Publications List
This is not a comprehensive list and only includes publications published in 2017 or later.
2023
Hoang, K. N. L., & Murphy, C. J. (2023). Adsorption and Molecular Display of a Redox-Active Protein on Gold Nanoparticle Surfaces. Langmuir. 39 (45), 15974-15985. DOI: 10.1021/acs.langmuir.3c01983
McClain, S. M., Milchberg, M. H., Rienstra, C. M., & Murphy, C. J. (2023). Biologically Representative Lipid-Coated Gold Nanoparticles and Phospholipid Vesicles for the Study of Alpha-Synuclein/Membrane Interactions. ACS nano.17, 20, 20387–20401. DOI: 10.1021/acsnano.3c0660
Tondini, S. M., Mackie, R. I., & McCann, J. C. (2023). Polyclonal antibodies inhibit growth of key cellulolytic rumen bacterial species. Frontiers in Microbiology, 14, 1196492.
Volkening, J. D., Spatz, S. J., Ponnuraj, N., Akbar, H., Arrington, J. V., Vega-Rodriguez, W., & Jarosinski, K. W. (2023). Viral proteogenomic and expression profiling during productive replication of a skin-tropic herpesvirus in the natural host. PLOS Pathogens, 19(6), e1011204. doi:10.1371/journal.ppat.1011204
Steiert, B., Icardi, C. M., Faris, R., McCaslin, P. N., Smith, P., Klingelhutz, A. J., Yau, P. M., & Weber, M. M. (2023). The Chlamydia trachomatis type III-secreted effector protein CteG induces centrosome amplification through interactions with centrin-2. Proceedings of the National Academy of Sciences of the United States of America, 120(20), e2303487120. doi:10.1073/pnas.2303487120
Ponnuraj, N., Akbar, H., Arrington, J. V., Spatz, S. J., Nagarajan, B., Desai, U. R., & Jarosinski, K. W. (2023). The alphaherpesvirus conserved pUS10 is important for natural infection and its expression is regulated by the conserved Herpesviridae protein kinase (CHPK). PLOS Pathogens, 19(2), e1010959. doi:10.1371/journal.ppat.1010959
2022
Ma, Q., Beal, J. R., Bhurke, A., & Bagchi, M. K. (2022). Extracellular vesicles secreted by human uterine stromal cells regulate decidualization, angiogenesis, and trophoblast differentiation. Proceedings of the National Academy of Sciences of the United States of America, 119(38), e2200252119. doi:10.1073/pnas.2200252119
Ayikpoe, R. S., Shi, C., Battiste, A. J., Eslami, S. M., Ramesh, S., Simon, M. A., … Zhao, H. (2022). A scalable platform to discover antimicrobials of ribosomal origin. Nature Communications, 13(1), 6135. doi:10.1038/s41467-022-33890-w
Hoang, K. N. L., Wheeler, K. E., & Murphy, C. J. (2022). Isolation methods influence the protein corona composition on gold-coated iron oxide nanoparticles. Analytical Chemistry, 94(11), 4737–4746. doi:10.1021/acs.analchem.1c05243
Nardi, J., Miller, L. A., Robertson, H. M., & Yau, P. M. (2022). Segmental pairs of dermal secretory cells release proteins into the hemolymph at the larval-pupal molt. Developmental Biology, 483, 107–111. doi:10.1016/j.ydbio.2022.01.003
Oh, S.-H., Martin-Yken, H., Coleman, D. A., Dague, E., & Hoyer, L. L. (2022). Development and use of a monoclonal antibody specific for the Candida albicans cell-surface protein Hwp1. Frontiers in Cellular and Infection Microbiology, 12, 907453. doi:10.3389/fcimb.2022.907453
Yu, Y., & van der Donk, W. A. (2022). Biosynthesis of 3-thia-α-amino acids on a carrier peptide. Proceedings of the National Academy of Sciences of the United States of America, 119(29), e2205285119. doi:10.1073/pnas.2205285119
2021
Capistrano da Silva, E., Arrington, J., Yau, P. M., Smith-Fleming, K. M., Canisso, I. F., & Martins, B. da C. (2021). Proteome composition of bovine amniotic membrane and its potential role in corneal healing. Investigative Ophthalmology & Visual Science, 62(2), 11. doi:10.1167/iovs.62.2.11
