نتائج البحث - "Gutiérrez, Marlen"

المصدر: National Center for Emerging and Zoonotic Infectious Diseases [https://www.cdc.gov/ncezid/dvbd/about.htmlTest]. ; Carrillo-Hernández MY, Ruiz-Saenz J, Villamizar LJ, Gómez-Rangel SY, Martínez-Gutierrez M. Co-circulation and simultaneous co-infection of dengue, chikungunya, and zika viruses in patients with febrile syndrome at the Colombian-Venezuelan border. BMC Infect Dis. 2018;18(1):61. https://doi.org/10.1186/s12879-018-2976-1Test. ; Mercado M, Acosta-Reyes J, Parra E, Pardo L, Rico A, Campo A, et al. Clinical and histopathological features of fatal cases with dengue and chikungunya virus co-infection in Colombia, 2014 to 2015. Eurosurveillance. 2016;21(22):30244. ; Strauss JH, Strauss EG. The alphaviruses: gene expression, replication, and evolution. Microbiol Mol Biol Rev. 1994;58(3):491–562. ; Halstead SB. ....

مصطلحات موضوعية: Zika virus, Chikungunya virus, Indole alkaloids, Molecular docking, Antiviral

وصف الملف: application/pdf

العلاقة: BMC Complementary Medicine and Therapies; https://bmccomplementmedtherapies.biomedcentral.com/articles/10.1186/s12906-021-03386-zTest; http://hdl.handle.net/20.500.12494/43636Test; Monsalve-Escudero, L.M., Loaiza-Cano, V., Pájaro-González, Y. et al. (2021) Indole alkaloids inhibit zika and chikungunya virus infection in different cell lines. BMC Complement Med Ther 21, 216 (2021). https://doi.org/10.1186/s12906-021-03386-zTest

الإتاحة: https://doi.org/20.500.12494/43636Test
https://doi.org/10.1186/s12879-018-2976-1Test
https://doi.org/10.3201/eid2104.141723Test
https://doi.org/10.1371/journal.pntd.0000389Test
https://doi.org/10.1016/j.trstmh.2010.01.011Test
https://doi.org/10.1007/s00705-006-0903-zTest
https://doi.org/10.1016/j.jneuroim.2017.03.001Test
https://doi.org/10.1056/NEJMoa1600651Test
https://doi.org/10.1056/NEJMoa1605564Test
https://doi.org/10.1099/vir.0.057422-0Test

View record in BASE

النص الكامل

4

دورية أكاديمية

Indole alkaloids inhibit zika and chikungunya virus infection in different cell lines

المؤلفون: Monsalve Escudero, Laura, Loaiza Cano, Vanessa, Pajaro Gonzalez, Yina, Oliveros Diaz, Andres, Diaz Castillo, Fredyc, Quiñones, Wiston, Robledo, Sara, Martínez Gutiérrez, Marlén

مصطلحات موضوعية: Zika virus, Chikungunya virus, Indole alkaloids, Molecular docking, Antiviral

