Evidence map›Paper›PMID 19678707›Full record

ArticleJournal of medicinal chemistry2009

Identification of critical ligand binding determinants in Mycobacterium tuberculosis adenosine-5'-phosphosulfate reductase.

Jiyoung A Hong, Devayani P Bhave, Kate S Carroll

Abstract read
In one paragraph

Article in Journal of medicinal chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. On the evolution of protein-adenine binding.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Article
  6. Functional Site Discovery in a Sulfur Metabolism Enzyme by Using Directed Evolution.Chembiochem : a European journal of chemical biology · 2016
    Article
  7. A universal entropy-driven mechanism for thioredoxin-target recognition.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

3 authors at 1 institution in 1 country.

Jiyoung A HongDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-2216, USA.
Devayani P Bhave
Kate S Carroll
Washtenaw Community College · US

Funding

Sulfur Metabolism in Human PathogensR01GM087638 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CARROLL, KATE SUZANNE · 2009 to 2025
$5.0M
NIGMS NIH HHS GM087638NIGMS NIH HHS R01 GM087638
6 · The paper itself

Abstract

Mycobacterium tuberculosis adenosine-5'-phosphosulfate (APS) reductase is an iron-sulfur protein and a validated target to develop new antitubercular agents, particularly for the treatment of latent infection. To facilitate the development of potent and specific inhibitors of APS reductase, we have probed the molecular determinants that underlie binding and specificity through a series of substrate and product analogues. Our study highlights the importance of specific substitutent groups for substrate binding and provides functional evidence for ligand-specific conformational states. An active site model has been developed for M. tuberculosis APS reductase that is in accord with the results presented here as well as prior structural data reported for Pseudomonas aeruginosa APS reductase and related enzymes. This model illustrates the functional features required for the interaction of APS reductase with a ligand and provides a pharmacological roadmap for the rational design of small molecules as potential inhibitors of APS reductase present in human pathogens, including M. tuberculosis.

Indexed as

Catalytic DomainDrug DesignEnzyme InhibitorsHumansHydrogen-Ion ConcentrationLigandsMagnesiumModels, MolecularMycobacterium tuberculosisOxidoreductases Acting on Sulfur Group DonorsPseudomonas aeruginosaStatic ElectricitySubstrate Specificityadenylylsulfate reductaseEnzyme InhibitorsLigandsMagnesiumOxidoreductases Acting on Sulfur Group Donors

Identifiers

PMID19678707
PMCPMC2749248
OpenAlexW2000300275

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.