Evidence map›Paper›PMID 19841631›Full record

ReviewNature chemical biology2009

Targeting proteins for degradation.

Erin K Schrader, Kristine G Harstad, Andreas Matouschek

Erratum issuedAbstract readReview
In one paragraph

Review in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 157 papers.

0numbers the graph read from it
0cells of the map it votes in
157citing papers in PubMed
–field-weighted citation impact
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

157 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Revisiting the structure of UBR box from human UBR6.Protein science : a publication of the Protein Society · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors.

Erin K SchraderDepartment of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois, USA.
Kristine G Harstad
Andreas Matouschek

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI MARKO, JOHN F · 2009 to 2013
$12.8M
TRAINING PROGRAM IN ONCOGENESIS &DEVELOPMENT BIOLOGYT32CA080621 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI EKLUND, ELIZABETH ANN · 2001 to 2018
$4.1M
Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
NCI NIH HHS T32 CA080621NCI NIH HHS U54 CA143869NIGMS NIH HHS R01 GM063004NIGMS NIH HHS R01GM64003NIGMS NIH HHS T32 GM008061
6 · The paper itself

Abstract

Protein degradation plays a central role in many cellular functions. Misfolded and damaged proteins are removed from the cell to avoid toxicity. The concentrations of regulatory proteins are adjusted by degradation at the appropriate time. Both foreign and native proteins are digested into small peptides as part of the adaptive immune response. In eukaryotic cells, an ATP-dependent protease called the proteasome is responsible for much of this proteolysis. Proteins are targeted for proteasomal degradation by a two-part degron, which consists of a proteasome binding signal and a degradation initiation site. Here we describe how both components contribute to the specificity of degradation.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsBinding SitesCell Cycle ProteinsCell Physiological PhenomenaOrnithine DecarboxylasePeptide Chain Initiation, TranslationalPeptide HydrolasesPeptidesProteasome Endopeptidase ComplexProtein FoldingProteinsUbiquitinValosin Containing ProteinAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsCell Cycle ProteinsOrnithine DecarboxylasePeptide HydrolasesPeptidesProteasome Endopeptidase ComplexProteinsUbiquitinValosin Containing Protein

Identifiers

PMID19841631
PMCPMC4228941

What OpenQuestion holds

Textmetadata
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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.