وصف الملف: application/pdf

العلاقة: https://bmccomplementmedtherapies.biomedcentral.com/articles/10.1186/s12906-021-03386-zTest; BMC Complementary Medicine and Therapies; National Center for Emerging and Zoonotic Infectious Diseases [https://www.cdc.gov/ncezid/dvbd/about.htmlTest].; Carrillo-Hernández MY, Ruiz-Saenz J, Villamizar LJ, Gómez-Rangel SY, Martínez-Gutierrez M. Co-circulation and simultaneous co-infection of dengue, chikungunya, and zika viruses in patients with febrile syndrome at the Colombian-Venezuelan border. BMC Infect Dis. 2018;18(1):61. https://doi.org/10.1186/s12879-018-2976-1Test.; Mercado M, Acosta-Reyes J, Parra E, Pardo L, Rico A, Campo A, et al. Clinical and histopathological features of fatal cases with dengue and chikungunya virus co-infection in Colombia, 2014 to 2015. Eurosurveillance. 2016;21(22):30244.; Strauss JH, Strauss EG. The alphaviruses: gene expression, replication, and evolution. Microbiol Mol Biol Rev. 1994;58(3):491–562.; Halstead SB. Reappearance of chikungunya, formerly called dengue, in the Americas. Emerg Infect Dis. 2015;21(4):557–61. https://doi.org/10.3201/eid2104.141723Test.; Sissoko D, Malvy D, Ezzedine K, Renault P, Moscetti F, Ledrans M, et al. Post-epidemic chikungunya disease on Reunion Island: course of rheumatic manifestations and associated factors over a 15-month period. PLoS Negl Trop Dis. 2009;3(3):e389. https://doi.org/10.1371/journal.pntd.0000389Test.; Manimunda SP, Vijayachari P, Uppoor R, Sugunan AP, Singh SS, Rai SK, et al. Clinical progression of chikungunya fever during acute and chronic arthritic stages and the changes in joint morphology as revealed by imaging. Trans R Soc Trop Med Hyg. 2010;104(6):392–9. https://doi.org/10.1016/j.trstmh.2010.01.011Test.; Baronti C, Piorkowski G, Charrel RN, Boubis L, Leparc-Goffart I, de Lamballerie X. Complete coding sequence of zika virus from a French polynesia outbreak in 2013. Genome Announc. 2014;2(3):e00500–14.; Kuno G, Chang G-J. Full-length sequencing and genomic characterization of Bagaza, Kedougou, and Zika viruses. Arch Virol. 2007;152(4):687–96. https://doi.org/10.1007/s00705-006-0903-zTest.; Song B-H, Yun S-I, Woolley M, Lee Y-M. Zika virus: history, epidemiology, transmission, and clinical presentation. J Neuroimmunol. 2017;308:50–64. https://doi.org/10.1016/j.jneuroim.2017.03.001Test.; Mlakar J, Korva M, Tul N, Popović M, Poljšak-Prijatelj M, Mraz J, et al. Zika virus associated with microcephaly. N Engl J Med. 2016;374(10):951–8. https://doi.org/10.1056/NEJMoa1600651Test.; Parra B, Lizarazo J, Jiménez-Arango JA, Zea-Vera AF, González-Manrique G, Vargas J, et al. Guillain–Barré syndrome associated with Zika virus infection in Colombia. N Engl J Med. 2016;375(16):1513–23. https://doi.org/10.1056/NEJMoa1605564Test.; Rainey SM, Shah P, Kohl A, Dietrich I. Understanding the Wolbachia-mediated inhibition of arboviruses in mosquitoes: progress and challenges. J Gen Virol. 2014;95(3):517–30. https://doi.org/10.1099/vir.0.057422-0Test.; Espinal MA, Andrus JK, Jauregui B, Waterman SH, Morens DM, Santos JI, et al. Emerging and reemerging Aedes-transmitted arbovirus infections in the region of the Americas: implications for health policy. Am J Public Health. 2019;109(3):387–92. https://doi.org/10.2105/AJPH.2018.304849Test.; Pattnaik A, Sahoo BR, Pattnaik AK. Current status of Zika virus vaccines: successes and challenges. Vaccines. 2020;8(2):266. https://doi.org/10.3390/vaccines8020266Test.; Silva JV Jr, Lopes TR, de Oliveira-Filho EF, Oliveira RA, Durães-Carvalho R, Gil LH. Current status, challenges and perspectives in the development of vaccines against yellow fever, dengue, Zika and chikungunya viruses. Acta Trop. 2018;182:257–63. https://doi.org/10.1016/j.actatropica.2018.03.009Test.; Ghildiyal R, Gabrani R. Antiviral therapeutics for chikungunya virus. Expert opinion on therapeutic patents. 2020;30(6):467–80. https://doi.org/10.1080/13543776.2020.1751817Test.; Goh VSL, Mok C-K, Chu JJH. Antiviral natural products for arbovirus infections. Molecules. 2020;25(12):2796. https://doi.org/10.3390/molecules25122796Test.; Pielnaa P, Al-Saadawe M, Saro A, Dama MF, Zhou M, Huang Y, et al. Zika virus-spread, epidemiology, genome, transmission cycle, clinical manifestation, associated challenges, vaccine and antiviral drug development. Virology. 2020;543:34–42. https://doi.org/10.1016/j.virol.2020.01.015Test.; Newman DJ, Cragg GM. Natural products as sources of new drugs over the nearly four decades from 01/1981 to 09/2019. J Nat Prod. 2020;83(3):770–803. https://doi.org/10.1021/acs.jnatprod.9b01285Test.; Dey A, Mukherjee A, Chaudhury M: Alkaloids from apocynaceae: origin, pharmacotherapeutic properties, and structure-activity studies. In: Studies in Natural Products Chemistry. Volume 52, edn.: Elsevier; 2017: 373–488.; Achenbach H, Benirschke M, Torrenegra R. Alkaloids and other compounds from seeds of Tabernaemontana cymosa. Phytochemistry. 1997;45(2):325–35. https://doi.org/10.1016/S0031-9422Test(96)00645-0.; Kadam RU, Wilson IA. Structural basis of influenza virus fusion inhibition by the antiviral drug Arbidol. Proc Natl Acad Sci. 2017;114(2):206–14. https://doi.org/10.1073/pnas.1617020114Test.; Devogelaere B, Berke JM, Vijgen L, Dehertogh P, Fransen E, Cleiren E, et al. TMC647055, a potent nonnucleoside hepatitis C virus NS5B polymerase inhibitor with cross-genotypic coverage. Antimicrob Agents Chemother. 2012;56(9):4676–84. https://doi.org/10.1128/AAC.00245-12Test.; Ruiz FX, Hoang A, Das K, Arnold E. Structural basis of HIV-1 inhibition by nucleotide-competing reverse transcriptase inhibitor INDOPY-1. J Med Chem. 2019;62(21):9996–10002. https://doi.org/10.1021/acs.jmedchem.9b01289Test.; Gómez-Calderón C, Mesa-Castro C, Robledo S, Gómez S, Bolivar-Avila S, Diaz-Castillo F, et al. Antiviral effect of compounds derived from the seeds of Mammea americana and Tabernaemontana cymosa on dengue and chikungunya virus infections. BMC Complement Altern Med. 2017;17(1):57. https://doi.org/10.1186/s12906-017-1562-1Test.; Monsalve-Escudero LM, Loaiza-Cano V, Zapata-Cardona MI, Quintero-Gil DC, Hernández-Mira E, Pájaro-González Y, et al. The antiviral and virucidal activities of voacangine and structural analogs extracted from Tabernaemontana cymosa depend on the dengue virus strain. Plants. 2021;10(7):1280. https://doi.org/10.3390/plants10071280Test.; Loaiza-Cano V, Monsalve-Escudero LM, Restrepo MP, Quintero-Gil DC, Pulido Muñoz SA, Galeano E, et al. In vitro and in silico anti-Arboviral activities of Dihalogenated phenolic Derivates of L-tyrosine. Molecules. 2021;26(11):3430. https://doi.org/10.3390/molecules26113430Test.; Denizot F, Lang R. Rapid colorimetric assay for cell growth and survival: modifications to the tetrazolium dye procedure giving improved sensitivity and reliability. J Immunol Methods. 1986;89(2):271–7. https://doi.org/10.1016/0022-1759Test(86)90368-6.; Sanner MF. Python: a programming language for software integration and development. J Mol Graph Model. 1999;17(1):57–61.; Trujillo-Correa AI, Quintero-Gil DC, Diaz-Castillo F, Quiñones W, Robledo SM, Martinez-Gutierrez M. In vitro and in silico anti-dengue activity of compounds obtained from Psidium guajava through bioprospecting. BMC Complement Altern Med. 2019;19(1):298. https://doi.org/10.1186/s12906-019-2695-1Test.; Lavi A, Ngan CH, Movshovitz-Attias D, Bohnuud T, Yueh C, Beglov D, et al. Detection of peptide-binding sites on protein surfaces: the first step toward the modeling and targeting of peptide-mediated interactions. Proteins: Structure, Function, and Bioinformatics. 2013;81(12):2096–105. https://doi.org/10.1002/prot.24422Test.; Brenke R, Kozakov D, Chuang G-Y, Beglov D, Hall D, Landon MR, et al. Fragment-based identification of druggable ‘hot spots’ of proteins using Fourier domain correlation techniques. Bioinformatics. 2009;25(5):621–7. https://doi.org/10.1093/bioinformatics/btp036Test.; Trott O, Olson AJ. