@article{yamamoto_blackburn_goshe_brown_migoswski_campanhon_moreira_ferreira_soares_2023, title={Tizoxanide Antiviral Activity on Dengue Virus Replication}, volume={15}, ISSN={["1999-4915"]}, DOI={10.3390/v15030696}, abstractNote={Dengue virus is an important circulating arbovirus in Brazil responsible for high morbidity and mortality worldwide, representing a huge economic and social burden, in addition to affecting public health. In this study, the biological activity, toxicity, and antiviral activity against dengue virus type 2 (DENV-2) of tizoxanide (TIZ) was evaluated in Vero cell culture. TIZ has a broad spectrum of action in inhibiting different pathogens, including bacteria, protozoa, and viruses. Cells were infected for 1 h with DENV-2 and then treated for 24 h with different concentrations of the drug. The quantification of viral production indicated the antiviral activity of TIZ. The protein profiles in infected Vero cells treated and not treated with TIZ were analyzed using the label-free quantitative proteomic approach. TIZ was able to inhibit virus replication mainly intracellularly after DENV-2 penetration and before the complete replication of the viral genome. Additionally, the study of the protein profile of infected not-treated and infected-treated Vero cells showed that TIZ interferes with cellular processes such as intracellular trafficking and vesicle-mediated transport and post-translational modifications when added after infection. Our results also point to the activation of immune response genes that would eventually lead to a decrease of DENV-2 production. TIZ is a promising therapeutic molecule for the treatment of DENV-2 infections.}, number={3}, journal={VIRUSES-BASEL}, author={Yamamoto, Kristie A. and Blackburn, Kevin and Goshe, Michael B. and Brown, Dennis T. and Migoswski, Edimilson and Campanhon, Isabele B. and Moreira, Monica F. and Ferreira, Davis F. and Soares, Marcia R.}, year={2023}, month={Mar} }
 @article{schuchman_vancini_piper_breuer_ribeiro_ferreira_magliocca_emmerich_hernandez_brown_2018, title={Role of the vacuolar ATPase in the Alphavirus replication cycle}, volume={4}, ISSN={2405-8440}, url={http://dx.doi.org/10.1016/J.HELIYON.2018.E00701}, DOI={10.1016/J.HELIYON.2018.E00701}, abstractNote={We have shown that Alphaviruses can enter cells by direct penetration at the plasma membrane (R. Vancini, G. Wang, D. Ferreira, R. Hernandez, and D. Brown, J Virol, 87:4352-4359, 2013). Direct penetration removes the requirement for receptor-mediated endocytosis exposure to low pH and membrane fusion in the process of RNA entry. Endosomal pH as well as the pH of the cell cytoplasm is maintained by the activity of the vacuolar ATPase (V-ATPase). Bafilomycin is a specific inhibitor of V-ATPase. To characterize the roll of the V-ATPase in viral replication we generated a Bafilomycin A1(BAF) resistant mutant of Sindbis virus (BRSV). BRSV produced mature virus and virus RNA in greater amounts than parent virus in BAF-treated cells. Sequence analysis revealed mutations in the E2 glycoprotein, T15I/Y18H, were responsible for the phenotype. These results show that a functional V-ATPase is required for efficient virus RNA synthesis and virus maturation in Alphavirus infection.}, number={7}, journal={Heliyon}, publisher={Elsevier BV}, author={Schuchman, Ryan M. and Vancini, Ricardo and Piper, Amanda and Breuer, Denitra and Ribeiro, Mariana and Ferreira, Davis and Magliocca, Joseph and Emmerich, Veronica and Hernandez, Raquel and Brown, Dennis T.}, year={2018}, month={Jul}, pages={e00701} }
 @article{magliocca_vancini_hernandez_brown_2016, title={Single-Site Glycoprotein Mutants Inhibit a Late Event in Sindbis Virus Assembly}, volume={90}, ISSN={["1098-5514"]}, DOI={10.1128/jvi.00948-16}, abstractNote={ABSTRACT}, number={18}, journal={JOURNAL OF VIROLOGY}, author={Magliocca, Joseph and Vancini, Ricardo and Hernandez, Raquel and Brown, Dennis T.}, year={2016}, month={Sep}, pages={8372–8380} }
 @article{schuchman_vancini_piper_breuer_ribeiro_farreira_magliocca_emmerich_hernandez_brown_2016, title={The role of the vacuolar ATPase in alphavirus replication.}, volume={27}, journal={Molecular Biology of the Cell}, author={Schuchman, R. and Vancini, R. and Piper, A. and Breuer, D. and Ribeiro, M. and Farreira, D. and Magliocca, J. and Emmerich, V. and Hernandez, R. and Brown, D.}, year={2016} }
 @misc{vancini_hernandez_brown_2015, title={Alphavirus Entry into Host Cells}, volume={129}, journal={Molecular basis of viral infection}, author={Vancini, R. and Hernandez, R. and Brown, D.}, year={2015}, pages={33–62} }
 @article{briggs_smith_piper_huitt_spears_quiles_ribeiro_thomas_brown_hernandez_2014, title={Live Attenuated Tetravalent Dengue Virus Host Range Vaccine Is Immunogenic in African Green Monkeys following a Single Vaccination}, volume={88}, ISSN={["1098-5514"]}, DOI={10.1128/jvi.00541-14}, abstractNote={ABSTRACT}, number={12}, journal={JOURNAL OF VIROLOGY}, author={Briggs, Caitlin M. and Smith, Katherine M. and Piper, Amanda and Huitt, Emerson and Spears, Carla J. and Quiles, Michelle and Ribeiro, Mariana and Thomas, Malcolm E. and Brown, Dennis T. and Hernandez, Raquel}, year={2014}, month={Jun}, pages={6729–6742} }
 @article{vancini_wang_ferreira_hernandez_brown_2013, title={Alphavirus Genome Delivery Occurs Directly at the Plasma Membrane in a Time- and Temperature-Dependent Process}, volume={87}, ISSN={["0022-538X"]}, DOI={10.1128/jvi.03412-12}, abstractNote={ABSTRACT}, number={8}, journal={JOURNAL OF VIROLOGY}, author={Vancini, Ricardo and Wang, Gongbo and Ferreira, Davis and Hernandez, Raquel and Brown, Dennis T.}, year={2013}, month={Apr}, pages={4352–4359} }
 @article{piper_ribeiro_smith_briggs_huitt_nanda_spears_quiles_cullen_thomas_et al._2013, title={Chikungunya Virus Host Range E2 Transmembrane Deletion Mutants Induce Protective Immunity against Challenge in C57BL/6J Mice}, volume={87}, ISSN={["1098-5514"]}, DOI={10.1128/jvi.03357-12}, abstractNote={ABSTRACT}, number={12}, journal={JOURNAL OF VIROLOGY}, author={Piper, Amanda and Ribeiro, Mariana and Smith, Katherine M. and Briggs, Caitlin M. and Huitt, Emerson and Nanda, Kavita and Spears, Carla J. and Quiles, Michelle and Cullen, John and Thomas, Malcolm E. and et al.}, year={2013}, month={Jun}, pages={6748–6757} }
