Evidence map›Paper›PMID 21235354›Full record

ArticleAntioxidants & redox signaling2011

Protein carbamylation renders high-density lipoprotein dysfunctional.

Michael Holzer, Martin Gauster, Thomas Pfeifer, Christian Wadsack, Guenter Fauler, Philipp Stiegler, Harald Koefeler, Eckhard Beubler, Rufina Schuligoi, Akos Heinemann and 1 more

Abstract read
In one paragraph

Article in Antioxidants & redox signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

75 citing papers in PubMed, 162 citations in OpenAlex.

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  6. Lifestyles, metabolome and diabetic kidney disease: a cohort study.QJM : monthly journal of the Association of Physicians · 2026
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  18. HDL and chronic kidney disease.Atherosclerosis plus · 2023
    Article
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15 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

11 authors at 1 institution in 1 country.

Michael HolzerInstitute of Experimental and Clinical Pharmacology, Medical University of Graz, Universitätsplatz 4, Graz, Austria.
Martin Gauster
Thomas Pfeifer
Christian Wadsack
Guenter Fauler
Philipp Stiegler
Harald Koefeler
Eckhard Beubler
Rufina Schuligoi
Akos Heinemann
Gunther Marsche
Medical University of Graz · AT

Funding

Austrian Science Fund FWF P 21004
6 · The paper itself

Abstract

Carbamylation of proteins through reactive cyanate has been demonstrated to predict an increased cardiovascular risk. Cyanate is formed in vivo by breakdown of urea and at sites of inflammation by the phagocyte protein myeloperoxidase. Because myeloperoxidase (MPO) associates with high-density lipoprotein (HDL) in human atherosclerotic intima, we examined in the present study whether cyanate specifically targets HDL. Mass spectrometry analysis revealed that protein carbamylation is a major posttranslational modification of HDL. The carbamyllysine content of lesion-derived HDL was more than 20-fold higher in comparison with 3-chlorotyrosine levels, a specific oxidation product of MPO. Notably, the carbamyllysine content of lesion-derived HDL was five- to eightfold higher when compared with lesion-derived low-density lipoprotein (LDL) or total lesion protein and increased with lesion severity. The carbamyllysine content of HDL, but not of LDL, correlated with levels of 3-chlorotyrosine, suggesting that MPO mediated carbamylation in the vessel wall. Remarkably, one carbamyllysine residue per HDL-associated apolipoprotein A-I was sufficient to induce cholesterol accumulation and lipid-droplet formation in macrophages through a pathway requiring the HDL-receptor scavenger receptor class B, type I. The present results raise the possibility that HDL carbamylation contributes to foam cell formation in atherosclerotic lesions.

Indexed as

Protein Processing, Post-TranslationalAdultAgedApolipoprotein A-IAtherosclerosisCD36 AntigensCells, CulturedCholesterolCyanatesHumansLipoproteins, HDLLipoproteins, LDLMacrophagesMass SpectrometryMiddle AgedOxidation-Reduction3-chlorotyrosineApolipoprotein A-ICD36 AntigensCholesterolCyanatesLipoproteins, HDLLipoproteins, LDLPeroxidaseTyrosine

Identifiers

PMID21235354
PMCPMC3380531
OpenAlexW2004163374

What OpenQuestion holds

Textmetadata
LicenceTDM
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.