Evidence map›Paper›PMID 29087330›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Probing the cooperativity of

Rui Huang, Felipe Pérez, Lewis E Kay

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. 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
2.0field-weighted citation impact, top 13% 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, 29 citations in OpenAlex.

  1. Article
  2. Client-scaffold interactions suppress aggregation of a client protein in model condensates.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Activation of caspase-9 on the apoptosome as studied by methyl-TROSY NMR.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Probing allosteric interactions in homo-oligomeric molecular machines using solution NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. An allosteric switch regulatesProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Exploring long-range cooperativity in the 20S proteasome core particle fromProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Review
  13. Article
  14. Article
  15. Cooperative subunit dynamics modulate p97 function.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Reversible inhibition of the ClpP protease via an N-terminal conformational switch.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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 2 institutions in 1 country.

Rui HuangDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.
Felipe PérezDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.
Lewis E KayDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada; kay@pound.med.utoronto.ca.
University of Toronto · CAHospital for Sick Children · CA

Funding

CIHR
6 · The paper itself

Abstract

The 20S proteasome core particle (20S CP) plays an integral role in cellular homeostasis by degrading proteins no longer required for function. The process is, in part, controlled via gating residues localized to the ends of the heptameric barrel-like CP structure that occlude substrate entry pores, preventing unregulated degradation of substrates that might otherwise enter the proteasome. Previously, we showed that the N-terminal residues of the α-subunits of the CP from the archaeon

Indexed as

Archaeal ProteinsEndopeptidasesMagnetic Resonance SpectroscopyModels, MolecularMutagenesisMutant ProteinsProtein ConformationProtein Interaction Domains and MotifsProtein SubunitsProteolysisSpin LabelsThermoplasmaArchaeal ProteinsEndopeptidasesMutant Proteinsproteasome, ThermoplasmaProtein SubunitsSpin Labelsin/out gate conformationmethyl-TROSYproteasome core particleproteasome gateα7 ring

Identifiers

PMID29087330
PMCPMC5699070
OpenAlexW2766049635

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.