Evidence map›Paper›PMID 40833116›Full record

ReviewJournal of bacteriology2025

Cysteine proteases and how YabG fits into clan CD of the MEROPS database.

Morgan S Osborne, Joseph A Sorg

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Journal of bacteriology, 2025. 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
–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

0 citing papers in PubMed.

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

2 authors.

Morgan S OsborneDepartment of Biology, Texas A&M University, College Station, Texas, USA.
Joseph A SorgDepartment of Biology, Texas A&M University, College Station, Texas, USA.ORCID 0000-0001-7822-2656

Funding

Mechanisms of Clostridium difficile spore germinationR01AI116895 · NIAID · TEXAS A&M UNIVERSITY · PI SORG, JOE · 2015 to 2024
$3.9M
Impact of the C. difficile small acid soluble proteins on spore physiologyR01AI172043 · NIAID · TEXAS A&M UNIVERSITY · PI SORG, JOE · 2022 to 2025
$2.5M
National Institute of Allergy and Infectious Diseases 5R01AI116895, 5R01AI172043NIAID NIH HHS R01 AI116895NIAID NIH HHS R01 AI172043
6 · The paper itself

Abstract

Cysteine proteases are hydrolases that share a common catalytic mechanism involving a nucleophilic cysteine thiol in a catalytic dyad or triad. Here, we review the current clans that make up the cysteine proteases in the MEROPS database as of March 2025. We also discuss cysteine proteases made by

Indexed as

Bacterial ProteinsClostridioides difficileCysteine ProteasesDatabases, ProteinBacillus subtilisSpores, BacterialBacterial ProteinsCysteine ProteasesBacillus subtilisClostridioides difficileMEROPSproteasespore

Identifiers

PMID40833116
PMCPMC12445089

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.