Evidence map›Paper›PMID 31778111›Full record

ArticleeLife2019

Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation.

Eric R Greene, Ellen A Goodall, Andres H de la Peña, Mary E Matyskiela, Gabriel C Lander, Andreas Martin

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

22 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Ubiquitin modulates 26Science advances · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Proteasomal conformation controls unfolding ability.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Mechanisms of substrate recognition by the 26S proteasome.Current opinion in structural biology · 2021
    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

6 authors at 2 institutions in 1 country.

Eric R Greene *Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.ORCID 0000-0003-1717-0914
Ellen A Goodall *Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.ORCID 0000-0001-9876-5973
Andres H de la PeñaDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, United States.
Mary E MatyskielaDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, United States.ORCID 0000-0003-4921-1135
Andreas MartinDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.ORCID 0000-0003-0923-3284
QB3 · USScripps Research Institute · US

Funding

ATP-Dependent Protein Unfolding and Translocation by the Eukaryotic ProteasomeR01GM094497 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI MARTIN, ANDREAS · 2011 to 2024
$3.7M
Molecular basis of axonal transport described by high-resolution 3D imagingDP2EB020402 · NIBIB · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2014 to 2014
$2.8M
COMPUTING AND DATA STORAGE CLUSTER FOR ELECTRON MICROSCOPYS10OD021634 · OD · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2016 to 2016
$531k
American Cancer Society 132279-PF-18-189-01-DMCNIGMS NIH HHS R01 GM094497NIH HHS DP2EB020402NIH HHS R01-GM094497NIH HHS S10OD021634
6 · The paper itself

Abstract

The 26S proteasome is essential for proteostasis and the regulation of vital processes through ATP-dependent degradation of ubiquitinated substrates. To accomplish the multi-step degradation process, the proteasome's regulatory particle, consisting of lid and base subcomplexes, undergoes major conformational changes whose origin is unknown. Investigating the

Indexed as

Adenosine TriphosphatasesEndosomal Sorting Complexes Required for TransportModels, MolecularNucleotidesProteasome Endopeptidase ComplexProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase ComplexesAdenosine TriphosphatasesATP dependent 26S proteaseEndosomal Sorting Complexes Required for TransportNucleotidesProteasome Endopeptidase ComplexRpn5 protein, S cerevisiaeRPT6 protein, S cerevisiaeRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin-Protein Ligase Complexes26S proteasomeAAA+ ATPasebiochemistrychemical biologyS. cerevisiaeubiquitin-proteasome System

Identifiers

PMID31778111
PMCPMC6910829
OpenAlexW2990885485

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.