 1, Page(s) 123.zh_TW
dc.relation.urihttps://www.ncbi.nlm.nih.gov/pubmed/28545444zh_TW
dc.subjectAspartate phosphorylationzh_TW
dc.subjectDrug resistancezh_TW
dc.subjectHistidine phosphorylationzh_TW
dc.subjectPathogenic bacteriazh_TW
dc.subjectPost-translational modificationzh_TW
dc.subjectProteomicszh_TW
dc.subjectAcinetobacter baumanniizh_TW
dc.subjectAmino Acidszh_TW
dc.subjectAspartic Acidzh_TW
dc.subjectBacteriazh_TW
dc.subjectBacterial Proteinszh_TW
dc.subjectBinding Siteszh_TW
dc.subjectHelicobacter pylorizh_TW
dc.subjectHistidinezh_TW
dc.subjectKlebsiella pneumoniaezh_TW
dc.subjectPhosphorylationzh_TW
dc.subjectProkaryotic Cellszh_TW
dc.subjectProtein Processing, Post-Translationalzh_TW
dc.subjectProteomicszh_TW
dc.subjectSequence Analysis, Proteinzh_TW
dc.subjectVibrio vulnificuszh_TW
dc.subjectZinczh_TW
dc.subjectDrug Resistancezh_TW
dc.titleSite-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistancezh_TW
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1186/s12866-017-1034-2zh_TW
item.openairetypeJournal Article-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextrestricted-
item.fulltextwith fulltext-
item.cerifentitytypePublications-
item.languageiso639-1en_US-
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