{"id":58,"date":"2019-03-27T18:42:57","date_gmt":"2019-03-27T18:42:57","guid":{"rendered":"https:\/\/navarrelab.ca\/?page_id=58"},"modified":"2025-01-30T22:06:11","modified_gmt":"2025-01-30T22:06:11","slug":"publications","status":"publish","type":"page","link":"https:\/\/navarrelab.ca\/?page_id=58","title":{"rendered":"Publications"},"content":{"rendered":"\n<p>Serrador, D., Campbell, J.R., Cheung, D., Shefraw, G., Kaul, R., and <strong>W.W. Navarre.<\/strong> (2025) <a href=\"https:\/\/www.biorxiv.org\/content\/10.1101\/2024.09.13.612917v2.full\"><strong>Practical media formulations for rapid growth of<em> Lactobacillus iners<\/em> and other vaginal bacteri<\/strong>a.<\/a> <em>BioRxiv<\/em> (https:\/\/doi.org\/10.1101\/2024.09.13.612917)<\/p>\n\n\n\n<p>Thakur, B.K., Malaise, Y., Choudhury, S.R., Wong, E.O-Y, Streutker, C., <strong>Navarre, W.W.<\/strong>, Jobin, C., and A. Martin. (2025) <strong>Dietary deficiency in soluble fiber and host genetics dictate the oncogenic potential of <em>pks+ E. coli<\/em> in colon carcinogenesis.<\/strong>\u00a0 <em>Nature Microbiology <\/em>(in press)<\/p>\n\n\n\n<p>Wong, A., Cordova, M., and <strong>W.W. Navarre<\/strong>. (2024) <a href=\"https:\/\/journals.asm.org\/doi\/10.1128\/mbio.02089-24\"><strong>Evolutionary and functional divergence of Sfx, a plasmid-encoded H-NS homolog, underlies the regulation of IncX plasmid conjugation. <\/strong><\/a><em>mBio<\/em> e0208924.\u00a0doi: 10.1128\/mbio.02089-24. <\/p>\n\n\n\n<p>Liu J, Malekoltojari A, Asokakumar A, Chow V, Li L, Li H, Grimaldi M, Dang N, Campbell J, Barrett H, Sun J,\u00a0<strong>Navarre W<\/strong>, Wilson D, Wang H, Mani S, Balaguer P, Anakk S, Peng H, and HM, Krause. (2024) <strong><a href=\"https:\/\/www.nature.com\/articles\/s41467-024-46559-3\">Diindoles produced from commensal microbiota metabolites function as endogenous CAR\/Nr1i3 ligands.<\/a><\/strong>\u00a0 <em>Nat Commun<\/em>. <strong>15<\/strong>(1):2563. doi: 10.1038\/s41467-024-46559-3.<\/p>\n\n\n\n<p>Afrizal A.,Jennings, S.A.V., Hitch, T.C.A., Riedel, T., de Oliveira, R., Basic, M., Panyot, A., Treichel, N., Hager, F.T., Br\u00fcck, R., Wong, E.O-Y., von Strempel, A. Eberl, C., Buhl, E.M., Abt, B., <strong>Navarre, W.W.<\/strong>, Tolba, R., Kiessling, F., Horz, H-P., Torow, N., Cerovic, V., Stecher, B., Strowig, T., Overmann, J., and T. Clavel. (2022) <strong><a href=\"https:\/\/doi.org\/10.1016\/j.chom.2022.09.011\">Enhanced cultured diversity of the mouse gut microbiota enables custom-made synthetic communities.<\/a><\/strong>\u00a0 <em>Cell Host Microbe, <\/em><strong>30<\/strong>(11):1630-1645.e25. doi: 10.1016\/j.chom.2022.09.011<em>.<\/em><\/p>\n\n\n\n<p>Brownlie, E.J.E., Chaharlangi, D., Wong, E.O-Y., Kim, D., and <strong>W.W. Navarre<\/strong>. (2022)<strong><a href=\"https:\/\/www.tandfonline.com\/doi\/full\/10.1080\/19490976.2022.2046452\"> Acids Produced by Lactobacilli Inhibit the Growth of Commensal Lachnospiraceae and S24-7 Bacteria.