Evidence map›Paper›PMID 28689658›Full record

ArticleMolecular cell2017

Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.

Ying Lu, Jiayi Wu, Yuanchen Dong, Shuobing Chen, Shuangwu Sun, Yong-Bei Ma, Qi Ouyang, Daniel Finley, Marc W Kirschner, Youdong Mao

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2017. 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
2.5field-weighted citation impact, top 10% 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, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
  5. Review
  6. Article
  7. Structural insights into the ubiquitin-independent midnolin-proteasome pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021
    Review
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.

Ying LuDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Jiayi WuState Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Center for Quantitative Biology, Peking University, Beijing 100871, China.
Yuanchen DongIntel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.
Shuobing ChenState Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Center for Quantitative Biology, Peking University, Beijing 100871, China.
Shuangwu SunDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Yong-Bei MaState Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Center for Quantitative Biology, Peking University, Beijing 100871, China.
Qi OuyangState Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Center for Quantitative Biology, Peking University, Beijing 100871, China; Peking-Tsinghua Joint Center for Life Science, Peking University, Beijing 100871, China.
Daniel FinleyDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Marc W KirschnerDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: marc@hms.harvard.edu.
Youdong MaoState Key Laboratory for Artificial Microstructures and Mesoscopic Physics, Institute of Condensed Matter Physics, School of Physics, Center for Quantitative Biology, Peking University, Beijing 100871, China; Intel Parallel Computing Center for Structural Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cancer Immunology and Virology, Dana-Farber Cancer Institute, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA. Electronic address: youdong_mao@dfci.harvard.edu.
Peking University · CNHarvard University · USIntel (United States) · USCenter for Systems Biology · US

Funding

Virus biology scientific research support componentUM1AI100645 · NIAID · DUKE UNIVERSITY · PI MONTEFIORI, DAVID C · 2012 to 2018
$204.7M
BIOCHEMICAL STUDIES OF MITOSISR01GM026875 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KIRSCHNER, MARC WALLACE · 1985 to 2019
$18.2M
UBIQUITIN-PROTEIN CONJUGATES AND FUSIONSR01GM043601 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FINLEY, DANIEL J · 1990 to 2020
$4.3M
Ubiquitin chain editing by the mammalian proteasomeR01GM095526 · NIGMS · HARVARD MEDICAL SCHOOL · PI FINLEY, DANIEL J · 2011 to 2014
$1.8M
NIAID NIH HHS UM1 AI100645NIGMS NIH HHS R01 GM026875NIGMS NIH HHS R01 GM043601NIGMS NIH HHS R01 GM095526
6 · The paper itself

Abstract

The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly.

Indexed as

Adaptor Proteins, Signal TransducingATPases Associated with Diverse Cellular ActivitiesCryoelectron MicroscopyHEK293 CellsHumansLIM Domain ProteinsModels, MolecularMolecular ChaperonesProteasome Endopeptidase ComplexProtein BindingProtein Structure, QuaternaryProtein SubunitsProto-Oncogene ProteinsStructure-Activity RelationshipTranscription FactorsTransfectionAdaptor Proteins, Signal TransducingATPases Associated with Diverse Cellular ActivitiesATP dependent 26S proteaseLIM Domain ProteinsMolecular ChaperonesProteasome Endopeptidase ComplexProtein SubunitsProto-Oncogene ProteinsPSMC4 protein, humanPSMC5 protein, humanPSMD10 protein, humanTranscription FactorsAAA-ATPaseassembly chaperoneconformational landscapecryo-EMgankyrinp28proteasomeregulatory particlesubstrate unfolding

Identifiers

PMID28689658
PMCPMC5580496
OpenAlexW2725118945

What OpenQuestion holds

Textmetadata
LicenceTDM
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.