 @article{vancini_kramer_ribeiro_hernandez_brown_2013, title={Flavivirus infection from mosquitoes in vitro reveals cell entry at the plasma membrane}, volume={435}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2012.10.013}, abstractNote={Dengue and West Nile viruses are enveloped RNA viruses that belong to genus Flavivirus (family Flaviviridae) and are considered important mosquito-borne viral pathogenic agents worldwide. A potential target for intervention strategies is the virus cell entry mechanism. Previous studies of flavivirus entry have focused on the effects of biochemical and molecular inhibitors on viral entry leading to controversial conclusions suggesting that the process is dependent upon endocytosis and low pH mediated membrane fusion. In this study we analyzed the early events in the infection process by means of electron microscopy and immuno-gold labeling of viral particles during cell entry, and used as a new approach for infecting cells with viruses obtained directly from mosquitoes. The results show that Dengue and West Nile viruses may infect cells by a mechanism that involves direct penetration of the host cell plasma membrane as proposed for alphaviruses.}, number={2}, journal={VIROLOGY}, author={Vancini, Ricardo and Kramer, Laura D. and Ribeiro, Mariana and Hernandez, Raquel and Brown, Dennis}, year={2013}, month={Jan}, pages={406–414} }
 @article{he_piper_meilleur_hernandez_heller_brown_2012, title={Conformational Changes in Sindbis Virus Induced by Decreased pH Are Revealed by Small-Angle Neutron Scattering}, volume={86}, ISSN={["0022-538X"]}, url={http://europepmc.org/abstract/med/22156534}, DOI={10.1128/jvi.06569-11}, abstractNote={ABSTRACT}, number={4}, journal={JOURNAL OF VIROLOGY}, author={He, Lilin and Piper, Amanda and Meilleur, Flora and Hernandez, Raquel and Heller, William T. and Brown, Dennis T.}, year={2012}, month={Feb}, pages={1982–1987} }
 @article{brown_hernandez_2012, title={Infection of cells by alphaviruses}, volume={726}, journal={Viral molecular machines}, author={Brown, D. T. and Hernandez, R.}, year={2012}, pages={181–199} }
 @article{smith_nanda_mccarl_spears_piper_ribeiro_quiles_briggs_thomas_thomas_et al._2012, title={Testing of Novel Dengue Virus 2 Vaccines in African Green Monkeys: Safety, Immunogenicity, and Efficacy}, volume={87}, ISSN={["1476-1645"]}, DOI={10.4269/ajtmh.2012.12-0004}, abstractNote={The immunogenicity and safety of three novel host-range vaccines containing deletions in the transmembrane domain of dengue virus serotype 2 (DV2) E glycoprotein were evaluated in African green monkeys. The shorter transmembrane domains are capable of functionally spanning an insect but not a mammalian cell membrane, resulting in production of viral mutants that have reduced infectivity in mammalian hosts but efficient growth in insect cells. Groups of four monkeys received one dose each of test vaccine candidate with no booster immunization. After immunization, levels of viremia produced by each vaccine were determined by infectious center assay. Vaccine recipient immune response to wild-type DV2 challenge was measured on Day 57 by enzyme-linked immunosorbent assay and plaque reduction neutralization test. Two vaccines, DV2ΔGVII and DV2G460P, generated neutralizing antibody in the range of 700–900 50% plaque reduction neutralization test units. All three vaccine strains decreased the length of viremia by at least two days. No safety concerns were identified.}, number={4}, journal={AMERICAN JOURNAL OF TROPICAL MEDICINE AND HYGIENE}, author={Smith, Katherine M. and Nanda, Kavita and McCarl, Victoria and Spears, Carla J. and Piper, Amanda and Ribeiro, Mariana and Quiles, Michelle and Briggs, Caitlin M. and Thomas, Gwynneth S. and Thomas, Malcolm E. and et al.}, year={2012}, month={Oct}, pages={743–753} }
 @article{kononchik_vancini_brown_2011, title={Alphavirus adsorption to mosquito cells as viewed by freeze fracture immunolabeling}, volume={415}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2011.04.011}, abstractNote={Sindbis Virus (SV), the prototype alphavirus in the family togaviridae, infects both mammalian and insect cells. The ability of SV to infect cells possessing significantly different biochemical environments suggests that there may be a common mode of entry into each cell type. Previous studies show that up to 4h post infection cells are permeable to small ions and alpha sarcin suggesting that the plasma membrane is compromised as infection takes place. Thin-section electron microscopy has also shown SV to bind to the plasma membrane and lose its electron dense core through a pore like structure developed upon interaction of the virus with the cell surface. Using freeze-fracture replicas, thin-sections and antibody labeling the data presented herein show virus associated with intramembrane particles on mosquito cells. These data suggest that the intramembrane particles associated with SV may be part of the pore structure consisting of virus proteins and cell receptor.}, number={2}, journal={VIROLOGY}, author={Kononchik, Joseph P. and Vancini, Ricardo and Brown, Dennis T.}, year={2011}, month={Jul}, pages={132–140} }
 @article{hunt_hernandez_brown_2011, title={Role of the Vacuolar-ATPase in Sindbis Virus Infection}, volume={85}, ISSN={["1098-5514"]}, DOI={10.1128/jvi.01864-10}, abstractNote={ABSTRACT}, number={3}, journal={JOURNAL OF VIROLOGY}, author={Hunt, Sabrina R. and Hernandez, Raquel and Brown, Dennis T.}, year={2011}, month={Feb}, pages={1257–1266} }
 @article{smith_nanda_spears_ribeiro_vancini_piper_thomas_thomas_brown_hernandez_2011, title={Structural mutants of dengue virus 2 transmembrane domains exhibit host-range phenotype}, volume={8}, ISSN={["1743-422X"]}, DOI={10.1186/1743-422x-8-289}, abstractNote={There are over 700 known arboviruses and at least 80 immunologically distinct types that cause disease in humans. Arboviruses are transmitted among vertebrates by biting insects, chiefly mosquitoes and ticks. These viruses are widely distributed throughout the world, depending on the presence of appropriate hosts (birds, horses, domestic animals, humans) and vectors. Mosquito-borne arboviruses present some of the most important examples of emerging and resurgent diseases of global significance. A strategy has been developed by which host-range mutants of Dengue virus can be constructed by generating deletions in the transmembrane domain (TMD) of the E glycoprotein. The host-range mutants produced and selected favored growth in the insect hosts. Mouse trials were conducted to determine if these mutants could initiate an immune response in an in vivo system. The DV2 E protein TMD defined as amino acids 452SWTMKILIGVIITWIG467 was found to contain specific residues which were required for the production of this host-range phenotype. Deletion mutants were found to be stable in vitro for 4 sequential passages in both host cell lines. The host-range mutants elicited neutralizing antibody above that seen for wild-type virus in mice and warrant further testing in primates as potential vaccine candidates. Novel host-range mutants of DV2 were created that have preferential growth in insect cells and impaired infectivity in mammalian cells. This method for creating live, attenuated viral mutants that generate safe and effective immunity may be applied to many other insect-borne viral diseases for which no current effective therapies exist.}, journal={VIROLOGY JOURNAL}, author={Smith, Katherine M. and Nanda, Kavita and Spears, Carla J. and Ribeiro, Mariana and Vancini, Ricardo and Piper, Amanda and Thomas, Gwynneth S. and Thomas, Malcolm E. and Brown, Dennis T. and Hernandez, Raquel}, year={2011}, month={Jun} }
