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Cell Research|June 3, 2017
The DUB blade goes snicker-snack: Novel ubiquitin cleavage by a Legionella effector proteinJudith A Ronau, Mark Hochstrasser
Cell Research|March 26, 2016
Substrate specificity of the ubiquitin and Ubl proteasesJudith A Ronau, John F Beckmann, Mark Hochstrasser
Nature Microbiology|March 2, 2017
A Wolbachia deubiquitylating enzyme induces cytoplasmic incompatibilityJohn F Beckmann, Judith A Ronau, Mark Hochstrasser
Proceedings of the National Academy of Sciences of the United States of America|October 17, 2019
A <i>Wolbachia</i> nuclease and its binding partner provide a distinct mechanism for cytoplasmic incompatibilityHongli Chen, Judith A Ronau, John F Beckmann, et al.
Acta Crystallographica. Section D, Biological Crystallography|January 1, 2013
Polarization-resolved second-harmonic generation microscopy as a method to visualize protein-crystal domainsEmma L DeWalt, Victoria J Begue, Judith A Ronau, et al.
Biochemistry|October 9, 2014
A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysisJudith A Ronau, Lake N Paul, Julian E Fuchs, et al.
Biochemistry|May 3, 2014
Insights into the mechanism of deubiquitination by JAMM deubiquitinases from cocrystal structures of the enzyme with the substrate and productRashmi K Shrestha, Judith A Ronau, Christopher W Davies, et al.
European Biophysics Journal : EBJ|June 8, 2011
Folding dynamics of phenylalanine hydroxylase depends on the enzyme's metallation state: the native metal, iron, protects against aggregate intermediatesAristobulo Loaiza, Judith A Ronau, Alexander Ribbe, et al.
Nature Communications|May 13, 2020
A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushiJason M Berk, Christopher Lim, Judith A Ronau, et al.
Biochemistry|September 15, 2015
Dynamics of an Active-Site Flap Contributes to Catalysis in a JAMM Family Metallo DeubiquitinaseAmy N Bueno, Rashmi K Shrestha, Judith A Ronau, et al.
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