Evidence map›Paper›PMID 28596380›Full record

ArticleThe Journal of biological chemistry2017

Identification of oxidative modifications of hemopexin and their predicted physiological relevance.

Peter Hahl, Rachel Hunt, Edward S Bjes, Andrew Skaff, Andrew Keightley, Ann Smith

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 26 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Peter HahlFrom the Department of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110-2239.
Rachel HuntFrom the Department of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110-2239.
Edward S BjesFrom the Department of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110-2239.
Andrew SkaffFrom the Department of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110-2239.
Andrew KeightleyFrom the Department of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110-2239.
Ann SmithFrom the Department of Molecular Biology and Biochemistry, School of Biological Sciences, University of Missouri-Kansas City, Kansas City, Missouri 64110-2239 smithan@umkc.edu.
University of Missouri–Kansas City · US

Funding

Mechanisms of Heme TransportR21DK064363 · NIDDK · UNIVERSITY OF MISSOURI KANSAS CITY · PI SMITH, ANN · 2004 to 2005
$294k
NIDDK NIH HHS R21 DK064363
6 · The paper itself

Abstract

Hemopexin protects against heme toxicity in hemolytic diseases and conditions, sepsis, and sickle cell disease. This protection is sustained by heme-hemopexin complexes in biological fluids that resist oxidative damage during heme-driven inflammation. However, apo-hemopexin is vulnerable to inactivation by reactive nitrogen (RNS) and oxygen species (ROS) that covalently modify amino acids. The resultant nitration of amino acids is considered a specific effect reflecting biological events. Using LC-MS, we discovered low endogenous levels of tyrosine nitration in the peptide YYCFQGNQFLR in the heme-binding site of human hemopexin, which was similarly nitrated in rabbit and rat hemopexins. Immunoblotting and selective reaction monitoring were used to quantify tyrosine nitration of

Indexed as

Models, MolecularAmino Acid SequenceAnimalsApoproteinsBinding SitesChromatography, High Pressure LiquidConserved SequenceHemeHemopexinHumansKineticsLigandsMolecular StructureOxidation-ReductionProtein ConformationRabbitsApoproteinsHemeHemopexinLigandsReactive Oxygen SpeciesTryptophanTyrosinecovalent modificationglycoproteinhemopexinmass spectrometry (MS)proteomicsreactive nitrogen species (RNS)reactive oxygen species (ROS)tyrosine nitration

Identifiers

PMID28596380
PMCPMC5566522
OpenAlexW2624590623

What OpenQuestion holds

Textmetadata
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.