Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm.

scientific article published on 9 April 2018

Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/ACS.BIOCHEM.8B00160
P932PMC publication ID6110390
P698PubMed publication ID29630358

P50authorJoAnne StubbeQ55280
Daniel G. NoceraQ3014070
Wankyu LeeQ86313948
Marina BennatiQ88306454
Cecilia TommosQ88306457
P2093author name stringMichael Huynh
Cyrille Costentin
Müge Kasanmascheff
Isabel Bejenke
Anthony Quartararo
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P433issue24
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)3402-3415
P577publication date2018-04-17
P1433published inBiochemistryQ764876
P1476titleProperties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm
P478volume57

Reverse relations

Q57050099Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radicalcites workP2860