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Modifying Methionine on Proteins.
Xie, Li-Jun; Liu, Li; Cheng, Liang.
Affiliation
  • Xie LJ; Beijing National Laboratory for Molecular Sciences (BNLMS), CAS Key Laboratory of Molecular Recognition and Function, CAS Research/Education Center for Excellence in Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing, 100190, P. R. China.
  • Liu L; University of Chinese Academy of Sciences, Beijing, 100049, P. R. China.
  • Cheng L; Beijing National Laboratory for Molecular Sciences (BNLMS), CAS Key Laboratory of Molecular Recognition and Function, CAS Research/Education Center for Excellence in Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing, 100190, P. R. China.
Chembiochem ; 21(4): 461-463, 2020 02 17.
Article in En | MEDLINE | ID: mdl-31609052
ABSTRACT
Methionine has been recognized as an ideal target for labeling proteins without disturbing their tasks. However, exploration in single post-transcriptional modification of methionine is sluggish. In this Highlight, we summarize some of the most exciting reports on the precise control of protein function by selectively modifying methionine residues.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Proteins / Protein Processing, Post-Translational / Methionine Language: En Journal: Chembiochem Journal subject: BIOQUIMICA Year: 2020 Document type: Article
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Proteins / Protein Processing, Post-Translational / Methionine Language: En Journal: Chembiochem Journal subject: BIOQUIMICA Year: 2020 Document type: Article