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Cited by 432

The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.

Antiangiogenic Activity of the Cleaved Conformation of the Serpin Antithrombin

O'Reilly, Michael S., Pirie-Shepherd, Steven, Lane, William S., Folkman, Judah·1999·Science

Abstract

Antithrombin, a member of the serpin family, functions as an inhibitor of thrombin and other enzymes. Cleavage of the carboxyl-terminal loop of antithrombin induces a conformational change in the molecule. Here it is shown that the cleaved conformation of antithrombin has potent antiangiogenic and antitumor activity in mouse models. The latent form of intact antithrombin, which is similar in conformation to the cleaved molecule, also inhibited angiogenesis and tumor growth. These data provide further evidence that the clotting and fibrinolytic pathways are directly involved in the regulation of angiogenesis.

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Crossref · 10.1126/science.285.5435.1926

Cites

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Citations

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Metadata

Authors
O'Reilly, M. S., Pirie-Shepherd, S., Lane, W. S., & Folkman, J.
Venue
Science
Published
1999-09-17
Volume
285
Issue
5435
Pages
1926-1928
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2141836567
Cited by
432
References
15
FWCI
18.49
Type
journal article
Language
en
Open access
closed

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This page
CoChat. (2026). Citation check: Antiangiogenic Activity of the Cleaved Conformation of the Serpin Antithrombin. https://app.cochat.ai/papers/10.1126/science.285.5435.1926
The paper
O'Reilly, M. S., Pirie-Shepherd, S., Lane, W. S., & Folkman, J. (1999). Antiangiogenic Activity of the Cleaved Conformation of the Serpin Antithrombin. Science. https://doi.org/10.1126/science.285.5435.1926

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.