Evidence map›Paper›PMID 35453991›Full record

ArticleDiagnostics (Basel, Switzerland)2022

Radiothermometric Study of the Effect of Amino Acid Mutation on the Characteristics of the Enzymatic System.

Yuri D Ivanov, Kristina A Malsagova, Natalia S Bukharina, Sergey G Vesnin, Sergey A Usanov, Vadim Yu Tatur, Andrei A Lukyanitsa, Nina D Ivanova, Vladimir A Konev, Vadim S Ziborov

Open access · goldAbstract read
In one paragraph

Article in Diagnostics (Basel, Switzerland), 2022. 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
0.2field-weighted citation impact, top 61% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

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

10 authors at 4 institutions in 2 countries.

Yuri D IvanovLaboratory of Nanobiotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10 Build. 8, 119121 Moscow, Russia.ORCID 0000-0001-5041-1914
Kristina A MalsagovaLaboratory of Nanobiotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10 Build. 8, 119121 Moscow, Russia.ORCID 0000-0001-9404-1660
Natalia S BukharinaLaboratory of Nanobiotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10 Build. 8, 119121 Moscow, Russia.
Sergey G VesninRES Ltd., Bolshaya Pochtovaya St. 22, 105082 Moscow, Russia.
Sergey A UsanovInstitute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Academician V.F. Kuprevich 5 Build. 2, 220141 Minsk, Belarus.
Vadim Yu TaturFoundation of Perspective Technologies and Novations, Shipilovskaya St. 64, 115682 Moscow, Russia.
Andrei A LukyanitsaFoundation of Perspective Technologies and Novations, Shipilovskaya St. 64, 115682 Moscow, Russia.
Nina D IvanovaSkryabin Moscow State Academy of Veterinary Medicine and Biotechnology, Academician Skryabin St. 23, 109472 Moscow, Russia.
Vladimir A KonevDepartment of Infectious Diseases in Children, Faculty of Pediatrics, Pirogov Russian National Research Medical University, Ostrovityanov St. 1, 117997 Moscow, Russia.
Vadim S ZiborovLaboratory of Nanobiotechnology, Institute of Biomedical Chemistry, Pogodinskaya St. 10 Build. 8, 119121 Moscow, Russia.
Institute of Biomedical Chemistry · RUMoscow State Academy of Veterinary Medicine and Biotechnology named after Skryabin · RUNational Academy of Sciences of Belarus · BYPirogov Russian National Research Medical University · RU

Funding

Ministry of Science and Higher Education of the Russian Federation within the framework of state support for the creation and development of the World-Class Research Center "Digital Biodesign and Personalized Healthcare", 75-15-2020-913.
6 · The paper itself

Abstract

The radiothermometry (RTM) study of a cytochrome-containing system (CYP102 A1) has been conducted in order to demonstrate the applicability of RTM for monitoring changes in the functional activity of an enzyme in case of its point mutation. The study has been performed with the example of the wild-type cytochrome (WT) and its mutant type A264K. CYP102 A1 is a nanoscale protein-enzymatic system of about 10 nm in size. RTM uses a radio detector and can record the corresponding brightness temperature (

Indexed as

brightness temperatureCYP102 A1cytochromeradiothermometry

Identifiers

PMID35453991
PMCPMC9024681
OpenAlexW4223529597

What OpenQuestion holds

Textmetadata
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.