Hu, Z., Ma, J., Chen, Y., Tong, W., Zhu, L., Wang, H., & Cronan, J. E. (2021). Escherichia coli FabG 3-ketoacyl-ACP reductase proteins lacking the assigned catalytic triad residues are active enzymes. The Journal of Biological Chemistry, 296(100365), 100365. doi:10.1016/j.jbc.2021.100365
Khatiwada, S., Delhon, G., Chaulagain, S., & Rock, D. L. (2021). The novel ORFV protein ORFV113 activates LPA-p38 signaling. PLoS Pathogens, 17(10), e1009971. doi:10.1371/journal.ppat.1009971
Liu, A., Si, Y., Dong, S.-H., Mahanta, N., Penkala, H. N., Nair, S. K., & Mitchell, D. A. (2021). Functional elucidation of TfuA in peptide backbone thioamidation. Nature Chemical Biology, 17(5), 585–592. doi:10.1038/s41589-021-00771-0
Murali, R., Pace, L. A., Sanford, R. A., Ward, L. M., Lynes, M., Hatzenpichler, R., … Hemp, J. (2021). Diversity and evolution of nitric oxide reduction. doi:10.1101/2021.10.15.464467
Turner, J. G., & Murphy, C. J. (2021). How do proteins associate with nanoscale metal-organic framework surfaces? Langmuir: The ACS Journal of Surfaces and Colloids, 37(32), 9910–9919. doi:10.1021/acs.langmuir.1c01664
2020
Barclay, R. D., Beals, J. W., Drnevich, J., Imai, B. S., Yau, P. M., Ulanov, A. V., … Mackenzie, R. W. (2020). Ingestion of lean meat elevates muscle inositol hexakisphosphate kinase 1 protein content independent of a distinct post-prandial circulating proteome in young adults with obesity. Metabolism: Clinical and Experimental, 102(153996), 153996. doi:10.1016/j.metabol.2019.153996
D’Alessandro-Gabazza, C. N., Kobayashi, T., Yasuma, T., Toda, M., Kim, H., Fujimoto, H., … Gabazza, E. C. (2020). A Staphylococcus pro-apoptotic peptide induces acute exacerbation of pulmonary fibrosis. Nature Communications, 11(1), 1539. doi:10.1038/s41467-020-15344-3
Hu, Y., & Cronan, J. E. (2020). α-proteobacteria synthesize biotin precursor pimeloyl-ACP using BioZ 3-ketoacyl-ACP synthase and lysine catabolism. Nature Communications, 11(1), 5598. doi:10.1038/s41467-020-19251-5
Kenny, P. J., Kim, M., Skariah, G., Nielsen, J., Lannom, M. C., & Ceman, S. (2020). The FMRP-MOV10 complex: a translational regulatory switch modulated by G-Quadruplexes. Nucleic Acids Research, 48(2), 862–878. doi:10.1093/nar/gkz1092
Mast, D. H., Checco, J. W., & Sweedler, J. V. (2020). Differential post-translational Amino acid isomerization found among neuropeptides in Aplysia californica. ACS Chemical Biology, 15(1), 272–281. doi:10.1021/acschembio.9b00910
McClain, S. M., Ojoawo, A. M., Lin, W., Rienstra, C. M., & Murphy, C. J. (2020). Interaction of alpha-synuclein and its mutants with rigid lipid vesicle mimics of varying surface curvature. ACS Nano, 14(8), 10153–10167. doi:10.1021/acsnano.0c03420
Rahman, I. R., Acedo, J. Z., Liu, X. R., Zhu, L., Arrington, J., Gross, M. L., & van der Donk, W. A. (2020). Substrate recognition by the class II lanthipeptide synthetase HalM2. ACS Chemical Biology, 15(6), 1473–1486. doi:10.1021/acschembio.0c00127
Srivastava, I., Khan, M. S., Dighe, K., Alafeef, M., Wang, Z., Banerjee, T., … Pan, D. (2020). On‐chip electrical monitoring of real‐time “soft” and “hard” protein corona formation on carbon nanoparticles. Small Methods, 4(7), 2000099. doi:10.1002/smtd.202000099
2019
Dong, Y., Sanford, R. A., Inskeep, W. P., Srivastava, V., Bulone, V., Fields, C. J., … Fouke, B. W. (2019). Physiology, metabolism, and fossilization of hot-spring filamentous microbial mats. Astrobiology, 19(12), 1442–1458. doi:10.1089/ast.2018.1965
Fu, H., Goettge, M. N., & Metcalf, W. W. (2019). Biochemical Characterization of the Methylmercaptopropionate:Cob(I)alamin Methyltransferase from Methanosarcina acetivorans. Journal of Bacteriology, 201(12). doi:10.1128/JB.00130-19
