Evidence map›Paper›PMID 32355042›Full record

ArticleActa crystallographica. Section D, Structural biology2020

Structure of the N-terminal domain of ClpC1 in complex with the antituberculosis natural product ecumicin reveals unique binding interactions.

Nina M Wolf, Hyun Lee, Daniel Zagal, Joo Won Nam, Dong Chan Oh, Hanki Lee, Joo Won Suh, Guido F Pauli, Sanghyun Cho, Celerino Abad-Zapatero

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 46 citations in OpenAlex.

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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

10 authors at 4 institutions in 2 countries.

Nina M WolfInstitute for Tuberculosis Research, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60612, USA.
Hyun LeeInstitute for Tuberculosis Research, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60612, USA.
Daniel ZagalDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60612, USA.
Joo Won NamDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60612, USA.
Dong Chan OhNatural Products Research Institute, College of Pharmacy, Seoul National University, Seoul 08826, Republic of Korea.
Hanki LeeCenter for Nutraceutical and Pharmaceutical Materials, Myongji University, Cheoin-gu, Yongin-si, Gyeonggi-do 17058, Republic of Korea.
Joo Won SuhCenter for Nutraceutical and Pharmaceutical Materials, Myongji University, Cheoin-gu, Yongin-si, Gyeonggi-do 17058, Republic of Korea.
Guido F PauliInstitute for Tuberculosis Research, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60612, USA.
Sanghyun ChoInstitute for Tuberculosis Research, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60612, USA.
Celerino Abad-ZapateroInstitute for Tuberculosis Research, College of Pharmacy, University of Illinois at Chicago, Chicago, IL 60612, USA.
University of Illinois Chicago · USMyongji University · KRSeoul National University · KRYeungnam University · KR

Funding

UIC: In vitro In vivo Mtb PharmacologyU19AI142735 · NIAID · GLOBAL ALLIANCE FOR TB DRUG DEVELOPMENT · PI FOTOUHI, NADER · 2019 to 2023
$28.5M
National Institute of Allergy and Infectious Diseases U19AI142735NIAID NIH HHS U19 AI142735Rural Development Administration PJ01328403 and PJ01319101
6 · The paper itself

Abstract

The biological processes related to protein homeostasis in Mycobacterium tuberculosis, the etiologic agent of tuberculosis, have recently been established as critical pathways for therapeutic intervention. Proteins of particular interest are ClpC1 and the ClpC1-ClpP1-ClpP2 proteasome complex. The structure of the potent antituberculosis macrocyclic depsipeptide ecumicin complexed with the N-terminal domain of ClpC1 (ClpC1-NTD) is presented here. Crystals of the ClpC1-NTD-ecumicin complex were monoclinic (unit-cell parameters a = 80.0, b = 130.0, c = 112.0 Å, β = 90.07°; space group P2

Indexed as

Antitubercular AgentsBacterial ProteinsBinding SitesBiological ProductsDepsipeptidesHeat-Shock ProteinsMycobacterium tuberculosisPeptides, CyclicProtein BindingProtein DomainsAntitubercular AgentsBacterial ProteinsBiological ProductsClpC1 protein, Mycobacterium tuberculosisDepsipeptidesecumicinHeat-Shock ProteinsPeptides, CyclicAAA+ ATPasesClpC1ecumicinMycobacterium tuberculosisohmyungsamicins

Identifiers

PMID32355042
PMCPMC7193532
OpenAlexW3019471649

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.