Evidence map›Paper›PMID 37916895›Full record

ReviewThe Biochemical journal2023

Targeting bacterial degradation machinery as an antibacterial strategy.

Radoslav Petkov, Amy H Camp, Rivka L Isaacson, James H Torpey

Abstract readReview
In one paragraph

Review in The Biochemical journal, 2023. 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. Proteostasis-targeted antibacterial strategies.Journal of microbiology (Seoul, Korea) · 2026
    Review
  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

4 authors.

Radoslav PetkovDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.
Amy H CampDepartment of Biological Sciences, Mount Holyoke College, 50 College Street, South Hadley, Massachusetts 01075, U.S.A.
Rivka L IsaacsonDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.
James H TorpeyDepartment of Chemistry, King's College London, Britannia House, 7 Trinity Street, London SE1 1DB, U.K.ORCID 0000-0003-3388-4992

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The exploitation of a cell's natural degradation machinery for therapeutic purposes is an exciting research area in its infancy with respect to bacteria. Here, we review current strategies targeting the ClpCP system, which is a proteolytic degradation complex essential in the biology of many bacterial species of scientific interest. Strategies include using natural product antibiotics or acyldepsipeptides to initiate the up- or down-regulation of ClpCP activity. We also examine exciting recent forays into BacPROTACs to trigger the degradation of specific proteins of interest through the hijacking of the ClpCP machinery. These strategies represent an important emerging avenue for combatting antimicrobial resistance.

Indexed as

Anti-Bacterial AgentsBiological ProductsBacteriaDown-RegulationPeptide HydrolasesAnti-Bacterial AgentsBiological ProductsPeptide HydrolasesAAA proteinsantibiotic resistancedegradationPROTACs

Identifiers

PMID37916895
PMCPMC10657178

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.