Evidence map›Paper›PMID 23169527›Full record

ReviewCold Spring Harbor perspectives in biology2013

The β-catenin destruction complex.

Jennifer L Stamos, William I Weis

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 641 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
641citing papers in PubMed, 1 pooled it
–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

641 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,048 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. CD8Cell reports. Medicine · 2026
    Review
  4. Review
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  6. Review
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  16. Review
  17. Article
  18. CTNNB1 Genetic Variation and Its Interaction With DLK1 in Type 2 Diabetes Mellitus.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  19. Article
  20. Article

581 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.

Jennifer L StamosDepartments of Structural Biology and Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
William I Weis
Stanford University · US

Funding

CATENINS, CADHERINS AND THEIR INTERACTIONSR01GM056169 · NIGMS · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 1997 to 2012
$5.0M
Molecular Basis of Wnt Receptor InteractionsR01AG039420 · NIA · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 2011 to 2015
$1.6M
Molecular Mechanisms of Wnt Signal TransductionR01GM119156 · NIGMS · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 2016 to 2019
$1.3M
NIA NIH HHS R01 AG039420NIGMS NIH HHS GM56169NIGMS NIH HHS R01 GM056169NIGMS NIH HHS R01 GM119156
6 · The paper itself

Abstract

The Wnt/β-catenin pathway is highly regulated to insure the correct temporal and spatial activation of its target genes. In the absence of a Wnt stimulus, the transcriptional coactivator β-catenin is degraded by a multiprotein "destruction complex" that includes the tumor suppressors Axin and adenomatous polyposis coli (APC), the Ser/Thr kinases GSK-3 and CK1, protein phosphatase 2A (PP2A), and the E3-ubiquitin ligase β-TrCP. The complex generates a β-TrCP recognition site by phosphorylation of a conserved Ser/Thr-rich sequence near the β-catenin amino terminus, a process that requires scaffolding of the kinases and β-catenin by Axin. Ubiquitinated β-catenin is degraded by the proteasome. The molecular mechanisms that underlie several aspects of destruction complex function are poorly understood, particularly the role of APC. Here we review the molecular mechanisms of destruction complex function and discuss several potential roles of APC in β-catenin destruction.

Indexed as

Adenomatous Polyposis Coli ProteinAmino Acid SequenceAxin ProteinAxin Signaling Complexbeta CateninBinding SitesGene Expression RegulationModels, BiologicalMolecular Sequence DataPhosphorylationProteasome Endopeptidase ComplexSignal TransductionUbiquitinationAdenomatous Polyposis Coli ProteinAxin ProteinAxin Signaling Complexbeta CateninProteasome Endopeptidase Complex

Identifiers

PMID23169527
PMCPMC3579403
OpenAlexW2096171021

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.