Aromatic and polar residues spanning the candidate fusion peptide of the Andes virus Gc protein are essential for membrane fusion and infection

dc.date.accessioned2016-11-29T20:54:19Z
dc.date.available2016-11-29T20:54:19Z
dc.date.created2016-11-29T20:54:19Z
dc.date.issued2011
dc.identifier0022-1317
dc.identifierhttp://hdl.handle.net/10533/134384
dc.identifier1100756
dc.identifierWOS:000288310700008
dc.languageeng
dc.publisherSOC GENERAL MICROBIOLOGY
dc.relationhttps://doi.org/10.1099/vir.0.027235-0
dc.relation10.1099/vir.0.027235-0
dc.relationinfo:eu-repo/grantAgreement/Fondecyt/1100756
dc.relationinfo:eu-repo/semantics/dataset/hdl.handle.net/10533/93477
dc.relationinstname: Conicyt
dc.relationreponame: Repositorio Digital RI2.0
dc.relationinstname: Conicyt
dc.relationreponame: Repositorio Digital RI2.0
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleAromatic and polar residues spanning the candidate fusion peptide of the Andes virus Gc protein are essential for membrane fusion and infection
dc.typeArticulo


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