 @article{hernandez_brown_2010, title={Growth and Maintenance of Baby Hamster Kidney (BHK) Cells}, volume={17}, ISSN={1934-8525}, url={http://dx.doi.org/10.1002/9780471729259.MCA04HS17}, DOI={10.1002/9780471729259.MCA04HS17}, abstractNote={Abstract}, number={1}, journal={Current Protocols in Microbiology}, publisher={Wiley}, author={Hernandez, Raquel and Brown, Dennis T.}, year={2010}, month={May}, pages={A.4H.1-A.4H.7} }
 @article{hernandez_brown_2010, title={Growth and Maintenance of Chick Embryo Fibroblasts (CEF)}, volume={17}, ISSN={1934-8525}, url={http://dx.doi.org/10.1002/9780471729259.MCA04IS17}, DOI={10.1002/9780471729259.MCA04IS17}, abstractNote={Abstract}, number={1}, journal={Current Protocols in Microbiology}, publisher={Wiley}, author={Hernandez, Raquel and Brown, Dennis T.}, year={2010}, month={May}, pages={A.4I.1-A.4I.8} }
 @article{hernandez_brown_2010, title={Growth and Maintenance of Mosquito Cell Lines}, volume={17}, ISSN={1934-8525}, url={http://dx.doi.org/10.1002/9780471729259.MCA04JS17}, DOI={10.1002/9780471729259.MCA04JS17}, abstractNote={Abstract}, number={1}, journal={Current Protocols in Microbiology}, publisher={Wiley}, author={Hernandez, Raquel and Brown, Dennis T.}, year={2010}, month={May}, pages={A.4J.1-A.4J.8} }
 @article{mudiganti_hernandez_brown_2010, title={Insect response to alphavirus infection-Establishment of alphavirus persistence in insect cells involves inhibition of viral polyprotein cleavage}, volume={150}, ISSN={["1872-7492"]}, DOI={10.1016/j.virusres.2010.02.016}, abstractNote={Alphavirus persistence in the insect vector is an essential element in the vector–host transmission cycle of the virus and provides a model to study the biochemical and molecular basis for virus–vector coexistence. The prototype alphavirus Sindbis (SV) establishes persistent infections in invertebrate cell cultures which are characterized by low levels of virus production. We hypothesized that antiviral factors may be involved in decreasing the virus levels as virus persistence is established in invertebrate cells. Transcription profiles in Drosophila S2 cells at 5 days post-infection with SV identified families of gene products that code for factors that can explain previous observations seen in insect cells infected with alphaviruses. Genomic array analysis identified up-regulation of gene products involved in intracellular membrane vesicle formation, cell growth rate changes and immune-related functions in S2 cells infected with SV. Transcripts coding for factors involved in different aspects of the Notch signaling pathway had increased in expression. Increased expression of ankyrin, plap, syx13, unc-13, csp, rab1 and rab8 may aid in formation of virus containing vesicles and in intracellular transport of viral structural proteins. Possible functions of these gene products and relevant hypotheses are discussed. We confirmed the up-regulation of a wide-spectrum protease inhibitor, Thiol-ester containing Protein (TEP) II. We report inhibition of the viral polyprotein cleavage at 5 days post-infection (dpi) and after superinfection of SV-infected cells at 5 dpi. We propose that inefficient cleavage of the polyprotein may, at least in part, lead to reduced levels of virus seen as persistence is established.}, number={1-2}, journal={VIRUS RESEARCH}, author={Mudiganti, Usharani and Hernandez, Raquel and Brown, Dennis T.}, year={2010}, month={Jun}, pages={73–84} }
 @article{he_piper_meilleur_myles_hernandez_brown_heller_2010, title={The Structure of Sindbis Virus Produced from Vertebrate and Invertebrate Hosts as Determined by Small-Angle Neutron Scattering}, volume={84}, ISSN={["1098-5514"]}, url={http://europepmc.org/abstract/med/20219936}, DOI={10.1128/jvi.00044-10}, abstractNote={ABSTRACT}, number={10}, journal={JOURNAL OF VIROLOGY}, author={He, Lilin and Piper, Amanda and Meilleur, Flora and Myles, Dean A. A. and Hernandez, Raquel and Brown, Dennis T. and Heller, William T.}, year={2010}, month={May}, pages={5270–5276} }
 @article{nanda_vancini_ribeiro_brown_hernandez_2009, title={A high capacity Alphavirus heterologous gene delivery system}, volume={390}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2009.05.026}, abstractNote={A novel replication competent Sindbis virus based gene delivery vector has been developed for the introduction of genetic cargo into cell lines in vitro and potentially, animal models in vivo. This delivery system expands the previous uses of Sindbis virus as a gene delivery system in that no replicons are required and the resulting cargo containing virus particles are infectious. The heterologous vector is based on a morphological mutant in C, Ser180/Gly183 which produces larger than the normal size T=4 virus particles of 70 nm in size. This mutant produced particles up to 205 nm in size equal to a triangulation number of 36. It was postulated that because the Ser180/Gly183 mutant was capable of assembling such large particles, that increasing the size of the RNA genome incorporated into this mutant capsid protein would favor the assembly of larger than T=4 wild type sized virions. The first generation prototype larger vehicle, described here, carries a approximately 18 kb cDNA insert, however it is conceivable that RNA as large as 32 kb could be transcribed and packaged. The large variant produces a high virus titer of approximately 10(9) pfu/ml from either mammalian or insect cells in culture. Multiple passages of the virus show no loss of the inserted genetic material.}, number={2}, journal={VIROLOGY}, author={Nanda, Kavita and Vancini, Ricardo and Ribeiro, Mariana and Brown, Dennis T. and Hernandez, Raquel}, year={2009}, month={Aug}, pages={368–373} }
 @article{hafer_whittlesey_brown_hernandez_2009, title={Differential Incorporation of Cholesterol by Sindbis Virus Grown in Mammalian or Insect Cells}, volume={83}, ISSN={["1098-5514"]}, DOI={10.1128/JVI.00755-09}, abstractNote={ABSTRACT}, number={18}, journal={JOURNAL OF VIROLOGY}, author={Hafer, Amanda and Whittlesey, Rebecca and Brown, Dennis T. and Hernandez, Raquel}, year={2009}, month={Sep}, pages={9113–9121} }
