Evidence map›Paper›PMID 29170371›Full record

ArticleNature communications2017

Multicomponent mapping of boron chemotypes furnishes selective enzyme inhibitors.

Joanne Tan, Armand B Cognetta Iii, Diego B Diaz, Kenneth M Lum, Shinya Adachi, Soumajit Kundu, Benjamin F Cravatt, Andrei K Yudin

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Boron in Diet and Medicine: Mechanisms of Delivery and Detection.Pharmaceuticals (Basel, Switzerland) · 2025
    Review
  4. Recent Development of Boron-Containing Small-Molecule Anticancer Agents.ACS pharmacology & translational science · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. 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

8 authors at 2 institutions in 2 countries.

Joanne TanDavenport Research Laboratories, Department of Chemistry, University of Toronto, 80 St George Street, Toronto, ON, Canada, M5S 3H6.
Armand B Cognetta IiiDepartment of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550N. Torrey Pines Rd., La Jolla, CA, 92037, USA.
Diego B DiazDavenport Research Laboratories, Department of Chemistry, University of Toronto, 80 St George Street, Toronto, ON, Canada, M5S 3H6.ORCID http://orcid.org/0000-0001-8293-1084
Kenneth M LumDepartment of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550N. Torrey Pines Rd., La Jolla, CA, 92037, USA.
Shinya AdachiDavenport Research Laboratories, Department of Chemistry, University of Toronto, 80 St George Street, Toronto, ON, Canada, M5S 3H6.
Soumajit KunduDepartment of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550N. Torrey Pines Rd., La Jolla, CA, 92037, USA.
Benjamin F CravattDepartment of Molecular Medicine, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550N. Torrey Pines Rd., La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0001-5330-3492
Andrei K YudinDavenport Research Laboratories, Department of Chemistry, University of Toronto, 80 St George Street, Toronto, ON, Canada, M5S 3H6. ayudin@chem.utoronto.ca.
Scripps Research Institute · USUniversity of Toronto · CA

Funding

CHEMOPROTEOMIC METHODS FOR SERINE HYDROLASE INHIBITOR DEVELOPMENTR01DA033760 · NIDA · SCRIPPS RESEARCH INSTITUTE, THE · PI CRAVATT, BENJAMIN F, SCAMPAVIA, LOUIS DANIEL · 2012 to 2021
$5.1M
CIHRNIDA NIH HHS R01 DA033760
6 · The paper itself

Abstract

Heteroatom-rich organoboron compounds have attracted attention as modulators of enzyme function. Driven by the unmet need to develop chemoselective access to boron chemotypes, we report herein the synthesis of α- and β-aminocyano(MIDA)boronates from borylated carbonyl compounds. Activity-based protein profiling of the resulting β-aminoboronic acids furnishes selective and cell-active inhibitors of the (ox)lipid-metabolizing enzyme α/β-hydrolase domain 3 (ABHD3). The most potent compound displays nanomolar in vitro and in situ IC

Indexed as

BoronBoron CompoundsEnzyme InhibitorsHumansMolecular StructurePhospholipasesPhospholipases A2ABHD3 protein, humanBoronBoron CompoundsEnzyme InhibitorsPhospholipasesPhospholipases A2

Identifiers

PMID29170371
PMCPMC5701053
OpenAlexW2769066285

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.