<\/a><\/strong> <em>Gut Microbes<\/em> <strong>14<\/strong>(1):2046452.<br>https:\/\/doi.org\/10.1080\/19490976.2022.2046452<\/p>\n\n\n\n<p>Wong, E.O-Y., Brownlie, E.J.E., Ng, K.M., Kathirgamanathan, S., Yu, F.B., Merril, B.D., Hwang, K.C., Martin, A., Tropini, C., and <strong>W.W. Navarre<\/strong>. (2022) <strong><a href=\"https:\/\/doi.org\/10.1128\/mbio.02949-21\">The CIAMIB: a large and metabolically diverse collection of inflammation-associated bacteria from the murine gut.<\/a><\/strong> <em>mBio<\/em> e0294921. doi: 10.1128\/mbio.02949-21.<\/p>\n\n\n\n<p>Hezaveh, K., Shinde, R., Kloetgen, A, Halaby, M.J., Lamorte, S., Ciudad, M.T., Quevedo, R., Neufeld, L., Liu, K., Jin, R., Gruenwald, B., Foerster, E.G., Chaharlangi, D., Guo, M., Makhijani, P., Zhang, X., Pugh, T.J., Pinto, D.M., Co, I., McGuigan, A., Jang, G.H., Khoka, R., Ohashi, P.S., O\u2019Kane, G., Gallinger, S., <strong>Navarre, W.W.<\/strong>, Maughan, H., Philpott, D., Brooks, D.G., and T.L. McGaha. (2022)<strong><a href=\"http:\/\/10.1016\/j.immuni.2022.01.006\"> Tryptophan-derived microbial metabolites activate the aryl hydrocarbon receptor in tumor-associated macrophages to suppress anti-tumor immunity.<\/a><\/strong> <em>Immunity<\/em> <strong>55<\/strong>(2):324-340. doi: 10.1016\/j.immuni.2022.01.006.<\/p>\n\n\n\n<p>Duan, B., Ding, P., <strong>Navarre, W.W<\/strong>., Liu, J., and B. Xia. (2021) Xenogeneic Silencing and Bacterial Genome Evolution: Mechanisms for DNA Recognition Imply Multifaceted Roles of Xenogeneic Silencers.<em> Molecular Biology and Evolution<\/em>. <strong>38<\/strong>(10):4135-4148. doi: 10.1093\/molbev\/msab136.<\/p>\n\n\n\n<p>Hersch, S.J., Radan, B., Ilyas, B., Lavoie, P. and <strong>W.W. Navarre.<\/strong> (2021) A stress-induced block in dicarboxylate uptake and utilization in Salmonella. <em>Journal of Bacteriology<\/em>. <strong>203<\/strong>(9):e00487-20. doi: 10.1128\/JB.00487-20.<\/p>\n\n\n\n<p>Hersch, S.J. and <strong>W.W. Navarre.<\/strong> (2020) <em>Salmonella<\/em> employs ItaR to respond to itaconate in mouse and interferon-activated human macrophage. Infection and Immunity. <strong>88<\/strong>(10):e00303-20. doi: 10.1128\/IAI.00303-20.<\/p>\n\n\n\n<p>Fields, F., Li, X., <strong>Navarre, W.W.<\/strong>, and M. Naito. (2020) Complete genome sequence of Streptococcus salivarius DB-B5, a novel probiotic candidate isolated from the supragingival plaque of a healthy female. Microbiol Resources Announcements. 9(40):e00916-20. doi: 10.1128\/MRA.00916-20.<\/p>\n\n\n\n<p>Irrazabal, T., Kang, M., Kumar Thakur, B., Streutker, C., Wong, E.O-Y, Copeland, J., Guttman, D.S., <strong>Navarre, W.W.<\/strong>, and A. Martin. (2020) Limiting Oxidative DNA Damage Reduces Microbe-Induced Colitis Associated Colorectal Cancer. Nature Communications, 11(1):1802. doi: 10.1038\/s41467-020-15549-6.