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The hepatitis E virus ORF1 X-domain N-terminal residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for RNA replication
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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Published by Elsevier B.V.
2015
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7172070/ http://dx.doi.org/10.1016/j.jcv.2015.06.011 |
| _version_ | 1783524183276257280 |
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| author | Parvez, M.K. |
| author_facet | Parvez, M.K. |
| author_sort | Parvez, M.K. |
| collection | PubMed |
| description | |
| format | Online Article Text |
| id | pubmed-7172070 |
| institution | National Center for Biotechnology Information |
| language | English |
| publishDate | 2015 |
| publisher | Published by Elsevier B.V. |
| record_format | MEDLINE/PubMed |
| spelling | pubmed-71720702020-04-22 The hepatitis E virus ORF1 X-domain N-terminal residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for RNA replication Parvez, M.K. J Clin Virol Article Published by Elsevier B.V. 2015-08 2015-07-22 /pmc/articles/PMC7172070/ http://dx.doi.org/10.1016/j.jcv.2015.06.011 Text en Copyright © 2015 Published by Elsevier B.V. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
| spellingShingle | Article Parvez, M.K. The hepatitis E virus ORF1 X-domain N-terminal residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for RNA replication |
| title | The hepatitis E virus ORF1 X-domain N-terminal residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for RNA replication |
| title_full | The hepatitis E virus ORF1 X-domain N-terminal residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for RNA replication |
| title_fullStr | The hepatitis E virus ORF1 X-domain N-terminal residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for RNA replication |
| title_full_unstemmed | The hepatitis E virus ORF1 X-domain N-terminal residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for RNA replication |
| title_short | The hepatitis E virus ORF1 X-domain N-terminal residues form a putative macrodomain protein/Appr-1″-pase catalytic-site, critical for RNA replication |
| title_sort | hepatitis e virus orf1 x-domain n-terminal residues form a putative macrodomain protein/appr-1″-pase catalytic-site, critical for rna replication |
| topic | Article |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7172070/ http://dx.doi.org/10.1016/j.jcv.2015.06.011 |
| work_keys_str_mv | AT parvezmk thehepatitisevirusorf1xdomainnterminalresiduesformaputativemacrodomainproteinappr1pasecatalyticsitecriticalforrnareplication AT parvezmk hepatitisevirusorf1xdomainnterminalresiduesformaputativemacrodomainproteinappr1pasecatalyticsitecriticalforrnareplication |