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A review on the cleavage priming of the spike protein on coronavirus by angiotensin-converting enzyme-2 and furin. J Biomol Struct Dyn. 2020. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1754293.","https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1754293",{"mag":449,"pmc":450,"openalex":451,"pm":452,"doi":453},"3015385976","7189411","W3015385976","32274964","10.1080\u002F07391102.2020.1754293",{"id":455,"text":456,"url":457,"identifiers":458},"4c68646b-0035-4279-8000-0006b275d4fa","Zhao R, Li X, Niu J, Yang P, Wu B, Wang H, Song W, Huang H, Zhu B, Bi N, Ma Y, Zhan X, Wang F, Hu L, Zhou T, Hu H, Zhou Z, Zhao W, Tan L, Lu W. Genomic characterisation and epidemiology of 2019 novel coronavirus: implications for virus origins and receptor binding. The Lancet. 2020;395(10224):565–74.","https:\u002F\u002Flink.springer.com\u002F10.1007\u002Fs10440-022-00541-7",{"doi":459},"10.1007\u002Fs10440-022-00541-7",{"id":461,"text":462,"url":463,"identifiers":464},"773b602e-25b9-47e1-9af7-a3bd510c90f4","Zhao F, Yu S, Chen B, Wang YM, Song W, Hu ZG, Tao Y, Tian ZW, Pei JH, Yuan YY, Zhang ML, Dai YL, Liu FH, Wang Y, Zheng QM, Xu JJ, Holmes L, Zhang EC, Wu YZ. A new coronavirus associated with human respiratory disease in China. Nature. 2020;579(7798):265–9.","https:\u002F\u002Fwww.nature.com\u002Farticles\u002Fs41586-020-2008-3",{"doi":465},"10.1038\u002Fs41586-020-2008-3",{"id":21,"text":467,"url":21,"identifiers":468},"Worldometers.info. (2020) COVID-19 coronavirus pandemic. [Online]",{},{"id":21,"text":470,"url":471,"identifiers":472},"Zia SA, Ashraf K, Uddin S, Ul-Haq R, Khan Z. Identification of chymotrypsin-like protease inhibitors of SARS-CoV-2 via integrated computational approach. J Biomol Struct Dyn. 2020. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1751298.","https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1751298",{"mag":473,"openalex":474,"pm":475,"doi":476},"3013468691","W3013468691","32238094","10.1080\u002F07391102.2020.1751298",{"id":455,"text":478,"url":457,"identifiers":479},"Chen F, Tan C, Yang W, Yang K, Wang H. Structure of main protease from human coronavirus NL63: Insights for wide spectrum anti-coronavirus drug design. Sci Rep. 2016;6(1):1–12.",{"doi":459},{"id":21,"text":481,"url":482,"identifiers":483},"Al-Obaidi AD, Ahin AS, Yelekc AT, Elmezayen IK. Drug repurposing for coronavirus (COVID-19): in silico screening of known drugs against coronavirus 3CL hydrolase and protease enzymes. J Biomol Struct Dyn. 2020. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1758791.","https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1758791",{"mag":484,"pmc":485,"openalex":486,"pm":487,"doi":488},"3016525638","7189413","W3016525638","32306862","10.1080\u002F07391102.2020.1758791",{"id":21,"text":490,"url":491,"identifiers":492},"Poma S, Kolandaivel AB, Boopathi P. Novel 2019 coronavirus structure, mechanism of action, antiviral drug promises and rule out against its treatment. J Biomol Struct Dyn. 2020. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1758788.","https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1758788",{"mag":493,"pmc":494,"openalex":495,"pm":496,"doi":497},"3016685184","7196923","W3016685184","32306836","10.1080\u002F07391102.2020.1758788",{"id":455,"text":499,"url":457,"identifiers":500},"Wang X, Liu XJ. Potential inhibitors against 2019-nCoV coronavirus M protease from clinically approved medicines. J Genet Genom. 2020;47(2):119–21.",{"doi":459},{"id":455,"text":502,"url":457,"identifiers":503},"Froeyen MU, Mirza M. Structural elucidation of SARS-CoV-2 vital proteins: computational methods reveal potential drug candidates against main protease. Nsp12 RNA-dependent RNA polymerase and Nsp13 helicase. J Pharm Anal. 2020;10:320–8.",{"doi":459},{"id":21,"text":505,"url":506,"identifiers":507},"Jha RJ, Amera RK, Jain G, Singh M, Pathak E, Singh A, Muthukumaran RP, Singh J, Khan AK. Targeting SARS-CoV-2: a systematic drug repurposing approach to identify promising inhibitors against 3C-like proteinase and 2’-O-ribosemethyltransferase. J Biomol Struct Dyn. 2020. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1753577.","http:\u002F\u002Fdx.doi.org\u002F10.1080\u002F07391102.2020.1753577",{"doi":508},"10.1080\u002F07391102.2020.1753577",{"id":21,"text":510,"url":21,"identifiers":511},"Barrila U, Velazquez-Campoy J, Leavitt A, Freire SA, Bacha E. Identification of novel inhibitors of the SARS coronavirus main protease 3CLpro. Biochem. 2004;43(17):4906–12.",{},{"id":455,"text":513,"url":457,"identifiers":514},"Sims TP, Leist AC, Schäfer SR, Won A, Brown J, Montgomery AJ, Hogg SA, Babusis A, Clarke D, Spahn MO, Bauer JE, Sellers L, Porter S, Feng D, Cihlar JY, Jordan T, Denison R, Baric MR, Sheahan RS. Comparative therapeutic efficacy of remdesivir and combination lopinavir, ritonavir, and interferon beta against MERS-CoV,\". Nat Commun. 2020;11(1):222.",{"doi":459},{"id":455,"text":516,"url":457,"identifiers":517},"Lin D, Sun X, Curth U, Drosten C, Sauerhering L, Becker S, Rox K, Hilgenfeld R, Zhang L. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved a-ketoamide inhibitors. Science. 2020;368:409–12.",{"doi":459},{"id":455,"text":519,"url":457,"identifiers":520},"Rolain P, Lagier JM, Brouqui JC, Raoult P, Colson D. Chloroquine and hydroxychloroquine as available weapons to fight COVID-19. Int J Antimicrob Agents. 2020;55(4):105932.",{"doi":459},{"id":455,"text":522,"url":457,"identifiers":523},"Gautret P, Lagier JC, Parola P, Hoang VT, Meddeb L, Mailhe M, Doudier B, Courjon J, Giordanengo V, Vieira VE, Tissot Dupont H, Honoré S, Colson P, Chabrière E, La Scola B, Rolain JM, Brouqui P, Raoult D. Hydroxychloroquine and azithromycin as a treatment of COVID-19: results of an open-label non-randomized clinical trial. Int J Antimicrob Agents. 