Evidence map›Paper›PMID 26670257›Full record

ReviewLife (Basel, Switzerland)2015

Evolutionary Limitation and Opportunities for Developing tRNA Synthetase Inhibitors with 5-Binding-Mode Classification.

Pengfei Fang, Min Guo

Open access · goldAbstract readReview
In one paragraph

Review in Life (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Aminoacyl-tRNA synthetases as therapeutic targets.Nature reviews. Drug discovery · 2019
    Review
  14. Lysyl-tRNA synthetase as a drug target in malaria and cryptosporidiosis.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. Review
  18. Evaluation of the characteristics of leucyl-tRNA synthetase (LeuRS) inhibitor AN3365 in combination with different antibiotic classes.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2016
    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

2 authors at 1 institution in 2 countries.

Pengfei FangState Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, 345 Lingling Road, Shanghai 200032, China. fangpengfei@sioc.ac.cn.
Min GuoDepartment of Cancer Biology, The Scripps Research Institute, Scripps Florida, 130 Scripps Way, Jupiter, FL 33458, USA. GuoMin@scripps.edu.
Scripps Research Institute · US

Funding

Structural and Functional Studies of LysRS in Mast Cell ActivationR01GM100136 · NIGMS · SCRIPPS FLORIDA · PI KODADEK, THOMAS J. · 2012 to 2016
$1.9M
HTS for Direct Targeting of the Transcription Factor MITFR01CA178315 · NCI · SCRIPPS FLORIDA · PI KODADEK, THOMAS J., SCAMPAVIA, LOUIS DANIEL · 2014 to 2016
$1.6M
Development of Assays for Inhibitors of LysRS in Mast Cell ActivationR01GM106134 · NIGMS · SCRIPPS FLORIDA · PI GUO, MIN · 2013 to 2015
$1.1M
NCI NIH HHS R01 CA178315NIGMS NIH HHS R01 GM100136NIGMS NIH HHS R01 GM106134
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases (aaRSs) are enzymes that catalyze the transfer of amino acids to their cognate tRNAs as building blocks for translation. Each of the aaRS families plays a pivotal role in protein biosynthesis and is indispensable for cell growth and survival. In addition, aaRSs in higher species have evolved important non-translational functions. These translational and non-translational functions of aaRS are attractive for developing antibacterial, antifungal, and antiparasitic agents and for treating other human diseases. The interplay between amino acids, tRNA, ATP, EF-Tu and non-canonical binding partners, had shaped each family with distinct pattern of key sites for regulation, with characters varying among species across the path of evolution. These sporadic variations in the aaRSs offer great opportunity to target these essential enzymes for therapy. Up to this day, growing numbers of aaRS inhibitors have been discovered and developed. Here, we summarize the latest developments and structural studies of aaRS inhibitors, and classify them with distinct binding modes into five categories.

Indexed as

aminoacyl-tRNA synthetase (aaRS)evolutioninhibitorprotein-ligand interactionspecies specificitystructure conservation

Identifiers

PMID26670257
PMCPMC4695845
OpenAlexW2191155010

What OpenQuestion holds

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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.