Evidence map›Paper›PMID 37695900›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Crystal structure and activity of a de novo enzyme, ferric enterobactin esterase Syn-F4.

Kodai Kurihara, Koji Umezawa, Ann E Donnelly, Brendan Sperling, Guanyu Liao, Michael H Hecht, Ryoichi Arai

Abstract read
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In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. A multiscaleJournal of applied crystallography · 2025
    Article
  3. Review
  4. Article
  5. 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

7 authors.

Kodai KuriharaDepartment of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda, Nagano 386-8567, Japan.
Koji UmezawaDepartment of Agricultural and Life Sciences, Faculty of Agriculture, Shinshu University, Minami-minowa, Kami-ina, Nagano 399-4598, Japan.ORCID 0000-0001-9361-0825
Ann E DonnellyDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0000-0002-6296-5401
Brendan SperlingDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0009-0001-6482-192X
Guanyu LiaoDepartment of Chemistry, Princeton University, Princeton, NJ 08544.
Michael H HechtDepartment of Chemistry, Princeton University, Princeton, NJ 08544.ORCID 0000-0002-5538-9813
Ryoichi AraiDepartment of Applied Biology, Faculty of Textile Science and Technology, Shinshu University, Ueda, Nagano 386-8567, Japan.ORCID 0000-0001-5606-8483

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Producing novel enzymes that are catalytically active in vitro and biologically functional in vivo is a key goal of synthetic biology. Previously, we reported Syn-F4, the first de novo protein that meets both criteria. Syn-F4 hydrolyzed the siderophore ferric enterobactin, and expression of Syn-F4 allowed an inviable strain of

Indexed as

EnterobactinSiderophoresCatalysisElectrolytesEscherichia coliIronIron, DietaryElectrolytesEnterobactinIronIron, DietarySiderophoresbinary patterned libraryde novo enzymede novo proteindimeric 4-helix bundleferric enterobactin esterase

Identifiers

PMID37695900
PMCPMC10515146

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.