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Molecular Microbiology|May 22, 2007
An acetylase with relaxed specificity catalyses protein N-terminal acetylation in Sulfolobus solfataricusDale T Mackay, Catherine H Botting, Garry L Taylor, et al.Nucleic Acids Research|December 17, 2009
PCNA and XPF cooperate to distort DNA substratesRichard D Hutton, Timothy D Craggs, Malcolm F White, et al.Nucleic Acids Research|October 25, 2008
PCNA stimulates catalysis by structure-specific nucleases using two distinct mechanisms: substrate targeting and catalytic stepRichard D Hutton, Jennifer A Roberts, J Carlos Penedo, et al.Critical Reviews in Biochemistry and Molecular Biology|November 28, 2008
The major architects of chromatin: architectural proteins in bacteria, archaea and eukaryotesMartijn S Luijsterburg, Malcolm F White, Roel van Driel, et al.Elife|July 3, 2018
Control of cyclic oligoadenylate synthesis in a type III CRISPR systemChristophe Rouillon, Januka S Athukoralage, Shirley Graham, et al.Journal of Molecular Biology|January 8, 2008
The archaeal XPB protein is a ssDNA-dependent ATPase with a novel partnerJodi D Richards, Liza Cubeddu, Jennifer Roberts, et al.Methods in Enzymology|January 30, 2019
Investigation of the cyclic oligoadenylate signaling pathway of type III CRISPR systemsChristophe Rouillon, Januka S Athukoralage, Shirley Graham, et al.Nucleic Acids Research|March 22, 2020
Regulation of the RNA and DNA nuclease activities required for Pyrococcus furiosus Type III-B CRISPR-Cas immunityKawanda Foster, Sabine Grüschow, Scott Bailey, et al.Nature|September 21, 2018
Ring nucleases deactivate type III CRISPR ribonucleases by degrading cyclic oligoadenylateJanuka S Athukoralage, Christophe Rouillon, Shirley Graham, et al.Proceedings of the National Academy of Sciences of the United States of America|June 13, 2018
An archaeal primase functions as a nanoscale caliper to define primer lengthJiangyu Yan, Sandro Holzer, Luca Pellegrini, et al.Pageof 23