<\/p>\n\n\n\n<p>Saha, S., Martin, A., and <strong>W.W. Navarre<\/strong>. (2019) Meta-analysis Identifies Microbial Signatures of Disease in Murine Models of Inflammatory Bowel Disease. BioRxiv (doi: https:\/\/doi.org\/10.1101\/515205)<\/p>\n\n\n\n<p>Li, C., Lam, E., Perez-Shibayama, C., Ward, L.A., Zhang, J., Lee, D., Nguyen, A., Ahmed, M., Brownlie, E., Korneev, K.V., Rojas, O., Sun, T., <strong>Navarre, W.W.,<\/strong> He, H.H., Liao, S., Martin, A., Ludewig, B., and J.L. Gommerman. (2019) Early-life Programming of Mesenteric Lymph Node Stromal Cell Identity by the Lymphotoxin Pathway Regulates Adult Mucosal Immunity. Science Immunology. 4(42):eaax1027.<\/p>\n\n\n\n<p>Rafiei, N., Cordova, M.,&nbsp;<strong>Navarre, W.W.<\/strong>, and Milstein, J. (2019) Growth phase dependent chromosome condensation and H-NS protein redistribution in&nbsp;<em>E. coli<\/em>&nbsp;under osmotic stress. (submitted &#8211; preprint on BioRxiv)&nbsp;<a href=\"https:\/\/www.biorxiv.org\/content\/10.1101\/559138v1\">https:\/\/www.biorxiv.org\/content\/10.1101\/559138v1<\/a><\/p>\n\n\n\n<p>Riccardi, E., van Mastbergen, E.C.,&nbsp;<strong>Navarre, W.W.<\/strong>&nbsp;and J. Vreede. (2019) <a href=\"https:\/\/journals.plos.org\/ploscompbiol\/article?id=10.1371\/journal.pcbi.1006845\">Predicting the mechanism and rate of H-NS binding to AT-rich DNA.<\/a> &nbsp;<em>PLoS Computational Biology<\/em>&nbsp;15(3):e1006845. doi: 10.1371\/journal.pcbi.1006845.<\/p>\n\n\n\n<p>Will, W.R, Brzovic, P, Le Trong, I., Stenkamp, R., Lawrenz, M.B., Karlinsey, J.D.,&nbsp;<strong>Navarre, W.W.<\/strong>, Main-Hester, K., Miller, V.L., Libby, S., and F.C. Fang (2019) <a href=\"https:\/\/mbio.asm.org\/content\/10\/2\/e00009-19.long\">The Evolution of SlyA\/RovA Transcription Factors From Repressors to Counter-Silencers in Enterobacteriaceae.<\/a> &nbsp;<em>mBio<\/em>&nbsp;10(2). pii: e00009-19. doi: 10.1128\/mBio.00009-19.<\/p>\n\n\n\n<p>Duan, B., Ding, P., Hughes, T.R.,&nbsp;<strong>Navarre, W.W.<\/strong>, Liu, J., and B. Xia. (2018) <a href=\"https:\/\/academic.oup.com\/nar\/article\/46\/19\/10514\/5106470\">How bacterial xenogeneic silencer Rok distinguishes foreign from self-DNA in its resident genome.<\/a>&nbsp;<em>Nucleic Acids Res.<\/em>&nbsp;46(19):10514-10529.<\/p>\n\n\n\n<p><strong>Navarre WW. <\/strong>(2016) <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S006529111630025X?via%3Dihub\">The impact of gene silencing on horizontal gene transfer and bacterial evolution. <\/a><em><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S006529111630025X?via%3Dihub\">Adv Microb Physiol<\/a><\/em><a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S006529111630025X?via%3Dihub\">. 69:157-186.<\/a> doi:<br> 10.1016\/bs.ampbs.2016.07.004.<\/p>\n\n\n\n<p>Singh K, Milstein JN, and <strong>W.W. Navarre<\/strong> (2016) <a href=\"https:\/\/www.annualreviews.org\/doi\/abs\/10.1146\/annurev-micro-102215-095301?rfr_dat=cr_pub%3Dpubmed&amp;url_ver=Z39.88-2003&amp;rfr_id=ori%3Arid%3Acrossref.org&amp;journalCode=micro\">Xenogeneic silencing and its impact on bacterial genomes.