Evidence map›Paper›PMID 29247897›Full record

ReviewRedox biology2018

Post-translational regulation of macrophage migration inhibitory factor: Basis for functional fine-tuning.

Lisa Schindler, Nina Dickerhof, Mark B Hampton, Jürgen Bernhagen

Open access · goldAbstract readReview
In one paragraph

Review in Redox biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.2field-weighted citation impact, top 12% of its field
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

26 citing papers in PubMed, 47 citations in OpenAlex.

  1. Cysteine thiol-to-sulfonate oxidation induces unfolding for the functional switching of the extracellular HMGB1 protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
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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

4 authors at 2 institutions in 2 countries.

Lisa SchindlerDepartment of Vascular Biology, Institute for Stroke and Dementia Research (ISD), Ludwig-Maximilians-University (LMU), Munich, Germany.
Nina DickerhofCentre for Free Radical Research, Department of Pathology, University of Otago, Christchurch, New Zealand.
Mark B HamptonCentre for Free Radical Research, Department of Pathology, University of Otago, Christchurch, New Zealand.
Jürgen BernhagenDepartment of Vascular Biology, Institute for Stroke and Dementia Research (ISD), Ludwig-Maximilians-University (LMU), Munich, Germany; Munich Cluster for System Neurology (EXC 1010 SyNergy), Munich, Germany. Electronic address: Juergen.Bernhagen@med.uni-muenchen.de.
Ludwig-Maximilians-Universität München · DEUniversity of Otago · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macrophage migration inhibitory factor (MIF) is a chemokine-like protein and an important mediator in the inflammatory response. Unlike most other pro-inflammatory cytokines, a number of cell types constitutively express MIF and secretion occurs from preformed stores. MIF is an evolutionarily conserved protein that shows a remarkable functional diversity, including specific binding to surface CD74 and chemokine receptors and the presence of two intrinsic tautomerase and oxidoreductase activities. Several studies have shown that MIF is subject to post-translational modification, particularly redox-dependent modification of the catalytic proline and cysteine residues. In this review, we summarize and discuss MIF post-translational modifications and their effects on the biological properties of this protein. We propose that the redox-sensitive residues in MIF will be modified at sites of inflammation and that this will add further depth to the functional diversity of this intriguing cytokine.

Indexed as

Oxidation-ReductionAmino Acid SequenceAnimalsAntigens, Differentiation, B-LymphocyteCysteineHistocompatibility Antigens Class IIHumansMacrophage Migration-Inhibitory FactorsProtein ConformationProtein Processing, Post-TranslationalAntigens, Differentiation, B-LymphocyteCysteineHistocompatibility Antigens Class IIinvariant chainMacrophage Migration-Inhibitory FactorsCarbamylationCytokineInflammationMyeloperoxidaseN-terminal prolineOxMIFPost-translational modificationRedox regulationTautomerase

Identifiers

PMID29247897
PMCPMC5975065
OpenAlexW2771899271

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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.