Evidence map›Paper›PMID 33066693›Full record

ArticleInternational journal of molecular sciences2020

Mechanism of the Affinity-Enhancing Effect of Isatin on Human Ferrochelatase and Adrenodoxin Reductase Complex Formation: Implication for Protein Interactome Regulation.

Pavel V Ershov, Alexander V Veselovsky, Yuri V Mezentsev, Evgeniy O Yablokov, Leonid A Kaluzhskiy, Anastasiya M Tumilovich, Anton A Kavaleuski, Andrei A Gilep, Taisiya V Moskovkina, Alexei E Medvedev and 1 more

Abstract read
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In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

11 authors.

Pavel V ErshovInstitute of Biomedical Chemistry, 10 Building 8, Pogodinskaya Street, 140006 Moscow, Russia.
Alexander V VeselovskyInstitute of Biomedical Chemistry, 10 Building 8, Pogodinskaya Street, 140006 Moscow, Russia.
Yuri V MezentsevInstitute of Biomedical Chemistry, 10 Building 8, Pogodinskaya Street, 140006 Moscow, Russia.
Evgeniy O YablokovInstitute of Biomedical Chemistry, 10 Building 8, Pogodinskaya Street, 140006 Moscow, Russia.
Leonid A KaluzhskiyInstitute of Biomedical Chemistry, 10 Building 8, Pogodinskaya Street, 140006 Moscow, Russia.
Anastasiya M TumilovichInstitute of Bioorganic Chemistry NASB, 5 Building 2, V.F. Kuprevich Street, 220141 Minsk, Belarus.
Anton A KavaleuskiInstitute of Bioorganic Chemistry NASB, 5 Building 2, V.F. Kuprevich Street, 220141 Minsk, Belarus.
Andrei A GilepInstitute of Bioorganic Chemistry NASB, 5 Building 2, V.F. Kuprevich Street, 220141 Minsk, Belarus.
Taisiya V MoskovkinaFar East Federal University, FEFU Campus, 10 Ajax Bay, Russky Island, 690922 Vladivostok, Russia.
Alexei E MedvedevInstitute of Biomedical Chemistry, 10 Building 8, Pogodinskaya Street, 140006 Moscow, Russia.
Alexis S IvanovInstitute of Biomedical Chemistry, 10 Building 8, Pogodinskaya Street, 140006 Moscow, Russia.

Funding

Ministry of Education and Science of the Russian Federation 075-15-2019-1502Russian Academy of Sciences Program of Basic Scientific Research of National Science Academies for 2013-2020
6 · The paper itself

Abstract

Isatin (indole-2, 3-dione) is a non-peptide endogenous bioregulator exhibiting a wide spectrum of biological activity, realized in the cell via interactions with numerous isatin-binding proteins, their complexes, and (sub) interactomes. There is increasing evidence that isatin may be involved in the regulation of complex formations by modulating the affinity of the interacting protein partners. Recently, using Surface Plasmon Resonance (SPR) analysis, we have found that isatin in a concentration dependent manner increased interaction between two human mitochondrial proteins, ferrochelatase (FECH), and adrenodoxine reductase (ADR). In this study, we have investigated the affinity-enhancing effect of isatin on the FECH/ADR interaction. The SPR analysis has shown that FECH forms not only homodimers, but also FECH/ADR heterodimers. The affinity-enhancing effect of isatin on the FECH/ADR interaction was highly specific and was not reproduced by structural analogues of isatin. Bioinformatic analysis performed using three dimensional (3D) models of the interacting proteins and in silico molecular docking revealed the most probable mechanism involving FECH/isatin/ADR ternary complex formation. In this complex, isatin is targeted to the interface of interacting FECH and ADR monomers, forming hydrogen bonds with both FECH and ADR. This is a new regulatory mechanism by which isatin can modulate protein-protein interactions (PPI).

Indexed as

Ferredoxin-NADP ReductaseFerrochelataseHumansIsatinMolecular Docking SimulationProtein BindingSurface Plasmon ResonanceFerredoxin-NADP ReductaseFerrochelataseIsatinadrenodoxin reductaseaffinitycomplex formationferrochelataseheterodimerizationin silicoisatinsurface plasmon resonance

Identifiers

PMID33066693
PMCPMC7593955

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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.