Evidence map›Paper›PMID 39012716›Full record

ArticleActa crystallographica. Section D, Structural biology2024

Crystallographic fragment-binding studies of the Mycobacterium tuberculosis trifunctional enzyme suggest binding pockets for the tails of the acyl-CoA substrates at its active sites and a potential substrate-channeling path between them.

Subhadra Dalwani, Alexander Metz, Franziska U Huschmann, Manfred S Weiss, Rik K Wierenga, Rajaram Venkatesan

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2024. 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

6 authors.

Subhadra DalwaniFaculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.ORCID 0000-0001-8281-9463
Alexander MetzDepartment of Pharmaceutical Chemistry, Philipps-University Marburg, Marburg, Germany.ORCID 0000-0002-9634-9033
Franziska U HuschmannDepartment of Pharmaceutical Chemistry, Philipps-University Marburg, Marburg, Germany.
Manfred S WeissMacromolecular Crystallography, Helmholtz-Zentrum Berlin, Berlin, Germany.ORCID 0000-0002-2362-7047
Rik K WierengaFaculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.ORCID 0000-0001-6554-471X
Rajaram VenkatesanFaculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.ORCID 0000-0002-7257-1211

Funding

Academy of Finland 289024Academy of Finland 293369Academy of Finland 319194
6 · The paper itself

Abstract

The Mycobacterium tuberculosis trifunctional enzyme (MtTFE) is an α

Indexed as

Acyl Coenzyme ABacterial ProteinsCatalytic DomainMycobacterium tuberculosis3-Hydroxyacyl CoA DehydrogenasesBinding SitesCrystallography, X-RayEnoyl-CoA HydrataseModels, MolecularProtein BindingSubstrate Specificity3-Hydroxyacyl CoA DehydrogenasesAcyl Coenzyme ABacterial ProteinsEnoyl-CoA HydrataseCoA-dependent enzymeselectrostatic surfacesfatty-acid β-oxidationlipid metabolismMycobacterium tuberculosissubstrate channelingtrifunctional enzymetuberculosis

Identifiers

PMID39012716
PMCPMC11301753

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.