Evidence map›Paper›PMID 28112148›Full record

ArticleNature communications2017

Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites.

David Braig, Tracy L Nero, Hans-Georg Koch, Benedict Kaiser, Xiaowei Wang, Jan R Thiele, Craig J Morton, Johannes Zeller, Jurij Kiefer, Lawrence A Potempa and 9 more

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed, 2 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

134 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Pooled it
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  10. Exosome-primed T cell immunity is facilitated by complement activation.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2026
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74 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

19 authors.

David BraigDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of Freiburg, 79106 Freiburg, Germany.
Tracy L NeroACRF Rational Drug Discovery Centre, St Vincent's Institute of Medical Research, Melbourne, Victoria 3065, Australia.
Hans-Georg KochInstitute for Biochemistry and Molecular Biology and Spemann-Graduate School for Biology and Medicine University of Freiburg, Medical Faculty of the University of Freiburg, 79104 Freiburg, Germany.
Benedict KaiserDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of Freiburg, 79106 Freiburg, Germany.
Xiaowei WangBaker IDI Heart and Diabetes Institute, Melbourne, Victoria 3004, Australia.
Jan R ThieleDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of Freiburg, 79106 Freiburg, Germany.
Craig J MortonACRF Rational Drug Discovery Centre, St Vincent's Institute of Medical Research, Melbourne, Victoria 3065, Australia.
Johannes ZellerDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of Freiburg, 79106 Freiburg, Germany.
Jurij KieferDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of Freiburg, 79106 Freiburg, Germany.
Lawrence A PotempaCollege of Pharmacy, Roosevelt University, Schaumburg, Illinois 60173, USA.
Natalie A MellettBaker IDI Heart and Diabetes Institute, Melbourne, Victoria 3004, Australia.
Luke A MilesACRF Rational Drug Discovery Centre, St Vincent's Institute of Medical Research, Melbourne, Victoria 3065, Australia.
Xiao-Jun DuBaker IDI Heart and Diabetes Institute, Melbourne, Victoria 3004, Australia.
Peter J MeikleBaker IDI Heart and Diabetes Institute, Melbourne, Victoria 3004, Australia.ORCID 0000-0002-2593-4665
Markus Huber-LangDepartment of Traumatology, Hand, Plastic, and Reconstructive Surgery, Center of Surgery, University of Ulm, 89081 Ulm, Germany.
G Björn StarkDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of Freiburg, 79106 Freiburg, Germany.
Michael W ParkerACRF Rational Drug Discovery Centre, St Vincent's Institute of Medical Research, Melbourne, Victoria 3065, Australia.ORCID 0000-0002-3101-1138
Karlheinz PeterBaker IDI Heart and Diabetes Institute, Melbourne, Victoria 3004, Australia.
Steffen U EisenhardtDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of Freiburg, 79106 Freiburg, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

C-reactive protein (CRP) concentrations rise in response to tissue injury or infection. Circulating pentameric CRP (pCRP) localizes to damaged tissue where it leads to complement activation and further tissue damage. In-depth knowledge of the pCRP activation mechanism is essential to develop therapeutic strategies to minimize tissue injury. Here we demonstrate that pCRP by binding to cell-derived microvesicles undergoes a structural change without disrupting the pentameric symmetry (pCRP*). pCRP* constitutes the major CRP species in human-inflamed tissue and allows binding of complement factor 1q (C1q) and activation of the classical complement pathway. pCRP*-microvesicle complexes lead to enhanced recruitment of leukocytes to inflamed tissue. A small-molecule inhibitor of pCRP (1,6-bis(phosphocholine)-hexane), which blocks the pCRP-microvesicle interactions, abrogates these proinflammatory effects. Reducing inflammation-mediated tissue injury by therapeutic inhibition might improve the outcome of myocardial infarction, stroke and other inflammatory conditions.

Indexed as

Amino Acid SequenceAnimalsBinding SitesC-Reactive ProteinGene Expression RegulationHexanesHumansInflammationLipopolysaccharidesModels, MolecularMonocytesMuscle, SkeletalPhosphorylcholineProtein BindingProtein ConformationRats1,6-bis(phosphocholine)-hexaneC-Reactive ProteinHexanesLipopolysaccharidesPhosphorylcholine

Identifiers

PMID28112148
PMCPMC5264208

What OpenQuestion holds

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Registered trials

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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.