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Cited by 285

The DOI matches its Crossref record; 134 of the 134 references it cites were found in a registry or an index.

C-reactive protein and inflammation: conformational changes affect function

Wu, Yi, Potempa, Lawrence A., El Kebir, Driss, Filep, János G.·2015·Biological Chemistry

Abstract

The prototypic acute-phase reactant C-reactive protein (CRP) has long been recognized as a useful marker and gauge of inflammation. CRP also plays an important role in host defense against invading pathogens as well as in inflammation. CRP consists of five identical subunits arranged as a cyclic pentamer. CRP exists in at least two conformationally distinct forms, i.e. native pentameric CRP (pCRP) and modified/monomeric CRP (mCRP). These isoforms bind to distinct receptors and lipid rafts, and exhibit distinct functional properties. Dissociation of pCRP into its subunits occurs within the inflammatory microenvironment and newly formed mCRP may then contribute to localizing the inflammatory response. Accumulating evidence indicates that pCRP possesses both pro- and anti-inflammatory actions in a context-dependent manner, whereas mCRP exerts potent pro-inflammatory actions on endothelial cells, endothelial progenitor cells, leukocytes and platelets, and thus may amplify inflammation. Here, we review recent advances that may explain how conformational changes in CRP contribute to shaping the inflammatory response and discuss CRP isomers as potential therapeutic targets to dampen inflammation.

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Metadata

Authors
Wu, Y., Potempa, L. A., El Kebir, D., & Filep, J. G.
Venue
Biological Chemistry
Published
2015-11-01
Volume
396
Issue
11
Pages
1181-1197
ISSN
  • 1431-6730 (ISSN-L)
  • 1437-4315
OpenAlex
W2469090867
Cited by
285
References
134
FWCI
5.36
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: C-reactive protein and inflammation: conformational changes affect function. https://app.cochat.ai/papers/10.1515/hsz-2015-0149
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Wu, Y., Potempa, L. A., El Kebir, D., & Filep, J. G. (2015). C-reactive protein and inflammation: conformational changes affect function. Biological Chemistry. https://doi.org/10.1515/hsz-2015-0149

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