Evidence map›Paper›PMID 32416922›Full record

ArticleMethods in enzymology2020

Gram-scale preparation of the antibiotic lead compound salicyl-AMS, a potent inhibitor of bacterial salicylate adenylation enzymes.

Nihar Kinarivala, Lisa C Standke, Tezcan Guney, Cheng Ji, Naoyoshi Noguchi, Yasutomi Asano, Derek S Tan

Open access · greenAbstract read
In one paragraph

Article in Methods in enzymology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Host-cell Interactions of Engineered T cell Micropharmacies.bioRxiv : the preprint server for biology · 2023
    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 1 country.

Nihar KinarivalaChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, United States.
Lisa C StandkePharmacology Program, Weill Cornell Graduate School of Medical Sciences, Memorial Sloan Kettering Cancer Center, New York, NY, United States.
Tezcan GuneyChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, United States.
Cheng JiChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, United States.
Naoyoshi NoguchiTri-Institutional Therapeutics Discovery Institute, New York, NY, United States.
Yasutomi AsanoTri-Institutional Therapeutics Discovery Institute, New York, NY, United States.
Derek S TanChemical Biology Program, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, New York, NY, United States; Pharmacology Program, Weill Cornell Graduate School of Medical Sciences, Memorial Sloan Kettering Cancer Center, New York, NY, United States; Tri-Institutional Research Program, Memorial Sloan Kettering Cancer Center, New York, NY, United States. Electronic address: tand@mskcc.org.
Memorial Sloan Kettering Cancer Center · USTri-Institutional Therapeutics Discovery Institute · USCornell University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
Small-Molecule Antibiotics Targeting Siderophore Biosynthesis in M. tuberculosisR01AI118224 · NIAID · SLOAN-KETTERING INST CAN RESEARCH · PI QUADRI, LUIS E, TAN, DEREK S · 2016 to 2020
$3.4M
Predoctoral Training in Pharmacological SciencesT32GM073546 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI GROSS, STEVEN S · 2006 to 2020
$3.1M
Development of Pharmacologically Optimized Inhibitors of M. tuberculosis MbtA as Novel AntibioticsF31AI129244 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI STANDKE, LISA CHARLOTTE · 2017 to 2019
$134k
NCI NIH HHS P30 CA008748NIAID NIH HHS F31 AI129244NIAID NIH HHS R01 AI118224NIGMS NIH HHS T32 GM073546
6 · The paper itself

Abstract

Salicyl-AMS (1) is a potent inhibitor of salicylate adenylation enzymes used in bacterial siderophore biosynthesis and a promising lead compound for the treatment of tuberculosis. An optimized, multigram synthesis is presented, which provides salicyl-AMS as its sodium salt (1·Na) in three synthetic steps followed by a two-step salt formation process. The synthesis proceeds in 11.6% overall yield from commercially available adenosine 2',3'-acetonide and provides highly purified material.

Indexed as

Anti-Bacterial AgentsMycobacterium tuberculosisLeadSalicylatesSiderophoresStructure-Activity RelationshipAnti-Bacterial AgentsLeadSalicylatesSiderophoresAntibioticDrug developmentTuberculosis

Identifiers

PMID32416922
PMCPMC7367610
OpenAlexW3021081787

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.