ArticleJournal of virology1996
Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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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
68 citing papers in PubMed, 197 citations in OpenAlex.
- Transmembrane Domain Length of Influenza a Virus M2 Does Not Determine Its Non-Lipid Raft Localization.Viruses · 2026Article
- Review
- Immune response in influenza virus infection and modulation of immune injury by viral neuraminidase.Virology journal · 2023Review
- Self-organization of apical membrane protein sorting in epithelial cells.The FEBS journal · 2022Article
- Review
- Influenza Neuraminidase Characteristics and Potential as a Vaccine Target.Frontiers in immunology · 2021Review
- Viroporins in the Influenza Virus.Cells · 2019Review
- Transcytosis maintains CFTR apical polarity in the face of constitutive and mutation-induced basolateral missorting.Journal of cell science · 2019Article
- Influenza Virus Neuraminidase Structure and Functions.Frontiers in microbiology · 2019Review
- Comprehensive profiling of translation initiation in influenza virus infected cells.PLoS pathogens · 2019Article
- Influenza A Virus M2 Protein Apical Targeting Is Required for Efficient Virus Replication.Journal of virology · 2018Article
- The lipid raft-dwelling protein US9 can be manipulated to target APP compartmentalization, APP processing, and neurodegenerative disease pathogenesis.Scientific reports · 2017Article
- The Diverse Forms of Lactose Intolerance and the Putative Linkage to Several Cancers.Nutrients · 2015Review
- Structural and functional analysis of endosomal compartments in epithelial cells.Methods in cell biology · 2015Article
- Influenza A virus hemagglutinin and neuraminidase mutually accelerate their apical targeting through clustering of lipid rafts.Journal of virology · 2014Article
- Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Viruses · 2014Review
- Trafficking to the apical and basolateral membranes in polarized epithelial cells.Journal of the American Society of Nephrology : JASN · 2014Review
- Palmitoylation is required for intracellular trafficking of influenza B virus NB protein and efficient influenza B virus growth in vitro.The Journal of general virology · 2014Article
- Specific nucleoprotein residues affect influenza virus morphology.Journal of virology · 2014Article
- A comprehensive map of the influenza A virus replication cycle.BMC systems biology · 2013Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The influenza virus neuraminidase (NA), a type II transmembrane protein, is directly transported to the apical plasma membrane in polarized MDCK cells. By using deletion mutants and chimeric constructs of influenza virus NA with the human transferrin receptor, a type II basolateral transmembrane protein, we investigated the location of the apical sorting signal of influenza virus NA. When these mutant and chimeric proteins were expressed in stably transfected polarized MDCK cells, the transmembrane domain of NA, and not the cytoplasmic tail, provided a determinant for apical targeting in polarized MDCK cells and this transmembrane signal was sufficient for sorting and transport of the ectodomain of a reporter protein (transferrin receptor) directly to the apical plasma membrane of polarized MDCK cells. In addition, by using differential detergent extraction, we demonstrated that influenza virus NA and the chimeras which were transported to the apical plasma membrane also became insoluble in Triton X-100 but soluble in octylglucoside after extraction from MDCK cells during exocytic transport. These data indicate that the transmembrane domain of NA provides the determinant(s) both for apical transport and for association with Triton X-100-insoluble lipids.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.