ArticleJournal of virology2005
Novel nuclear export signal-interacting protein, NESI, critical for the assembly of hepatitis delta virus.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 1 synthesis or guideline pooled it, 33 citations in OpenAlex.
- Pooled it
- Structural basis for LMBD1-dependent trafficking and cobalamin export of ABCD4.Nature communications · 2026Article
- Hepatitis B virus entry, assembly, and egress.Microbiology and molecular biology reviews : MMBR · 2024Review
- HDV-Like Viruses.Viruses · 2021Review
- Insight into the Contribution and Disruption of Host Processes during HDV Replication.Viruses · 2018Review
- Cellular Nuclear Export Factors TAP and Aly Are Required for HDAg-L-mediated Assembly of Hepatitis Delta Virus.The Journal of biological chemistry · 2016Article
- Lmbrd1 expression is essential for the initiation of gastrulation.Journal of cellular and molecular medicine · 2016Article
- Animal models of chronic hepatitis delta virus infection host-virus immunologic interactions.Pathogens (Basel, Switzerland) · 2015Review
- LMBD1 protein serves as a specific adaptor for insulin receptor internalization.The Journal of biological chemistry · 2013Article
- Nuclear export signal-interacting protein forms complexes with lamin A/C-Nups to mediate the CRM1-independent nuclear export of large hepatitis delta antigen.Journal of virology · 2013Article
- Identification and targeting of an interaction between a tyrosine motif within hepatitis C virus core protein and AP2M1 essential for viral assembly.PLoS pathogens · 2012Article
- The heterogeneous ribonuclear protein C interacts with the hepatitis delta virus small antigen.Virology journal · 2011Article
- LMBRD1: the gene for the cblF defect of vitamin B₁₂ metabolism.Journal of inherited metabolic disease · 2011Review
- In Vivo Interaction of the Hepatitis Delta Virus Small Antigen with the ELAV-Like Protein HuR.The open virology journal · 2011Article
- Insights into lysosomal cobalamin trafficking: lessons learned from cblF disease.Journal of molecular medicine (Berlin, Germany) · 2010Review
- A novel mutation in LMBRD1 causes the cblF defect of vitamin B(12) metabolism in a Turkish patient.Journal of inherited metabolic disease · 2010Article
- Article
- Evolution and diversity of the human hepatitis d virus genome.Advances in bioinformatics · 2010Article
- Clathrin-mediated post-Golgi membrane trafficking in the morphogenesis of hepatitis delta virus.Journal of virology · 2009Article
- Identification of a putative lysosomal cobalamin exporter altered in the cblF defect of vitamin B12 metabolism.Nature genetics · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The process of host factor-mediated nucleocytoplasmic transport is critical for diverse cellular events in eukaryotes and the life cycle of viruses. We have previously identified a chromosome region maintenance 1-independent nuclear export signal (NES) at the C terminus of the large form of hepatitis delta antigen (HDAg), designated NES(HDAg-L) that is required for the assembly of hepatitis delta virus (HDV) (C.-H. Lee et al., J. Biol. Chem. 276:8142-8148, 2001). To look for interacting proteins of the NES(HDAg-L), yeast two-hybrid screening was applied using the GAL4-binding domain fused to the NES(HDAg-L) as bait. Among the positive clones, one encodes a protein, designated NESI [NES(HDAg-L) interacting protein] that specifically interacted with the wild-type NES(HDAg-L) but not with the export/package-defective HDAg-L mutant, NES*(HDAg-L), in which Pro-205 has been replaced by Ala. Northern blot analysis revealed NESI as the gene product of a 1.9-kb endogenous mRNA transcript that is present predominantly in human liver tissue. NESI consists of 467 amino acid residues and bears a putative actin-binding site and a bipartite nuclear localization signal. Specific interaction between HDAg-L and NESI was further confirmed by coimmunoprecipitation and immunofluorescence staining. Overexpression of antisense NESI RNAs inhibited the expression of NESI and abolished HDAg-L-mediated nuclear export and assembly of HDV genomic RNA. These data indicate a critical role of NESI in the assembly of HDV through interaction with HDAg-L.
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