ArticleThe Journal of cell biology1987
Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores.
Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 220 papers.
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Who cites it
220 citing papers in PubMed, 514 citations in OpenAlex.
- Bound for the nucleus: defining the molecular principles of cargo selection by importin 9.bioRxiv : the preprint server for biology · 2026Article
- Nanoscale Mapping of the Subcellular Glycosylation Landscape.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Review
- O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- SARS-CoV-2 Orf6 is positioned in the nuclear pore complex by Rae1 to inhibit nucleocytoplasmic transport.Molecular biology of the cell · 2024Article
- Quantitative comparison of nuclear transport inhibition by SARS coronavirus ORF6 reveals the importance of oligomerization.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- SUN1 facilitates CHMP7 nuclear influx and injury cascades in sporadic amyotrophic lateral sclerosis.Brain : a journal of neurology · 2024Article
- Dynamic molecular mechanism of the nuclear pore complex permeability barrier.bioRxiv : the preprint server for biology · 2023Article
- Mechanomemory in protein diffusivity of chromatin and nucleoplasm after force cessation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- An Epigenetic Role of Mitochondria in Cancer.Cells · 2022Review
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- Blocking the BKCa channel induces NF-κB nuclear translocation by increasing nuclear calcium concentration†.Biology of reproduction · 2022Article
- Intranuclear HSV-1 DNA ejection induces major mechanical transformations suggesting mechanoprotection of nucleus integrity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Reconstituted virus-nucleus system reveals mechanics of herpesvirus genome uncoating.QRB discovery · 2022Article
- Methods to separate nuclear soluble fractions reflecting localizations in living cells.iScience · 2021Article
- Role of HSV-1 Capsid Vertex-Specific Component (CVSC) and Viral Terminal DNA in Capsid Docking at the Nuclear Pore.Viruses · 2021Article
- The role of DDK and Treslin-MTBP in coordinating replication licensing and pre-initiation complex formation.Open biology · 2021Article
- Measuring and Interpreting Nuclear Transport in Neurodegenerative Disease-The Example of C9orf72 ALS.International journal of molecular sciences · 2021Review
- Recapitulation of selective nuclear import and export with a perfectly repeated 12mer GLFG peptide.Nature communications · 2021Article
160 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.
Funding
Abstract
Selective transport of proteins is a major mechanism by which biochemical differences are maintained between the cytoplasm and nucleus. To begin to investigate the molecular mechanism of nuclear transport, we used an in vitro transport system composed of a Xenopus egg extract, rat liver nuclei, and a fluorescently labeled nuclear protein, nucleoplasmin. With this system, we screened for inhibitors of transport. We found that the lectin, wheat germ agglutinin (WGA), completely inhibits the nuclear transport of fluorescently labeled nucleoplasmin. No other lectin tested affected nuclear transport. The inhibition by WGA was not seen when N-acetylglucosamine was present and was reversible by subsequent addition of sugar. When rat liver nuclei that had been incubated with ferritin-labeled WGA were examined by electron microscopy, multiple molecules of WGA were found bound to the cytoplasmic face of each nuclear pore. Gel electrophoresis and nitrocellulose transfer identified one major and several minor nuclear protein bands as binding 125I-labeled WGA. The most abundant protein of these, a 63-65-kD glycoprotein, is a candidate for the inhibitory site of action of WGA on nuclear protein transport. WGA is the first identified inhibitor of nuclear protein transport and interacts directly with the nuclear pore.
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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.