ArticleChromosoma1988
Monoclonal antibodies to a Mr 68,000 pore complex glycoprotein interfere with nuclear protein uptake in Xenopus oocytes.
Article in Chromosoma, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 97 citations in OpenAlex.
- The nuclear pore complex: understanding its function through structural insight.Nature reviews. Molecular cell biology · 2017Review
- Nucleolar adaptation in human cancer.Cancer investigation · 2005Review
- The nucleoporin nup153 plays a critical role in multiple types of nuclear export.Molecular biology of the cell · 1999Article
- Chromosomal proteins HMG-14 and HMG-17 are released from mitotic chromosomes and imported into the nucleus by active transport.The Journal of cell biology · 1998Article
- The nuclear pore complex.Plant molecular biology · 1998Review
- The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways.The Journal of cell biology · 1997Article
- In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p.Molecular biology of the cell · 1997Article
- A GTPase distinct from Ran is involved in nuclear protein import.The Journal of cell biology · 1996Article
- The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor.The Journal of cell biology · 1995Article
- Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation.The Journal of cell biology · 1995Article
- Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes.Molecular biology of the cell · 1995Article
- Reconstituted nuclei depleted of a vertebrate GLFG nuclear pore protein, p97, import but are defective in nuclear growth and replication.The Journal of cell biology · 1995Article
- Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: binding of nucleoporin p54 to the rod domain of p62.The Journal of cell biology · 1995Article
- Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p.The EMBO journal · 1995Article
- In vitro nuclear import of snRNPs: cytosolic factors mediate m3G-cap dependence of U1 and U2 snRNP transport.The EMBO journal · 1994Article
- Nup180, a novel nuclear pore complex protein localizing to the cytoplasmic ring and associated fibrils.The Journal of cell biology · 1993Article
- Intranuclear filaments containing a nuclear pore complex protein.The Journal of cell biology · 1993Article
- Isolation of the yeast nuclear pore complex.The Journal of cell biology · 1993Article
- Nup155 is a novel nuclear pore complex protein that contains neither repetitive sequence motifs nor reacts with WGA.The Journal of cell biology · 1993Article
- High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores.The Journal of cell biology · 1992Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Using a monoclonal antibody (PI1) raised against mouse lymphocyte nuclear matrix fractions we have identified a N-acetylglucosamine (GlcNAc)-containing glycoprotein of Mr 68,000 as a component of the nuclear pore complexes of Xenopus laevis oocytes. The antigenic determinant recognized by antibody PI1 comprises both the sugar moiety and protein sequences since, on the one hand, added GlcNAc competed effectively for antibody binding and, on the other hand, the antibody reacted in immunoblots with only one member of the GlcNAc-containing pore complex glycoprotein family. By using immunogold-electron microscopy we could demonstrate that the Mr 68,000 glycoprotein was located preferentially to the cytoplasmic side of the pore complex channel. When radiolabeled soluble nuclear proteins were injected into the cytoplasm of Xenopus oocytes, their reentry into the nucleus was almost completely inhibited in the presence of antibody PI1 as shown by two-dimensional gel electrophoresis. The results indicate that the evolutionarily conserved Mr 68,000 glycoprotein is involved in transport processes of karyophilic proteins from the cytoplasm into the nucleus.
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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.