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem. 2010;31(2):455–61. https://doi.org/10.1002/jcc.21334Test.; Wallace AC, Laskowski RA, Thornton JM. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng Des Sel. 1995;8(2):127–34. https://doi.org/10.1093/protein/8.2.127Test.; Mounce BC, Cesaro T, Carrau L, Vallet T, Vignuzzi M. Curcumin inhibits Zika and chikungunya virus infection by inhibiting cell binding. Antivir Res. 2017;142:148–57. https://doi.org/10.1016/j.antiviral.2017.03.014Test.; Wu L, Dai J, Zhao X, Chen Y, Wang G, Li K. Chloroquine enhances replication of influenza a virus a/WSN/33 (H1N1) in dose-, time-, and MOI-dependent manners in human lung epithelial cells A549. J Med Virol. 2015;87(7):1096–103. https://doi.org/10.1002/jmv.24135Test.; Diosa-Toro M, Troost B, Van De Pol D, Heberle AM, Urcuqui-Inchima S, Thedieck K, et al. Tomatidine, a novel antiviral compound towards dengue virus. Antivir Res. 2019;161:90–9. https://doi.org/10.1016/j.antiviral.2018.11.011Test.; Gulick RM, Lalezari J, Goodrich J, Clumeck N, DeJesus E, Horban A, et al. Maraviroc for previously treated patients with R5 HIV-1 infection. N Engl J Med. 2008;359(14):1429–41. https://doi.org/10.1056/NEJMoa0803152Test.; Nowicka-Sans B, Gong Y-F, McAuliffe B, Dicker I, Ho H-T, Zhou N, et al. In vitro antiviral characteristics of HIV-1 attachment inhibitor BMS−626529, the active component of the prodrug BMS-663068. Antimicrob Agents Chemother. 2012;56(7):3498–507. https://doi.org/10.1128/AAC.00426-12Test.; Wang Y-M, Lu J-W, Lin C-C, Chin Y-F, Wu T-Y, Lin L-I, et al. Antiviral activities of niclosamide and nitazoxanide against chikungunya virus entry and transmission. Antivir Res. 2016;135:81–90. https://doi.org/10.1016/j.antiviral.2016.10.003Test.; Abraham R, Mudaliar P, Jaleel A, Srikanth J, Sreekumar E. High throughput proteomic analysis and a comparative review identify the nuclear chaperone, Nucleophosmin among the common set of proteins modulated in chikungunya virus infection. J Proteome. 2015;120:126–41. https://doi.org/10.1016/j.jprot.2015.03.007Test.; Abraham R, Singh S, Nair SR, Hulyalkar NV, Surendran A, Jaleel A, et al. Nucleophosmin (NPM1)/B23 in the proteome of human astrocytic cells restricts chikungunya virus replication. J Proteome Res. 2017;16(11):4144–55. https://doi.org/10.1021/acs.jproteome.7b00513Test.; Matusali G, Colavita F, Bordi L, Lalle E, Ippolito G, Capobianchi MR, et al. Tropism of the chikungunya virus. Viruses. 2019;11(2):175. https://doi.org/10.3390/v11020175Test.; Miner JJ, Diamond MS. Zika virus pathogenesis and tissue tropism. Cell Host Microbe. 2017;21(2):134–42. https://doi.org/10.1016/j.chom.2017.01.004Test.; Ferraz AC, TdFS M, da Cruz Nizer WS, dos Santos M, Tótola AH, JMS F, et al. Virucidal activity of proanthocyanidin against Mayaro virus. Antivir Res. 2019;168:76–81. https://doi.org/10.1016/j.antiviral.2019.05.008Test.; Sharma N, Murali A, Singh SK, Giri R. Epigallocatechin gallate, an active green tea compound inhibits the Zika virus entry into host cells via binding the envelope protein. Int J Biol Macromol. 2017;104(Pt A):1046–54. https://doi.org/10.1016/j.ijbiomac.2017.06.105Test.; Lai Z-Z, Ho Y-J, Lu J-W. Harringtonine inhibits Zika virus infection through multiple mechanisms. Molecules. 2020;25(18):4082. https://doi.org/10.3390/molecules25184082Test.; Kaur P, Thiruchelvan M, Lee RCH, Chen H, Chen KC, Ng ML, et al. Inhibition of chikungunya virus replication by harringtonine, a novel antiviral that suppresses viral protein expression. Antimicrob Agents Chemother. 2013;57(1):155–67. https://doi.org/10.1128/AAC.01467-12Test.; Lai Z-Z, Ho Y-J, Lu J-W. Cephalotaxine inhibits Zika infection by impeding viral replication and stability. Biochem Biophys Res Commun. 2020;522(4):1052–8. https://doi.org/10.1016/j.bbrc.2019.12.012Test.; Passos GFS, Gomes MGM, TMd A, JXd A-J, SJMd S, JPM C, et al. Computer-aided design, synthesis, and antiviral evaluation of novel acrylamides as potential inhibitors of E3-E2-E1 glycoproteins complex from chikungunya virus. Pharmaceuticals. 2020;13(7):141.; Saxena T, Tandon B, Sharma S, Chameettachal S, Ray P, Ray AR, et al. Combined miRNA and mRNA signature identifies key molecular players and pathways involved in chikungunya virus infection in human cells. PLoS One. 2013;8(11):e79886. https://doi.org/10.1371/journal.pone.0079886Test.; Mehrbod P, Ande SR, Alizadeh J, Rahimizadeh S, Shariati A, Malek H, et al. The roles of apoptosis, autophagy and unfolded protein response in arbovirus, influenza virus, and HIV infections. Virulence. 2019;10(1):376–413. https://doi.org/10.1080/21505594.2019.1605803Test.; Franco EJ, Rodriquez JL, Pomeroy JJ, Hanrahan KC, Brown AN. The effectiveness of antiviral agents with broad-spectrum activity against chikungunya virus varies between host cell lines. Antivir Chem Chemother. 2018;26:2040206618807580.; Martínez-Gutierrez M, Castellanos JE, Gallego-Gómez JC. Statins reduce dengue virus production via decreased virion assembly. Intervirology. 2011;54(4):202–16. https://doi.org/10.1159/000321892Test.; Huang C-T, Chao T-L, Kao H-C, Pang Y-H, Lee W-H, Hsieh C-H, Chang S-Y, Huang H-C, Juan H-F: Enhancement of the IFN-β-induced host signature informs repurposed drugs for COVID-19. Heliyon 2020:e05646, 6, 12, DOI: https://doi.org/10.1016/j.heliyon.2020.e05646Test.; Brooks MJ, Burtseva EI, Ellery PJ, Marsh GA, Lew AM, Slepushkin AN, et al. Antiviral activity of arbidol, a broad-spectrum drug for use against respiratory viruses, varies according to test conditions. J Med Virol. 2012;84(1):170–81. https://doi.org/10.1002/jmv.22234Test.; Samuel CE. Antiviral actions of interferons. Clin Microbiol Rev. 2001;14(4):778–809. https://doi.org/10.1128/CMR.14.4.778-809.2001Test.; Dong B, Xu L, Zhou A, Hassel BA, Lee X, Torrence PF, et al. Intrinsic molecular activities of the interferon-induced 2-5A-dependent RNase. J Biol Chem. 1994;269(19):14153–8. https://doi.org/10.1016/S0021-9258Test(17)36767-4.; Kottkamp AC, De Jesus E, Grande R, Brown JA, Jacobs AR, Lim JK, Stapleford KA. Atovaquone Inhibits Arbovirus Replication through the Depletion of Intracellular Nucleotides. J Virol. 2019;93(11):e00389–19. https://doi.org/10.1128/JVI.00389-19Test.; Marra RK, Kümmerle AE, Guedes GP. Barros CdS, Gomes RS, Cirne-Santos CC, Paixão ICN, Neves AP: quinolone-N-Acylhydrazone hybrids as potent Zika and chikungunya virus inhibitors. Bioorg Med Chem Lett. 2019;30(2):126881.; Xue L, Fang X, Hyman JM. Comparing the effectiveness of different strains of Wolbachia for controlling chikungunya, dengue fever, and zika. PLoS Negl Trop Dis. 2018;12(7):e0006666. https://doi.org/10.1371/journal.pntd.0006666Test.; Beltrán-Silva S, Chacón-Hernández S, Moreno-Palacios E, Pereyra-Molina J. Clinical and differential diagnosis: dengue, chikungunya and Zika. Revista Médica del Hospital General de México. 2018;81(3):146–53. https://doi.org/10.1016/j.hgmx.2016.09.011Test.; Chen H, Lao Z, Xu J, Li Z, Long H, Li D, et al. Antiviral activity of lycorine against Zika virus in vivo and in vitro. Virology. 2020;546:88–97. https://doi.org/10.1016/j.virol.2020.04.009Test.; Terstappen GC, Reggiani A. In silico research in drug discovery. Trends Pharmacol Sci. 2001;22(1):23–6. https://doi.org/10.1016/S0165-6147Test(00)01584-4.; Velásquez M, Drosos J, Gueto C, Márquez J, Vivas-Reyes R. Autodock-PM6 method to choose the better pose in molecular docking studies. Revista Colombiana de Química. 2013;42(1):101–24.; Plemper RK. Cell entry of enveloped viruses. Curr Opin Virol. 2011;1(2):92–100. https://doi.org/10.1016/j.coviro.2011.06.002Test.; https://hdl.handle.net/20.500.12494/43636Test; Monsalve-Escudero, L.M., Loaiza-Cano, V., Pájaro-González, Y. et al. (2021) Indole alkaloids inhibit zika and chikungunya virus infection in different cell lines. BMC Complement Med Ther 21, 216 (2021). https://doi.org/10.1186/s12906-021-03386-zTest

