Direct photoaffinity labeling of ribonucleotide reductase from Escherichia coli using dTTP: characterization of the photoproducts
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00413a054
Reference39 articles.
1. Direct ATP photolabeling of Escherichia coli RecA proteins: identification of regions required for ATP binding
2. Nucleoside triphosphate binding to DNA polymerase III holoenzyme of Escherichia coli. A direct photoaffinity labeling study.
3. Ultraviolet absorption spectra of adenosine-5′-triphosphate and related 5′-ribonucleotides
4. Direct photoaffinity labeling of an allosteric site of subunit protein M1 of mouse ribonucleotide reductase by dATP. Evidence for two independent binding interactions within the allosteric specificity site.
5. Direct photoaffinity labeling of the catalytic site of mouse ribonucleotide reductase by CDP.
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1. ATP and Mg2+ Promote the Reversible Oligomerization and Aggregation of Chloroplast 2-Cys Peroxiredoxin;Journal of Biological Chemistry;2011-07
2. Photochemical Labeling: Can Photoaffinity Labeling be Differentiated from Site-Directed Photochemical Coupling?;Photochemistry and Photobiology;1997-02
3. The Cys292→Ala Substitution in Protein R1 of Class I Ribonucleotide Reductase from Escherichia Coli has a Global Effect on Nucleotide Binding at the Specificity-Determining Allosteric Site;European Journal of Biochemistry;1996-10
4. Recent Trends in Photoaffinity Labeling;Angewandte Chemie International Edition in English;1995-07-07
5. Neue Entwicklungen bei der Photoaffinitätsmarkierung;Angewandte Chemie;1995-06-20
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