2020;56(1):105949.",{"doi":459},{"id":455,"text":525,"url":457,"identifiers":526},"Cao M, Zhang R, Yang L, Liu X, Xu J, Shi M, Hu Z, Zhong Z, Xiao W, Wang G. Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro. Cell Res. 2020;30(3):269–71.",{"doi":459},{"id":21,"text":528,"url":529,"identifiers":530},"Vemula MK, Donde S, Gouda R, Behera G, Vadde L, Gupta R. In-silico approaches to detect inhibitors of the human severe acute respiratory syndrome coronavirus envelope protein ion channel. J Biomol Struct Dyn. 2020. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1751300.","https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1751300",{"mag":531,"pmc":532,"openalex":533,"pm":534,"doi":535},"3013772162","7171389","W3013772162","32238078","10.1080\u002F07391102.2020.1751300",{"id":21,"text":537,"url":538,"identifiers":539},"Belhassan I, El Khatabi A, Lakhlifi K, El Idrissi T, Bouachrine M, Aanouz M. Moroccan medicinal plants as inhibitors of COVID-19: computational investigations. J Biomol Struct Dyn. 2020. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1758790.","https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1758790",{"doi":540},"10.1080\u002F07391102.2020.1758790",{"id":455,"text":542,"url":457,"identifiers":543},"Jadhav HR. Antioxidant properties of Indian medicinal plants. Phytother Res. 2002;16(8):771–3.",{"doi":459},{"id":455,"text":545,"url":457,"identifiers":546},"Vijayakumar M, Pushpangadan P, Govindarajan R. Antioxidant approach to disease management and the role of ’Rasayana’ herbs of Ayurveda. J Ethnopharmacol. 2005;99(2):165–78.",{"doi":459},{"id":21,"text":548,"url":21,"identifiers":549},"Nair AM, Kamal KK, Saraf MN, Mungantiwar AA. Adaptogenic activity of aqueous extract of the roots of Boerhaavia diffusa Linn. Indian Drugs. 1997;34(4):184–9.",{},{"id":21,"text":551,"url":21,"identifiers":552},"Nair AM, Shinde UA, Saraf MN, Muntgantiwar AA. Effect of stress on plasma and adrenal cortisol levels and immune responsiveness in rats: modulation by alkaloidal fraction of Boerhaavia diffusa. Fitoterapia. 1997;68(6):498–500.",{},{"id":455,"text":554,"url":457,"identifiers":555},"Mustafa SS, Sumanth M. Antistress, adoptogenic and immunopotentiating activity roots of Boerhaavia diffusa in mice. Int J Pharmacol. 2007;3(5):416–20.",{"doi":459},{"id":21,"text":557,"url":21,"identifiers":558},"Saluja D, Chopra M, Srivastava R. (2005) Isolation and screening of anticancer metabolites from Boerhavia diffusa. Indian J Med Res. 2005;151(1):S19.",{},{"id":455,"text":560,"url":457,"identifiers":561},"Sreeja S. An in vitro study on antiproliferative and antiestrogenic effects of Boerhaavia diffusa L. extracts. J Ethnopharmacol. 2009;126(2):221–5.",{"doi":459},{"id":455,"text":563,"url":457,"identifiers":564},"Lini CC, Kuttan G, Leyon PV. (2005) Inhibitory effect of Boerhaavia diffusa on experimental metastasis by B16F10 melanoma in C57BL\u002F6 mice. Life Sci. 2005;76(2):1339–49.",{"doi":459},{"id":455,"text":566,"url":457,"identifiers":567},"Kuttan G, Manu KA. (2007) Effect of punarnavine, an alkaloid from Boerhaavia diffusa, on cell-mediated immune responses and TIMP-1 in B16F–10 metastatic melanoma-bearing mice. Immunopharmacol Immunotoxicol. 2007;29(3–4):569–86.",{"doi":459},{"id":455,"text":569,"url":457,"identifiers":570},"Pari L, Satheesh MA. Antioxidant effect of Boerhavia diffusa L. in tissues of alloxan induced diabetic rats. Indian J Exp Biol. 2004;42(10):989–92.",{"doi":459},{"id":455,"text":572,"url":457,"identifiers":573},"Orisakwe OE, Afonne OJ, Gamaniel KS, Vongtau OH, Obi E, Chude MA. Hypoglycaemic effect of the aqueous extract of Boerhavia diffusa leaves. Indian J Pharmacol. 2001;33(3):215–6.",{"doi":459},{"id":455,"text":575,"url":457,"identifiers":576},"Amarnath Satheesh M, Pari L. Antidiabetic effect of Boerhavia diffusa: effect on serum and tissue lipids in experimental diabetes. J Med Food. 2004;7(4):472–6.",{"doi":459},{"id":21,"text":578,"url":21,"identifiers":579},"Mudgal V. Studies on medicinal properties of Convolvulus pluricaulis and Boerhaavia diffusa. Planta Med. 1975;28(1):62–8.",{},{"id":455,"text":581,"url":457,"identifiers":582},"Gracioso JS, Bighetti EJB, Germonsen Robineou L, Souza Brito ARM, Hiruma-Lima CA. The juice of fresh leaves of Boerhaavia diffusa L. (Nyctaginaceae) markedly reduces pain in mice. J Ethnopharmacol. 2000;71(1–2):267–74.",{"doi":459},{"id":21,"text":584,"url":21,"identifiers":585},"Asadulla S. Anti-inflammatory activities of Boerhavia diffusa roots in Albino rats. Arch Pharm Sci Res. 2010;2:267–70.",{},{"id":455,"text":587,"url":457,"identifiers":588},"Nayak P, Thirunavoukkarasu M. A review of the plant Boerhaavia diffusa: its chemistry, pharmacology and therapeutical potential. J Phytopharmacology. 2016;5(2):83–92.",{"doi":459},{"id":21,"text":590,"url":591,"identifiers":592},"Aeri V, Gaur PK, Jachak SM, Mishra S. Phytochemical, therapeutic, and ethnopharmacological overview for a traditionally important herb: Boerhavia diffusa Linn. BioMed Res Int. 2014. https:\u002F\u002Fdoi.org\u002F10.1155\u002F2014\u002F808302.","https:\u002F\u002Fdoi.org\u002F10.1155\u002F2014\u002F808302",{"mag":593,"pmc":594,"openalex":595,"pm":596,"doi":597},"2082000115","4053255","W2082000115","24949473","10.1155\u002F2014\u002F808302",{"id":21,"text":599,"url":600,"identifiers":601},"Srivastava A, Jachak SM, Bairwa K. Quantitative analysis of Boeravinones in the roots of Boerhaavia diffusa by UPLC\u002FPDA. Phytochem Anal. 2014. https:\u002F\u002Fdoi.org\u002F10.1002\u002Fpca.2509.","https:\u002F\u002Fdoi.org\u002F10.1002\u002Fpca.2509",{"mag":602,"openalex":603,"pm":604,"doi":605},"2125488541","W2125488541","24677242","10.1002\u002Fpca.2509",{"id":455,"text":607,"url":457,"identifiers":608},"Noba K, Ba AT, Gaydou EM, Kornprobst JM, Miralles J. Chemotaxonomy in Nyctagynaceae family: sterols and fatty acids from the leaves of three Boerhaavia species. Biochem Syst Ecol. 1988;16(5):475–8.",{"doi":459},{"id":455,"text":610,"url":457,"identifiers":611},"Bikadi Z, Hazai E. Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock. J Cheminf. 2009;1(1):1–16.",{"doi":459},{"id":455,"text":613,"url":457,"identifiers":614},"Halgren Merck TA. Molecular force field. I. Basis, form, scope, parametrization, and performance of MMFF94. J Comput Chem. 1998;17(5–6):490–519.",{"doi":459},{"id":455,"text":616,"url":457,"identifiers":617},"Morris GM, Goodsell DS. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem. 1998;19(14):1639–62.",{"doi":459},{"id":455,"text":619,"url":457,"identifiers":620},"Solis FJ, Wets RJB. Minimization by random search techniques. Math Oper Res. 1981;6(1):19–30.",{"doi":459},{"id":455,"text":622,"url":457,"identifiers":623},"Palanisamy M, Palanisamy S, Subramanian A, Rathinavel STT. Phytochemical 6-Gingerol–A promising Drug of choice for COVID-19. Int J Adv Sci Eng. 2020;6(4):1482–9.",{"doi":459},{"id":21,"text":625,"url":626,"identifiers":627},"Shakya A, Prasad SK, Singh S, Gurav NS, Prasad RS, Gurav SS, Sinha SK. An in-silico evaluation of different Saikosaponins for their potency against SARS-CoV-2 using NSP15 and fusion spike glycoprotein as targets. J Biomol Struct Dyn. 2020. https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1762741.","https:\u002F\u002Fdoi.org\u002F10.1080\u002F07391102.2020.1762741",{"mag":628,"pmc":629,"openalex":630,"pm":631,"doi":632},"3018056400","7232888","W3018056400","32345124","10.1080\u002F07391102.2020.1762741",{"id":634,"createTime":635,"updateTime":636,"relativeEntities":637,"slug":638,"properties":639,"entityType":135,"verifyStatus":136,"verifyTime":650,"verifyNote":138,"languages":21,"translateLanguages":21,"viewCount":22,"primaryUrl":651,"fullTextUrl":21,"authors":652,"publicationType":238,"publisherRelationship":737,"citationCount":22,"citationInfo":777,"publishDate":780,"publishYear":778,"citationAnalyzeStatus":20,"lastCitationAnalyze":781,"indexDatabases":782,"openAccess":21,"references":21,"isForceReanalyzing":341},"f6e07f30-a083-4aea-8102-dae9bb14430d","2024-02-09T00:33:31.615+00:00","2026-07-10T08:57:36.341+00:00",[],"Chikungunya-a-reemerging-infection-spreading-during-2010-dengue-fever-outbreak-in-National-Capital-Region-of-India",{"abstract":640,"title":642,"gsPaper":644,"references":646,"doi":648},{"EN":641},"Chikungunya fever is an important reemerging arbovirus illness, which is transmitted by the same vector as of dengue virus. Many cases of concurrent infections with multiple dengue virus serotypes have been reported in many countries. Also, concurrent infection with Chikungunya virus and dengue virus has been reported in the past in Delhi. Therefore, this study was done to detect Chikungunya IgM antibodies in suspected dengue fever patients. In this study, 1666 serum samples suspected of dengue fever and collected during the outbreak period (August 2010–December 2010) were tested for dengue IgM antibodies, of which 736 tested negative. Of the 736 dengue IgM negative sera, 666 were tested for Chikungunya IgM antibodies. The demographic profile and essential laboratory investigations were recorded. Chikungunya IgM was detected in 9.91 % of the patients. During the post-monsoon period though dengue dominated in numbers, the number of Chikungunya fever cases increased gradually followed by an abrupt decrease with the onset of winter. The Chikungunya IgM positive patients were suffering from fever of more than 5 days duration and had thrombocytopenia. Due to similarity in clinical features and vector transmitting dengue and Chikungunya virus, continuous surveillance of both dengue fever and Chikungunya fever is desirable for better management and epidemiological assessment.",{"EN":643},"Chikungunya: a reemerging infection spreading during 2010 dengue fever outbreak in National Capital Region of India",{"VOID":645},"[\"8533741514193018257\"]",{"VOID":647},"Afreen N, Deeba F, Khan WH, Haider SH, Kazim SN, Ishrat R, Naqvi IH, Shareef MY, Broor S, Ahmed A, Parveen S. Molecular characterization of dengue and chikungunya virus strains circulating in New Delhi, India. Microbiol Immunol. 2014;58(12):688–96.\nAraújo FMC, Nogueira RMR, Araújo JMG, Ramalho ILC, Sá Roriz MLF, Melo MEL, Coelho ICB. Concurrent infection with dengue virus type-2 and DENV-3 in a patient from Ceará, Brazil. 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Am J Trop Med Hyg. 1985;34(1):170–3.\nLahariya C, Pradhan SK. Emergence of chikungunya virus in Indian subcontinent after 32 years: a review. J Vect Borne Dis. 2006;43(4):151–60.\nMavalankar D, Shastri P, Bandyopadhyay T, Parmar J, Ramani KV. Increased mortality rate associated with chikungunya epidemic, Ahmedabad, India. Emerg Infect Dis. 2008;14(3):412–5.\nMyers RM, Carey DE. Concurrent isolation from patient of two arboviruses, chikungunya and dengue type 2. Science. 1967;157(3794):1307–8.\nNagpal BN, Saxena R, Srivastava A, Singh N, Ghosh SK, Sharma SK, Kumar A, Kumar H, Sharma AS, Chand SK, Ojha VP, Mohanty SS, Mohanty AK, Dasgupta RK, Dhillon GPS, Dash AP. Retrospective study of chikungunya outbreak in urban areas of India. Indian J Med Res. 2012;135:351–8.\nRocco IM, Barbosa ML, Kanomata EH. Simultaneous infection with dengue 1 and 2 in a Brazilian patient. 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PLoS Negl Trop Dis. 2010;4(6):e706. doi:10.1371\u002Fjournal.pntd.0000706.",{"VOID":649},"10.1007\u002Fs13337-016-0314-z","2024-05-16T01:07:59.086+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13337-016-0314-z",[653,670,685,707,724],{"id":654,"sortIndex":22,"researcher":21,"roles":655,"affiliations":656,"properties":665,"displayName":667,"givenName":21,"familyName":21},"eea86743-0552-4901-a8d7-a6cf269ce071",[363],[657],{"id":658,"sortIndex":22,"affiliation":659,"properties":21},"5de9c828-9fe7-4d80-9116-127c9894291e",{"id":658,"createTime":21,"updateTime":21,"relativeEntities":660,"slug":21,"properties":661,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":664,"statistic":21},[],{"title":662},{"VI":663},"Department of Microbiology, University College of Medical Sciences and Guru Teg Bahadur Hospital, Delhi, India",[],{"title":666,"gsAuthor":668},{"VI":667},"V. G. 