الإتاحة: https://doi.org/20.500.12494/43636Test
https://doi.org/10.1186/s12879-018-2976-1Test
https://doi.org/10.3201/eid2104.141723Test
https://doi.org/10.1371/journal.pntd.0000389Test
https://doi.org/10.1016/j.trstmh.2010.01.011Test
https://doi.org/10.1007/s00705-006-0903-zTest
https://doi.org/10.1016/j.jneuroim.2017.03.001Test
https://doi.org/10.1056/NEJMoa1600651Test
https://doi.org/10.1056/NEJMoa1605564Test
https://doi.org/10.1099/vir.0.057422-0Test

View record in BASE

النص الكامل

5

The antiviral and virucidal activities of voacangine and structural analogs extracted from Tabernaemontana cymosa depend on the Dengue virus strain

المؤلفون: Monsalve Escudero, Laura, Loaiza Cano, Vanessa, Zapata, Maria, Quintero Gil, Diana Carolina, Hernandez Mira, Estiven, Pajaro Gonzalez, Yina, Oliveros Diaz, Andres, Diaz castillo, Fredyc, Quiñones, Wiston, Robledo, Sara, Martínez Gutiérrez, Marlén

مصطلحات موضوعية: dengue virus, Tabernaemontana cymosa, indole alkaloids, molecular docking, antivirals

