Evidence map›Paper›PMID 23414347›Full record

ReviewAnnual review of biophysics2013

Structural biology of the proteasome.

Erik Kish-Trier, Christopher P Hill

Open access · greenAbstract readReview
In one paragraph

Review in Annual review of biophysics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed, 1 pooled it
10.5field-weighted citation impact, top 1% 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

124 citing papers in PubMed, 1 synthesis or guideline pooled it, 218 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. The 19S proteasome as a therapeutic target in hematologic malignancies.Frontiers in cell and developmental biology · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Proteostasis in T cell aging.Seminars in immunology · 2023
    Review
  16. Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Article

64 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Erik Kish-TrierDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, Utah 84112-5650, USA.
Christopher P Hill
University of Utah · US

Funding

Structures of Proteasome ActivatorsR01GM059135 · NIGMS · UNIVERSITY OF UTAH · PI HILL, CHRISTOPHER P. · 1999 to 2012
$3.4M
Structure and function of proteasome biogenesis associated proteins 1 and 2F32GM099195 · NIGMS · UNIVERSITY OF UTAH · PI KISH-TRIER, ERIK · 2011 to 2013
$91k
NCI NIH HHS T32CA092347NIGMS NIH HHS F32GM099195NIGMS NIH HHS R01 GM059135NIGMS NIH HHS R01 GM59135
6 · The paper itself

Abstract

The proteasome refers to a collection of complexes centered on the 20S proteasome core particle (20S CP), a complex of 28 subunits that houses proteolytic sites in its hollow interior. Proteasomes are found in eukaryotes, archaea, and some eubacteria, and their activity is critical for many cellular pathways. Important recent advances include inhibitor binding studies and the structure of the immunoproteasome, whose specificity is altered by the incorporation of inducible catalytic subunits. The inherent repression of the 20S CP is relieved by the ATP-independent activators 11S and Blm10/PA200, whose structures reveal principles of proteasome mechanism. The structure of the ATP-dependent 19S regulatory particle, which mediates degradation of polyubiquitylated proteins, is being revealed by a combination of crystal or NMR structures of individual subunits and electron microscopy reconstruction of the intact complex. Other recent structural advances inform us about mechanisms of assembly and the role of conformational changes in the functional cycle.

Indexed as

AnimalsArchaeaBacteriaEukaryotaHumansModels, MolecularMolecular ChaperonesNuclear Magnetic Resonance, BiomolecularProteasome Endopeptidase ComplexProtein SubunitsMolecular ChaperonesProteasome Endopeptidase ComplexProtein Subunits

Identifiers

PMID23414347
PMCPMC4878838
OpenAlexW2139837621

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.