Evidence map›Paper›PMID 32632589›Full record

ArticleDoklady. Biochemistry and biophysics2020

The Structural-Functional Damage of Fibrinogen Oxidized by Hydrogen Peroxide.

L V Yurina, A D Vasilyeva, V L Kononenko, A E Bugrova, M I Indeykina, A S Kononikhin, E N Nikolaev, M A Rosenfeld

Abstract read
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In one paragraph

Article in Doklady. Biochemistry and biophysics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 24% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
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

8 authors at 3 institutions in 1 country.

L V YurinaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia. lyu.yurina@gmail.com.
A D VasilyevaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
V L KononenkoEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
A E BugrovaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
M I IndeykinaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
A S KononikhinMoscow Institute of Physics and Technology, Dolgoprudny, Moscow, Russia.
E N NikolaevSkolkovo Institute of Science and Technology, Skolkovo, Russia.
M A RosenfeldEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, Russia.
Institute of Biochemical Physics NM Emanuel · RUMoscow Institute of Physics and Technology · RUSkolkovo Institute of Science and Technology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The effect of peroxide-induced oxidation of fibrinogen on modification of its primary structure and functional properties was investigated. The oxidation sites were shown to be Met, Trp, and His residues. Using the DLS method, it was found that the oxidative modification of fibrinogen results in the change of microrheological characteristics of fibrin network. The fibrinogen oxidation diminishes its tolerance to plasmin hydrolysis and deteriorates the factor XIIIa ability to stabilize the fibrin gel.

Indexed as

Factor XIIIaFibrinFibrinogenFibrinolysinHumansHydrogen PeroxideOxidantsOxidation-ReductionStructure-Activity RelationshipFactor XIIIaFibrinFibrinogenFibrinolysinHydrogen PeroxideOxidantsfibrin gelfibrinogenHPLC-MS/MSmicrorheologyoxidationoxidation sitesPAGE

Identifiers

PMID32632589
OpenAlexW3040076587

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.