<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9(5)</volume><submitter>Bauer A</submitter><pubmed_abstract>Membrane envelopment and budding of negative strand RNA viruses (NSVs) is mainly driven by viral matrix proteins (M). In addition, several M proteins are also known to be involved in host cell manipulation. Knowledge about the cellular targets and detailed molecular mechanisms, however, is poor for many M proteins. For instance, Nipah Virus (NiV) M protein trafficking through the nucleus is essential for virus release, but nuclear targets of NiV M remain unknown. To identify cellular interactors of henipavirus M proteins, tagged Hendra Virus (HeV) M proteins were expressed and M-containing protein complexes were isolated and analysed. Presence of acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) in the complex suggested that this protein represents a direct or indirect</pubmed_abstract><journal>PloS one</journal><pagination>e97233</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4019565</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>ANP32B is a nuclear target of henipavirus M proteins.</pubmed_title><pmcid>PMC4019565</pmcid><pubmed_authors>Lamp B</pubmed_authors><pubmed_authors>Neumann S</pubmed_authors><pubmed_authors>Karger A</pubmed_authors><pubmed_authors>Kwasnitschka L</pubmed_authors><pubmed_authors>Bauer A</pubmed_authors><pubmed_authors>Henning AK</pubmed_authors><pubmed_authors>Dietzel E</pubmed_authors><pubmed_authors>Balkema-Buschmann A</pubmed_authors><pubmed_authors>Finke S</pubmed_authors><pubmed_authors>Maisner A</pubmed_authors><pubmed_authors>Keil GM</pubmed_authors></additional><is_claimable>false</is_claimable><name>ANP32B is a nuclear target of henipavirus M proteins.</name><description>Membrane envelopment and budding of negative strand RNA viruses (NSVs) is mainly driven by viral matrix proteins (M). In addition, several M proteins are also known to be involved in host cell manipulation. Knowledge about the cellular targets and detailed molecular mechanisms, however, is poor for many M proteins. For instance, Nipah Virus (NiV) M protein trafficking through the nucleus is essential for virus release, but nuclear targets of NiV M remain unknown. To identify cellular interactors of henipavirus M proteins, tagged Hendra Virus (HeV) M proteins were expressed and M-containing protein complexes were isolated and analysed. Presence of acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) in the complex suggested that this protein represents a direct or indirect</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014</publication><modification>2025-04-19T01:31:17.821Z</modification><creation>2019-06-06T12:44:39Z</creation></dates><accession>S-EPMC4019565</accession><cross_references><pubmed>24823948</pubmed><doi>10.1371/journal.pone.0097233</doi></cross_references></HashMap>