Evidence map›Paper›PMID 36119373›Full record

ArticleACS bio & med chem Au2022

RadicalSAM.org: A Resource to Interpret Sequence-Function Space and Discover New Radical SAM Enzyme Chemistry.

Nils Oberg, Timothy W Precord, Douglas A Mitchell, John A Gerlt

Open access · goldAbstract read
In one paragraph

Article in ACS bio & med chem Au, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

66 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Mechanistic insight into radicalNatural product reports · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. The radical SAM enzyme EpeE exhibits distinct site reactivity during the biosynthesis of the RiPP natural product epipeptide.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. RadicalJournal of the American Chemical Society · 2026
    Article
  13. Structural basis for iterative methylation by a cobalamin-dependent radicalProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  14. Article
  15. Diverse thioether macrocyclized peptides through a radical SAM maturase.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. RadicalNature catalysis · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Structural Evidence for DUF512 as a RadicalACS bio & med chem Au · 2024
    Article

6 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Nils ObergCarl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 1206 West Gregory Drive, Urbana, Illinois 61801, United States.
Timothy W PrecordCarl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 1206 West Gregory Drive, Urbana, Illinois 61801, United States.
Douglas A MitchellCarl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 1206 West Gregory Drive, Urbana, Illinois 61801, United States.ORCID 0000-0002-9564-0953
John A GerltCarl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, 1206 West Gregory Drive, Urbana, Illinois 61801, United States.ORCID 0000-0002-5625-1218
University of Illinois Urbana-Champaign · US

Funding

Core H: MicrobiologyU54GM093342 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI CRONAN, JOHN E. · 2010 to 2015
$34.6M
Protein/Structure CoreP01GM118303 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GERLT, JOHN A · 2016 to 2020
$11.4M
Genomics-Accelerated Natural Product DiscoveryR01GM123998 · NIGMS · VANDERBILT UNIVERSITY · PI MITCHELL, DOUGLAS ALAN · 2017 to 2024
$2.6M
NIGMS NIH HHS P01 GM118303NIGMS NIH HHS R01 GM123998NIGMS NIH HHS U54 GM093342
6 · The paper itself

Abstract

The radical SAM superfamily (RSS), arguably the most functionally diverse enzyme superfamily, is also one of the largest with ~700K members currently in the UniProt database. The vast majority of the members have uncharacterized enzymatic activities and metabolic functions. In this Perspective, we describe RadicalSAM.org, a new web-based resource that enables a user-friendly genomic enzymology strategy to explore sequence-function space in the RSS. The resource attempts to enable identification of isofunctional groups of radical SAM enzymes using sequence similarity networks (SSNs) and the genome context of the bacterial, archaeal, and fungal members provided by genome neighborhood diagrams (GNDs). Enzymatic activities and

Indexed as

functional assignmentgenome neighborhood diagramsgenomic enzymologyisofunctional familiesRadical SAM superfamilysequence similarity networksweb resource

Identifiers

PMID36119373
PMCPMC9477430
OpenAlexW4200562442

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.