 @article{kononchik_nelson_hernandez_brown_2009, title={Helical virus particles formed from morphological subunits of a membrane containing icosahedral virus}, volume={385}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2008.12.015}, abstractNote={The classic publication by Caspar and Klug in 1962 [Physical principles in the construction of regular viruses. Cold Spring Harbor Symp. Quant. Biol. 27:1–24.] has formed the basis of much research on virus assembly. Caspar and Klug predicted that a single virus morphological unit could form a two dimensional lattice composed of 6-fold arrays (primitive plane), a family of icosahedra of increasing triangulation numbers (T) and helical arrays of varying length. We have shown that icosahedral viruses of varying T numbers can be produced using Sindbis virus [Ferreira, D. F. et al. 2003. Morphological variants of Sindbis virus produced by a mutation in the capsid protein. Virology 307:54–66]. Other studies have shown that Sindbis glycoproteins can also form a 2-dimensional lattice confirming Caspar and Klug's prediction of the primitive plane as a biologically relevant structure [VonBonsdorff, C. H., and S. C. Harrison. 1978. Sindbis virus glycoproteins form a regular icosahedral surface lattice. J. Virol. 28:578]. In this study we have used mutations in the glycoproteins of membrane containing Sindbis virus to create helical-virus-like particles from the morphological subunits of a virus of icosahedral geometry. The resulting virus particles were examined for subunit organization and were determined to be constructed of only 6-fold rotational arrays of the virus glycoproteins. A model of the tubular virus particles created from the 6-fold rotational arrays of Sindbis virus confirmed the observed structure. These experiments show that a common morphological unit (the Sindbis E1–E2 heterodimer) can produce three different morphological entities of varying dimensions in a membrane-containing virus system.}, number={2}, journal={VIROLOGY}, author={Kononchik, Joseph R., Jr. and Nelson, Steevenson and Hernandez, Raquel and Brown, Dennis I.}, year={2009}, month={Mar}, pages={285–293} }
 @article{smith_nanda_slominski_hernandez_brown_thomas_2008, title={Construction and characterization of mutant Dengue2 virus vaccine candidates displaying a host-range phenotype}, journal={Vaccine}, author={Smith, K. M. and Nanda, K. and Slominski, C. J. and Hernandez, R. and Brown, D. T. and Thomas, M. E.}, year={2008} }
 @article{hernandez_paredes_brown_2008, title={Sindbis virus conformational changes induced by a neutralizing anti-E1 monoclonal antibody}, volume={82}, ISSN={["0022-538X"]}, DOI={10.1128/JVI.02673-07}, abstractNote={ABSTRACT}, number={12}, journal={JOURNAL OF VIROLOGY}, author={Hernandez, Raquel and Paredes, Angel and Brown, Dennis T.}, year={2008}, month={Jun}, pages={5750–5760} }
 @article{wang_hernandez_keith_brown_2007, title={Infection of cells by Sindbis virus at low temperature}, volume={362}, DOI={10.1016/j.virol.2006.12.036}, abstractNote={Sindbis virus, which belongs to the family Togaviridae genus Alphavirus infects a variety of vertebrate and invertebrate cells. The initial steps of Sindbis virus infection involve attachment, penetration and uncoating. Two different pathways of infection have been proposed for Alphaviruses. One proposed mechanism involves receptor mediated virion endocytosis followed by membrane fusion triggered by endosome acidification. This virus–host membrane fusion model, well established by influenza virus, has been applied to other unrelated membrane-containing viruses including Alphaviruses. The other mechanism proposes direct penetration of the cell plasma membrane by the virus glycoproteins in the absence of membrane fusion. This alternate model is supported by both ultrastructural [Paredes, A.M., Ferreira, D., Horton, M., Saad, A., Tsuruta, H., Johnston, R., Klimstra, W., Ryman, K., Hernandez, R., Chiu, W., Brown, D.T., 2004. Conformational changes in Sindbis virions resulting from exposure to low pH and interactions with cells suggest that cell penetration may occur at the cell surface in the absence of membrane fusion. Virology 324(2), 373–386] and biochemical [Koschinski, A., Wengler, G., Wengler, G., and Repp, H., 2005. Rare earth ions block the ion pores generated by the class II fusion proteins of alphaviruses and allow analysis of the biological functions of these pores. J. Gen. Virol. 86(Pt. 12), 3311–3320] studies. We have examined the ability of Sindbis virus to infect Baby Hamster Kidney (BHK) cells at temperatures which block endocytosis. We have found that under these conditions Sindbis virus infects cells in a temperature- and time-dependent fashion.}, number={2}, journal={Virology}, author={Wang, G. B. and Hernandez, R. and keith and Brown, D. T.}, year={2007}, pages={461–467} }
 @article{whitehurst_soderblom_west_hernandez_goshe_brown_2007, title={Location and role of free cysteinyl residues in the Sindbis virus E1 and E2 glycoproteins}, volume={81}, ISSN={["0022-538X"]}, DOI={10.1128/JVI.02859-06}, abstractNote={ABSTRACT}, number={12}, journal={JOURNAL OF VIROLOGY}, author={Whitehurst, Christopher B. and Soderblom, Erik J. and West, Michelle L. and Hernandez, Raquel and Goshe, Michael B. and Brown, Dennis T.}, year={2007}, month={Jun}, pages={6231–6240} }
 @article{heldt_hernandez_mudiganti_gurgel_brown_carbonell_2006, title={A  colorimetric assay for viral agents that produce cytopathic effects}, volume={135}, DOI={10.1016/j.j.viromet.2006.01.022}, number={1}, journal={Journal of Virological Methods}, author={Heldt, C. L. and Hernandez, R. and Mudiganti, U. and Gurgel, P. V. and Brown, D. T. and Carbonell, R. G.}, year={2006}, pages={56–65} }
 @article{heldt_hernandez_mudiganti_gurgel_brown_carbonell_2006, title={A colorimetric assay for viral agents that produce cytopathic effects}, volume={135}, ISSN={0166-0934}, url={http://dx.doi.org/10.1016/j.jviromet.2006.01.022}, DOI={10.1016/j.jviromet.2006.01.022}, abstractNote={Many animal viruses produce cytopathic effects in their host cells during a productive infection. While some virus infections can be assayed by the production of plaques, many viruses, while producing cytotoxicity, do not easily form plaques, or do not form plaques at all. Additionally, viruses within families such as the parvoviruses may have different preferred forms of titration making comparative virology difficult even among related groups. Porcine parvovirus (PPV), canine parvovirus (CPV), and minute virus of mice (MVM) are usually titrated using different infectivity assays. A direct comparison of infectious virus titer between these parvoviruses was sought, and a tetrazolium salt assay, MTT has been applied to measure cytopathic effect produced by viral infection for different members of the parvovirus family. Infectious PPV measured using the MTT and the TCID50 assays exhibited excellent correlation and titers for CPV and MVM were consistently duplicated using the MTT assay. The MTT assay was also applied to an unrelated virus, Sindbis, which is routinely titrated by plaque assay. MTT titration of Sindbis virus mutants was found to be valuable for preliminary screening. This assay can be adapted, by correlation to an accepted titration method, to any viral system which produces measurable cytopathic effect.}, number={1}, journal={Journal of Virological Methods}, publisher={Elsevier BV}, author={Heldt, Caryn L. and Hernandez, Raquel and Mudiganti, Usharani and Gurgel, Patrick V. and Brown, Dennis T. and Carbonell, Ruben G.}, year={2006}, month={Jul}, pages={56–65} }
