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Cited by 481

The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.

Properdin: binding to C3b and stabilization of the C3b-dependent C3 convertase.

Open access
Fearon, D T, Austen, K F·1975·The Journal of experimental medicine

Abstract

A function of P in the alternative complement pathway is to prolong the first order decay of the hemolytic sites on EAC43B in a dose-dependent manner. As the number of initial convertase sites is not changed, even when activated properdin (P) increases the t1/2 10-fold or more, P acts to stabilize rather than to uncover additional sites. P binds to EAC43 to generate EAC43P in a reaction that proceeds slightly more rapidly at 15 degrees C than at 0 degrees C, but reaches the same plateau and does not require divalent cations. The presence of P on EAC43P not only stabilizes the convertase subsequently formed on that cell, but, alternatively, permits transfer to convertase sites on other cells with the stability of the recipient intermediate being dependent on the P available for transfer. The capacity of P to bind to C3b and stabilize C3B contrasts with the inhibitory effect of the C3b inactivator on formation of this amplification convertase.

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Metadata

Authors
Fearon, D. T., & Austen, K. F.
Venue
The Journal of experimental medicine
Published
1975-10-01
Volume
142
Issue
4
Pages
856-863
ISSN
  • 0022-1007 (ISSN-L)
  • 1540-9538
OpenAlex
W2014513484
Cited by
481
References
8
FWCI
8.63
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Properdin: binding to C3b and stabilization of the C3b-dependent C3 convertase. https://app.cochat.ai/papers/10.1084/jem.142.4.856
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Fearon, D. T., & Austen, K. F. (1975). Properdin: binding to C3b and stabilization of the C3b-dependent C3 convertase. The Journal of experimental medicine. https://doi.org/10.1084/jem.142.4.856

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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.