Evidence map›Paper›PMID 24900839›Full record

ArticleACS medicinal chemistry letters2014

Interkingdom pharmacology of Angiotensin-I converting enzyme inhibitor phosphonates produced by actinomycetes.

Glenna J Kramer, Akif Mohd, Sylva L U Schwager, Geoffrey Masuyer, K Ravi Acharya, Edward D Sturrock, Brian O Bachmann

Open access · hybridAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2014. 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
1.0field-weighted citation impact, top 23% 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, 35 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Phosphonic acid: preparation and applications.Beilstein journal of organic chemistry · 2017
    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

7 authors at 3 institutions in 3 countries.

Glenna J KramerVanderbilt University Department of Chemistry, 7300 Stevenson Center, Nashville, Tennessee 37204, United States.
Akif MohdUniversity of Bath , Department of Biology & Biochemistry, Bath BA2 7AY, United Kingdom.
Sylva L U SchwagerUniversity of Cape Town , The Division of Medical Biochemistry, Institute of Infectious Disease and Molecular Medicine, Observatory 7925, South Africa.
Geoffrey MasuyerUniversity of Bath , Department of Biology & Biochemistry, Bath BA2 7AY, United Kingdom.
K Ravi AcharyaUniversity of Bath , Department of Biology & Biochemistry, Bath BA2 7AY, United Kingdom.
Edward D SturrockUniversity of Cape Town , The Division of Medical Biochemistry, Institute of Infectious Disease and Molecular Medicine, Observatory 7925, South Africa.
Brian O BachmannVanderbilt University Department of Chemistry, 7300 Stevenson Center, Nashville, Tennessee 37204, United States.
University of Bath · GBUniversity of Cape Town · ZAVanderbilt University · US

Funding

Biosynthesis of Hypotensive Phosphonopeptide Natural ProductsR01GM077189 · NIGMS · VANDERBILT UNIVERSITY · PI BACHMANN, BRIAN O · 2006 to 2010
$1.1M
Medical Research Council G1001685NIGMS NIH HHS R01 GM077189Wellcome Trust 088464
6 · The paper itself

Abstract

The K-26 family of bacterial secondary metabolites are N-modified tripeptides terminated by an unusual phosphonate analog of tyrosine. These natural products, produced via three different actinomycetales, are potent inhibitors of human angiotensin-I converting enzyme (ACE). Herein we investigate the interkingdom pharmacology of the K-26 family by synthesizing these metabolites and assessing their potency as inhibitors of both the N-terminal and C-terminal domains of human ACE. In most cases, selectivity for the C-terminal domain of ACE is displayed. Co-crystallization of K-26 in both domains of human ACE reveals the structural basis of the potent inhibition and has shown an unusual binding motif that may guide future design of domain-selective inhibitors. Finally, the activity of K-26 is assayed against a cohort of microbially produced ACE relatives. In contrast to the synthetic ACE inhibitor captopril, which demonstrates broad interkingdom inhibition of ACE-like enzymes, K-26 selectively targets the eukaryotic family.

Indexed as

ACE inhibitorAngiotensin-I converting enzyme (ACE)bacterial dicarboxypeptidaseK-26

Identifiers

PMID24900839
PMCPMC4027624
OpenAlexW2007219212

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.