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ongoing pandemic Coronavirus disease (COVID-19), caused by a newly emerged Coronavirus, SARS-CoV-2 has affected millions of people globally. One of the most crucial structural proteins  of SARS-CoV-2 is the Spike glycoprotein (S-glycoprotein), for which the first de novo modelling was envisaged by our group in early 2020, and was superimposed to its predecessor SARS-CoV S-glycoprotein, to determine structural divergence, glycosylation and antigenic variation between SARS-CoV-2 and SARS-CoV. S-glycoprotein is involved  in binding with the cellular receptor, membrane fusion, internalization via angiotensin-converting enzyme 2 (ACE2) receptor, and tissue tropism. Upon internalization into the target host cells, the viral genome encodes two precursor polypeptides which get processed into 16 mature nonstructural proteins that play a crucial role in replication and transcription of SARS-CoV-2. Currently S-glycoprotein is one of the most vital targets for vaccine and therapeutics development for COVID-19.",{"EN":793},"Chasing COVID-19 through SARS-CoV-2 spike glycoprotein",{"VOID":795},"[]",{"VOID":797},"Pneumonia of unknown cause – China, World health Organization 2020. https:\u002F\u002Fwww.who.int\u002Fcsr\u002Fdon\u002F05-january-2020-pneumonia-of-unkown-cause-china\u002Fen\u002F. Accessed 10 Nov 2020.\nYang P, Wang X. COVID-19: a new challenge for human beings. Cell Mol Immunol. 2020;17:555–7. https:\u002F\u002Fdoi.org\u002F10.1038\u002Fs41423-020-0407-x.\nYadav T, Saxena SK. Transmission Cycle of SARS-CoV and SARS-CoV-2. Coronavirus Disease 2019 (COVID-19). 2020. https:\u002F\u002Fdoi.org\u002F10.1007\u002F978-981-15-4814-7_4.\nShereen MA, Khan S, Kazmi A, Bashir N, Siddique R. COVID-19 infection: Origin, transmission, and characteristics of human coronaviruses. 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Lancet. 2020;395:1845–54. https:\u002F\u002Fdoi.org\u002F10.1016\u002FS0140-6736(20)31208-3.",{"VOID":799},"10.1007\u002Fs13337-020-00642-7","2024-06-23T19:24:52.301+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13337-020-00642-7",[803,818,831,846,861,874],{"id":804,"sortIndex":22,"researcher":21,"roles":805,"affiliations":806,"properties":815,"displayName":817,"givenName":21,"familyName":21},"ec3cc4b0-ce1f-4eeb-b02f-03c5760a097d",[363],[807],{"id":808,"sortIndex":22,"affiliation":809,"properties":21},"b2f644e9-ac97-4533-ad7d-85f42298e33b",{"id":808,"createTime":21,"updateTime":21,"relativeEntities":810,"slug":21,"properties":811,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":814,"statistic":21},[],{"title":812},{"VI":813},"Centre for Advanced Research (CFAR), Faculty of Medicine, King George’s Medical University (KGMU), Lucknow, India",[],{"title":816},{"VI":817},"Shailendra K. 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It has become the worldwide pandemic in recent few years. It is a kind of haemorrhagic fever, caused by SFTS virus (SFTSV), a novel phlebovirus of family Bunyaviridae. This syndrome is also a tick-borne zoonosis that means the virus transmitted from tick bite (having virus) into human body, i.e. infection spread from animals to humans and also transmitted from human to human. Epidemiological data of SFTS was collected to know the nature\u002Fsymptoms of SFTSV. First case of this disease has been reported in China, followed by Japan, South korea, Taiwan, USA and many other countries. Vertebrates are the host of this disease and tick functions as a vector, where the virus can undergo brisk changes using gene mutation, homologous recombination and reassortments. The major symptoms of hemorrhagic fever are fever, thrombocytopenia, leucopenia and gastrointestinal abnormalities. Sometimes in very severe cases, full body organ failure may also take place and average death rate in humans is nearly 10 %. Old aged peoples are more prone to SFTSV infection. Apart from the fact of increasing SFTSV related health problems to humans, the pathogenesis of SFTS virus in human is not entirely understood and no treatment to this virus is still available. The simplest way to protect our self from this infection is to refrain from tick bite. Therefore, this disease has evolved to produce serious health issues to humans in various countries of world including china. This review discussing about causative agent, epidemiology, pathogenesis, diagnosis and treatment of SFTS. In order to control the spread of SFTSV, we have to stop the viral transmission or to protect the easily vulnerable population from tick bites, avoiding direct contact of infectious and also to use personal protective devices for SFTS patients. So, the weather conditions, mode of transmission and creation of new therapeutics like vaccines and drugs are the main areas of forthcoming research.",{"EN":945},"A new emerging pandemic of severe fever with thrombocytopenia syndrome (SFTS)",{"VOID":947},"[\"1549098745723877632\"]",{"VOID":949},"10.1007\u002Fs13337-021-00656-9","2024-04-29T18:15:34.530+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13337-021-00656-9",[953,970],{"id":954,"sortIndex":22,"researcher":21,"roles":955,"affiliations":956,"properties":965,"displayName":967,"givenName":21,"familyName":21},"d0b7b5b8-a413-43ed-af5e-d83119eacb9a",[363],[957],{"id":958,"sortIndex":22,"affiliation":959,"properties":21},"e4711936-498f-409a-8d21-e6bdb977e144",{"id":958,"createTime":21,"updateTime":21,"relativeEntities":960,"slug":21,"properties":961,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":964,"statistic":21},[],{"title":962},{"VI":963},"Department of Life Sciences, IAMR College, Ghaziabad, India",[],{"title":966,"gsAuthor":968},{"VI":967},"Divya