Evidence map›Paper›PMID 41843674›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.

Yingke Liang, Stephanie A Bueler, John L Rubinstein

Abstract read
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In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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

3 authors.

Yingke LiangMolecular Medicine Program, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.ORCID 0000-0001-6247-8294
Stephanie A BuelerMolecular Medicine Program, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.
John L RubinsteinMolecular Medicine Program, The Hospital for Sick Children, Toronto, ON M5G 0A4, Canada.ORCID 0000-0003-0566-2209

Funding

Canada Research Chairs (CRC) CRC Tier 1Canadian Institutes of Health Research (CIHR) CGS-DCanadian Institutes of Health Research (CIHR) PJT191893
6 · The paper itself

Abstract

The presence of mycolic acid is a defining feature of the mycobacterial cell wall, which provides a highly impermeable barrier to many antibiotics. Biosynthesis of this fatty acid, as well as tuberculostearic acid, requires precursor molecules produced by the essential long-chain acyl-coenzyme A (CoA) carboxylase (LCC) complex. The LCC complex catalyzes carboxylation of the α-carbon of long-chain acyl-CoA, but also short-chain acetyl-CoA and propionyl-CoA. The complex includes the subunits AccA3, which contains a biotin carboxylase (BC) domain and a biotin carboxyl carrier protein (BCCP) domain, the long-chain acyl-CoA carboxyltransferase AccD4, the short-chain acyl-CoA carboxyltransferase AccD5, and the incompletely characterized protein AccE. We used electron cryomicroscopy (cryo-EM) to determine structures of the LCC complex from

Indexed as

Bacterial ProteinsCarbon-Carbon LigasesMycobacterium smegmatisAcyl Coenzyme ACarbon-Nitrogen LigasesCryoelectron MicroscopyModels, MolecularMycolic AcidsProtein BindingSubstrate Specificityacyl-CoA carboxylaseAcyl Coenzyme ABacterial Proteinsbiotin carboxylaseCarbon-Carbon LigasesCarbon-Nitrogen LigasesMycolic Acidslong chain carboxylase complexmethylcrotonyl-CoA carboxylase complexMSMEG_0435 and MSMEG_0436Mycobacterium smegmatisRv0263c and Rv0264c

Identifiers

PMID41843674
PMCPMC13012033

What OpenQuestion holds

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Registered trials

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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.