Evidence map›Paper›PMID 37924287›Full record

ArticleBiochemistry2023

Unveiling the Catalytic Mechanism of a Processive Metalloaminopeptidase.

Martha Clementine Simpson, Christopher John Harding, Ricardo Melo Czekster, Laura Remmel, Bela E Bode, Clarissa Melo Czekster

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 17% 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

4 citing papers in PubMed, 5 citations in OpenAlex.

  1. Leucine Aminopeptidase fromBiomolecules · 2026
    Article
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  3. Article
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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

6 authors at 2 institutions in 1 country.

Martha Clementine SimpsonSchool of Biology, University of St Andrews, North Haugh, Biomolecular Sciences Building, KY16 9ST, Saint Andrews, United Kingdom.
Christopher John HardingSchool of Biology, University of St Andrews, North Haugh, Biomolecular Sciences Building, KY16 9ST, Saint Andrews, United Kingdom.
Ricardo Melo CzeksterSchool of Computer Science and Digital Technologies, Department of Software Engineering and Cybersecurity, Aston University, B4 7ET, Birmingham,United Kingdom.
Laura RemmelSchool of Chemistry, University of St Andrews, North Haugh, Purdie Building, KY16 9ST, Saint Andrews , United Kingdom.ORCID 0009-0003-5563-8925
Bela E BodeSchool of Chemistry, University of St Andrews, North Haugh, Purdie Building, KY16 9ST, Saint Andrews , United Kingdom.ORCID 0000-0002-3384-271X
Clarissa Melo CzeksterSchool of Biology, University of St Andrews, North Haugh, Biomolecular Sciences Building, KY16 9ST, Saint Andrews, United Kingdom.ORCID 0000-0002-7163-4057
University of St Andrews · GBAston University · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Intracellular leucine aminopeptidases (PepA) are metalloproteases from the family M17. These enzymes catalyze peptide bond cleavage, removing N-terminal residues from peptide and protein substrates, with consequences for protein homeostasis and quality control. While general mechanistic studies using model substrates have been conducted on PepA enzymes from various organisms, specific information about their substrate preferences and promiscuity, choice of metal, activation mechanisms, and the steps that limit steady-state turnover remain unexplored. Here, we dissected the catalytic and chemical mechanisms of

Indexed as

Leucyl AminopeptidasePeptidesCatalysisHydrolysisKineticsLeucineMetalsSubstrate SpecificityLeucineLeucyl AminopeptidaseMetalsPeptides

Identifiers

PMID37924287
PMCPMC10666288
OpenAlexW4388339389

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.