McCoy, A. M., Arrington, J., & Yau, P. M. (2019). Effect of preparation method on the protein profile of equine amnion dressings. Journal of Proteome Research, 18(6), 2676–2685. doi:10.1021/acs.jproteome.9b00240
Nayak, D. D., Liu, A., Agrawal, N., Rodriguez-Carerro, R., Dong, S.-H., Mitchell, D. A., … Metcalf, W. W. (2020). Functional interactions between posttranslationally modified amino acids of methyl-coenzyme M reductase in Methanosarcina acetivorans. PLoS Biology, 18(2), e3000507. doi:10.1371/journal.pbio.3000507
Susanti, D., Frazier, M. C., & Mukhopadhyay, B. (2019). A genetic system for Methanocaldococcus jannaschii: An evolutionary deeply rooted hyperthermophilic methanarchaeon. Frontiers in Microbiology, 10, 1256. doi:10.3389/fmicb.2019.01256
2018
Anapindi, K. D. B., Romanova, E. V., Southey, B. R., & Sweedler, J. V. (2018). Peptide identifications and false discovery rates using different mass spectrometry platforms. Talanta, 182, 456–463. doi:10.1016/j.talanta.2018.01.062
Checco, J. W., Zhang, G., Yuan, W.-D., Yu, K., Yin, S.-Y., Roberts-Galbraith, R. H., … Sweedler, J. V. (2018). Molecular and physiological characterization of a receptor for d-amino acid-containing neuropeptides. ACS Chemical Biology, 13(5), 1343–1352. doi:10.1021/acschembio.8b00167
Davis, R. G., Park, H.-M., Kim, K., Greer, J. B., Fellers, R. T., LeDuc, R. D., … Kelleher, N. L. (2018). Top-down proteomics enables comparative analysis of brain proteoforms between mouse strains. Analytical Chemistry, 90(6), 3802–3810. doi:10.1021/acs.analchem.7b04108
Grenz, J. R., Cott Chubiz, J. E., Thaprawat, P., & Slauch, J. M. (2018). HilE regulates HilD by blocking DNA binding in Salmonella enterica serovar typhimurium. Journal of Bacteriology, 200(8). doi:10.1128/JB.00750-17
Negreiros, R. S., Lander, N., Huang, G., Cordeiro, C. D., Smith, S. A., Morrissey, J. H., & Docampo, R. (2018). Inorganic polyphosphate interacts with nucleolar and glycosomal proteins in trypanosomatids. Molecular Microbiology, 110(6), 973–994. doi:10.1111/mmi.14131
Ren, H., Biswas, S., Ho, S., van der Donk, W. A., & Zhao, H. (2018). Rapid Discovery of Glycocins through Pathway Refactoring in Escherichia coli. ACS Chemical Biology, 13(10), 2966–2972. doi:10.1021/acschembio.8b00599
Sivaguru, M., Saw, J. J., Williams, J. C., Jr, Lieske, J. C., Krambeck, A. E., Romero, M. F., … Fouke, B. W. (2018). Geobiology reveals how human kidney stones dissolve in vivo. Scientific Reports, 8(1), 13731. doi:10.1038/s41598-018-31890-9
2017
Cao, X., Zhu, L., Hu, Z., & Cronan, J. E. (2017). Expression and activity of the BioH esterase of biotin synthesis is independent of genome context. Scientific Reports, 7(1), 2141. doi:10.1038/s41598-017-01490-0
Nayak, D. D., Mahanta, N., Mitchell, D. A., & Metcalf, W. W. (2017). Post-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in methanogenic and methanotrophic Archaea. ELife, 6. doi:10.7554/eLife.29218
Ortiz-Martinez, M., Gonzalez de Mejia, E., García-Lara, S., Aguilar, O., Lopez-Castillo, L. M., & Otero-Pappatheodorou, J. T. (2017). Antiproliferative effect of peptide fractions isolated from a quality protein maize, a white hybrid maize, and their derived peptides on hepatocarcinoma human HepG2 cells. Journal of Functional Foods, 34, 36–48. doi:10.1016/j.jff.2017.04.015
Roy, J., Wycislo, K. L., Pondenis, H., Fan, T. M., & Das, A. (2017). Comparative proteomic investigation of metastatic and non-metastatic osteosarcoma cells of human and canine origin. PloS One, 12(9), e0183930. doi:10.1371/journal.pone.0183930
Silva, E., Frost, D., Li, L., Bovin, N., & Miller, D. J. (2017). Lactadherin is a candidate oviduct Lewis X trisaccharide receptor on porcine spermatozoa. Andrology, 5(3), 589–597. doi:10.1111/andr.12340