ArticleThe Journal of biological chemistry2012
Exposing a hidden functional site of C-reactive protein by site-directed mutagenesis.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 36 citations in OpenAlex.
- Protection against prolonged pneumococcal infection involves structural changes in C-reactive protein and subsequent binding to both phosphocholine and amyloids on the bacterial surface.Frontiers in immunology · 2025Article
- An evolutionarily conserved function of C-reactive protein is to prevent the formation of amyloid fibrils.Frontiers in immunology · 2024Article
- C-reactive protein: a target for therapy to reduce inflammation.Frontiers in immunology · 2023Review
- Structurally Altered, Not Wild-Type, Pentameric C-Reactive Protein Inhibits Formation of Amyloid-β Fibrils.Journal of immunology (Baltimore, Md. : 1950) · 2022Article
- Biochemically prepared C-reactive protein conformational states differentially affect C1q binding.BBA advances · 2022Article
- Cryo-Electron Microscopy and Biochemical Analysis Offer Insights Into the Effects of Acidic pH, Such as Occur During Acidosis, on the Complement Binding Properties of C-Reactive Protein.Frontiers in immunology · 2021Article
- Intra-subunit Disulfide Determines the Conversion and Structural Stability of CRP Isoforms.Inflammation · 2020Article
- C-Reactive Protein-Based Strategy to Reduce Antibiotic Dosing for the Treatment of Pneumococcal Infection.Frontiers in immunology · 2020Article
- Treatment of Pneumococcal Infection by Using Engineered Human C-Reactive Protein in a Mouse Model.Frontiers in immunology · 2020Article
- Conformationally Altered C-Reactive Protein Capable of Binding to Atherogenic Lipoproteins Reduces Atherosclerosis.Frontiers in immunology · 2020Article
- Structure-Function Relationships of C-Reactive Protein in Bacterial Infection.Frontiers in immunology · 2019Review
- Evolution of C-Reactive Protein.Frontiers in immunology · 2019Review
- Functionality of C-Reactive Protein for Atheroprotection.Frontiers in immunology · 2019Review
- Monomeric C-Reactive Protein and Cerebral Hemorrhage: From Bench to Bedside.Frontiers in immunology · 2018Review
- Functional Transformation of C-reactive Protein by Hydrogen Peroxide.The Journal of biological chemistry · 2017Article
- Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites.Nature communications · 2017Article
- Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro.Scientific reports · 2016Article
- The Carbohydrate-linked Phosphorylcholine of the Parasitic Nematode Product ES-62 Modulates Complement Activation.The Journal of biological chemistry · 2016Article
- Factor H-related protein 5 interacts with pentraxin 3 and the extracellular matrix and modulates complement activation.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- C-reactive protein protects mice against pneumococcal infection via both phosphocholine-dependent and phosphocholine-independent mechanisms.Infection and immunity · 2015Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
C-reactive protein (CRP) is a cyclic pentameric protein whose major binding specificity, at physiological pH, is for substances bearing exposed phosphocholine moieties. Another pentameric form of CRP, which exists at acidic pH, displays binding activity for oxidized LDL (ox-LDL). The ox-LDL-binding site in CRP, which is hidden at physiological pH, is exposed by acidic pH-induced structural changes in pentameric CRP. The aim of this study was to expose the hidden ox-LDL-binding site of CRP by site-directed mutagenesis and to generate a CRP mutant that can bind to ox-LDL without the requirement of acidic pH. Mutation of Glu(42), an amino acid that participates in intersubunit interactions in the CRP pentamer and is buried, to Gln resulted in a CRP mutant (E42Q) that showed significant binding activity for ox-LDL at physiological pH. For maximal binding to ox-LDL, E42Q CRP required a pH much less acidic than that required by wild-type CRP. At any given pH, E42Q CRP was more efficient than wild-type CRP in binding to ox-LDL. Like wild-type CRP, E42Q CRP remained pentameric at acidic pH. Also, E42Q CRP was more efficient than wild-type CRP in binding to several other deposited, conformationally altered proteins. The E42Q CRP mutant provides a tool to investigate the functions of CRP in defined animal models of inflammatory diseases including atherosclerosis because wild-type CRP requires acidic pH to bind to deposited, conformationally altered proteins, including ox-LDL, and available animal models may not have sufficient acidosis or other possible modifiers of the pentameric structure of CRP at the sites of inflammation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.