The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway.
Open accessAbstract
Using a monoclonal antibody (mAb 414), we previously identified a protein of 62 kDa (p62) that was localized to the nuclear pore complex by immunoelectron microscopy. We also showed that p62 binds specifically to wheat germ agglutinin. Therefore, we proposed that this nuclear pore complex protein might be a member of a recently characterized family of glycoproteins that are labeled by in vitro galactosylation of rat liver nuclei and contain O-linked monosaccharidic GlcNAc residues. In support of this, we now show that incubation with N-acetylglucosaminidase reduces the molecular mass of p62 by approximately 3 kDa because of the removal of terminal GlcNAc residues. Moreover, p62 can be galactosylated in vitro by using UDP-[3H]galactose and galactosyltransferase. We also show that most of the GlcNAc residues are added within 5 min of synthesis, when p62 is soluble and cytosolic. Thus, the addition of GlcNAc is carried out in the cytoplasm and is clearly distinct from the N- and O-linked glycosylation pathways of the endoplasmic reticulum and Golgi complex. Using another mAb with a broad specificity for nuclear GlcNAc-containing proteins, we show by immunofluorescence and protein blotting of subnuclear fractions that some of these proteins are in the interior of the nucleus, and others are most likely located in the pore complex.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cleveland, D. W., Fischer, S. G., Kirschner, M. W., & Laemmli, U. K. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75212-0 · Cited by 5,556
Nuclei from Rat Liver: Isolation Method That Combines Purity with High Yield
Blobel, G., & Potter, V. R. (1966) · Science · doi:10.1126/science.154.3757.1662 · Cited by 1,667
Self-citationTorres, C. R., & Hart, G. W. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43295-9 · Cited by 1,131
Purification and Properties of an Endo-β-N-acetylglucosaminidase from Streptomyces griseus
Tarentino, A. L., & Maley, F. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43001-9 · Cited by 850
Tkacz, J. S., & Lampen, J. O. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(75)80086-6 · Cited by 843
Identification and characterization of a nuclear pore complex protein
Davis, L. I., & Blobel, G. (1986) · Cell · doi:10.1016/0092-8674(86)90784-1 · Cited by 617
Self-citationTUNICAMYCIN, A NEW ANTIBIOTIC. I
TAKATSUKI, A., ARIMA, K., & TAMURA, G. (1971) · The Journal of Antibiotics · doi:10.7164/antibiotics.24.215 · Cited by 557
Monoclonal antibodies identify a group of nuclear pore complex glycoproteins.
Snow, C. M., Senior, A., & Gerace, L. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.5.1143 · Cited by 538
Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores.
Finlay, D. R., Newmeyer, D. D., Price, T. M., & Forbes, D. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.2.189 · Cited by 509
Holt, G. D., & Hart, G. W. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57510-x · Cited by 497
Cited by
D'Angelo, M. A., Raices, M., Panowski, S. H., & Hetzer, M. W. (2009) · Cell · doi:10.1016/j.cell.2008.11.037 · Cited by 565
A chemical approach for identifying O -GlcNAc-modified proteins in cells
Vocadlo, D. J., Hang, H. C., Kim, E.-J., Hanover, J. A., & Bertozzi, C. R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1632821100 · Cited by 538
Glycan-dependent signaling: O-linked N-acetylglucosamine
HANOVER, J. A. (2001) · The FASEB Journal · doi:10.1096/fj.01-0094rev · Cited by 283
O-GlcNAc occurs cotranslationally to stabilize nascent polypeptide chains
Zhu, Y., Liu, T.-W., Cecioni, S., Eskandari, R., Zandberg, W. F., & Vocadlo, D. J. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1774 · Cited by 134
Starr, C. M., & Hanover, J. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39229-4 · Cited by 87
Metadata
- Authors
- Davis, L. I., & Blobel, G.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1987-11
- Volume
- 84
- Issue
- 21
- Pages
- 7552-7556
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2015646338
- Cited by
- 337
- References
- 15
- FWCI
- 6.08
- Type
- journal article
- Language
- en
- Open access
- green
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway. https://app.cochat.ai/papers/10.1073/pnas.84.21.7552
- The paper
- Davis, L. I., & Blobel, G. (1987). Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.84.21.7552
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
