Evidence map›Paper›PMID 33527832›Full record

ArticleACS infectious diseases2021

Whole Cell Active Inhibitors of Mycobacterial Lipoamide Dehydrogenase Afford Selectivity over the Human Enzyme through Tight Binding Interactions.

John Ginn, Xiuju Jiang, Shan Sun, Mayako Michino, David J Huggins, Zodwa Mbambo, Robert Jansen, Kyu Y Rhee, Nancy Arango, Christopher D Lima and 10 more

Open access · greenAbstract read
In one paragraph

Article in ACS infectious diseases, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. 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

20 authors at 4 institutions in 1 country.

John GinnTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Xiuju Jiang
Shan SunTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Mayako MichinoTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
David J HugginsTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.ORCID 0000-0003-1579-2496
Zodwa Mbambo
Robert Jansen
Kyu Y Rhee
Nancy ArangoStructural Biology Program, Sloan Kettering Institute, New York, New York 10065, United States.
Christopher D LimaStructural Biology Program, Sloan Kettering Institute, New York, New York 10065, United States.ORCID 0000-0002-9163-6092
Nigel LivertonTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Toshihiro ImaedaTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Rei OkamotoTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Takanobu KuroitaTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Kazuyoshi AsoTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Andrew StamfordTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Michael FoleyTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Peter T MeinkeTri-Institutional Therapeutics Discovery Institute, New York, New York 10065, United States.
Carl Nathan
Tri-Institutional Therapeutics Discovery Institute · USCornell University · USHoward Hughes Medical Institute · USKettering University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
Structural studies of RNA processing and ubiquitin-like protein modificationR35GM118080 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI CHRISTOPHER D. LIMA · 2016 to 2026
$5.0M
NCI NIH HHS P30 CA008748NIGMS NIH HHS R35 GM118080
6 · The paper itself

Abstract

Tuberculosis remains a leading cause of death from a single bacterial infection worldwide. Efforts to develop new treatment options call for expansion into an unexplored target space to expand the drug pipeline and bypass resistance to current antibiotics. Lipoamide dehydrogenase is a metabolic and antioxidant enzyme critical for mycobacterial growth and survival in mice. Sulfonamide analogs were previously identified as potent and selective inhibitors of mycobacterial lipoamide dehydrogenase

Indexed as

Mycobacterium tuberculosisTuberculosisAnimalsAnti-Bacterial AgentsDihydrolipoamide DehydrogenaseHumansKineticsMiceAnti-Bacterial AgentsDihydrolipoamide Dehydrogenaseinhibitorlipoamide dehydrogenasemycobacteriaresidence timeslow bindingtight bindingtuberculosis

Identifiers

PMID33527832
PMCPMC7888283
OpenAlexW3129015826

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.