 @article{west_hernandez_ferreira_brown_2006, title={Mutations in the endodomain of Sindbis virus glycoprotein E2 define sequences critical for virus assembly}, volume={80}, ISSN={["1098-5514"]}, DOI={10.1128/jvi.80.9.4458-4468.2006}, abstractNote={ABSTRACT}, number={9}, journal={JOURNAL OF VIROLOGY}, author={West, J and Hernandez, R and Ferreira, D and Brown, DT}, year={2006}, month={May}, pages={4458–4468} }
 @article{west_brown_2006, title={Role of a conserved tripeptide in the endodomain of Sindbis virus glycoprotein E2 in virus assembly and function}, volume={87}, ISSN={["1465-2099"]}, DOI={10.1099/vir.0.81304-0}, abstractNote={Envelopment of Sindbis virus (SV) at the plasma membrane begins with the interaction of the E2 glycoprotein endodomain with a hydrophobic cleft in the surface of the pre-assembled nucleocapsid. The driving force for this budding event is thought to reside in this virus type-specific association at the surface of the cell. The specific amino acids involved in this interaction have not been identified; however, it has been proposed that a conserved motif (TPY) at aa 398–400 in the E2 tail plays a critical role in this interaction. This interaction has been examined with virus containing mutations at two positions in this conserved domain, T398A and Y400N. The viruses produced have very low infectivity (as determined by particle : p.f.u. ratios); however, there appears to be no defect in assembly, as the virus has wild-type density and electron microscopy shows assembled particles with no obvious aberrant structural changes. The loss of infectivity in the double mutant is accompanied by the loss of the ability to fuse cells after brief exposure to acid pH. These data support the idea that these residues are vital for production of infectious/functional virus; however, they are dispensable for assembly. These results, combined with other published observations, expand our understanding of the interaction of the E2 endodomain with the capsid protein.}, journal={JOURNAL OF GENERAL VIROLOGY}, author={West, J and Brown, DT}, year={2006}, month={Mar}, pages={657–664} }
 @article{mudiganti_hernandez_ferreira_brown_2006, title={Sindbis virus infection of two model insect cell systems - A comparative study}, volume={122}, DOI={10.1016/j.virusres.2006.06.007}, abstractNote={Sindbis, the prototype of the Alphaviruses causes mosquito-borne diseases in mammals and replicates in a wide variety of vertebrate and invertebrate cell cultures. This characteristic can be exploited to use the vast array of Drosophila genetic information available for investigations of the interaction of Sindbis virus with an alternate invertebrate host. For this purpose, a comparative study of Sindbis virus infection of Schnieder-2 Drosophila (S2) cells to cells of the mosquito Aedes albopictus (clone U4.4) was undertaken. After infection, vertebrate cells die within 24–48 h, while invertebrate cell cultures survive an acute phase of infection and become persistently infected. In this study, infection of a model Drosophila system, S2 cells, was compared to U4.4 cells. Virus production, the time course of the establishment of persistence and changes in growth properties of the S2 cells upon infection, were studied in comparison to those of the U4.4 cells. S2 cells survived acute Sindbis infection without any significant cytopathology and continued to produce low levels of virus characteristic of persistently infected cells. S2 cells produced 10 PFU/cell on day 1 post-infection, which falls to 2 PFU/cell on day 2. This result is in contrast to U4.4 cells, which produce peak virus titer on day 2 post-infection and establish persistence by day 5. Onset of the persistent phase of infection of either U4.4 or S2 cells did not result in any change in morphology or growth characteristics. This study establishes S2 cells as an additional invertebrate model system to study the interactions of an invertebrate host with Sindbis virus.}, number={1-2}, journal={Virus Research}, author={Mudiganti, U. and Hernandez, R. and Ferreira, D. and Brown, D. T.}, year={2006}, pages={28–34} }
 @article{whitehurst_willis_sinodis_hernandez_brown_2006, title={Single and multiple deletions in the transmembrane domain of the Sindbis virus E2 glycoprotein identify a region critical for normal virus growth}, volume={347}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2005.11.029}, abstractNote={Sindbis virus is composed of two nested T = 4 icosahedral protein shells containing 240 copies each of three structural proteins: E1, E2, and Capsid in a 1:1:1 stoichiometric ratio. E2 is a 423 amino acid glycoprotein with a membrane spanning domain 26 amino acids in length and a 33 amino acid cytoplasmic endodomain. The interaction of the endodomain with the nucleocapsid is an essential step in virus maturation and directs the formation of the outer protein shell as envelopment occurs. A previous study had determined that deletions in the transmembrane domain could affect virus assembly and infectivity (Hernandez et al., 2003. J. Virol. 77 (23), 12710-12719). Unexpectedly, a single deletion mutant (from 26 to 25 amino acids) resulted in a 1000-fold decrease in infectious virus production while another deletion of eight amino acids had no affect on infectious virus production. To further investigate the importance of these mutants, other single deletion mutants and another eight amino acid deletion mutant were constructed. We found that deletions located closer to the cytoplasmic (inner leaflet) of the membrane bilayer had a more detrimental effect on virus assembly and infectivity than those located closer to the luminal (outer leaflet) of the membrane bilayer. We also found that selective pressure can restore single amino acid deletions in the transmembrane domain but not necessarily to the wild type sequence. The partial restoration of an eight amino acid deletion (from 18 to 22 amino acids) also partially restored infectious virus production. The amount of infectious virus produced by this revertant was equivalent to that produced for the four amino acid deletion produced by site directed mutagenesis. These results suggest that the position of the deletion and the length of the C terminal region of the E2 transmembrane domain is vital for normal virus production. Deletion mutants resulting in decreased infectivity produce particles that appear to be processed and transported correctly suggesting a role involved in virus entry.}, number={1}, journal={VIROLOGY}, author={Whitehurst, CB and Willis, JH and Sinodis, CN and Hernandez, R and Brown, DT}, year={2006}, month={Mar}, pages={199–207} }
