Evidence map›Paper›PMID 34641382›Full record

ArticleMolecules (Basel, Switzerland)2021

Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose.

Jing-Jing Liu, Yong You, Shu-Qin Gao, Shuai Tang, Lei Chen, Ge-Bo Wen, Ying-Wu Lin

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. 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
1.0field-weighted citation impact, top 27% 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, 11 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

7 authors at 1 institution in 1 country.

Jing-Jing LiuSchool of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China.
Yong YouLaboratory of Protein Structure and Function, University of South China, Hengyang 421001, China.
Shu-Qin GaoLaboratory of Protein Structure and Function, University of South China, Hengyang 421001, China.
Shuai TangSchool of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China.
Lei ChenSchool of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China.
Ge-Bo WenLaboratory of Protein Structure and Function, University of South China, Hengyang 421001, China.
Ying-Wu LinSchool of Chemistry and Chemical Engineering, University of South China, Hengyang 421001, China.
University of South China · CN

Funding

National Natural Science Foundation of China 22007045 and 21977042the Research Foundation of Education Bureau of Hunan Province, China 19A441
6 · The paper itself

Abstract

Protein glycation is an important protein post-translational modification and is one of the main pathogenesis of diabetic angiopathy. Other than glycated hemoglobin, the protein glycation of other globins such as myoglobin (Mb) is less studied. The protein glycation of human Mb with ribose has not been reported, and the glycation sites in the Mb remain unknown. This article reports that d-ribose undergoes rapid protein glycation of human myoglobin (HMb) at lysine residues (K34, K87, K56, and K147) on the protein surface, as identified by ultra-high performance liquid chromatography-mass spectrometry (UHPLC-MS) and electrospray ionization tandem mass spectrometry (ESI-MS/MS). Moreover, glycation by d-ribose at these sites slightly decreased the rate of the met heme (Fe

Indexed as

Chromatography, LiquidFerric CompoundsGlycosylationHemeHumansHydrogen PeroxideMyoglobinRiboseSpectrometry, Mass, Electrospray IonizationFerric CompoundsHemeHydrogen PeroxideMyoglobinRibosediabetesd-riboseglycosylation siteshuman myoglobinprotein glycation

Identifiers

PMID34641382
PMCPMC8512392
OpenAlexW3202575811

What OpenQuestion holds

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LicenceCC BY
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.