<\/a> <em>Annu Rev Microbiol<\/em>. 70:199-213.<\/p>\n\n\n\n<p>Ding, P., McFarland, K.A., Jin, S., Tong, G., Duan, B., Yang, A., Hughes, T.R., Liu, J., Dove, S.L.,&nbsp;<strong>Navarre, W.W<\/strong>., and B. Xia (2015) <a href=\"https:\/\/journals.plos.org\/plospathogens\/article?id=10.1371\/journal.ppat.1004967\">A Novel AT-Rich DNA Recognition Mechanism for Bacterial Xenogeneic Silencer MvaT.<\/a>&nbsp;<em>PLoS Pathogens.<\/em>11(6):e1004967.&nbsp;<\/p>\n\n\n\n<p>Rajkovic, A., Erickson, S., Witzky, A., Branson, O.E., Seo, J., Gafken, P.R., Frietas, M.A., Whitelegge, J.P., Faull, K.F.,&nbsp;<strong>Navarre, W.<\/strong>, Darwin, A.J., and M. Ibba (2015) <a href=\"https:\/\/mbio.asm.org\/content\/6\/3\/e00823-15.long\">Cyclic Rhamnosylated Elongation Factor P Establishes Antibiotic Resistance in <\/a><em><a href=\"https:\/\/mbio.asm.org\/content\/6\/3\/e00823-15.long\">Pseudomonas aeruginosa<\/a><\/em><a href=\"https:\/\/mbio.asm.org\/content\/6\/3\/e00823-15.long\">.<\/a>&nbsp;<em>mBio<\/em>. 6(3):e00823-15.<\/p>\n\n\n\n<p>Ali, S.S., Soo, J., Rao, C., Leung, A.S., Ngai, D.H-M., Ensminger, A.W., and&nbsp;<strong>W.W. Navarre.&nbsp;<\/strong>(2014)&nbsp;<a href=\"http:\/\/www.plospathogens.org\/article\/info:doi\/10.1371\/journal.ppat.1004500\">Silencing by H-NS potentiated the evolution of&nbsp;<\/a><em><a href=\"http:\/\/www.plospathogens.org\/article\/info:doi\/10.1371\/journal.ppat.1004500\">Salmonella<\/a><\/em><a href=\"http:\/\/www.plospathogens.org\/article\/info:doi\/10.1371\/journal.ppat.1004500\">.<\/a>&nbsp;&nbsp;<em>PLoS Pathogens&nbsp;<\/em>10(11): e1004500. doi:10.1371\/journal.ppat.1004500.<\/p>\n\n\n\n<p>Will, W.R.,&nbsp;<strong>Navarre, W.W.<\/strong>, and F.C. Fang (2014) <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1369527414001453?via%3Dihub\">Integrated Circuits: How Transcriptional Silencing and Counter-Silencing Facilitate Bacterial Evolution.<\/a> &nbsp;Current Opinion in Microbiology&nbsp;23:8-13. doi: 10.1016\/j.mib.2014.10.005.<\/p>\n\n\n\n<p>Wang, H., Epstein, S., Ali, S.S.,&nbsp;<strong>Navarre, W.W.<\/strong>&nbsp;and J. Milstein (2014)&nbsp;<a href=\"http:\/\/nar.oxfordjournals.org\/cgi\/content\/full\/gku896?ijkey=t0NooAVxDn2cIzM&amp;keytype=ref\" target=\"_blank\" rel=\"noreferrer noopener\">A biomechanical mechanism for initiating DNA packaging<\/a>. &nbsp;<em>Nucleic Acids Research<\/em>&nbsp;doi: 10.1093\/nar\/gku896<\/p>\n\n\n\n<p>Hersch, S.J., Elgamal, S., Katz, A., Ibba, M., and&nbsp;<strong>W.W. Navarre<\/strong>&nbsp;(2014)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/25148683\" target=\"_blank\" rel=\"noreferrer noopener\">Translation Initiation Rate Determines the Impact of Ribosome Stalling on Bacterial Protein Synthesis.