 @article{sharp_nelson_brown_tomer_2006, title={Structural characterization of the E2 glycoprotein from Sindbis by lysine biotinylation and LC-MS/MS}, volume={348}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2005.12.020}, abstractNote={Sindbis is an Alphavirus capable of infecting and replicating in both vertebrate and invertebrate hosts. Mature Sindbis virus particles consist of an inner capsid surrounded by a host-derived lipid bilayer, which in turn is surrounded by a protein shell consisting of the E1 and E2 glycoproteins. While a homolog of the E1 glycoprotein has been structurally characterized, the amount of structural data on the E2 glycoprotein is considerably less. In this study, the organization of the E2 glycoprotein was probed by surface biotinylation of intact virions. The virus remained fully infectious, demonstrating that the biotinylation did not alter the topology of the proteins involved in infection. Seven sites of modification were identified in the E2 glycoprotein (K70, K76, K97, K131, K149, K202, and K235), while one site of modification in the E1 glycoprotein (K16) was identified, confirming that the E1 protein is almost completely buried in the virus structure.}, number={1}, journal={VIROLOGY}, author={Sharp, JS and Nelson, S and Brown, D and Tomer, KB}, year={2006}, month={Apr}, pages={216–223} }
 @article{nelson_hernandez_ferreira_brown_2005, title={In vivo processing and isolation of furin protease-sensitive alphavirus glycoproteins: a new technique for producing mutations in virus assembly}, volume={332}, ISSN={["0042-6822"]}, DOI={10.1016/j.virol.2004.12.013}, abstractNote={Sindbis virus particles are composed of three structural proteins (Capsid/E2/E1). In the mature virion the E1 glycoprotein is organized in a highly constrained, energy-rich conformation. It is hypothesized that this energy is utilized to drive events that deliver the viral genome to the cytoplasm of a host cell. The extraction of the E1 glycoprotein from virus membranes with detergent results in disulfide-bridge rearrangement and the collapse of the protein to a number of low-energy, non-native configurations. In a new approach to the production of membrane-free membrane glycoproteins, furin protease recognition motifs were installed at various positions in the E1 glycoprotein ectodomain. Proteins containing the furin-sensitive sites undergo normal folding and assembly in the endoplasmic reticulum and only experience the consequence of the mutation during transport to the cell surface. Processing by furin in the Golgi results in the release of the protein from the membrane. Processing of the proteins also impacts the envelopment of the nucleocapsid in the modified plasma membrane. This technique provides a unique method for studying the mechanism of virus assembly and protein structure without altering crucial early events in protein assembly, folding, and maturation.}, number={2}, journal={VIROLOGY}, author={Nelson, S and Hernandez, R and Ferreira, D and Brown, DT}, year={2005}, month={Feb}, pages={629–639} }
 @article{hernandez_ferreira_sinodis_litton_brown_2005, title={Single amino acid insertions at the junction of the Sindbis virus e2 transmembrane domain and endodomain disrupt virus envelopment and alter infectivity}, volume={79}, DOI={10.1128/JVI.79.7682-7697.2005}, number={12}, journal={Journal of Virology}, author={Hernandez, R. and Ferreira, D. and Sinodis, C. and Litton, K. and Brown, D. T.}, year={2005}, pages={7682–7697} }
 @inbook{altunay_brown_byrd_dean_2005, series={Lecture Notes in Computer Science}, title={Trust-Based Secure Workflow Path Construction}, volume={3826}, ISBN={9783540749738 9783540749745}, ISSN={0302-9743 1611-3349}, url={http://dx.doi.org/10.1007/11596141_29}, DOI={10.1007/11596141_29}, abstractNote={Security and trust relationships between services significantly govern their willingness to collaborate and participate in a workflow. Existing workflow tools do not consider such relationships as an integral part of their planning logic: rather, they approach security as a run-time issue. We present a workflow management framework that fully integrates trust and security into the workflow planning logic. It considers not only trust relationships between the workflow requestor and individual services, but also trust relationships among the services themselves. It allows each service owner to define an upper layer of collaboration policies (rules that specify the terms under which participation in a workflow is allowed) and integrates them into the planning logic. Services that are unfit for collaboration due to security violations are replaced at the planning stage. This approach increases the services owners’ control over the workflow path, their willingness for collaboration, and avoids run-time security failures.}, booktitle={Service-Oriented Computing – ICSOC 2007}, publisher={Springer Berlin Heidelberg}, author={Altunay, M. and Brown, D. and Byrd, G. and Dean, R.}, editor={Benatallah, B. and Casati, F. and Traverso, P.Editors}, year={2005}, pages={382–395}, collection={Lecture Notes in Computer Science} }
 @article{paredes_ferreira_horton_saad_tsuruta_johnston_klimstra_ryman_hernandez_chiu_et al._2004, title={Conformational changes in Sindbis virions resulting from exposure to low pH and interactions with cells suggest that cell penetration may occur at the cell surface in the absence of membrane fusion}, volume={324}, DOI={10.1016/j.virus.2004.03.046}, number={2}, journal={Virology}, author={Paredes, A. M. and Ferreira, D. and Horton, M. and Saad, A. and Tsuruta, H. and Johnston, R. and Klimstra, W. and Ryman, K. and Hernandez, R. and Chiu, W. and et al.}, year={2004}, pages={373–386} }
 @article{paredes_ferreira_horton_saad_tsuruta_johnston_klimstra_ryman_hernandez_chiu_et al._2004, title={Conformational changes in Sindbis virions resulting from exposure to low pH and interactions with cells suggest that cell penetration may occur at the cell surface in the absence of membrane fusion}, volume={324}, ISSN={0042-6822}, url={http://dx.doi.org/10.1016/j.virol.2004.03.046}, DOI={10.1016/j.virol.2004.03.046}, abstractNote={Alphaviruses have the ability to induce cell–cell fusion after exposure to acid pH. This observation has served as an article of proof that these membrane-containing viruses infect cells by fusion of the virus membrane with a host cell membrane upon exposure to acid pH after incorporation into a cell endosome. We have investigated the requirements for the induction of virus-mediated, low pH-induced cell–cell fusion and cell–virus fusion. We have correlated the pH requirements for this process to structural changes they produce in the virus by electron cryo-microscopy. We found that exposure to acid pH was required to establish conditions for membrane fusion but that membrane fusion did not occur until return to neutral pH. Electron cryo-microscopy revealed dramatic changes in the structure of the virion as it was moved to acid pH and then returned to neutral pH. None of these treatments resulted in the disassembly of the virus protein icosahedral shell that is a requisite for the process of virus membrane–cell membrane fusion. The appearance of a prominent protruding structure upon exposure to acid pH and its disappearance upon return to neutral pH suggested that the production of a “pore”-like structure at the fivefold axis may facilitate cell penetration as has been proposed for polio (J. Virol. 