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Cited by 342

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2.

Open access
Bischoff, J R, Friedman, P N, Marshak, D R, Prives, C, Beach, D·1990·Proceedings of the National Academy of Sciences

Abstract

The human anti-oncoprotein p53 is shown to be a substrate of cdc2. The primary site of phosphorylation is serine-315. Serine-315 is phosphorylated by both p60-cdc2 and cyclin B-cdc2 enzymes. The phosphorylation of p53 is cell cycle-dependent. The abundance of p53 also oscillates during the cell cycle. The protein is largely absent from cells that have just completed division but accumulates in cells during G1 phase. Phosphorylation by cdc2 might regulate the antiproliferative activity of p53.

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Crossref · 10.1073/pnas.87.12.4766

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Metadata

Authors
Bischoff, J. R., Friedman, P. N., Marshak, D. R., Prives, C., & Beach, D.
Venue
Proceedings of the National Academy of Sciences
Published
1990-06
Volume
87
Issue
12
Pages
4766-4770
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2078731043
Cited by
342
References
2
FWCI
20.91
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2. https://app.cochat.ai/papers/10.1073/pnas.87.12.4766
The paper
Bischoff, J. R., Friedman, P. N., Marshak, D. R., Prives, C., & Beach, D. (1990). Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.87.12.4766

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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.