<\/a>&nbsp;<em>Journal of Biological Chemistry<\/em>&nbsp;289(41):28160-28171<\/p>\n\n\n\n<p>Elgamal, S., Katz, A., Hersch, S.J., Newsom, D., White, P.,&nbsp;<strong>Navarre, W.W.<\/strong>&nbsp;and M. Ibba (2014)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/25144653\">EF-P dependent pauses integrate proximal and distal signals during translation.<\/a>&nbsp;<em>PLoS Genetics&nbsp;<\/em>10(8):e1004553. doi:10.1371\/journal.pgen.1004553<\/p>\n\n\n\n<p>Belcheva, A., Irrazabal, T., Robertson, S.J., Streutker, C., Maughan, H., Rubino, S., Moriyama, E.H., Copeland, J.K., Kumar, S., Green, B., Geddes, K., Pezo, R.C.,&nbsp;<strong>Navarre, W.W.<\/strong>, Milosevic, M., Wilson, B.C., Girardin, S.E., Wolever, T.M., Edelmann, W., Guttman, D.S., Philpott, D.J. and A. Martin. (2014) &nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/25036629\">Gut microbial metabolism drives transformation of Msh2-deficient&nbsp;colon epithelial cells.<\/a>&nbsp;&nbsp;<em>Cell<\/em>&nbsp;158(2):288-99<\/p>\n\n\n\n<p>Katz, A., Solden, L., Zou, S.B.,&nbsp;<strong>Navarre W.W.<\/strong>, and M. Ibba (2014)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/24335280\">Molecular evolution of&nbsp;protein-RNA mimicry as a mechanism for translational control.<\/a>&nbsp;<em>Nucleic Acids Research<\/em>&nbsp;42(5):3261-3271<\/p>\n\n\n\n<p>Hersch, S.J., Wang, M., Zou, S.B., Moon, K-M., Foster, L.J., Ibba, M., and&nbsp;<strong>W.W. Navarre<\/strong>&nbsp;(2013)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23611909\">Divergent protein motifs direct EF-P mediated translational regulation in&nbsp;<em>Salmonella&nbsp;<\/em>and<em>&nbsp;E. coli.<\/em><\/a>&nbsp;&nbsp;<em>mBio<\/em>&nbsp;4(2) e00180-13. &nbsp;doi: 10.1128\/mBio.00180-13<\/p>\n\n\n\n<p>Ali, S.S., Whitney, J.C., Stevenson, J., Robinson, H., Howell, P.L., and&nbsp;<strong>W.W. Navarre<\/strong>&nbsp;(2013)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23515315\">Structural Insights into the Regulation of Foreign Genes in Salmonella by the Hha\/H-NS Complex.<\/a>&nbsp;<em>Journal of Biological Chemistry<\/em>&nbsp;288(19):13356-13369<\/p>\n\n\n\n<p>Bullwinkle, T.J., Zou, S.B., Rajkovic, A., Hersch, S.J., Elgamal, S., Robinson, N., Smil, D.,&nbsp;<strong>Navarre, W.W.<\/strong>, and M. Ibba (2013)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/23277358\">(R)-beta-lysine modified elongation factor P functions in translation elongation.<\/a>&nbsp;&nbsp;<em>Journal of Biological Chemistry<\/em>. 288(6):4416-4423<\/p>\n\n\n\n<p>Ibba, M. and&nbsp;<strong>W.W. Navarre<\/strong>&nbsp;(2012) Elongation Factor P \u2013 Putting a eukaryotic twist on bacterial gene expression. &nbsp;<em>Microbe<\/em>&nbsp;7(10) 449-454<\/p>\n\n\n\n<p>Ali, S.S., Xia, B., Liu, J., and<strong>&nbsp;W. W. Navarre<\/strong>&nbsp;(2012)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/22265250\">Silencing of foreign DNA in bacteria.