وصف الملف: application/pdf

العلاقة: https://www.mdpi.com/2223-7747/10/7/1280Test; Plants; Tapia-Conyer, R.; Betancourt-Cravioto, M.; Méndez-Galván, J. Dengue: An escalating public health problem in Latin America. Paediatr. Int. Child Health 2012, 32, 14–17.; Gubler, D.J. Aedes aegypti and Aedes aegypti-Borne Disease Control in the 1990s: Top Down or Bottom Up. Am. J. Trop. Med. Hyg. 1989, 40, 571–578.; Istúriz, R.E.; Gubler, D.J.; Del Castillo, J.B. Dengue and dengue hemorrhagic fever in Latin America and the Caribbean. Infect. Dis. Clin. 2000, 14, 121–140; Apte-Sengupta, S.; Sirohi, D.; Kuhn, R.J. Coupling of replication and assembly in flaviviruses. Curr. Opin. Virol. 2014, 9, 134–142.; Chambers, T.J.; Hahn, C.S.; Galler, R.; Rice, C.M. Flavivirus genome organization, expression, and replication. Annu. Rev. Microbiol. 1990, 44, 649–688.; Rico-Hesse, R.; Nisalak, A.; Harrison, L.M.; Vaughn, D.W.; Green, S.; Ennis, F.A.; Kalayanarooj, S.; Rothman, A.L. Molecular evolution of dengue type 2 virus in Thailand. Am. J. Trop. Med. Hyg. 1998, 58, 96–101.; Leitmeyer, K.C.; Vaughn, D.W.; Watts, D.M.; Salas, R.; Villalobos, I.; Chacon, D.; Ramos, C.; Rico-Hesse, R. Dengue Virus Structural Differences That Correlate with Pathogenesis. J. Virol. 1999, 73, 4738–4747.; Martínez-Betancur, V.; Marín-Villa, M.; Martínez-Gutierrez, M. Infection of epithelial cells with dengue virus promotes the expression of proteins favoring the replication of certain viral strains. J. Med. Virol. 2014, 86, 1448–1458.; Martínez-Betancur, V.; Martinez-Gutierrez, M. Proteomic profile of human monocytic cells infected with dengue virus. Asian Pac. J. Trop. Biomed. 2016, 6, 914–923. [; Cruz-Oliveira, C.; Freire, J.M.; Conceição, T.M.; Higa, L.M.; Castanho, M.A.; Da Poian, A.T. Receptors and routes of dengue virus entry into the host cells. FEMS Microbiol. Rev. 2015, 39, 155–170.; Mosso, C.; Galván-Mendoza, I.J.; Ludert, J.E.; del Angel, R.M. Endocytic pathway followed by dengue virus to infect the mosquito cell line C6/36 HT. Virology 2008, 378, 193–199.; Elshuber, S.; Allison, S.L.; Heinz, F.X.; Mandl, C.W. Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virusFN1. J. Gen. Virol. 2003, 84, 183–191.; Magden, J.; Kääriäinen, L.; Ahola, T. Inhibitors of virus replication: Recent developments and prospects. Appl. Microbiol. Biotechnol. 2005, 66, 612–621; Denaro, M.; Smeriglio, A.; Barreca, D.; De Francesco, C.; Occhiuto, C.; Milano, G.; Trombetta, D. Antiviral activity of plants and their isolated bioactive compounds: An update. Phytother. Res. 2020, 34, 742–768.; Cortez-Gallardo, V.; Macedo-Ceja, J.P.; Hernández-Arroyo, M.; Arteaga-Aureoles, G.; Espinosa-Galván, D.; Rodríguez-Landa, J.F. Farmacognosia: Breve historia de sus orígenes y su relación con las ciencias médicas. Rev. Bioméd. 2004, 15, 123–136; Hernández-Castro, C.; Diaz-Castillo, F.; Martinez-Gutierrez, M. Ethanol extracts of Cassia grandis and Tabernaemontana cymosa inhibit the in vitro replication of dengue virus serotype 2. Asian Pac. J. Trop. Dis. 2015, 5, 98–106; Gómez-Calderón, C.; Mesa-Castro, C.; Robledo, S.; Gómez, S.; Bolivar-Avila, S.; Diaz-Castillo, F.; Martínez-Gutierrez, M. Antiviral effect of compounds derived from the seeds of Mammea americana and Tabernaemontana cymosa on Dengue and Chikungunya virus infections. BMC Complement. Altern. Med. 2017, 17, 1–12; Trujillo-Correa, A.I.; Quintero-Gil, D.C.; Diaz-Castillo, F.; Quiñones, W.; Robledo, S.M.; Martinez-Gutierrez, M. In vitro and in silico anti-dengue activity of compounds obtained from Psidium guajava through bioprospecting. BMC Complement. Altern. Med. 2019, 19, 1–16.; Endress, M.E.; Liede-Schumann, S.; Meve, U. An updated classification for Apocynaceae. Phytotaxa 2014, 159, 175–194.; Dey, A.; Mukherjee, A.; Chaudhury, M. Alkaloids from apocynaceae: Origin, pharmacotherapeutic properties, and structure-activity studies. In Studies in Natural Products Chemistry; Elsevier: Amsterdam, The Netherlands, 2017; Volume 52, pp. 373–488.; Anbukkarasi, M.; Thomas, P.A.; Sheu, J.-R.; Geraldine, P. In vitro antioxidant and anticataractogenic potential of silver nanoparticles biosynthesized using an ethanolic extract of Tabernaemontana divaricata leaves. Biomed. Pharmacother. 2017, 91, 467–475.; Thambi, P.T.; Kuzhivelil, B.; Sabu, M.; Jolly, C. Antioxidant and antiinflammatory activities of the flowers of Tabernaemontana coronaria (L) R.BR. Indian J. Pharm. Sci. 2006, 68, 352–355.; De Almeida, L.; Cintra, A.C.; Veronese, E.L.; Nomizo, A.; Franco, J.J.; Arantes, E.C.; Giglio, J.R.; Sampaio, S.V. Anticrotalic and antitumoral activities of gel filtration fractions of aqueous extract from Tabernaemontana catharinensis (Apocynaceae). Comp. Biochem. Physiol. Part C Toxicol. Pharm. 2004, 137, 19–27.; Van Beek, T.; Kuijlaars, F.; Thomassen, P.; Verpoorte, R.; Svendsen, A.B. Antimicrobially active alkaloids from Tabernaemontana pachysiphon. Phytochemistry 1984, 23, 1771–1778.; Díaz Castillo, F.; Morelos Cardona, S.M.; Carrascal Medina, M.; Pájaro González, Y.; Gómez Estrada, H. Actividad larvicida de extractos etanólicos de Tabernaemontana cymosa y Trichilia hirta sobre larvas de estadio III y IV de Aedes aegypti (Diptera: Culicidae). Rev. Cuba. Plantas Med. 2012, 17, 256–267.; Pereira, P.S.; França, S.D.C.; De Oliveira, P.V.A.; Breves, C.M.D.S.; Pereira, S.I.V.; Sampaio, S.V.; Nomizo, A.; Dias, D.A. Chemical constituents from Tabernaemontana catharinensis root bark: A brief NMR review of indole alkaloids and in vitro cytotoxicity. Quím. Nova 2008, 31, 20–24.; Sharma, P.; Cordell, G.A. Heyneanine Hydroxyindolenine, A New Indole Alkaloid from Ervatamia coronaria var. plena. J. Nat. Prod. 1988, 51, 528–531.; Husain, K.; Said, I.M.; Din, L.B.; Takayama, H.; Kitajima, M.; Aimi, N. Alkaloids from The Roots of Tabernaemontana Macrocarpa Jack. Nat. Prod. Sci. 1997, 3, 42–48.; Achenbach, H.; Benirschke, M.; Torrenegra, R. Alkaloids and other compounds from seeds of Tabernaemontana cymosa. Phytochemistry 1997, 45, 325–335; Farrow, S.C.; Kamileen, M.O.; Meades, J.; Ameyaw, B.; Xiao, Y.; O’Connor, S.E. Cytochrome P450 and O-methyltransferase catalyze the final steps in the biosynthesis of the anti-addictive alkaloid ibogaine from Tabernanthe iboga. J. Biol. Chem. 2018, 293, 13821–13833; Krengel, F.; Herrera Santoyo, J.; Olivera Flores, T.D.J.; Chávez Ávila, V.M.; Pérez Flores, F.J.; Reyes Chilpa, R. Quantification of anti-addictive alkaloids ibogaine and voacangine in in vivo-and in vitro-grown plants of two Mexican Tabernaemontana species. Chem. Biodivers. 2016, 13, 1730–1737; Bardiot, D.; Koukni, M.; Smets, W.; Carlens, G.; McNaughton, M.; Kaptein, S.; Dallmeier, K.; Chaltin, P.; Neyts, J.; Marchand, A. Discovery of Indole Derivatives as Novel and Potent Dengue Virus Inhibitors. J. Med. Chem. 2018, 61, 8390–8401.; Laura, G.F.M.; Njoya, E.M.; Jouda, J.