Evidence map›Paper›PMID 29339506›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Development and retention of a primordial moonlighting pathway of protein modification in the absence of selection presents a puzzle.

Xinyun Cao, Yaoqin Hong, Lei Zhu, Yuanyuan Hu, John E Cronan

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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
2.3field-weighted citation impact, top 14% 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, 28 citations in OpenAlex.

  1. Article
  2. Fatty acid synthesis and utilization in gram-positive bacteria: insights fromMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  3. Article
  4. Article
  5. Lipoic acid attachment to proteins: stimulating new developments.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  6. Article
  7. Pathway Driven Target Selection inFrontiers in cellular and infection microbiology · 2022
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Functional Identification and Structural Analysis of a New Lipoate Protein Ligase inFrontiers in cellular and infection microbiology · 2020
    Article
  13. Review
  14. Advances in synthesis of biotin and assembly of lipoic acid.Current opinion in chemical biology · 2018
    Review
  15. Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Article
  17. QnAs with John E. Cronan.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. Article
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

5 authors at 1 institution in 1 country.

Xinyun CaoDepartment of Biochemistry, University of Illinois at Urbana-Champagne, Urbana, IL 61801.
Yaoqin HongDepartment of Microbiology, University of Illinois at Urbana-Champagne, Urbana, IL 61801.ORCID 0000-0002-4408-2648
Lei ZhuDepartment of Microbiology, University of Illinois at Urbana-Champagne, Urbana, IL 61801.
Yuanyuan HuDepartment of Biochemistry, University of Illinois at Urbana-Champagne, Urbana, IL 61801.
John E CronanDepartment of Biochemistry, University of Illinois at Urbana-Champagne, Urbana, IL 61801; j-cronan@life.uiuc.edu.ORCID 0000-0002-7064-312X
University of Illinois Urbana-Champaign · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lipoic acid is synthesized by a remarkably atypical pathway in which the cofactor is assembled on its cognate proteins. An octanoyl moiety diverted from fatty acid synthesis is covalently attached to the acceptor protein, and sulfur insertion at carbons 6 and 8 of the octanoyl moiety form the lipoyl cofactor. Covalent attachment of this cofactor is required for function of several central metabolism enzymes, including the glycine cleavage H protein (GcvH). In

Indexed as

AcyltransferasesAmino Acid OxidoreductasesAmino Acid SequenceBacillus subtilisBacterial ProteinsBiological EvolutionCarrier ProteinsEscherichia coliEvolution, MolecularGram-Negative BacteriaGram-Positive BacteriaLipoylationMultienzyme ComplexesPeptide SynthasesProtein Processing, Post-TranslationalThioctic AcidAcyltransferasesAmino Acid OxidoreductasesBacterial ProteinsCarrier Proteinsglycine cleavage systemLipA protein, Bacterialipase activator protein, BacteriaMultienzyme ComplexesPeptide SynthasesThioctic AcidTransferasesaerobic metabolismC1 metabolismenzyme moonlightingglycine cleavagelipoic acid

Identifiers

PMID29339506
PMCPMC5789953
OpenAlexW2783994839

What OpenQuestion holds

Textmetadata
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.