<\/a>&nbsp;<em>Current Opinion in Microbiology&nbsp;<\/em>15(2):175-181<\/p>\n\n\n\n<p>Zou, S.B., Hersch, S.J., Roy, H., Wiggers, J.B., Leung, A.L., Buranyi, S.G., Xie, J.L., Dare, K., Ibba, M., and&nbsp;<strong>W.W. Navarre<\/strong>&nbsp;(2012)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/22081389\">Loss of elongation factor P disrupts bacterial outer membrane integrity<\/a>.&nbsp;<em>Journal of Bacteriology<\/em>194(2):413-425 &nbsp; &nbsp;<em>* Note: Authors correction in Journal of Bacteriology (2012), 194(16):4484.<\/em><\/p>\n\n\n\n<p>Glireath, M.S., Roy, H., Bullwinkle, T.J., Katz, A.,&nbsp;<strong>Navarre, W.W.<\/strong>&nbsp;and M. Ibba (2011)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21925499\">Beta-lysine discrimination by lysyl-tRNA synthetase.<\/a><em>&nbsp;FEBS Journal<\/em>&nbsp;585(20):3284-3288<\/p>\n\n\n\n<p>Roy, H., Zou S.B., Bullwinkle, T.B., Wolfe, B.S., Gilreath, M.S., Forsyth, C.J.,&nbsp;<strong>Navarre, W.W.,<\/strong>&nbsp;and M. Ibba &nbsp;(2011)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21841797\">The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-\u03b2-lysine.<\/a>&nbsp;<em>Nature Chemical Biology<\/em>, 7(10):667-669<\/p>\n\n\n\n<p>Ali, S.S., Beckett, E., Bae, S.J., and&nbsp;<strong>W.W. Navarre<\/strong>&nbsp;(2011)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21764926\">The 5.5 protein of phage T7 inhibits H-NS through interactions with the central oligomerization domain.&nbsp;<\/a><em>Journal of Bacteriology<\/em>, 193(18):4881-4892<\/p>\n\n\n\n<p>Gordon, B.R., Li, Y., Cote, A., Weirauch, M., Ding, P., Hughes, T.,&nbsp;<strong>Navarre, W.W.<\/strong>, Xia, B. and J. Liu (2011)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21673140\">Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.<\/a>&nbsp;<em>&nbsp;Proc. Natl. Acad. Sci. USA.<\/em>108(26):10690-10695<\/p>\n\n\n\n<p>Zou, S.B., Roy, H., Ibba, M., and&nbsp;<strong>W.W. Navarre<\/strong>&nbsp;(2011)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/21317554\">Elongation Factor P mediates a novel post-transcriptional regulatory pathway critical for bacterial virulence.<\/a>&nbsp;&nbsp;<em>Virulence<\/em>&nbsp;2(2): 147-51.<\/p>\n\n\n\n<p><strong>Navarre, W.W*<\/strong>., Zou, S., Roy, H., Xie, J.L., Savchenko, A., Singer, A., Edvokimova, E., Prost, L.R., Kumar, R., Ibba, M. Fang, F.C. (2010)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/20670890\">PoxA, YjeK and Elongation Factor P Coordinately Modulate Virulence and Drug Resistance in&nbsp;<em>Salmonella enterica<\/em>.<\/a>&nbsp;<em>Molecular Cell<\/em>, 39(2):209-221 (*sole corresponding author)<\/p>\n\n\n\n<p>Gordon, B.R., Li, Y., Wang, L., Sintsova, A., van Bakel, H., Tian, S.,&nbsp;<strong>Navarre, W.W.<\/strong>, Xia, B., and J. Liu &nbsp;(2010)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/20133735\">Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in&nbsp;<em>Mycobacterium tuberculosis<\/em>.<\/a>&nbsp;<em>Proc. Natl. Acad. Sci. USA<\/em>. 