Bacterial infections and immunology

• Structure-function characterization of the conserved regulatory mechanism of the Escherichia coli M48-metalloprotease BepA

  Bryant, Jack A., Cadby, Ian T., Chong, Zhi-Soon, Boelter, Gabriela, Sevastsyanovich, Yanina R., Morris, Faye C., Cunningham, Adam F., Kritikos, George, Meek, Richard W., Banzhaf, Manuel, Chng, Shu-Sin, Lovering, Andrew L. and Henderson, Ian R. (2021). Structure-function characterization of the conserved regulatory mechanism of the Escherichia coli M48-metalloprotease BepA. Journal of Bacteriology, 203 (2) e00434-20, e00434-20. doi: 10.1128/jb.00434-20

• Structure of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localization

  Bryant, Jack Alfred, Morris, Faye C., Knowles, Timothy J., Maderbocus, Riyaz, Heinz, Eva, Boelter, Gabriela, Alodaini, Dema, Colyer, Adam, Wotherspoon, Peter J., Staunton, Kara A., Jeeves, Mark, Browning, Douglas F., Sevastsyanovich, Yanina R., Wells, Timothy J., Rossiter, Amanda E., Bavro, Vassiliy N., Sridhar, Pooja, Ward, Douglas G., Chong, Zhi-Soon, Goodall, Emily C. A., Icke, Christopher, Teo, Alvin, Chng, Shu-Sin, Roper, David I., Lithgow, Trevor, Cunningham, Adam F., Banzhaf, Manuel, Overduin, Michael and Henderson, Ian R. (2020). Structure of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localization. eLife, 9. doi: 10.7554/elife.62614

• Mice deficient in T-bet form inducible NO synthase-positive granulomas that fail to constrain Salmonella

  Perez-Toledo, Marisol, Beristain-Covarrubias, Nonantzin, Channell, William M., Hitchcock, Jessica R., Cook, Charlotte N., Coughlan, Ruth E., Bobat, Saeeda, Jones, Nicholas D., Nakamura, Kyoko, Ross, Ewan A., Rossiter, Amanda E., Rooke, Jessica, Garcia-Gimenez, Alicia, Jossi, Sian, Persaud, Ruby R., Marcial-Juarez, Edith, Flores-Langarica, Adriana, Henderson, Ian R., Withers, David R., Watson, Steve P. and Cunningham, Adam F. (2020). Mice deficient in T-bet form inducible NO synthase-positive granulomas that fail to constrain Salmonella. Journal of Immunology, 205 (3), 708-719. doi: 10.4049/jimmunol.2000089

• ASY1 acts as a dosage-dependent antagonist of telomere-led recombination and mediates crossover interference in Arabidopsis

  Lambing, Christophe, Kuo, Pallas C., Tock, Andrew J., Topp, Stephanie D. and Henderson, Ian R. (2020). ASY1 acts as a dosage-dependent antagonist of telomere-led recombination and mediates crossover interference in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America, 117 (24), 13647-13658. doi: 10.1073/pnas.1921055117

View all publications