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Cited by 288

The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.

Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition.

Open access
Kayalar, C, Ord, T, Testa, M P, Zhong, L T, Bredesen, D E·1996·Proceedings of the National Academy of Sciences

Abstract

Three of the predominant features of apoptosis are internucleosomal DNA fragmentation, plasma membrane bleb formation, and retraction of cell processes. We demonstrate that actin is a substrate for the proapoptotic cysteine protease interleukin 1beta-converting enzyme. Actin cleaved by interleukin 1beta-converting enzyme can neither inhibit DNase I nor polymerize to its filamentous form as effectively as intact actin. These findings suggest a mechanism for the coordination of the proteolytic, endonucleolytic, and morphogenetic aspects of apoptosis.

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Crossref · 10.1073/pnas.93.5.2234

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Metadata

Authors
Kayalar, C., Ord, T., Testa, M. P., Zhong, L. T., & Bredesen, D. E.
Venue
Proceedings of the National Academy of Sciences
Published
1996-03-05
Volume
93
Issue
5
Pages
2234-2238
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2052759051
Cited by
288
References
34
FWCI
15.34
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition. https://app.cochat.ai/papers/10.1073/pnas.93.5.2234
The paper
Kayalar, C., Ord, T., Testa, M. P., Zhong, L. T., & Bredesen, D. E. (1996). Cleavage of actin by interleukin 1 beta-converting enzyme to reverse DNase I inhibition. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.93.5.2234

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.