Sharma",{"VOID":969},"[\"O74_uq0AAAAJ\"]",{"id":971,"sortIndex":164,"researcher":21,"roles":972,"affiliations":973,"properties":980,"displayName":982,"givenName":21,"familyName":21},"36d04103-6db5-4141-96e0-fdf7d13e83ec",[363],[974],{"id":958,"sortIndex":22,"affiliation":975,"properties":21},{"id":958,"createTime":21,"updateTime":21,"relativeEntities":976,"slug":21,"properties":977,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":979,"statistic":21},[],{"title":978},{"VI":963},[],{"title":981,"gsAuthor":983},{"VI":982},"Mohit Kamthania",{"VOID":984},"[\"vnGFYBwAAAAJ\"]",{"url":951,"publisher":986,"properties":1020},{"id":6,"createTime":7,"updateTime":8,"relativeEntities":987,"slug":10,"properties":988,"entityType":19,"verifyStatus":20,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":22,"subjectFields":992,"manageAffiliations":1001,"indexDatabases":1007,"url":21,"thumbnailPath":21,"statistic":1015,"gsStatistic":21,"type":109,"analyzePriority":21},[],{"issn":989,"title":990,"eissn":991},{"VOID":15},{"EN":10},{"VOID":13},[993,997],{"id":25,"createTime":21,"updateTime":21,"relativeEntities":994,"label":995,"description":996,"parentId":21,"standard":21,"scholarHubFieldId":21},[],{"EN":28},{},{"id":31,"createTime":21,"updateTime":21,"relativeEntities":998,"label":999,"description":1000,"parentId":21,"standard":21,"scholarHubFieldId":21},[],{"EN":34},{},[1002],{"id":38,"createTime":21,"updateTime":21,"relativeEntities":1003,"slug":21,"properties":1004,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":1006,"statistic":21},[],{"title":1005},{"EN":42},[44],[1008],{"id":47,"indexDatabase":1009,"url":58,"indexYears":59,"academicFieldIds":1014,"indexDatabaseRanking":63},{"id":49,"createTime":21,"updateTime":21,"relativeEntities":1010,"label":1011,"description":1012,"key":55,"publicationTags":1013,"standard":21},[],{"EN":52,"VI":52},{"EN":52,"VI":54},[57],[61,62],{"impactFactor":22,"impactFactorByYear":1016,"i10Index":73,"i10IndexLast5Year":74,"totalPublication":75,"totalPublicationByYear":1017,"totalCitation":86,"totalCitationByYear":1018,"totalCitationPerPublication":96,"totalCitationPerPublicationByYear":1019,"hindexLast5Year":108,"hindex":108},{"2015":66,"2016":67,"2017":68,"2018":69,"2019":69,"2020":70,"2021":71,"2022":72,"2023":67},{"2013":77,"2014":78,"2015":79,"2016":80,"2017":81,"2018":82,"2019":78,"2020":83,"2021":84,"2022":79,"2023":81,"2024":85},{"2014":88,"2015":89,"2016":89,"2017":84,"2018":90,"2019":91,"2020":92,"2021":93,"2022":94,"2023":95},{"2014":98,"2015":99,"2016":100,"2017":101,"2018":102,"2019":103,"2020":104,"2021":105,"2022":106,"2023":107},{"pages":1021,"volume":1023},{"VOID":1022},"220-227",{"VOID":432},{"total":22,"publishYear":435,"statisticByYear":1025},{},"2021-04-29",[63],[1029,1032,1035,1041,1044,1047,1050,1053,1061,1070,1073,1076,1079,1082,1085,1088,1091,1100,1103,1109,1112,1115,1118,1121,1124,1127,1131,1134,1137,1141,1145,1148,1151,1155,1158,1161,1164,1170,1173,1176,1179,1182,1185,1188,1191,1194,1197,1200,1203,1206,1212,1215,1218,1224,1230,1233,1236,1242,1245,1248,1251,1254,1257,1260,1263,1266,1269],{"id":455,"text":1030,"url":457,"identifiers":1031},"Zhang L, Liu Y, Ni D, Li Q, Yu Y, Yu XJ, et al. 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Emerg Microbes Infect. 2020;9(1):148–51. https:\u002F\u002Fdoi.org\u002F10.1080\u002F22221751.2019.1710436.","https:\u002F\u002Fdoi.org\u002F10.1080\u002F22221751.2019.1710436",{"mag":1095,"pmc":1096,"openalex":1097,"pm":1098,"doi":1099},"2999370134","6968498","W2999370134","31918622","10.1080\u002F22221751.2019.1710436",{"id":455,"text":1101,"url":457,"identifiers":1102},"Liu Q, Biao H, Si-Yang H, Feng W, Xing-Quan Z, et al. Severe fever with thrombocytopenia syndrome, an emerging tick-borne zoonosis. Lancet Infect Dis. 2014;14:763–72.",{"doi":459},{"id":1104,"text":1105,"url":1106,"identifiers":1107},"b5cdb801-e35a-4763-aff8-d3c37d8be8c8","Lei X-P, Liu M, Yu X. Severe fever with thrombocytopenia syndrome and its pathogen SFTSV. Microbes Infect. 2015;17:149–54.","https:\u002F\u002Fwww.sciencedirect.com\u002Fscience\u002Farticle\u002Fpii\u002FS1286457914003086",{"doi":1108},"10.1016\u002Fj.micinf.2014.12.002",{"id":455,"text":1110,"url":457,"identifiers":1111},"Silvas J, Aguilar P. 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SP, Huang YC, Li WC, Chiu CH, Huang CG, Tsao KC, Lin TY. Comparison of clinical features between coxsackievirus A2 and enterovirus 71 during the enterovirus outbreak in Taiwan, 2008: a children’s hospital experience. J Microbiol Immunol Infect. 2010;43:99–104.",{"doi":1483},"10.1016\u002FS1684-1182(10)60016-3",{"id":21,"text":1485,"url":21,"identifiers":1486},"Chu PY, Lu PL, Tsai YL, Hsi E, Yao CY, Chen YH, Hsu LC, Wang SY, Wu HS, Lin YY, Su HJ, Lin KH. Spatiotemporal phylogenetic analysis and molecular characterization of coxsackievirus A4. Infect Genet Evol. 2011;11:1426–35.",{"doi":1487},"10.1016\u002Fj.meegid.2011.05.010",{"id":21,"text":1489,"url":21,"identifiers":1490},"Gaunt E, Harvala H, Österback R, Sreenu VB, Thomson E, Waris M, Simmonds P. Genetic characterization of human coxsackievirus A6 variants associated with atypical hand, foot and mouth disease: a potential role of recombination in emergence and pathogenicity. J Gen Virol. 2015;96:1067–79.",{"doi":1491},"10.1099\u002Fvir.0.000062",{"id":21,"text":1493,"url":21,"identifiers":1494},"Hu YF, Yang F, Du J, Dong J, Zhang T, Wu ZQ, Xue Y, Jin Q. Complete genome analysis of coxsackievirus A2, A4, A5, and A10 strains isolated from hand, foot, and mouth disease patients in China revealing frequent recombination of human enterovirus A. J Clin Microbiol. 2011;49:2426–34.",{"doi":1495},"10.1128\u002FJCM.00007-11",{"id":21,"text":1497,"url":21,"identifiers":1498},"Lee ST, Ki CS, Lee NY. Molecular characterization of enteroviruses isolated from patients with aseptic meningitis in Korea, 2005. Arch Virol. 