de Oliveira Silva, Y.R.*, Zheng, D.*, Peters, S.C., Fisher, O.S. Stabilization of a Cu-binding site by a highly conserved tryptophan residue. 2024. J Inorg Biochem. doi: 10.1016/j.jinorgbio.2024.112501.
Guo, J. and Fisher, O.S. Orchestrating copper binding: structure and variations on the cupredoxin fold. 2022. J Biol Inorg Chem. doi: 10.1007/s00775-022-01955-2.
Damle, M.S., Singh, A.N., Peters, S.C., Szalai, V.A., Fisher, O.S. The YcnI protein from Bacillis subtilis contains a copper-binding domain. 2021. J Biol Chem. Sep;297(3):101078. doi: 10.1016/j.jbc.2021.101078.
Fisher, O.S.*, Li, X.*, Liu, W.*, Zhang, R.*, Boggon, T.J. Crystallographic studies of the cerebral cavernous malformations proteins. 2020. Methods Mol Biol. 2152, 291-302. doi: 10.1007/978-1-0716-0640-7_21
2016 – 2019
Fisher, O.S., Sendzik, M.R., Ross, M.O., Lawton, T.J., Hoffman, B.M., Rosenzweig, A.C. PCuAC domains from methane-oxidizing bacteria use a histidine brace to bind copper. 2019. J Biol Chem. Nov 1;294(44):16351-16363. doi: 10.1074/jbc.RA119.010093.
Miller, C.J., Lou, H.J., Simpson, C., van de Kooij, B., Ha, B.H., Fisher, O.S., Pirman, N.L., Boggon, T.J., Rinehart, J., Yaffe, M.B., Linding, R., Turk, B.E. Comprehensive profiling of the STE20 kinase family defines features essential for selective substrate targeting and signaling output. 2019. PLoS Biol. 17, e2006540. DOI: 10.1371/journal.pbio.2006540
Ross, M.O.*, Fisher, O.S.*, Morgada, M.N., Krzyaniak,M.D., Wasielewski, M., Vila, A.J., Hoffman, B.M., Rosenzweig, A.C. Formation and electronic structure of an atypical CuA site. 2019. J Am Chem Soc. 141, 4678-4686. DOI: 10.1021/jacs.8b13610
Fisher, O.S., Kenney, G.E., Ross, M.O., Ro, S.Y., Lemma, B.E., Batelu, S., Thomas, P.M., Sosnowski, V.C., DeHart, C.J., Kelleher, N.L., Stemmler, T.L., Hoffman, B.M., Rosenzweig, A.C. Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria. 2018. Nat Commun. 9, 4276. DOI: 10.1038/s41467-018-06681-5
Wang, W., Nguyen, L.T.T., Burlak, C., Chegini, F., Guo, F., Chataway, T., Ju, S., Fisher, O.S., Miller, D.W., Datta, D., Wu, F., Wu, C., Landeru, A., Wells, J.A., Cookson, M.R., Boxer, M.B., Thomas, C.J., Gai, W., Ringe, D., Petsko, G.A., Hoang, Q.Q. Caspase-1 causes truncation and aggregation of the Parkinson disease-associated protein α-synuclein. 2016. Proc Natl Acad Sci U S A. 113(34), 9587-92. DOI: 10.1073/pnas.1610099113
2015 and earlier
Li, X., Fisher, O.S., Boggon, T.J. The cerebral cavernous malformations proteins. 2015. Oncotarget. 6, 32279-32280. DOI: 10.18632/oncotarget.5443
Fisher, O. S.*, Deng, H.*, Liu, D.*, Zhang, Y., Wei, R., Deng, Y. Zhang, F., Louvi, A., Turk, B.E., Boggon, T.J.*, Su, B.*. Structure and vascular function of MEKK3-cerebral cavernous malformations complex. 2015. Nat Commun. 6, 7937. DOI: 10.1038/ncomms8937
Draheim, K.M.*, Li, X.*, Zhang, R., Fisher, O.S., Villari, G., Calderwood, D.A., Boggon, T.J. Structural determinants of a CCM3:CCM2 interaction that stabilizes protein expression and permits endothelial network formation. 2015. J Cell Biol. 208, 987-1001. DOI: 10.1083/jcb.201407129
Fisher, O.S., Liu, W., Zhang, R., Stiegler, A.L., Ghedia, S., Weber, J.L., Boggon, T.J. Structural basis for the disruption of the Cerebral Cavernous Malformations 2 (CCM2) interaction with Krev Interaction Trapped 1 (KRIT1) by disease-associated mutations. 2015. J Biol Chem. 290, 2842-53. DOI: 10.1074/jbc.M114.616433
Fisher, O.S. and Boggon, T.J. Signaling pathways and the cerebral cavernous malformations proteins: lessons from structural biology. 2014. Cell Mol Life Sci 71, 1881-1892. DOI: 10.1242/jcs.138388
Draheim, K.M., Fisher, O.S., Boggon, T.J., and Calderwood, D.A. Cerebral cavernous malformation proteins at a glance. 2014. J Cell Sci 127, 701-707. DOI: 10.1007/s00018-013-1532-9
Fisher, O.S., Zhang, R., Li, X., Murphy, J.W., Demeler, B., and Boggon, T.J. Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. 2013. FEBS Lett 587, 272-277. DOI: 10.1016/j.febslet.2012.12.011