107(11):5154-5159<\/p>\n\n\n\n<p><strong>Navarre, W.W.<\/strong>&nbsp;(2010) H-NS as a Defence System. in Bacterial Chromatin (editors: Dame R.T. and Dorman C.J.), Springer press. p.p. 251-322<\/p>\n\n\n\n<p>Gordon, B.R., Imperial, R., Wang, L.,&nbsp;<strong>Navarre, W.W.<\/strong>&nbsp;and J. Liu (2008)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/18776007\">Lsr2 of Mycobacterium represents a novel class of H-NS-like proteins.<\/a>&nbsp;<em>Journal of Bacteriology<\/em>&nbsp;190(21):7052-7059<\/p>\n\n\n\n<p>Noom, M.C.,&nbsp;<strong>Navarre, W.W.<\/strong>, Oshima, T., Wuite, G.J.L, and R.T. Dame (2007)&nbsp;<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/17983565\">H-NS promotes looped domain formation in the bacterial chromosome.<\/a>&nbsp;&nbsp;<em>Current Biology<\/em>&nbsp;&nbsp;17(21):R913-R914.<\/p>\n\n\n\n<p class=\"has-text-color has-background\" style=\"background-color:#00204e;color:#ffffff\"><strong>NAVARRE POSTDOCTORAL PUBLICATIONS FROM THE FANG LAB<\/strong><\/p>\n\n\n\n<p>Richardson, A.R., Payne, E.C., Younger, N., Karlinsey, J.E., Thomas, V.C., Becker, L.A.,&nbsp;<strong>Navarre, W.W.<\/strong>, Castor, M.E., Libby S.J., and F.C. Fang (2011) &nbsp;Multiple Targets of Nitric Oxide in the Tricarboxylic Acid (TCA) Cycle of&nbsp;<em>Salmonella enterica<\/em>&nbsp;Serovar Typhimurium.&nbsp;<em>Cell Host &amp; Microbe<\/em>, 10(1):33-43<\/p>\n\n\n\n<p>Walthers, D., Carroll, R.K.,&nbsp;<strong>Navarre, W.W.<\/strong>, Libby, S.J., Fang, F.C., and L. Kenney. (2007) &nbsp;The response regulator SsrB activates expression of diverse&nbsp;<em>Salmonella<\/em>&nbsp;pathogenicity island 2 promoters and counters silencing by the nucleoid-associated protein H-NS.&nbsp;<em>Mol. Microbiol.<\/em>&nbsp;65(2):477-493<\/p>\n\n\n\n<p><strong>Navarre, W.W.<\/strong>, McClelland, M., Libby, S.J., and F.C. Fang. (2007) &nbsp;Silencing of xenogeneic DNA by H-NS &#8211; facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA (Review). &nbsp;<em>Genes Dev.<\/em>&nbsp;21(12):1456-1471.<\/p>\n\n\n\n<p><strong>Navarre, W.W.<\/strong>, Porwollik, S., Wang, Y., McClelland, M., Rosen, H., Libby, S.J., and F.C. Fang. (2006) The H-NS protein selectively silences foreign DNA with low GC content in&nbsp;<em>Salmonella<\/em>. &nbsp;<em>Science<\/em>&nbsp;313(5784):236-238<\/p>\n\n\n\n<p><strong>Navarre, W.W.<\/strong>, Halsey T.A., Walthers, D., Frye, J., McClelland, M., Potter, J., Kenney, L., Gunn, J.S., Fang, F.C., and S.J. Libby (2005) Co-regulation of&nbsp;<em>Salmonella enterica<\/em>&nbsp;genes required for virulence and resistance to antimicrobial peptides by SlyA and PhoP\/PhoQ.&nbsp;<em>Mol. Microbiol.<\/em>&nbsp;&nbsp;56(2):492-508<\/p>\n\n\n\n<p>Monsieurs, P., De Keersmaecker, S.,&nbsp;<strong>Navarre, W.W.<\/strong>, Bader, M., De Smet, F., McClelland, M., Fang, F.C., De Moor, B., Vanderleyden, J., and K. Marchal (2005) Comparison of the PhoPQ regulon in&nbsp;<em>Escherichia coli<\/em>&nbsp;and&nbsp;<em>Salmonella typhimurium.