Skip to search formSkip to main contentSkip to account menu

3,5-difluorotyrosine

Known as: Tyrosine, 3,5-difluoro, difluorotyrosine 
National Institutes of Health

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2017
2017
Redox-active tyrosines (Ys) play essential roles in enzymes involved in primary metabolism including energy transduction and… 
2017
2017
Escherichia coli class Ia ribonucleotide reductase (RNR) is composed of two subunits that form an active α2β2 complex. The… 
2016
2016
Escherichia coli class Ia ribonucleotide reductase (RNR) converts ribonucleotides to deoxynucleotides. A diferric-tyrosyl radical… 
2016
2016
Ribonucleotide reductase (RNR) catalyzes the reduction of nucleotides to 2'deoxynucleotides, providing the monomeric precursors… 
2015
2015
Background: Peripheral membrane proteins can interact with zwitterionic phospholipid headgroups or lipid tails. Results… 
2014
2014
Among many of biophysical methods, F NMR spectroscopy has emerged as a powerful tool for characterizing protein structure… 
2013
2013
The reversible Y-O•/Y-OH redox properties of the α3Y model protein allow access to the electrochemical and thermodynamic… 
2013
2013
Tyrosine phosphorylation is a pivotal post-translational modification (PTM) which regulates enzymatic activity, protein… 
2008
2008
Fully protected 3,5-difluorotyrosine (F2Y), Fmoc-F2Y(tBu)-OH, is efficiently prepared by a chemoenzymatic process and…