The primary products of our academic research laboratory are publications in peer-reviewed academic journals.

Tax-payers shouldn’t face paywalls to read about research they funded. Should you encounter any difficulty accessing our publications please contact us and we will be happy to provide you a copy free of charge.

Publications

(† denotes authors contributed equally)

Zhou, B., Szymanski, C., Baylink, A. (2022) Bacterial Chemotaxis in Human Diseases. Trends in Microbiology (Accepted).

O’Neal, L.† and Perkins, A.† (2021). Rural exclusion from science and academia. Trends in Microbiology, 29(11) 953-956. doi: 10.1016/j.tim.2021.06.012

Perkins A., Tudorica, D. A., Teixeira, R. D., Schirmer, T., Zumwalt, L., Ogba, M. O., Cassidy, C. K., Stansfeld, P. J., Guillemin, K. (2021). A bacterial inflammation sensor regulates c-di-GMP signaling, adhesion, and biofilm formation. mBio, 12(3), e00173-21. doi: 10.1128/mBio.00173-21

Robinson C., Sweeney, E. G., Ngo J., Ma, E., Perkins, A., Smith, T. J., Fernandez, N. L., Waters C. M., Remington, S. J., Bohannan, B. J. M., Guillemin K. (2021). Host-emitted amino acid cues regulate bacterial chemokinesis to enhance host colonization. Cell Host & Microbe, 29(8), 1121-1213. doi: 10.1016/j.chom.2021.06.003

Zumwalt, L., Perkins, A., Ogba, O. M. (2020). Mechanism and Chemoselectivity for HOCl-mediated Oxidation of Zinc-Bound Thiolates. ChemPhysChem, 21, 1-5. doi: 10.1002/cphc.202000634

Wheeler, L. C.†, Perkins, A.†, Wong, C. E., Harms, M. J. (2020).  Learning peptide recognition rules for a low-specificity protein. Protein Science, 1-15. doi: 10.1002/pro3958

Perkins, A., Tudorica, D. A., Amieva, M. R., Remington, S. J., & Guillemin, K. (2019). Helicobacter pylori senses bleach (HOCl) as a chemoattractant using a cytosolic chemoreceptor. PLoS Biology, 17(8), e3000395. doi: 10.1371/journal.pbio.3000395

Sweeney, E. G.†, Perkins, A.†, Kallio, K., Remington, S. J., & Guillemin, K. (2018). Structures of the ligand‐binding domain of Helicobacter pylori chemoreceptor TlpA. Protein Science, 27(11), 1961-1968. doi: 10.1002/pro.3503

Rolig, A. S., Sweeney, E. G., Kaye, L. E., DeSantis, M. D., Perkins, A., Banse, A. V., Hamilton, M. K., & Guillemin, K. (2018). A bacterial immunomodulatory protein with lipocalin-like domains facilitates host–bacteria mutualism in larval zebrafish. eLIFE, 7, e37172. doi: 10.7554/eLife.37172

Nelson, K. J.†, Perkins, A.†, Van Swearingen, A. E., Hartman, S., Brereton, A. E., Parsonage, D., Karplus, P. A., & Poole, L. B. (2018). Experimentally dissecting the origins of peroxiredoxin catalysis. Antioxidants & Redox Signaling, 28(7), 521-536. doi: 10.1089/ars.2016.6922

Perkins, A., Parsonage, D., Nelson, K. J., Ogba, O. M., Cheong, P. H. Y., Poole, L. B., & Karplus, P. A. (2016). Peroxiredoxin catalysis at atomic resolution. Structure, 24(10), 1668-1678. doi: 10.1016/j.str.2016.07.012

Buchko, G. W., Perkins, A., Parsonage, D., Poole, L. B., & Karplus, P. A. (2016). Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: A dramatic change in backbone dynamics. Biomolecular NMR Assignments, 10(1), 57-61. doi: 10.1007/s12104-015-9637-8

Perkins, A., Nelson, K. J., Parsonage, D., Poole, L. B., & Karplus, P. A., & (2015). Peroxiredoxins: Guardians against oxidative stress and modulators of peroxide signaling. Trends in Biochemical Sciences, 40(8), 435-445. doi: 10.1016/j.tibs.2015.05.001

Perkins, A., Poole, L. B., & Karplus, P. A. (2014). Tuning of peroxiredoxin catalysis for various physiological roles. Biochemistry, 53(49), 7693-7705. doi: 10.1021/bi5013222

Perkins, A.†, Phillips, J.†, Kerkvliet, N., Tanguay, R., Perdew, G., Kolluri, S., & Bisson, W. (2014). A structural switch between agonist and antagonist bound conformations for a ligand-optimized model of the human aryl hydrocarbon receptor ligand binding domain. Biology, 3(4), 645-669. doi: 10.3390/biology3040645

Perkins, A., Nelson, K. J., Williams, J. R., Parsonage, D., Poole, L. B., & Karplus, P. A. (2013). The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin. Biochemistry, 52(48), 8708-8721. doi: 10.1021/bi4011573

Perkins, A., Gretes, M. C., Nelson, K. J., Poole, L. B., & Karplus, P. A. (2012). Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes. Biochemistry, 51(38), 7638-7650. doi: 10.1021/bi301017s