<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Lateef Z</submitter><funding>Health Research Council of New Zealand</funding><pagination>39</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5217272</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>18(1)</volume><pubmed_abstract>&lt;h4>Background&lt;/h4>The GII.4 Sydney 2012 strain of human norovirus (HuNoV) is a pandemic strain that is responsible for the majority of norovirus outbreaks in healthcare settings. The function of the non-structural (NS)1-2 protein from HuNoV is unknown.&lt;h4>Results&lt;/h4>In silico analysis of human norovirus NS1-2 protein showed that it shares features with the murine NS1-2 protein, including a disordered region, a transmembrane domain and H-box and NC sequence motifs. The proteins also contain caspase cleavage and phosphorylation sites, indicating that processing and phosphorylation may be a conserved feature of norovirus NS1-2 proteins. In this study, RNA transcripts of human and murine norovirus full-length and the disordered region of NS1-2 were transfected into monocytes, and next genera</pubmed_abstract><journal>BMC genomics</journal><pubmed_title>Transcriptomic analysis of human norovirus NS1-2 protein highlights a multifunctional role in murine monocytes.</pubmed_title><pmcid>PMC5217272</pmcid><funding_grant_id>12-057 Career Development Award</funding_grant_id><pubmed_authors>Baker ES</pubmed_authors><pubmed_authors>Ward VK</pubmed_authors><pubmed_authors>Gimenez G</pubmed_authors><pubmed_authors>Lateef Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Transcriptomic analysis of human norovirus NS1-2 protein highlights a multifunctional role in murine monocytes.</name><description>&lt;h4>Background&lt;/h4>The GII.4 Sydney 2012 strain of human norovirus (HuNoV) is a pandemic strain that is responsible for the majority of norovirus outbreaks in healthcare settings. The function of the non-structural (NS)1-2 protein from HuNoV is unknown.&lt;h4>Results&lt;/h4>In silico analysis of human norovirus NS1-2 protein showed that it shares features with the murine NS1-2 protein, including a disordered region, a transmembrane domain and H-box and NC sequence motifs. The proteins also contain caspase cleavage and phosphorylation sites, indicating that processing and phosphorylation may be a conserved feature of norovirus NS1-2 proteins. In this study, RNA transcripts of human and murine norovirus full-length and the disordered region of NS1-2 were transfected into monocytes, and next genera</description><dates><release>2017-01-01T00:00:00Z</release><publication>2017 Jan</publication><modification>2026-06-10T05:43:32.76Z</modification><creation>2019-06-06T16:50:15Z</creation></dates><accession>S-EPMC5217272</accession><cross_references><pubmed>28056773</pubmed><doi>10.1186/s12864-016-3417-4</doi></cross_references></HashMap>