Evidence map›Paper›PMID 41613874›Full record

ReviewBiophysical reviews2025

Antioxidant evolution of fibrinogen: a crucial role of methionines.

Mark A Rosenfeld, Lyubov V Yurina, Alexandra D Vasilyeva

Abstract readReview
In one paragraph

Review in Biophysical reviews, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Mark A RosenfeldN. M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334 Russia.
Lyubov V YurinaN. M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334 Russia.
Alexandra D VasilyevaN. M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 119334 Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This review aims to provide evidence that the fibrinogen-like structures of invertebrates (on the example of the intracellular coagulation protein coagulogen from horseshoe crabs) and fibrinogen of vertebrates (such as lampreys, which are among the most primitive extant vertebrates, as well as higher-ordered animals on the phylogenetic evolutionary scale, such as chickens and humans) reflect their methionine-dependent adaptation to the steady-state level of reactive oxygen species (ROS). Since methionine residues disposed in primary structure of proteins may serve as ROS interceptors, the absence of methionines in the coagulogen structure suggests that it is not subject to ROS attack in the same extent as vertebrate extracellular fibrinogen. The structures of vertebrate fibrinogens (such as the central E-nodule composed of the NH

Indexed as

Antioxidant evolutionChicken fibrinogenHorseshoe crab coagulogenHuman fibrinogenLamprey fibrinogenReactive oxygen speciesStructureSurface-localized methionines

Identifiers

PMID41613874
PMCPMC12847593

What Socratic 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 Socratic graph.