-B.; Kweka, B.N.W.; Mbazoa, C.D.; Wang, F.; Seguin, E.; Wandji, J. A new cytotoxic indole alkaloid from Tabernaemontana inconspicua stapf. Nat. Prod. Res. 2021, 35, 1590–1595; Sundar, L.; Chang, F.N. Antimicrobial activity and biosynthesis of indole antibiotics produced by Xenorhabdus nematophilus. Microbiology 1993, 139, 3139–3148; O’Brien, S.; Schiller, G.; Lister, J.; Damon, L.; Goldberg, S.; Aulitzky, W.; Ben-Yehuda, D.; Stock, W.; Coutre, S.; Douer, D.; et al. High-Dose Vincristine Sulfate Liposome Injection for Advanced, Relapsed, and Refractory Adult Philadelphia Chromosome–Negative Acute Lymphoblastic Leukemia. J. Clin. Oncol. 2013, 31, 676–683.; Diwaker, D.; Mishra, K.P.; Ganju, L.; Singh, S.B. Protein Disulfide Isomerase Mediates Dengue Virus Entry in Association with Lipid Rafts. Viral Immunol. 2015, 28, 153–160.; Limjindaporn, T.; Wongwiwat, W.; Noisakran, S.; Srisawat, C.; Netsawang, J.; Puttikhunt, C.; Kasinrerk, W.; Avirutnan, P.; Thiemmeca, S.; Sriburi, R.; et al. Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production. Biochem. Biophys. Res. Commun. 2009, 379, 196–200.; Choy, M.M.; Zhang, S.L.; Costa, V.V.; Tan, H.C.; Horrevorts, S.; Ooi, E.E. Proteasome Inhibition Suppresses Dengue Virus Egress in Antibody Dependent Infection. PLoS Negl. Trop. Dis. 2015, 9, e0004058; Teissier, E.; Zandomeneghi, G.; Loquet, A.; Lavillette, D.; Lavergne, J.-P.; Montserret, R.; Cosset, F.-L.; Böckmann, A.; Meier, B.H.; Penin, F.; et al. Mechanism of Inhibition of Enveloped Virus Membrane Fusion by the Antiviral Drug Arbidol. PLoS ONE 2011, 6, e15874.; Germi, R.; Crance, J.-M.; Garin, D.; Guimet, J.; Lortat-Jacob, H.; Ruigrok, R.W.; Zarski, J.-P.; Drouet, E. Heparan Sulfate-Mediated Binding of Infectious Dengue Virus Type 2 and Yellow Fever Virus. Virology 2002, 292, 162–168.; Nelson, J.; McFerran, N.V.; Pivato, G.; Chambers, E.; Doherty, C.; Steele, D.; Timson, D.J. The 67 kDa laminin receptor: Structure, function and role in disease. Biosci. Rep. 2008, 28, 33–48.; Tassaneetrithep, B.; Burgess, T.H.; Granelli-Piperno, A.; Trumpfheller, C.; Finke, J.; Sun, W.; Eller, M.A.; Pattanapanyasat, K.; Sarasombath, S.; Birx, D.L.; et al. DC-SIGN (CD209) Mediates Dengue Virus Infection of Human Dendritic Cells. J. Exp. Med. 2003, 197, 823–829.; Talarico, L.B.; Pujol, C.A.; Zibetti, R.G.M.; Faría, P.C.S.; Noseda, M.D.; Duarte, M.E.R.; Damonte, E.B. The antiviral activity of sulfated polysaccharides against dengue virus is dependent on virus serotype and host cell. Antivir. Res. 2005, 66, 103–110.; Goo, L.; VanBlargan, L.A.; Dowd, K.A.; Diamond, M.S.; Pierson, T.C. A single mutation in the envelope protein modulates flavivirus antigenicity, stability, and pathogenesis. PLoS Pathog. 2017, 13, e1006178.; Hishiki, T.; Kato, F.; Tajima, S.; Toume, K.; Umezaki, M.; Takasaki, T.; Miura, T. Hirsutine, an Indole Alkaloid of Uncaria rhynchophylla, Inhibits Late Step in Dengue Virus Lifecycle. Front. Microbiol. 2017, 8, 1674; Hitakarun, A.; Khongwichit, S.; Wikan, N.; Roytrakul, S.; Yoksan, S.; Rajakam, S.; Davidson, A.D.; Smith, D.R. Evaluation of the antiviral activity of orlistat (tetrahydrolipstatin) against dengue virus, Japanese encephalitis virus, Zika virus and chikungunya virus. Sci. Rep. 2020, 10, 1499.; Loaiza-Cano, V.; Monsalve-Escudero, L.M.; Quintero-Gil, C.; Pastrana, M.; Andres, P.M.S.; Galeano, E.; Wildeman, Z.; Martinez-Gutierrez, M. In Vitro and In Silico Anti-Arboviral Activities of Dihalogenated Phenolic Derivates of L-Tyrosine. Molecules 2021, 26, 3430.; Terstappen, G.C.; Reggiani, A. In silico research in drug discovery. Trends Pharm. Sci. 2001, 22, 23–26; Velásquez, M.; Drosos, J.; Gueto, C.; Márquez, J.; Vivas-Reyes, R. Autodock-PM6 method to choose the better pose in molecular docking studies. Rev. Colomb. Quím. 2013, 42, 101–124.; Murgueitio, M.S.; Bermudez, M.; Mortier, J.; Wolber, G. In silico virtual screening approaches for anti-viral drug discovery. Drug Discov. Today Technol. 2012, 9, e219–e225.; Ekins, S.; Mestres, J.; Testa, B. In silico pharmacology for drug discovery: Applications to targets and beyond. Br. J. Pharm. 2007, 152, 21–37.; Scheiner, S.; Kar, T.; Pattanayak, J. Comparison of Various Types of Hydrogen Bonds Involving Aromatic Amino Acids. J. Am. Chem. Soc. 2002, 124, 13257–13264.; Quintero-Gil, C.; Parra-Suescún, J.; Lopez-Herrera, A.; Orduz, S. In-silico design and molecular docking evaluation of peptides derivatives from bacteriocins and porcine beta defensin-2 as inhibitors of Hepatitis E virus capsid protein. Virusdisease 2017, 28, 281–288.; Domingo, C.; Niedrig, M.; Teichmann, A.; Kaiser, M.; Rumer, L.; Jarman, R.G.; Donoso-Mantke, O. 2nd International External Quality Control Assessment for the Molecular Diagnosis of Dengue Infections. PLoS Negl. Trop. Dis. 2010, 4, e833.; Cockburn, J.; Sanchez, M.E.N.; Fretes, N.; Urvoas, A.; Staropoli, I.; Kikuti, C.M.; Coffey, L.L.; Seisdedos, F.A.; Bedouelle, H.; Rey, F.A. Mechanism of Dengue Virus Broad Cross-Neutralization by a Monoclonal Antibody. Structure 2012, 20, 303–314.; Trott, O.; Olson, A.J. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 2010, 31, 455–461.; Lavi, A.; Ngan, C.H.; Movshovitz-Attias, D.; Bohnuud, T.; Yueh, C.; Beglov, D.; Schueler-Furman, O.; Kozakov, D. Detection of peptide-binding sites on protein surfaces: The first step toward the modeling and targeting of peptide-mediated interactions. Proteins Struct. Funct. Bioinform. 2013, 81, 2096–2105.; Berendsen, H.; Van Der Spoel, D.; Van Drunen, R. GROMACS: A message-passing parallel molecular dynamics implementation. Comput. Phys. Commun. 1995, 91, 43–56.; Lemkul, J. From Proteins to Perturbed Hamiltonians: A Suite of Tutorials for the GROMACS-2018 Molecular Simulation Package [Article v1.0]. Living J. Comput. Mol. Sci. 2019, 1, 5068.; MacKerell, A.D., Jr.; Brooks, B.; Brooks, C.L., III; Nilsson, L.; Roux, B.; Won, Y.; Karplus, M. CHARMM: The energy function and its parameterization. Encycl. Comput. Chem. 2002, 1, 271.; Vanommeslaeghe, K.; Hatcher, E.; Acharya, C.; Kundu, S.; Zhong, S.; Shim, J.; Darian, E.; Guvench, O.; Lopes, P.; Vorobyov, I.; et al. CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields. J. Comput. Chem. 2009, 31, 671–690.; Selvaraj, C.; Dinesh, D.C.; Panwar, U.; Abhirami, R.; Boura, E.; Singh, S.K. Structure-based virtual screening and molecular dynamics simulation of SARS-CoV-2 Guanine-N7 methyltransferase (nsp14) for identifying antiviral inhibitors against COVID-19. J. Biomol. Struct. Dyn. 2020, 38, 1–12.; Sinha, S.; Wang, S.M. Classification of VUS and unclassified variants in BRCA1 BRCT repeats by molecular dynamics simulation. Comput. Struct. Biotechnol. J. 2020, 18, 723–736.; Kaushik, A.C.; Sahi, S. Molecular modeling and molecular dynamics simulation-based structural analysis of GPR3. Netw. Model. Anal. Health Inform. Bioinform. 2017, 6, 9.; https://hdl.handle.net/20.500.12494/43618Test; Monsalve-Escudero, L.M.; Loaiza-Cano, V.; Zapata-Cardona, M.I.; Quintero-Gil, D.C.; Hernández-Mira, E.; Pájaro-González, Y.; Oliveros-Díaz, A.F.; Diaz-Castillo, F.; Quiñones, W.; Robledo, S.; Martinez-Gutierrez, M. The Antiviral and Virucidal Activities of Voacangine and Structural Analogs Extracted from Tabernaemontana cymosa Depend on the Dengue Virus Strain. Plants 2021, 10, 1280. https://doi.org/10.3390/plants10071280Test

