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Publicação:
1H, 15N and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the endemic human coronavirus HKU1

dc.contributor.authorde Luna Marques, Aline
dc.contributor.authorCaruso, Icaro Putinhon [UNESP]
dc.contributor.authorSantana-Silva, Marcos Caique
dc.contributor.authorBezerra, Peter Reis
dc.contributor.authorAraujo, Gabriela Rocha
dc.contributor.authorAlmeida, Fabio Ceneviva Lacerda
dc.contributor.authorAmorim, Gisele Cardoso
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionRio BioNMR Network
dc.date.accessioned2021-06-25T10:48:12Z
dc.date.available2021-06-25T10:48:12Z
dc.date.issued2021-04-01
dc.description.abstractCoronaviruses have become of great medical and scientific interest because of the Covid-19 pandemic. The hCoV-HKU1 is an endemic betacoronavirus that causes mild respiratory symptoms, although the infection can progress to severe lung disease and death. During viral replication, a discontinuous transcription of the genome takes place, producing the subgenomic messenger RNAs. The nucleocapsid protein (N) plays a pivotal role in the regulation of this process, acting as an RNA chaperone and participating in the nucleocapsid assembly. The isolated N-terminal domain of protein N (N-NTD) specifically binds to the transcriptional regulatory sequences and control the melting of the double-stranded RNA. Here, we report the resonance assignments of the N-NTD of HKU1-CoV.en
dc.description.affiliationNUMPEX-BIO Campus Duque de Caxias Federal University of Rio de Janeiro (UFRJ)
dc.description.affiliationInstitute of Medical Biochemistry Leopoldo de Meis (IBqM) and National Center for Structural Biology and Bioimaging (CENABIO) Federal University of Rio de Janeiro (UFRJ)
dc.description.affiliationMultiuser Center for Biomolecular Innovation (CMIB) and Department of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University (UNESP)
dc.description.affiliationRio BioNMR Network
dc.description.affiliationUnespMultiuser Center for Biomolecular Innovation (CMIB) and Department of Physics Institute of Biosciences Letters and Exact Sciences (IBILCE) São Paulo State University (UNESP)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipIdFAPERJ: 202.279/2018
dc.description.sponsorshipIdFAPERJ: 239.229/2018
dc.description.sponsorshipIdFAPERJ: 255.940/2020
dc.description.sponsorshipIdCNPq: 309564/2017-4
dc.format.extent153-157
dc.identifierhttp://dx.doi.org/10.1007/s12104-020-09998-9
dc.identifier.citationBiomolecular NMR Assignments, v. 15, n. 1, p. 153-157, 2021.
dc.identifier.doi10.1007/s12104-020-09998-9
dc.identifier.issn1874-270X
dc.identifier.issn1874-2718
dc.identifier.scopus2-s2.0-85098594902
dc.identifier.urihttp://hdl.handle.net/11449/207055
dc.language.isoeng
dc.relation.ispartofBiomolecular NMR Assignments
dc.sourceScopus
dc.subjectHKU1
dc.subjectHuman betacoronavirus
dc.subjectN-terminal domain
dc.subjectNMR assignment
dc.subjectNucleocapsid protein
dc.title1H, 15N and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the endemic human coronavirus HKU1en
dc.typeArtigo
dspace.entity.typePublication
unesp.author.orcid0000-0001-9730-5764[1]
unesp.author.orcid0000-0003-4464-0520[2]
unesp.author.orcid0000-0001-6744-1669[3]
unesp.author.orcid0000-0002-6439-1931[5]
unesp.author.orcid0000-0001-6046-7006[6]
unesp.author.orcid0000-0003-4348-9515[7]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Letras e Ciências Exatas, São José do Rio Pretopt
unesp.departmentFísica - IBILCEpt

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