Evidence map›Paper›PMID 31548692›Full record

ArticleNature chemical biology2019

A family of radical halogenases for the engineering of amino-acid-based products.

Monica E Neugebauer, Kiera H Sumida, Jeffrey G Pelton, Jonathan L McMurry, Jorge A Marchand, Michelle C Y Chang

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 167 citations in OpenAlex.

  1. Functionalization of Peptides via Radical Arylation.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Emerging classes of copper enzymes.Current opinion in chemical biology · 2026
    Review
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  11. Total Synthesis of (+)-12-The Journal of organic chemistry · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Examining Pseudohalide (NJournal of inorganic biochemistry · 2026
    Article
  16. Article
  17. Article
  18. Article
  19. Bimolecular Homolytic Substitution (SACS central science · 2025
    Review
  20. Article

18 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

6 authors at 2 institutions in 1 country.

Monica E NeugebauerDepartment of Chemical and Biomolecular Engineering, University of California, Berkeley, Berkeley, CA, USA.ORCID http://orcid.org/0000-0003-4223-9071
Kiera H SumidaDepartment of Chemistry, University of California, Berkeley, Berkeley, CA, USA.
Jeffrey G PeltonQB3 Institute, University of California, Berkeley, Berkeley, CA, USA.
Jonathan L McMurryDepartment of Chemistry, University of California, Berkeley, Berkeley, CA, USA.
Jorge A MarchandDepartment of Chemical and Biomolecular Engineering, University of California, Berkeley, Berkeley, CA, USA.
Michelle C Y ChangDepartment of Chemical and Biomolecular Engineering, University of California, Berkeley, Berkeley, CA, USA. mcchang@berkeley.edu.ORCID http://orcid.org/0000-0003-3747-7630
University of California, Berkeley · USBerkeley College · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The integration of synthetic and biological catalysis enables new approaches to the synthesis of small molecules by combining the high selectivity of enzymes with the reaction diversity offered by synthetic chemistry. While organohalogens are valued for their bioactivity and utility as synthetic building blocks, only a handful of enzymes that carry out the regioselective halogenation of unactivated [Formula: see text] bonds have previously been identified. In this context, we report the structural characterization of BesD, a recently discovered radical halogenase from the Fe

Indexed as

Protein EngineeringAmino AcidsBacterial ProteinsComputational BiologyGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicStreptomycesAmino AcidsBacterial Proteins

Identifiers

PMID31548692
OpenAlexW2973258793

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.