2007;152:963–70.",{"doi":1499},"10.1007\u002Fs00705-006-0901-1",{"id":21,"text":1501,"url":21,"identifiers":1502},"Linsuwanon P, Payungporn S, Samransamruajkit R, Posuwan N, Makkoch J, Theanboonlers A, Poovorawan Y. High prevalence of human rhinovirus C infection in Thai children with acute lower respiratory tract disease. J Infect. 2009;59:115–21.",{"doi":1503},"10.1016\u002Fj.jinf.2009.05.009",{"id":21,"text":1505,"url":21,"identifiers":1506},"Lugo D, Krogstad P. Enteroviruses in the early 21st century: new manifestations and challenges. Curr Opin Pediatr. 2016;28:107–13.",{"doi":1507},"10.1097\u002FMOP.0000000000000303",{"id":21,"text":1509,"url":21,"identifiers":1510},"Mauleekoonphairoj J, Puenpa J, Korkong S, Vongpunsawad S, Poovorawan Y. Prevalence of human enterovirus among patients with hand, foot, and mouth disease and herpangina in Thailand. Southeast Asian J Trop Med Public Health. 2015;46:1013–20.",{},{"id":21,"text":1512,"url":21,"identifiers":1513},"Molet L, Saloum K, Marque-Juillet S, Garbarg-Chenon A, Henquell C, Schuffenecker I, Peigue-Lafeuille H, Rozenberg F, Mirand A. Enterovirus infections in hospitals of Ile de France region over 2013. J Clin Virol. 2016;74:37–42.",{"doi":1514},"10.1016\u002Fj.jcv.2015.11.024",{"id":21,"text":1516,"url":21,"identifiers":1517},"Pons-Salort M, Parker EP, Grassly NC. The epidemiology of non-polio enteroviruses: recent advances and outstanding questions. Curr Opin Infect Dis. 2015;28:479–87.",{"doi":1518},"10.1097\u002FQCO.0000000000000187",{"id":21,"text":1520,"url":21,"identifiers":1521},"Puenpa J, Chieochansin T, Linsuwanon P, Korkong S, Thongkomplew S, Vichaiwattana P, Theamboonlers A, Poovorawan Y. Hand, foot, and mouth disease caused by coxsackievirus A6, Thailand, 2012. Emerg Infect Dis. 2013;19:641–3.",{"doi":1522},"10.3201\u002Feid1904.121666",{"id":21,"text":1524,"url":21,"identifiers":1525},"Solomon T, Lewthwaite P, Perera D, Cardosa MJ, McMinn P, Ooi MH. Virology, epidemiology, pathogenesis, and control of enterovirus 71. Lancet Infect Dis. 2010;10:778–90.",{"doi":1526},"10.1016\u002FS1473-3099(10)70194-8",{"id":21,"text":1528,"url":21,"identifiers":1529},"Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol. 2011;28:2731–9.",{"doi":1530},"10.1093\u002Fmolbev\u002Fmsr121",{"id":21,"text":1532,"url":21,"identifiers":1533},"Yip CC, Lau SK, Woo PC, Wong SS, Tsang TH, Lo JY, Lam WK, Tsang CC, Chan KH, Yuen KY. Recombinant coxsackievirus A2 and deaths of children, Hong Kong, 2012. Emerg Infect Dis. 2013;19:1285–8.",{"doi":1534},"10.3201\u002Feid1908.121498",{"id":1536,"createTime":1537,"updateTime":1538,"relativeEntities":1539,"slug":1540,"properties":1541,"entityType":135,"verifyStatus":136,"verifyTime":1552,"verifyNote":138,"languages":21,"translateLanguages":21,"viewCount":22,"primaryUrl":1553,"fullTextUrl":21,"authors":1554,"publicationType":238,"publisherRelationship":1646,"citationCount":21,"citationInfo":21,"publishDate":1686,"publishYear":1687,"citationAnalyzeStatus":20,"lastCitationAnalyze":1688,"indexDatabases":1689,"openAccess":21,"references":21,"isForceReanalyzing":341},"9734c3aa-dd9c-44ef-80e1-603d1150fe44","2024-02-19T18:52:11.503+00:00","2026-03-23T19:21:50.368+00:00",[],"Detection-of-Aleutian-disease-virus-by-loop-mediated-isothermal-amplification",{"abstract":1542,"title":1544,"gsPaper":1546,"references":1548,"doi":1550},{"EN":1543},"In this study, a loop-mediated isothermal amplification (LAMP) assay was developed and optimized for the detection of Aleutian disease virus (ADV) in minks. The amplification could be completed within 45 min under isothermal condition by employing a set of six ADV genome-specific primers. The amplification results could be visualized directly with the naked eye by using fluorescent dye. Comparative experiments showed that the LAMP assay is superior to conventional polymerase chain reaction for the detection of both experimental and field samples. Results of current study indicated that the LAMP assay is a rapid and reliable technique for routine diagnosis of ADV infection in minks.",{"EN":1545},"Detection of Aleutian disease virus by loop-mediated isothermal amplification",{"VOID":1547},"[\"1718814413807561253\"]",{"VOID":1549},"Aasted B, Alexandersen S, Cohn A, Hansen M. Counter current line absorption immunoelectrophoresis in an alternative diagnostic screening test to counter current immunoelectrophoresis in Aleutian disease (AD) eradication programs. Acta Vet Scand. 1986;27(3):410–20.\nAasted B, Cohn A. Inhibition of precipitation in counter current electrophoresis. A sensitive method for detection of mink antibodies to Aleutian disease virus. Acta Pathol Microbiol Immunol Scand C. 1982;90(1):15–9.\nAlexandersen S. Pathogenesis of disease caused by Aleutian mink disease parvovirus. APMIS Suppl. 1990;14:1–32.\nAlexandersen S, Bloom ME, Wolfinbarger J, Race RE. In situ molecular hybridization for detection of Aleutian mink disease parvovirus DNA by using strand-specific probes: identification of target cells for viral replication in cell cultures and in mink kits with virus-induced interstitial pneumonia. J Virol. 1987;61(8):2407–19.\nAlexandersen S, Hau J. Rocket line immunoelectrophoresis: an improved assay for simultaneous quantification of a mink parvovirus (Aleutian disease virus) antigen and antibody. J Virol Methods. 1985;10(2):145–51.\nAndersson AM, Wallgren P. Evaluation of two enzyme-linked immunosorbent assays for serodiagnosis of Aleutian mink disease virus infection in mink. Acta Vet Scand. 2013;55:86.\nBloom ME, Kanno H, Mori S, Wolfinbarger JB. Aleutian mink disease: puzzles and paradigms. Infect Agents Dis. 1994;3(6):279–301.\nCrawford TB, McGuire TC, Porter DD, Cho HJ. A comparative study of detection methods for Aleutian disease viral antibody. J Immunol. 1977;118(4):1249–51.\nDam-Tuxen R, Dahl J, Jensen TH, Dam-Tuxen T, Struve T, Bruun L. Diagnosing Aleutian mink disease infection by a new fully automated ELISA or by counter current immunoelectrophoresis: a comparison of sensitivity and specificity. J Virol Methods. 