Evidence map›Paper›PMID 29941580›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Reversible inhibition of the ClpP protease via an N-terminal conformational switch.

Siavash Vahidi, Zev A Ripstein, Massimiliano Bonomi, Tairan Yuwen, Mark F Mabanglo, Jordan B Juravsky, Kamran Rizzolo, Algirdas Velyvis, Walid A Houry, Michele Vendruscolo and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 69 citations in OpenAlex.

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  5. Mechanism of allosteric activation in human mitochondrial ClpP protease.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  16. Rational design of ASCT2 inhibitors using an integrated experimental-computational approach.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  18. Review
  19. Data-Driven Molecular Dynamics: A Multifaceted Challenge.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  20. 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

12 authors at 3 institutions in 2 countries.

Siavash VahidiDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.
Zev A RipsteinDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
Massimiliano BonomiCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.
Tairan YuwenDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.
Mark F MabangloDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
Jordan B JuravskyProgram in Molecular Medicine, The Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Kamran RizzoloDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
Algirdas VelyvisDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.
Walid A HouryDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada.
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, CB2 1EW Cambridge, United Kingdom.
John L RubinsteinDepartment of Biochemistry, University of Toronto, Toronto, ON M5S 1A8, Canada; john.rubinstein@utoronto.ca kay@pound.med.utoronto.ca.
Lewis E KayDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada; john.rubinstein@utoronto.ca kay@pound.med.utoronto.ca.
Hospital for Sick Children · CAUniversity of Toronto · CAUniversity of Cambridge · GB

Funding

CIHR
6 · The paper itself

Abstract

Protein homeostasis is critically important for cell viability. Key to this process is the refolding of misfolded or aggregated proteins by molecular chaperones or, alternatively, their degradation by proteases. In most prokaryotes and in chloroplasts and mitochondria, protein degradation is performed by the caseinolytic protease ClpP, a tetradecamer barrel-like proteolytic complex. Dysregulating ClpP function has shown promise in fighting antibiotic resistance and as a potential therapy for acute myeloid leukemia. Here we use methyl-transverse relaxation-optimized spectroscopy (TROSY)-based NMR, cryo-EM, biochemical assays, and molecular dynamics simulations to characterize the structural dynamics of ClpP from

Indexed as

Molecular Dynamics SimulationBacterial ProteinsEndopeptidase ClpHydrophobic and Hydrophilic InteractionsProtein DomainsStaphylococcus aureusBacterial ProteinsEndopeptidase ClpallosteryClpPconformational dynamicscryo-EMmethyl-TROSY NMR

Identifiers

PMID29941580
PMCPMC6048506
OpenAlexW2810527308

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.