الإتاحة: https://doi.org/20.500.12494/43618Test
https://doi.org/10.3390/plants10071280Test
https://hdl.handle.net/20.500.12494/43618Test

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النص الكامل

6

SARS CoV-2 Spike protein in silico interaction with ACE2 receptors from wild and domestic species

المؤلفون: Rendon Marin, Santiago, Martínez Gutiérrez, Marlén, Whittaker, Gary, Jaimes, Javier Andres, Ruiz Saenz, Julian

مصطلحات موضوعية: SARS-CoV-2, COVID-19, Homology modeling, Molecular docking, Spike protein

وصف الملف: application/pdf

العلاقة: Front genetics; Al-Tawfiq, J. A., Zumla, A., and Memish, Z. A. (2014). Travel implications of emerging coronaviruses: SARS and MERS-CoV. Travel Med. Infect. Dis. 12, 422–428. doi:10.1016/j.tmaid.2014.06.007; Benkert, P., Biasini, M., and Schwede, T. (2011). Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics 27, 343–350. doi:10.1093/bioinformatics/btq662; Bonilla-Aldana, D. K., Ruiz-Saenz, J., Martinez-Gutierrez, M., Tiwari, R., Dhama, K., Jaimes, J. A., et al. (2020). Concerns on the emerging research of SARS-CoV-2 on felines: could they be significant hosts/reservoirs. J. Pure Appl. Microbiol. 14, 1–6. doi:10.22207/JPAM.14.SPL1.04; Brooke, G. N., and Prischi, F. (2020). Structural and functional modelling of SARS-CoV-2 entry in animal models. Sci. Rep. 10:15917. doi:10.1038/ s41598-020-72528-z; Cao, Y., Li, L., Feng, Z., Wan, S., Huang, P., Sun, X., et al. (2020). Comparative genetic analysis of the novel coronavirus (2019-nCoV/SARS-CoV-2) receptor ACE2 in different populations. Cell Discov. 6:11. doi:10.1038/s41421-020- 0147-1; CDC (2020). "Confirmation of COVID-19 in Two Pet Cats in New York", (ed.) U.S.C.F.D.C.A.P. (Cdc).; Chan, J. F. -W., Yuan, S., Kok, K. -H., Toi, K. K. -W., Chu, H., Yang, J., et al. (2020a). A familial cluster of pneumonia associated with the 2019 novel coronavirus indicating person-to-person transmission: a study of a family cluster. Lancet 395, 514–523. doi:10.1016/S0140-6736(20)30154-9; Chan, J. F. -W., Zhang, A. J., Yuan, S., Poon, V. K. -M., Chan, C. C. -S., Lee, A. C. -Y., et al. (2020b). Simulation of the clinical and pathological manifestations of Coronavirus disease 2019 (COVID-19) in golden Syrian hamster model: implications for disease pathogenesis and transmissibility. Clin. Infect. Dis. 71, 2428–2446. doi:10.1093/cid/ciaa325; Chen, N., Zhou, M., Dong, X., Qu, J., Gong, F., Han, Y., et al. (2020). Epidemiological and clinical characteristics of 99 cases of 2019 novel coronavirus pneumonia in Wuhan, China: a descriptive study. Lancet 395, 507–513. doi:10.1016/S0140-6736(20)30211-7; Cleary, S. J., Pitchford, S. C., Amison, R. T., Carrington, R., Robaina Cabrera, C. L., Magnen, M., et al. (2020). Animal models of mechanisms of SARS-CoV-2 infection and COVID-19 pathology. Br. J. Pharmacol. 177, 4851–4865. doi:10.1111/bph.15143; Conceicao, C., Thakur, N., Human, S., Kelly, J. T., Logan, L., Bialy, D., et al. (2020). The SARS-CoV-2 spike protein has a broad tropism for mammalian ACE2 proteins. PLoS Biol. 18:e3001016. doi:10.1371/journal.pbio.3001016; Cui, J., Li, F., and Shi, Z. L. (2019). Origin and evolution of pathogenic coronaviruses. Nat. Rev. Microbiol. 17, 181–192. doi:10.1038/s41579-018-0118-9; Li, W., Zhang, C., Sui, J., Kuhn, J. H., Moore, M. J., Luo, S., et al. (2005). Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2. EMBO J. 24, 1634–1643. doi:10.1038/sj.emboj.7600640; Luan, J., Lu, Y., Jin, X., and Zhang, L. (2020). Spike protein recognition of mammalian ACE2 predicts the host range and an optimized ACE2 for SARS-CoV-2 infection. Biochem. Biophys. Res. Commun. 526, 165–169. doi:10.1016/j.bbrc.2020.03.047; Martina, B. E., Haagmans, B. L., Kuiken, T., Fouchier, R. A., Rimmelzwaan, G. F., van Amerongen, G., et al. (2003). Virology: SARS virus infection of cats and ferrets. Nature 425:915. doi:10.1038/425915a; Millet, J. K., Jaimes, J. A., and Whittaker, G. R. (2020). Molecular diversity of coronavirus host cell entry receptors. FEMS Microbiol. Rev. fuaa057. doi:10.1093/femsre/fuaa057; OIE (2020). Questions and Answers on the COVID-19. Available at: https:// www.oie.int/en/scientific-expertise/specific-information-and-recommendations/ questions-and-answers-on-2019novel-coronavirus/ [Online]; Ortiz, M. E., Thurman, A., Pezzulo, A. A., Leidinger, M. R., Klesney-Tait, J. A., Karp, P. H., et al. (2020). Heterogeneous expression of the SARS-Coronavirus-2 receptor ACE2 in the human respiratory tract. EBioMedicine 60:102976. doi:10.1016/j.ebiom.2020.102976; Richard, M., Kok, A., de Meulder, D., Bestebroer, T. M., Lamers, M. M., Okba, N. M., et al. (2020). SARS-CoV-2 is transmitted via contact and via the air between ferrets. bioRxiv. doi:10.1101/2020.04.16.044503 [Preprint]x; Zhai, X., Sun, J., Yan, Z., Zhang, J., Zhao, J., Zhao, Z., et al. (2020). Comparison of severe acute respiratory syndrome coronavirus 2 spike protein binding to ACE2 receptors from Human, pets, farm animals, and putative intermediate hosts. J. Virol. 94, e00831-20. doi:10.1128/JVI.00831-20; Zhang, Q., Zhang, H., Huang, K., Yang, Y., Hui, X., Gao, J., et al. (2020). SARS-CoV-2 neutralizing serum antibodies in cats: a serological investigation. bioRxiv. doi:10.1101/2020.04.01.021196 [Preprint].; Zhu, N., Zhang, D., Wang, W., Li, X., Yang, B., Song, J., et al. (2020). A Novel Coronavirus from patients with pneumonia in China, 2019. N. Engl. J. Med. 382, 727–733. doi:10.1056/NEJMoa2001017; https://hdl.handle.net/20.500.12494/32931Test; Rendon-Marin, S., Martínez-Gutiérrez, M., Whittaker, G.R., Jaimes, JA., Ruiz-Saenz, J. (2021). SARS CoV-2 Spike Protein in Silico Interaction With ACE2 Receptors From Wild and Domestic Species. Front. Genet. 12:571707. doi:10.3389/fgene.2021.571707

