000858397 001__ 858397
000858397 005__ 20210129235938.0
000858397 0247_ $$2doi$$a10.1016/j.antiviral.2018.10.019
000858397 0247_ $$2ISSN$$a0166-3542
000858397 0247_ $$2ISSN$$a1872-9096
000858397 0247_ $$2pmid$$apmid:30393012
000858397 0247_ $$2WOS$$aWOS:000451936000014
000858397 0247_ $$2altmetric$$aaltmetric:50880889
000858397 037__ $$aFZJ-2018-07283
000858397 082__ $$a610
000858397 1001_ $$0P:(DE-HGF)0$$aCoronado, Monika Aparecida$$b0
000858397 245__ $$aZika virus NS2B/NS3 proteinase: A new target for an old drug - Suramin a lead compound for NS2B/NS3 proteinase inhibition-
000858397 260__ $$aAmsterdam [u.a.]$$bElsevier Science$$c2018
000858397 3367_ $$2DRIVER$$aarticle
000858397 3367_ $$2DataCite$$aOutput Types/Journal article
000858397 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1546498016_29398
000858397 3367_ $$2BibTeX$$aARTICLE
000858397 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000858397 3367_ $$00$$2EndNote$$aJournal Article
000858397 520__ $$aZika virus infection is the focus of much research due to the medical and social repercussions. Due the role of the viral NS2B/NS3 proteinase in maturation of the viral proteins, it had become an attractive antiviral target. Numerous investigations on viral epidemiology, structure and function analysis, vaccines, and therapeutic drugs have been conducted around the world. At present, no approved vaccine or even drugs have been reported. Thus, there is an urgent need to develop therapeutic agents to cure this epidemic disease. In the present study, we identified the polyanion suramin, an approved antiparasitic drug with antiviral properties, as a potential inhibitor of Zika virus complex NS2B/NS3 proteinase with IC50 of 47 μM. Using fluorescence spectroscopy results we could determine a kd value of 28 μM and had shown that the ligand does not affect the thermal stability of the protein. STD NMR spectroscopy experiments and molecular docking followed by molecular dynamics simulation identified the binding epitopes of the molecule and shows the mode of interaction, respectively. The computational analysis showed that suramin block the Ser135 residue and interact with the catalytically histidine residue.
000858397 536__ $$0G:(DE-HGF)POF3-553$$a553 - Physical Basis of Diseases (POF3-553)$$cPOF3-553$$fPOF III$$x0
000858397 588__ $$aDataset connected to CrossRef
000858397 7001_ $$0P:(DE-HGF)0$$aEberle, Raphael Josef$$b1
000858397 7001_ $$0P:(DE-Juel1)131977$$aBleffert, Nicole$$b2$$ufzj
000858397 7001_ $$0P:(DE-Juel1)162167$$aFeuerstein, Sophie$$b3$$ufzj
000858397 7001_ $$00000-0003-1269-3783$$aOlivier, Danilo Silva$$b4
000858397 7001_ $$00000-0002-0425-0352$$ade Moraes, Fabio Rogerio$$b5
000858397 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b6
000858397 7001_ $$0P:(DE-HGF)0$$aArni, Raghuvir Krishnaswamy$$b7$$eCorresponding author
000858397 773__ $$0PERI:(DE-600)1495861-2$$a10.1016/j.antiviral.2018.10.019$$gVol. 160, p. 118 - 125$$p118 - 125$$tAntiviral research$$v160$$x0166-3542$$y2018
000858397 8564_ $$uhttps://juser.fz-juelich.de/record/858397/files/Zika%20virus%20NS2B%2CNS3%20proteinase%20A%20new%20target%20for%20an%20old%20drug%20-%20Suramin%20a%20lead%20compound%20for%20NS2B%2C%20NS3%20proteinase%20inhibition.pdf$$yRestricted
000858397 8564_ $$uhttps://juser.fz-juelich.de/record/858397/files/Zika%20virus%20NS2B%2CNS3%20proteinase%20A%20new%20target%20for%20an%20old%20drug%20-%20Suramin%20a%20lead%20compound%20for%20NS2B%2C%20NS3%20proteinase%20inhibition.pdf?subformat=pdfa$$xpdfa$$yRestricted
000858397 909CO $$ooai:juser.fz-juelich.de:858397$$pVDB
000858397 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131977$$aForschungszentrum Jülich$$b2$$kFZJ
000858397 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)162167$$aForschungszentrum Jülich$$b3$$kFZJ
000858397 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)132029$$aForschungszentrum Jülich$$b6$$kFZJ
000858397 9131_ $$0G:(DE-HGF)POF3-553$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vPhysical Basis of Diseases$$x0
000858397 9141_ $$y2018
000858397 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000858397 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000858397 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000858397 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bANTIVIR RES : 2017
000858397 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000858397 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search
000858397 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC
000858397 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bClarivate Analytics Master Journal List
000858397 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000858397 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000858397 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000858397 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000858397 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000858397 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000858397 920__ $$lyes
000858397 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000858397 980__ $$ajournal
000858397 980__ $$aVDB
000858397 980__ $$aI:(DE-Juel1)ICS-6-20110106
000858397 980__ $$aUNRESTRICTED
000858397 981__ $$aI:(DE-Juel1)IBI-7-20200312