Evidence map›Paper›PMID 26268344›Full record

ReviewCurrent topics in medicinal chemistry2016

Advances in Bacterial Methionine Aminopeptidase Inhibition.

Travis R Helgren, Phumvadee Wangtrakuldee, Bart L Staker, Timothy J Hagen

Open access · greenAbstract readReview
In one paragraph

Review in Current topics in medicinal chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

17 citing papers in PubMed, 42 citations in OpenAlex.

  1. Eleutherin and Isoeleutherin Activity againstInternational journal of molecular sciences · 2024
    Article
  2. Article
  3. Unraveling Potential Glyoxalase-I Inhibitors Utilizing Structure-Based Drug Design Techniques.Advances and applications in bioinformatics and chemistry : AABC · 2024
    Article
  4. Article
  5. Identification of promising methionine aminopeptidase enzyme inhibitors: A combine study of comprehensive virtual screening and dynamics simulation study.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2023
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. N-Terminal Methionine Processing.Current protocols in protein science · 2017
    Article
  15. Article
  16. Article
  17. 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

4 authors at 1 institution in 1 country.

Travis R Helgren
Phumvadee Wangtrakuldee
Bart L Staker
Timothy J HagenNorthern Illinois University, Department of Chemistry and Biochemistry, DeKalb, IL 60115 USA. thagen@niu.edu.
Northern Illinois University · US

Funding

NIAID NIH HHS HHSN272201200025CPHS HHS HHSN272201200025C
6 · The paper itself

Abstract

Methionine aminopeptidases (MetAPs) are metalloenzymes that cleave the N-terminal methionine from newly synthesized peptides and proteins. These MetAP enzymes are present in bacteria, and knockout experiments have shown that MetAP activity is essential for cell life, suggesting that MetAPs are good antibacterial drug targets. MetAP enzymes are also present in the human host and selectivity is essential. There have been significant structural biology efforts and over 65 protein crystal structures of bacterial MetAPs are deposited into the PDB. This review highlights the available crystallographic data for bacterial MetAPs. Structural comparison of bacterial MetAPs with human MetAPs highlights differences that can lead to selectivity. In addition, this review includes the chemical diversity of molecules that bind and inhibit the bacterial MetAP enzymes. Analysis of the structural biology and chemical space of known bacterial MetAP inhibitors leads to a greater understanding of this antibacterial target and the likely development of potential antibacterial agents.

Indexed as

Anti-Bacterial AgentsEnzyme InhibitorsEscherichia coliHumansMethionyl AminopeptidasesMicrobial Sensitivity TestsModels, MolecularMolecular StructureStructure-Activity RelationshipAnti-Bacterial AgentsEnzyme InhibitorsMethionyl Aminopeptidases

Identifiers

PMID26268344
PMCPMC5009474
OpenAlexW2199660586

What OpenQuestion holds

Textmetadata
LicenceTDM
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.