Evidence map›Paper›PMID 26929360›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Structure of an endogenous yeast 26S proteasome reveals two major conformational states.

Bai Luan, Xiuliang Huang, Jianping Wu, Ziqing Mei, Yiwei Wang, Xiaobin Xue, Chuangye Yan, Jiawei Wang, Daniel J Finley, Yigong Shi and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Locating Polyubiquitin Receptors on the 19S Regulatory Proteasome ofJournal of the American Society for Mass Spectrometry · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. USP13: Multiple Functions and Target Inhibition.Frontiers in cell and developmental biology · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021
    Review
  16. Review
  17. Review
  18. Article
  19. Article
  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

11 authors at 4 institutions in 2 countries.

Bai LuanMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;
Xiuliang HuangMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;
Jianping WuMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;
Ziqing MeiBiotechnology Research Institute, Chinese Academy of Agricultural Sciences, Beijing 10081, China;
Yiwei WangMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;
Xiaobin XueMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;
Chuangye YanMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;
Jiawei WangMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China;
Daniel J FinleyDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115.
Yigong ShiMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China; shi-lab@tsinghua.edu.cn wfeng@tsinghua.edu.cn.
Feng WangMinistry of Education Key Laboratory of Protein Science, Tsinghua-Peking Joint Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China; shi-lab@tsinghua.edu.cn wfeng@tsinghua.edu.cn.
Tsinghua University · CNCenter for Life Sciences · CNBiotechnology Research Institute · CNHarvard University · US

Funding

Functional Analysis of the Proteasome BaseR37GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 2004 to 2013
$5.9M
UBIQUITIN-PROTEIN CONJUGATES AND FUSIONSR01GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 1990 to 2020
$4.3M
NIGMS NIH HHS R01 GM043601NIGMS NIH HHS R37 GM043601NIGMS NIH HHS R37-GM043601
6 · The paper itself

Abstract

The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function.

Indexed as

Protein ConformationCryoelectron MicroscopyCrystallography, X-RayModels, MolecularProteasome Endopeptidase ComplexProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityATP dependent 26S proteaseProteasome Endopeptidase ComplexSaccharomyces cerevisiae Proteinscryo-EMproteasomeprotein degradationstructure

Identifiers

PMID26929360
PMCPMC4790998
OpenAlexW2291084428

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.