<\/em>&nbsp;&nbsp;<em>J. Mol. Evol.<\/em>&nbsp;60(4):462-474<\/p>\n\n\n\n<p>Bader, M.W.,&nbsp;<strong>Navarre, W.W.<\/strong>, Siau, W., Nikaido, H., Frye, J., McClelland, M., Fang, F.C. and S.I. Miller (2003) Regulation of&nbsp;<em>Salmonella typhimurium<\/em>&nbsp;Virulence Gene Expression by Cationic Antimicrobial Peptides. &nbsp;<em>Mol. Microbiol.<\/em>&nbsp;&nbsp;50(1): 219-230<\/p>\n\n\n\n<p class=\"has-text-color has-background\" style=\"background-color:#00204e;color:#ffffff\"><strong>NAVARRE POST-DOCTORAL WORK FROM ZYCHLINSKY LAB<\/strong><\/p>\n\n\n\n<p>Monack D.M.,&nbsp;<strong>Navarre W.W.<\/strong>&nbsp;and S. Falkow (2001)&nbsp;<em>Salmonella<\/em>-induced macrophage death: the role of caspase-1 in death and inflammation (Review).&nbsp;<em>Microbes Infect.<\/em>&nbsp;3(14-15):1201-1212<\/p>\n\n\n\n<p><strong>Navarre W.W.<\/strong>&nbsp;and A. Zychlinsky (2000) Pathogen-induced apoptosis of macrophages: a common end for different pathogenic strategies (Review). &nbsp;<em>Cell Microbiol.&nbsp;<\/em>2(4):265-273<\/p>\n\n\n\n<p class=\"has-text-color has-background\" style=\"background-color:#00204e;color:#ffffff\"><strong>NAVARRE GRADUATE WORK FROM OLAF SCHNEEWIND&#8217;S LAB<\/strong><\/p>\n\n\n\n<p><strong>Navarre, W.W.<\/strong>, Ton-That, H., Faull, K. and O. Schneewind (1999) Multiple enzymatic activities of the murein hydrolase from staphylococcal phage phi-11. Identification of a D-alanyl-glycine endopeptidase activity. &nbsp;<em>J. Biol. Chem.<\/em>&nbsp;274(22): 15847-15856<\/p>\n\n\n\n<p><strong>Navarre, W.W.<\/strong>&nbsp;and O. Schneewind (1999) Protein targeting mechanisms to the cell wall of Gram-positive bacteria (Review). &nbsp;<em>Microbiol. Mol. Biol. Rev.<\/em>, 63(1): 174-229<\/p>\n\n\n\n<p><strong>Navarre, W.W.<\/strong>, Ton-That, H., Faull, K. and O. Schneewind (1998) Anchor structure of surface proteins in&nbsp;<em>Staphylococcus aureus<\/em>. &nbsp;Analysis of muramidase released anchor peptides. &nbsp;J. Biol. Chem., 273(44): 29135-29142<\/p>\n\n\n\n<p><strong>Navarre, W.W.,<\/strong>&nbsp;Daefler, S. and O. Schneewind (1996) Cell wall sorting of lipoproteins in&nbsp;<em>Staphylococcus aureus. J. Bacteriol<\/em>., 178(2): 441-446<\/p>\n\n\n\n<p>Emami, K.H.,&nbsp;<strong>Navarre, W.W.<\/strong>&nbsp;and S.T. Smale (1995) Core promoter specificities of the Sp1 and VP16 transcriptional activation domains. &nbsp;<em>Mol. Cell. Biol.<\/em>, 15(11): 5906-5916<\/p>\n\n\n\n<p><strong>Navarre, W.W.<\/strong>&nbsp;and O. Schneewind (1994) Proteolytic cleavage and cell wall anchoring at the LPXTG motif of surface proteins in Gram-positive bacteria. &nbsp;<em>Mol. Microbiol.,<\/em>&nbsp;14(1): 115-121<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Serrador, D., Campbell, J.R., Cheung, D., Shefraw, G., Kaul, R., and W.W. Navarre. 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