74 (2000) 1342) and human rhino virus (Mol. Cell 10 (2002) 317). This transient structural change also provided an explanation for how membrane fusion occurs after return to neutral pH. Examination of virus–cell complexes at neutral pH supported the contention that infection occurs at the cell surface at neutral pH by the production of a virus structure that breaches the plasma membrane bilayer. These data suggest an alternative route of infection for Sindbis virus that occurs by a process that does not involve membrane fusion and does not require disassembly of the virus protein shell.}, number={2}, journal={Virology}, publisher={Elsevier BV}, author={Paredes, Angel M and Ferreira, Davis and Horton, Michelle and Saad, Ali and Tsuruta, Hiro and Johnston, Robert and Klimstra, William and Ryman, Kate and Hernandez, Raquel and Chiu, Wah and et al.}, year={2004}, month={Jul}, pages={373–386} }
 @article{hernandez_nelson_salm_brown_alpert_2004, title={Rapid preparative purification of West Nile and Sindbis virus PCR products utilizing a microbore anion-exchange column}, volume={120}, DOI={10.1016/j.viromet.2004.04.013}, number={2}, journal={Journal of Virological Methods}, author={Hernandez, R. and Nelson, S. and Salm, J. R. and Brown, D. T. and Alpert, A. J.}, year={2004}, pages={141–149} }
 @article{hernandez_nelson_salm_brown_alpert_2004, title={Rapid preparative purification of West Nile and Sindbis virus PCR products utilizing a microbore anion-exchange column}, volume={120}, ISSN={0166-0934}, url={http://dx.doi.org/10.1016/j.jviromet.2004.04.013}, DOI={10.1016/j.jviromet.2004.04.013}, abstractNote={Analysis and purification of specific PCR products from PCR reactions can be problematic due to several issues relating to amplification and low product yield. The use of HPLC as a preparative tool in PCR product analysis is common but has not replaced traditional electrophoretic techniques for purifying DNA to be used in subsequent experiments. Gel purification of PCR products can result in a net loss greater than 50% of the starting DNA amount. Thus, this method of recovery can become the limiting factor in the overall cloning protocol. This paper describes a simple and relatively inexpensive micro-preparative HPLC method to purify and analyze nM quantities of DNA. A microbore polyethyleneimine-based anion-exchange column fractionates PCR mixtures in less than 40 min with a recovery of the purified specific product as high as 80%, thus eliminating the need for gel purification. Using this method, nested PCR products from Sindbis virus differing by 18 bp in some cases and a 277 bp fragment from West Nile virus were resolved and quantified. This method differs from existing methodologies because separation is based on size and charge as well as the overall G + C content of the PCR product.}, number={2}, journal={Journal of Virological Methods}, publisher={Elsevier BV}, author={Hernandez, Raquel and Nelson, Steevenson and Salm, Jeffery R and Brown, Dennis T and Alpert, Andrew J}, year={2004}, month={Sep}, pages={141–149} }
 @article{hernandez_sinodis_horton_ferreira_yang_brown_2003, title={Deletions in the transmembrane domain of a Sindbis virus glycoprotein alter virus infectivity, stability, and host range}, volume={77}, ISSN={["0022-538X"]}, DOI={10.1128/JVI.77.23.12710-12719.2003}, abstractNote={ABSTRACT}, number={23}, journal={JOURNAL OF VIROLOGY}, author={Hernandez, R and Sinodis, C and Horton, M and Ferreira, D and Yang, CN and Brown, DT}, year={2003}, month={Dec}, pages={12710–12719} }
 @article{ferreira_hernandez_horton_brown_2003, title={Morphological variants of Sindbis virus produced by a mutation in the capsid protein}, volume={307}, ISSN={["0042-6822"]}, DOI={10.1016/S0042-6822(02)00034-X}, abstractNote={Sindbis virus is a complex aggregate of RNA, protein and lipid. The virus is organized as two nested T = 4 icosahedral protein shells between which is sandwiched a lipid bilayer. The virus RNA resides within the inner protein shell. The inner protein shell is attached to the outer protein shell through contacts to proteins in the outer shell, which penetrate the lipid bilayer. The data presented in the following manuscript show that mutations in the capsid protein can result in the assembly of the virus structural proteins into icosahedra of different triangulation numbers. The triangulation numbers calculated, for these morphological variants, follow the sequence T = 4, 9, 16, 25 and 36. All fall into the class P = 1 of icosadeltahedra as was predicted by Caspar and Klug (1962). The data support their hypothesis that families of icosahedra would be developed by altering the distance between the points of insertion of the five-fold axis. This capsid protein defect also results in the incorporation of much of the capsid protein, into large cytoplasmic aggregates of protein and RNA. These observations support models suggesting that the geometry of a pre-formed nucleocapsid organizes the assembly of the virus membrane proteins into a structure of identical configuration and argues against models suggesting that assembly of the membrane glycoproteins directs the assembly of the nucleocapsid.}, number={1}, journal={VIROLOGY}, author={Ferreira, D and Hernandez, R and Horton, M and Brown, DT}, year={2003}, month={Mar}, pages={54–66} }
 @article{hernandez_luo_brown_2001, title={Exposure to low pH is not required for penetration of mosquito cells by Sindbis virus}, volume={75}, ISSN={["0022-538X"]}, DOI={10.1128/jvi.75.4.2010-2013.2001}, abstractNote={ABSTRACT}, number={4}, journal={JOURNAL OF VIROLOGY}, author={Hernandez, R and Luo, TC and Brown, DT}, year={2001}, month={Feb}, pages={2010–2013} }
