Evidence map›Paper›PMID 30250274›Full record

ArticleNature communications2018

Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolution.

Nadav Elad, Szilvia Baron, Yoav Peleg, Shira Albeck, Jacob Grunwald, Gal Raviv, Zippora Shakked, Oren Zimhony, Ron Diskin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Structural basis of product recognition by Mycobacterium tuberculosis fatty acid synthase.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Screening of Microbial Fermentation Products for Anti-Animals : an open access journal from MDPI · 2022
    Article
  9. Review
  10. Article
  11. Review
  12. Tuberculosis: Past, present and future of the treatment and drug discovery research.Current research in pharmacology and drug discovery · 2021
    Review
  13. Article
  14. The primary step of biotin synthesis in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Type I fatty acid synthase trapped in the octanoyl-bound state.Protein science : a publication of the Protein Society · 2020
    Article
  16. Article
  17. Article
  18. New therapeutic strategies forExpert review of anti-infective therapy
    Review
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

9 authors at 2 institutions in 1 country.

Nadav EladDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Szilvia BaronDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, 7610001, Israel.ORCID http://orcid.org/0000-0002-0406-1359
Yoav PelegStructural Proteomics Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Shira AlbeckStructural Proteomics Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Jacob GrunwaldStructural Proteomics Unit, Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Gal RavivDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Zippora ShakkedDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, 7610001, Israel.
Oren ZimhonyKaplan Medical Center, Rehovot, affiliated to the School of Medicine, Hebrew University, Jerusalem, 7661041, Israel. Oren.Zimhony@weizmann.ac.il.
Ron DiskinDepartment of Structural Biology, Weizmann Institute of Science, Rehovot, 7610001, Israel. ron.diskin@weizmann.ac.il.ORCID http://orcid.org/0000-0002-2837-5897
Weizmann Institute of Science · ILKaplan Medical Center · IL

Funding

Israel Science Foundation (ISF) 1629/10Israel Science Foundation (ISF) 682/16
6 · The paper itself

Abstract

Tuberculosis (TB) is a devastating and rapidly spreading disease caused by Mycobacterium tuberculosis (Mtb). Therapy requires prolonged treatment with a combination of multiple agents and interruptions in the treatment regimen result in emergence and spread of multi-drug resistant (MDR) Mtb strains. MDR Mtb poses a significant global health problem, calling for urgent development of novel drugs to combat TB. Here, we report the 3.3 Å resolution structure of the ~2 MDa type-I fatty acid synthase (FAS-I) from Mtb, determined by single particle cryo-EM. Mtb FAS-I is an essential enzymatic complex that contributes to the virulence of Mtb, and thus a prime target for anti-TB drugs. The structural information for Mtb FAS-I we have obtained enables computer-based drug discovery approaches, and the resolution achieved by cryo-EM is sufficient for elucidating inhibition mechanisms by putative small molecular weight inhibitors.

Indexed as

Antitubercular AgentsBacterial ProteinsCatalytic DomainCryoelectron MicroscopyDrug DiscoveryFatty Acid SynthasesModels, MolecularMycobacterium tuberculosisRecombinant ProteinsTuberculosisVirulenceAntitubercular AgentsBacterial Proteinsfatty acid synthase I, mycobacteriaFatty Acid SynthasesRecombinant Proteins

Identifiers

PMID30250274
PMCPMC6155276
OpenAlexW2889752627

What OpenQuestion holds

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LicenceCC BY
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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.