الإتاحة: https://doi.org/20.500.12494/32931Test
https://doi.org/10.3389/fgene.2021.571707Test
https://doi.org/10.1016/j.tmaid.2014.06.007Test
https://doi.org/10.1093/bioinformatics/btq662Test
https://doi.org/10.22207/JPAM.14.SPL1.04Test
https://doi.org/10.1038/s41421-020Test
https://doi.org/10.1016/S0140-6736Test(20)30154-9
https://doi.org/10.1093/cid/ciaa325Test
https://doi.org/10.1016/S0140-6736Test(20)30211-7
https://doi.org/10.1111/bph.15143Test

View record in BASE

النص الكامل

7

The antiviral and virucidal activities of voacangine and structural analogs extracted from Tabernaemontana cymosa depend on the Dengue virus strain

المؤلفون: Monsalve Escudero, Laura, Loaiza Cano, Vanessa, Zapata, Maria, Quintero Gil, Diana Carolina, Hernandez Mira, Estiven, Pajaro Gonzalez, Yina, Oliveros Diaz, Andres, Diaz castillo, Fredyc, Quiñones, Wiston, Robledo, Sara, MARTINEZ GUTIERREZ, MARLEN

المصدر: Tapia-Conyer, R.; Betancourt-Cravioto, M.; Méndez-Galván, J. Dengue: An escalating public health problem in Latin America. Paediatr. Int. Child Health 2012, 32, 14–17. ; Gubler, D.J. Aedes aegypti and Aedes aegypti-Borne Disease Control in the 1990s: Top Down or Bottom Up. Am. J. Trop. Med. Hyg. 1989, 40, 571–578. ; Istúriz, R.E.; Gubler, D.J.; Del Castillo, J.B. Dengue and dengue hemorrhagic fever in Latin America and the Caribbean. Infect. Dis. Clin. 2000, 14, 121–140 ; Apte-Sengupta, S.; Sirohi, D.; Kuhn, R.J. Coupling of replication and assembly in flaviviruses. Curr. Opin. Virol. 2014, 9, 134–142. ; Chambers, T.J.; Hahn, C.S.; Galler, ....

مصطلحات موضوعية: dengue virus, Tabernaemontana cymosa, indole alkaloids, molecular docking, antivirals

وصف الملف: application/pdf

العلاقة: Plants; https://www.mdpi.com/2223-7747/10/7/1280Test; http://hdl.handle.net/20.500.12494/43618Test; Monsalve-Escudero, L.M.; Loaiza-Cano, V.; Zapata-Cardona, M.I.; Quintero-Gil, D.C.; Hernández-Mira, E.; Pájaro-González, Y.; Oliveros-Díaz, A.F.; Diaz-Castillo, F.; Quiñones, W.; Robledo, S.; Martinez-Gutierrez, M. The Antiviral and Virucidal Activities of Voacangine and Structural Analogs Extracted from Tabernaemontana cymosa Depend on the Dengue Virus Strain. Plants 2021, 10, 1280. https://doi.org/10.3390/plants10071280Test

الإتاحة: https://doi.org/20.500.12494/43618Test
https://doi.org/10.3390/plants10071280Test
https://hdl.handle.net/20.500.12494/43618Test

View record in BASE

النص الكامل

8

SARS CoV-2 Spike protein in silico interaction with ACE2 receptors from wild and domestic species

المؤلفون: Rendon Marin, Santiago, Martinez Gutierrez, Marlen, Whittaker, Gary, Jaimes, Javier Andres, Ruiz Saenz, Julian

المصدر: Al-Tawfiq, J. A., Zumla, A., and Memish, Z. A. (2014). Travel implications of emerging coronaviruses: SARS and MERS-CoV. Travel Med. Infect. Dis. 12, 422–428. doi:10.1016/j.tmaid.2014.06.007 ; Benkert, P., Biasini, M., and Schwede, T. (2011). Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics 27, 343–350. doi:10.1093/bioinformatics/btq662 ; Bonilla-Aldana, D. K., Ruiz-Saenz, J., Martinez-Gutierrez, M., Tiwari, R., Dhama, K., Jaimes, J. A., et al. (2020). Concerns on the emerging research of SARS-CoV-2 on felines: could they be significant hosts/reservoirs. J. Pure Appl. Microbiol. 14, 1–6. doi:10.22207/JPAM.14.SPL1.04 ; Brooke, G. N., and Prischi, F. (2020). Structural and ....

مصطلحات موضوعية: SARS-CoV-2, COVID-19, Homology modeling, Molecular docking, Spike protein

وصف الملف: application/pdf

العلاقة: Front genetics; http://hdl.handle.net/20.500.12494/32931Test; Rendon-Marin, S., Martínez-Gutiérrez, M., Whittaker, G.R., Jaimes, JA., Ruiz-Saenz, J. (2021). SARS CoV-2 Spike Protein in Silico Interaction With ACE2 Receptors From Wild and Domestic Species. Front. Genet. 12:571707. doi:10.3389/fgene.2021.571707

الإتاحة: https://doi.org/20.500.12494/32931Test
https://doi.org/10.3389/fgene.2021.571707Test
https://doi.org/10.1016/j.tmaid.2014.06.007Test
https://doi.org/10.1093/bioinformatics/btq662Test
https://doi.org/10.22207/JPAM.14.SPL1.04Test
https://doi.org/10.1038/s41421-020Test
https://doi.org/10.1016/S0140-6736Test(20)30154-9
https://doi.org/10.1093/cid/ciaa325Test
https://doi.org/10.1016/S0140-6736Test(20)30211-7
https://doi.org/10.1111/bph.15143Test

View record in BASE

النص الكامل

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