The DOI matches its Crossref record.
Cytomegalovirus Recruitment of Cellular Kinases to Dissolve the Nuclear Lamina
Abstract
The passage of large-sized herpesviral capsids through the nuclear lamina and the inner nuclear membrane to leave the nucleus requires a dissolution of the nuclear lamina. Here, we report on the functions of M50/p35, a β-herpesviral protein of murine cytomegalovirus. M50/p35 inserts into the inner nuclear membrane and is aggregated by a second viral protein, M53/p38, to form the capsid docking site. M50/p35 recruits the cellular protein kinase C for phosphorylation and dissolution of the nuclear lamina, suggesting that herpesviruses target a critical element of nuclear architecture.
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
Cited by
Dechat, T., Pfleghaar, K., Sengupta, K., Shimi, T., Shumaker, D. K., Solimando, L., & Goldman, R. D. (2008) · Genes & Development · doi:10.1101/gad.1652708 · Cited by 940
Herpesviruses remodel host membranes for virus egress
Johnson, D. C., & Baines, J. D. (2011) · Nature Reviews Microbiology · doi:10.1038/nrmicro2559 · Cited by 450
Irvine, R. F. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1100 · Cited by 406
Mechanisms and functions of nuclear envelope remodelling
Ungricht, R., & Kutay, U. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.153 · Cited by 346
Herpesvirus assembly: a tale of two membranes
Mettenleiter, T. C., Klupp, B. G., & Granzow, H. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.06.013 · Cited by 265
Metadata
- Authors
- Muranyi, W., Haas, J., Wagner, M., Krohne, G., & Koszinowski, U. H.
- Venue
- Science
- Published
- 2002-08-02
- Volume
- 297
- Issue
- 5582
- Pages
- 854-857
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2113221891
- Cited by
- 276
- References
- 0
- FWCI
- 10.46
- Type
- journal article
- Language
- en
- Open access
- closed
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: Cytomegalovirus Recruitment of Cellular Kinases to Dissolve the Nuclear Lamina. https://app.cochat.ai/papers/10.1126/science.1071506
- The paper
- Muranyi, W., Haas, J., Wagner, M., Krohne, G., & Koszinowski, U. H. (2002). Cytomegalovirus Recruitment of Cellular Kinases to Dissolve the Nuclear Lamina. Science. https://doi.org/10.1126/science.1071506
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.
