<HashMap><database>iProX</database><scores/><additional><omics_type>Proteomics</omics_type><submitter>Yongyong Shi</submitter><species>Homo Sapiens</species><species>Hendra Virus Horse/australia/hendra/1994</species><species>Nipah Henipavirus</species><full_dataset_link>http://www.iprox.org/page/project.html?id=IPX0017739000</full_dataset_link><submitter_email>shiyongyong@gmail.com</submitter_email><submitter_affiliation>Shanghai Jiao Tong University</submitter_affiliation><sample_protocol></sample_protocol><repository>iProX</repository><data_protocol></data_protocol></additional><is_claimable>false</is_claimable><name>Protein-resolved multi-omic mapping identifies convergent host regulatory nodes in henipa-related paramyxoviruses</name><description>Protein-resolved multi-omic mapping defines a comparative virus–host atlas for LayV, NiV and HeV, integrating interactomes, matched transcriptomes, quantitative proteomes and structural models across 26 viral proteins.  Henipa-related viral proteins retain substantial interaction specificity, yet converge on shared host regulatory programs, revealing host-node convergence as a conserved organizing principle across divergent paramyxoviruses.  Matrix proteins emerge as conserved host-engagement hubs that connect henipa-related viruses to two host-control axes: ABT1-linked transcriptional regulation and MRPS35-linked mitochondrial ribosome function.  M–MRPS35 engagement is conserved across multiple henipa-related viruses and is associated with progressive mitochondrial ultrastructural damage, membrane-potential collapse and loss of cellular fitness.  ABT1 chromatin profiling reveals that M proteins redirect a basal transcription-associated regulator toward altered antiviral and immune-related transcriptional pro</description><dates><publication>Tue Jun 23 00:00:00 GMT+01:00 2026</publication></dates><accession>PXD080026</accession><cross_references><TAXONOMY>928303</TAXONOMY><TAXONOMY>9606</TAXONOMY><TAXONOMY>121791</TAXONOMY></cross_references></HashMap>