 @article{thomas_brown_franzen_boxer_2001, title={FTIR and resonance Raman studies of nitric oxide binding to H93G cavity mutants of myoglobin}, volume={40}, ISSN={["0006-2960"]}, DOI={10.1021/bi011440l}, abstractNote={Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a five- or six-coordinate Fe-NO complex. The H93G mutation eliminates the covalent attachment between the protein and the proximal ligand, allowing NO to bind H93G possibly from the proximal side of the heme rather than the typical diatomic binding pocket on the distal side. The question of whether NO binds on the distal or proximal side was addressed by FTIR spectroscopy of the N-O vibrational frequency nuN(-O) for a set of Mb mutants that perturb the electrostatic environment of the heme pocket. Vibrational spectra of five- and six-coordinate MbNO complexes indicate that nu(N-O) shifts (by as much as 26 cm(-1)) to higher energies for the distal mutants H64V and H64V/H93G relative to the energies of wild-type and H93G MbNO, while nu(N-O) is not affected by the proximal side mutation S92A/H93G. This result suggests that NO binds on the distal side of heme in the five- and six-coordinate MbNO complexes of H93G. Additionally, values of the Fe-NO vibrational frequency nu(Fe-NO) as measured by resonance Raman spectroscopy are reported for the distal and proximal double mutants of H93G. These results suggest that nu(Fe-NO) is not very sensitive to mutations that perturb the electrostatic environment of the heme pocket, leading to the observation that nu(N-O) and nu(Fe-NO) are not quantitatively correlated for the MbNO complexes presented here. Furthermore, nu(N-O) and nu(Fe-NO) do not correlate well with equilibrium constants for imidazole binding to the five-coordinate MbNO complexes of the H93G double mutants. The data presented here do not appear to support the presence of pi-back-bonding or an inverse trans effect of NO binding in Mb mutants that alter the electrostatic environment of the heme pocket.}, number={49}, journal={BIOCHEMISTRY}, author={Thomas, MR and Brown, D and Franzen, S and Boxer, SG}, year={2001}, month={Dec}, pages={15047–15056} }
 @article{pletnev_zhang_mukhopadhyay_fisher_hernandez_brown_baker_rossmann_kuhn_2001, title={Locations of carbohydrate sites on alphavirus glycoproteins show that E1 forms an icosahedral scaffold}, volume={105}, ISSN={["0092-8674"]}, DOI={10.1016/S0092-8674(01)00302-6}, abstractNote={There are 80 spikes on the surface of Sindbis virus arranged as an icosahedral surface lattice. Each spike consists of three copies of each of the glycoproteins E1 and E2. There are two glycosylation sites on E1 and two on E2. These four sites have been located by removal of the glycosylation recognition motifs using site-specific mutagenesis, followed by cryoelectron microscopy. The positions of these sites have demonstrated that E2 forms the protruding spikes and that E1 must be long and narrow, lying flat on the viral surface, forming an icosahedral scaffold analogous to the arrangement of the E glycoprotein in flaviviruses. This arrangement of E1 leads to both dimeric and trimeric intermolecular contacts, consistent with the observed structural changes that occur on fusion with host cell membranes, suggesting a similar fusion mechanism for alpha- and flaviviruses.}, number={1}, journal={CELL}, author={Pletnev, SV and Zhang, W and Mukhopadhyay, S and Fisher, BR and Hernandez, R and Brown, DT and Baker, TS and Rossmann, MG and Kuhn, RJ}, year={2001}, month={Apr}, pages={127–136} }
 @article{hernandez_lee_nelson_brown_2000, title={A single deletion in the membrane-proximal region of the Sindbis virus glycoprotein E2 endodomain blocks virus assembly}, volume={74}, ISSN={["1098-5514"]}, DOI={10.1128/JVI.74.9.4220-4228.2000}, abstractNote={ABSTRACT}, number={9}, journal={JOURNAL OF VIROLOGY}, author={Hernandez, R and Lee, H and Nelson, C and Brown, DT}, year={2000}, month={May}, pages={4220–4228} }
 @article{phinney_brown_2000, title={Sindbis virus glycoprotein E1 is divided into two discrete domains at amino acid 129 by disulfide bridge connections}, volume={74}, ISSN={["0022-538X"]}, DOI={10.1128/JVI.74.19.9313-9316.2000}, abstractNote={ABSTRACT}, number={19}, journal={JOURNAL OF VIROLOGY}, author={Phinney, BS and Brown, DT}, year={2000}, month={Oct}, pages={9313–9316} }
 @article{phinney_blackburn_brown_2000, title={The surface conformation of sindbis virus glycoproteins E1 and E2 at neutral and low pH, as determined by mass spectrometry-based mapping}, volume={74}, ISSN={["0022-538X"]}, DOI={10.1128/JVI.74.12.5667-5678.2000}, abstractNote={ABSTRACT}, number={12}, journal={JOURNAL OF VIROLOGY}, author={Phinney, BS and Blackburn, K and Brown, DT}, year={2000}, month={Jun}, pages={5667–5678} }
 @article{karpf_brown_1998, title={Comparison of Sindbis virus-induced pathology in mosquito and vertebrate cell cultures}, volume={240}, ISSN={["0042-6822"]}, DOI={10.1006/viro.1997.8914}, abstractNote={We have compared Sindbis virus-induced cytopathology in vertebrate and mosquito (Aedes albopictus) cell cultures. It has been shown that vertebrate cells undergo apoptosis when infected by Sindbis virus and this was confirmed here using hamster cells (BHK). The occurrence of cell death in Sindbis virus-infected A. albopictus cells is a cell clone-specific phenomenon and, unlike in BHK cell cultures, mosquito cell death does not correlate with a large induction of apoptosis, as determined by assays testing for DNA fragmentation or reduced cellular DNA content. Cell cycle distribution changes were observed in Sindbis virus-infected BHK and C7-10 cell cultures, and the changes are distinct, both in the time of induction and the types of perturbations. In Sindbis virus-infected BHK cells, the major cell cycle profile change is the early accumulation of cells with sub-G1 DNA content and a corresponding reduction in the proportion of cells in G1 and G2/M. For Sindbis virus-infected C7-10 cells, the major perturbations are an increased proportion of cells showing G2/M or polyploid DNA content and a reduction in the proportion of G1 and S phase cells. These data suggest that the pathology induced in mosquito cell cultures by Sindbis virus infection may be distinct from the pathology which appears in vertebrate cell cultures.}, number={2}, journal={VIROLOGY}, author={Karpf, AR and Brown, DT}, year={1998}, month={Jan}, pages={193–201} }
 @article{chan_lu_bell_motamedi_frederickson_brown_kovach_welch_1998, title={Laser assisted soldering: Microdroplet accumulation with a microjet device}, volume={23}, DOI={10.1002/(sici)1096-9101(1998)23:4<213::aid-lsm4>3.0.co;2-8}, abstractNote={We investigated the feasibility of a microjet to dispense protein solder for laser assisted soldering.}, number={4}, journal={Lasers in Surgery and Medicine}, author={Chan, E. K. and Lu, Q. and Bell, B. and Motamedi, M. and Frederickson, C. and Brown, D. T. and Kovach, I. S. and Welch, A. J.}, year={1998}, pages={213–220} }
 @article{karpf_lenches_strauss_strauss_brown_1997, title={Superinfection exclusion of alphaviruses in three mosquito cell lines persistently infected with sindbis virus}, volume={71}, number={9}, journal={Journal of Virology}, author={Karpf, A. R. and Lenches, E. and Strauss, E. G. and Strauss, J. H. and Brown, D. T.}, year={1997}, pages={7119–7123} }
 @article{carleton_brown_1997, title={The formation of intramolecular disulfide bridges is required for induction of the Sindbis virus mutant TS23 phenotype}, volume={71}, number={10}, journal={Journal of Virology}, author={Carleton, M. and Brown, D. T.}, year={1997}, pages={7696–7703} }