Evidence map›Paper›PMID 35628272›Full record

ReviewInternational journal of molecular sciences2022

Amyloidogenic Peptides: New Class of Antimicrobial Peptides with the Novel Mechanism of Activity.

Oxana V Galzitskaya, Stanislav R Kurpe, Alexander V Panfilov, Anna V Glyakina, Sergei Y Grishin, Alexey P Kochetov, Evgeniya I Deryusheva, Andrey V Machulin, Sergey V Kravchenko, Pavel A Domnin and 3 more

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
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  8. State-of-the-Art Molecular Biophysics in Russia.International journal of molecular sciences · 2024
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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

13 authors at 8 institutions in 1 country.

Oxana V GalzitskayaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0002-3962-1520
Stanislav R KurpeInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0002-7171-3329
Alexander V PanfilovInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Anna V GlyakinaInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Sergei Y GrishinInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0001-7373-9808
Alexey P KochetovThe Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia.
Evgeniya I DeryushevaInstitute for Biological Instrumentation, Federal Research Center "Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences", 142290 Pushchino, Russia.
Andrey V MachulinSkryabin Institute of Biochemistry and Physiology of Microorganisms, Federal Research Center "Pushchino Scientific Center for Biological Research of the Russian Academy of Science", 142290 Pushchino, Russia.ORCID 0000-0002-4859-7219
Sergey V KravchenkoInstitute of Environmental and Agricultural Biology (X-BIO), Tyumen State University, 625003 Tyumen, Russia.ORCID 0000-0002-1261-7919
Pavel A DomninGamaleya Research Centre of Epidemiology and Microbiology, 123098 Moscow, Russia.
Alexey K SurinInstitute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Russia.
Viacheslav N AzevThe Branch of the Institute of Bioorganic Chemistry, Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0003-3275-4811
Svetlana A ErmolaevaGamaleya Research Centre of Epidemiology and Microbiology, 123098 Moscow, Russia.ORCID 0000-0003-3396-6816
Institute of Protein Research · RUInstitute of Bioorganic Chemistry · RUGamalei Institute of Epidemiology and Microbiology · RUG. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms · RUInstitute for Biological Instrumentation · RUInstitute of Theoretical and Experimental Biophysics · RULomonosov Moscow State University · RUUniversity of Tyumen · RU

Funding

Russian Science Foundation 18-14-00321
6 · The paper itself

Abstract

Antibiotic-resistant bacteria are recognized as one of the leading causes of death in the world. We proposed and successfully tested peptides with a new mechanism of antimicrobial action "protein silencing" based on directed co-aggregation. The amyloidogenic antimicrobial peptide (AAMP) interacts with the target protein of model or pathogenic bacteria and forms aggregates, thereby knocking out the protein from its working condition. In this review, we consider antimicrobial effects of the designed peptides on two model organisms,

Indexed as

Antimicrobial Cationic PeptidesAntimicrobial PeptidesAnti-Bacterial AgentsBacteriaEscherichia coliPseudomonas aeruginosaStaphylococcus aureusAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial Peptidesamyloidogenic peptidesamyloidsantibacterial peptidesco-aggregationmembranepenetration

Identifiers

PMID35628272
PMCPMC9140876
OpenAlexW4280535791

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.