Fred Goldberg machines in the pathogenesis of Mycobacterium tuberculosis.

K Heran Darwin

Abstract readReview

In one paragraph

Review in The Journal of biological chemistry, 2026. 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

1 author.

K Heran DarwinDepartment of Microbiology, NYU Grossman School of Medicine, New York, New York, USA. Electronic address: heran.darwin@nyulangone.org.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulated proteolysis is found in all forms of life, from bacteria to humans, and plays essential roles in all areas of physiology. The bacterial pathogen Mycobacterium tuberculosis has three, chambered ATP-dependent proteases needed to cause lethal infections in animals, making them attractive targets for drug development. Here, I review the latest developments in what is known about how caseinolytic proteases and proteasomes function to contribute to the virulence of one of the world's deadliest pathogens.

Indexed as

Bacterial ProteinsMycobacterium tuberculosisProteasome Endopeptidase ComplexTuberculosisAnimalsEndopeptidase ClpHumansBacterial ProteinsEndopeptidase ClpProteasome Endopeptidase ComplexClp proteaseMycobacterium tuberculosisproteasome

Identifiers

PMID41850402

DOI10.1016/j.jbc.2026.111373

PMCPMC13091356

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.