Evidence map›Paper›PMID 30819615›Full record

ArticleRedox biology2019

2-Alkenal modification of hemoglobin: Identification of a novel hemoglobin-specific alkanoic acid-histidine adduct.

Jun Yoshitake, Takahiro Shibata, Chihiro Shimayama, Koji Uchida

Open access · goldAbstract read
In one paragraph

Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

6 citing papers in PubMed, 18 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

4 authors at 2 institutions in 1 country.

Jun YoshitakeInstitute of Nano-Life-Systems, Institutes of Innovation for Future Society, Nagoya University, Nagoya 464-8601, Japan.
Takahiro ShibataInstitute of Nano-Life-Systems, Institutes of Innovation for Future Society, Nagoya University, Nagoya 464-8601, Japan; Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
Chihiro ShimayamaGraduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.
Koji UchidaGraduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo 113-8657, Japan; Japan Agency for Medical Research and Development, CREST, Tokyo, Japan. Electronic address: a-uchida@mail.ecc.u-tokyo.ac.jp.
Nagoya University · JPJapan Agency for Medical Research and Development · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α,β-Unsaturated aldehydes generated during lipid peroxidation, such as 2-alkenals, give rise to protein degeneration in a variety of pathological states. 2-Alkenals are highly reactive toward nucleophilic amino acid residues, such as histidine and lysine, to form Schiff base adducts or Michael addition adducts. In this study, upon the reaction of hemoglobin with 2-octenal, we unexpectedly detected a product corresponding to the reduced form of the 2-octenal-histidine Michael adduct plus 14 mass unit. Based on the LC-ESI-MS/MS analysis of synthetic adduct candidates, the adduct was identified to be N

Indexed as

Amino AcidsChromatography, LiquidErythrocytesHemeHemoglobinsHistidineHumansHydrolysisIronLipid PeroxidationOxidation-ReductionSpectrometry, Mass, Electrospray IonizationTandem Mass SpectrometryAmino AcidsHemeHemoglobinsHistidineIronAldehydeHemoglobinLipid peroxidationProtein chemical modificationRed blood cells

Identifiers

PMID30819615
PMCPMC6859543
OpenAlexW2917109090

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.