2014;199:53–60.\nHadlow WJ, Race RE, Kennedy RC. Comparative pathogenicity of four strains of Aleutian disease virus for pastel and sapphire mink. Infect Immun. 1983;41(3):1016–23.\nJensen TH, Christensen LS, Chriel M, Uttenthal A, Hammer AS. Implementation and validation of a sensitive PCR detection method in the eradication campaign against Aleutian mink disease virus. J Virol Methods. 2011;171(1):81–5.\nKnuuttila A, Aronen P, Eerola M, Gardner IA, Virtala AM, Vapalahti O. Validation of an automated ELISA system for detection of antibodies to Aleutian mink disease virus using blood samples collected in filter paper strips. Virol J. 2014;11:141.\nKnuuttila A, Aronen P, Saarinen A, Vapalahti O. Development and evaluation of an enzyme-linked immunosorbent assay based on recombinant VP2 capsids for the detection of antibodies to Aleutian mink disease virus. Clin Vaccine Immunol. 2009;16(9):1360–5.\nMurakami M, Matsuba C, Une Y, Nomura Y, Fujitani H. Nucleotide sequence and polymerase chain reaction\u002Frestriction fragment length polymorphism analyses of Aleutian disease virus in ferrets in Japan. J Vet Diagn Investig. 2001;13(4):337–40.\nNotomi T, Okayama H, Masubuchi H, Yonekawa T, Watanabe K, Amino N, Hase T. Loop mediated isothermal amplification of DNA. Nucleic Acids Res. 2000;28(12):E63.\nPorter DD, Larsen AE, Cox NA, Porter HG, Suffin SC. Isolation of Aleutian disease virus of mink in cell culture. Intervirology. 1977;8(3):129–44.\nPrieto A, Diaz-Cao JM, Fernandez-Antonio R, Panadero R, Diaz P, Lopez C, Morrondo P, Diez-Banos P, Fernandez G. Application of real-time PCR to detect Aleutian Mink Disease Virus on environmental farm sources. Vet Microbiol. 2014;173(3–4):355–9.\nSaifuddin M, Fox JG. Identification of a DNA segment in ferret Aleutian disease virus similar to a hypervariable capsid region of mink Aleutian disease parvovirus. Arch Virol. 1996;141(7):1329–36.\nUttenthal A. Screening for antibodies against Aleutian disease virus (ADV) in mink. Elucidation of dubious results by additive counterimmunoelectrophoresis. Appl Theor Electrophor. 1992;3(2):83–4.\nWright PF, Wilkie BN. Detection of antibody in Aleutian disease of mink: comparison of enzyme-linked immunosorbent assay and counterimmunoelectrophoresis. Am J Vet Res. 1982;43(5):865–8.",{"VOID":1551},"10.1007\u002Fs13337-015-0265-9","2024-05-16T22:08:20.596+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13337-015-0265-9",[1555,1579,1592,1605,1618,1633],{"id":1556,"sortIndex":22,"researcher":21,"roles":1557,"affiliations":1558,"properties":1576,"displayName":1578,"givenName":21,"familyName":21},"37732439-7388-49f6-aa60-8277cd198b2a",[363],[1559,1567],{"id":1560,"sortIndex":22,"affiliation":1561,"properties":21},"190c4d21-3b1d-4feb-ae45-bac747928451",{"id":1560,"createTime":21,"updateTime":21,"relativeEntities":1562,"slug":21,"properties":1563,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":1566,"statistic":21},[],{"title":1564},{"VI":1565},"College of Veterinary Medicine, Northeast Agricultural University, Harbin, 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present study was carried out to monitor influenza viruses by identifying the virus and studying the seasonal variation during 2007–2009 in Mumbai. A total of 193 clinical respiratory samples (nasal and throat swab) were collected from patients having influenza like illness in Mumbai region. One-step real-time reverse-transcriptase PCR (rRTPCR) was used to detect Influenza type A (H1 and H3) and Influenza type B virus. Isolation of the virus was carried out using in vitro system which was further confirmed and typed by hemagglutination assay and hemagglutination inhibition assay. Out of 193 samples 24 (12.4 3%) samples tested positive for influenza virus, of which 13 (6.73 %) were influenza type A virus and 10 (5.18 %) were influenza type B virus, while 1 sample (0.51 %) was positive for both. By culture methods, 3 (1.55 %) viral isolates were obtained. All the three isolates were found to be Influenza type B\u002FMalaysia (Victoria lineage) by Hemagglutination Inhibition Assay. The data generated from the present study reveals that both Influenza type A and B are prevalent in Mumbai with considerable activity. The peak activity was observed during monsoon season.",{"EN":1700},"Characterization of influenza virus among influenza like illness cases in Mumbai, India",{"VOID":795},{"VOID":1703},"Agrawal MS, Chakarbarti S. Comparative evaluation of real time PCR and conventional RT-PCR during a 2 year surveillance for influenza and respiratory syncytial virus among children with acute respiratory infections in Kolkata, India, reveals a district seasonality of infection. J Med Microbiol. 2009;58:1616–22.\nDavid-west TS, Cooke AR. Laboratory and clinical investigation o the 1974 influenza epidemic in Nigeria. Bull World Health Organ. 1974;51:103–5.\nJian J-W, et al. Genetic and epidemiological analysis of influenza virus epidemics in Taiwan during 2003 to 2006. J clin microbiol. 2008;46(4):1426–1434.\nKeech M. The impact of influenza and influenza-like illness on productivity and healthcare resource utilization in a working population. Occup Med. 1998;48:85–90.\nKrauss S, Walker D, Webster R. Influenza virus. Methods Mol Biol. 2012;865:11–2.\nPaget J, Marquet R, Meijer A, Velden K. Influenza activity in Europe during eight seasons (1999–2007): an evaluation of the indicators used to measure activity and an assessment of the timing, length and course of peak activity (Spread) across Europe. BMC Infect Dis. 2007;7:141.\nRao BL. Influenza surveillance in Pune, India 1978–1990. Bull World Health Organ. 1993;71:177–81.\nRoy S, Patil D, Dahake R, Mukherjee S, Athlekar SV, Deshmukh RA, Chowdhary A. Prevalence of influenza virus among the pediatric population in Mumbai during 2007–2009. Indian J Med Microbiol. 2012;30:155–8.