Evidence map›Paper›PMID 24452470›Full record

ReviewNature reviews. Molecular cell biology2014

Regulated protein turnover: snapshots of the proteasome in action.

Sucharita Bhattacharyya, Houqing Yu, Carsten Mim, Andreas Matouschek

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.

0numbers the graph read from it
0cells of the map it votes in
143citing papers in PubMed
15.2field-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

143 citing papers in PubMed, 241 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Programming DNA machines to move.Nature reviews. Chemistry · 2026
    Review
  8. PAR-Driven Condensation Maintains Stalled Replication Fork Stability.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. Bimodular architecture of bacterial effector SAP05 that drives ubiquitin-independent targeted protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  16. Article
  17. Transcriptomic Response of the Liver Tissue inAnimals : an open access journal from MDPI · 2023
    Article
  18. Article
  19. Article
  20. Article

83 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

4 authors at 2 institutions in 1 country.

Sucharita BhattacharyyaDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA.
Houqing Yu1] Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA. [2] Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, Texas 78712, USA.
Carsten MimDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA.
Andreas Matouschek1] Department of Molecular Biosciences, Northwestern University, Evanston, Illinois 60208, USA. [2] Department of Chemistry and Biochemistry, The University of Texas at Austin, Austin, Texas 78712, USA.
Northwestern University · USThe University of Texas at Austin · US

Funding

TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI KOPP, PETER ANDREAS · 2009 to 2013
$12.8M
Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017
$3.7M
Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
Structural Biology of Membrane ScaffoldsR01GM094479 · NIGMS · NORTHWESTERN UNIVERSITY · PI UNGER, VINZENZ · 2010 to 2013
$1.6M
NCI NIH HHS U54 CA143869NIGMS NIH HHS R01 GM063004NIGMS NIH HHS R01 GM094479NIGMS NIH HHS R01 GM63004NIGMS NIH HHS U54 GM105816
6 · The paper itself

Abstract

The ubiquitin proteasome system (UPS) is the main ATP-dependent protein degradation pathway in the cytosol and nucleus of eukaryotic cells. At its centre is the 26S proteasome, which degrades regulatory proteins and misfolded or damaged proteins. In a major breakthrough, several groups have determined high-resolution structures of the entire 26S proteasome particle in different nucleotide conditions and with and without substrate using cryo-electron microscopy combined with other techniques. These structures provide some surprising insights into the functional mechanism of the proteasome and will give invaluable guidance for genetic and biochemical studies of this key regulatory system.

Indexed as

Cell NucleusCryoelectron MicroscopyCytosolMultiprotein ComplexesProteasome Endopeptidase ComplexProteinsProteolysisUbiquitinATP dependent 26S proteaseMultiprotein ComplexesProteasome Endopeptidase ComplexProteinsUbiquitin

Identifiers

PMID24452470
PMCPMC4384331
OpenAlexW2068408381

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.