\nSmith D, et al. Mapping the antigenic and genetic evolution of influenza virus. Science. 2004;305:371.\nWebster R, Cox N, Stoler K. Laboratory methods, WHO manual on animal influenza diagnosis and surveillance; 2012. p. 15–16; 55–61.\nYeolekar LR, et al. Influenza virus infection during a pilgrimage at Pandharpur M, India. 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MMWR. 2022;71:196–201.",{},{"id":21,"text":2074,"url":2075,"identifiers":2076},"CDC (2022) Rubella for healthcare professionals. https:\u002F\u002Fwww.cdc.gov\u002Frubella\u002Fhcp.html Accessed Jun 7, 2022","https:\u002F\u002Fwww.cdc.gov\u002Frubella\u002Fhcp.htmlAccessed",{},{"id":21,"text":2078,"url":2079,"identifiers":2080},"WHO (2022) Manual for the laboratory-based surveillance of Measles, Rubella, and congenital rubella syndrome. https:\u002F\u002Fwww.who.int\u002Fpublications\u002Fm\u002Fitem\u002Fchapter-1-manual-for-the-laboratory-based-surveillance-of-measles-rubella-and-congenital-rubella-syndrome Accessed Jun 7, 2022","https:\u002F\u002Fwww.who.int\u002Fpublications\u002Fm\u002Fitem\u002Fchapter-1-manual-for-the-laboratory-based-surveillance-of-measles-rubella-and-congenital-rubella-",{},{"id":455,"text":2082,"url":457,"identifiers":2083},"Jindai K, Funaki T, Nishijima T, Takakura S, Noda H, Miyake K. Towards rubella elimination in Japan. Lancet Infect Dis. 2018;18:713–4.",{"doi":459},{"id":21,"text":2085,"url":21,"identifiers":2086},"WHO. Standardization of the nomenclature for genetic characteristics of wildtype rubella viruses. Wkl Epidemiol Rec. 2005;14:126–32.",{},{"id":21,"text":2088,"url":21,"identifiers":2089},"Kanbayashi D, Kurata T, Kubo H, Kaida A, Yamamoto SP, Egawa K, Hirai Y, Okada K, Ikemori R, Yumisashi T, Yamamoto A, Yoshida H, Hirayama T, Ikuta K, Motomura K. Ongoing rubella epidemic in Osaka, Japan, in 2018–2019. Western Pac Surveill Response J. 2020;11:48–50.",{},{"id":455,"text":2091,"url":457,"identifiers":2092},"Kumar S, Stecher G, Li M, Knyaz C, Tamura KMEGAX. Molecular evolutionary genetics analysis across computing platforms. Mol Biol Evol. 2018;35:1547–9.",{"doi":459},{"id":21,"text":2094,"url":21,"identifiers":2095},"Murauchi K, Okazaki T, Shibasaki S, Hasegawa M, Shinkai T, Akiba T, Hirai A, Sadamasu K. Isolation of the rubella virus from patients diagnosed with congentital rubella syndrome in Tokyo. Ann Rep Tokyo Metr Inst Pub Health. 2016;67:69–74.",{},{"id":21,"text":2097,"url":21,"identifiers":2098},"Thomas S, Hiebert J, Gubbay JB, Gournis E, Sharron J, Severini A, Jiaravuthisan M, Shane A, Jaeger V, Crowcroft NS, Fediurek J, Sander B, Mazzulli T, Schulz H, Deeks SL. Measles outbreak with unique virus genotyping, Ontario, Canada, 2015. Emerg Infect Dis. 2017;23:1063–9.",{},{"id":21,"text":2100,"url":2101,"identifiers":2102},"WHO Guidelines on Verification of Measles and Rubella Elimination in the Western Pacific Region, second edition, (2019) https:\u002F\u002Fapps.who.int\u002Firis\u002Frest\u002Fbitstreams\u002F1269996\u002Fretrieve, Accessed Sep 13, 2022","https:\u002F\u002Fapps.who.int\u002Firis\u002Frest\u002Fbitstreams\u002F1269996\u002Fretrieve",{},{"id":2104,"createTime":2105,"updateTime":2106,"relativeEntities":2107,"slug":2108,"properties":2109,"entityType":135,"verifyStatus":136,"verifyTime":2106,"verifyNote":138,"languages":21,"translateLanguages":21,"viewCount":22,"primaryUrl":2118,"fullTextUrl":21,"authors":2119,"publicationType":238,"publisherRelationship":2161,"citationCount":21,"citationInfo":21,"publishDate":2200,"publishYear":1687,"citationAnalyzeStatus":20,"lastCitationAnalyze":21,"indexDatabases":2201,"openAccess":21,"references":21,"isForceReanalyzing":341},"7c8d8412-8506-47be-b557-13e5258e5365","2024-02-09T06:10:59.667+00:00","2025-02-27T00:37:12.406+00:00",[],"Computational-analysis-reveal-inhibitory-action-of-nimbin-against-dengue-viral-envelope-protein",{"abstract":2110,"title":2112,"references":2114,"doi":2116},{"EN":2111},"\nDengue has emerged to be global health problem worldwide. Hence there is an immediate need to adopt new strategies in the development of effective anti-dengue drugs. Extracts from the leaves of Azadirachta indica has been traditionally used in folk medicine for viral infections. In the present study we report the anti-viral potency of nimbin, the active compound from the neem leaf extract against the envelope protein of dengue virus. Progression of viral entry into the host cell is facilitated by the envelope protein of dengue virus, suggesting; it as an effective anti-viral target. Nimbin is found to be effective against the envelope protein of all four types of dengue virus (dengue 1–4), which is evident from our in silico analysis. Our findings suggest the clinical importance of nimbin, which can serve as effective lead compound for further analysis.",{"EN":2113},"Computational analysis reveal inhibitory action of nimbin against dengue viral envelope protein",{"VOID":2115},"Alavijeh MS, Chishty M, Palmer AM. 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Structure. 2004;12(9):1607–8.",{"VOID":2117},"10.1007\u002Fs13337-015-0280-x","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13337-015-0280-x",[2120,2135,2148],{"id":2121,"sortIndex":22,"researcher":21,"roles":2122,"affiliations":2123,"properties":2132,"displayName":2134,"givenName":21,"familyName":21},"c6f16452-ad6f-4dca-bb47-69197f496cc2",[363],[2124],{"id":2125,"sortIndex":22,"affiliation":2126,"properties":21},"152cae29-5ec9-4a1b-bbf5-d3442d9e4060",{"id":2125,"createTime":21,"updateTime":21,"relativeEntities":2127,"slug":21,"properties":2128,"entityType":21,"verifyStatus":21,"verifyTime":21,"verifyNote":21,"languages":21,"translateLanguages":21,"viewCount":21,"url":21,"parentIds":2131,"statistic":21},[],{"title":2129},{"VI":2130},"Medical and Biological Computing Laboratory, School of Biosciences and Technology, VIT University, Vellore, India",[],{"title":2133},{"VI":2134},"P. 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