Evidence map›Paper›PMID 10811618›Full record

ArticleThe EMBO journal2000

Structural basis of the Axin-adenomatous polyposis coli interaction.

K E Spink, P Polakis, W I Weis

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

86 citing papers in PubMed, 207 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Discovering Root Causal Genes with High Throughput Perturbations.bioRxiv : the preprint server for biology · 2024
    Article
  7. Why Is Wnt/β-Catenin Not Yet Targeted in Routine Cancer Care?Pharmaceuticals (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Rare Genetic Variants in HumanInternational journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Wnt/β-catenin signaling in cancers and targeted therapies.Signal transduction and targeted therapy · 2021
    Review
  19. Article
  20. Article

26 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

3 authors at 2 institutions in 1 country.

K E SpinkDepartment of Structural Biology, Stanford University School of Medicine, 299 Campus Drive West, Stanford, CA 94305, USA.
P Polakis
W I Weis
Stanford University · USRapt Therapeutics (United States) · US

Funding

CATENINS, CADHERINS AND THEIR INTERACTIONSR01GM056169 · NIGMS · STANFORD UNIVERSITY · PI WEIS, WILLIAM I · 1997 to 2012
$5.0M
NIGMS NIH HHS R01 GM056169NIGMS NIH HHS R01GM56169
6 · The paper itself

Abstract

Axin and the adenomatous polyposis coli (APC) tumor suppressor protein are components of the Wnt/Wingless growth factor signaling pathway. In the absence of Wnt signal, Axin and APC regulate cytoplasmic levels of the proto-oncogene beta-catenin through the formation of a large complex containing these three proteins, glycogen synthase kinase 3beta (GSK3beta) and several other proteins. Both Axin and APC are known to be critical for beta-catenin regulation, and truncations in APC that eliminate the Axin-binding site result in human cancers. A protease-resistant domain of Axin that contains the APC-binding site is a member of the regulators of G-protein signaling (RGS) superfamily. The crystal structures of this domain alone and in complex with an Axin-binding sequence from APC reveal that the Axin-APC interaction occurs at a conserved groove on a face of the protein that is distinct from the G-protein interface of classical RGS proteins. The molecular interactions observed in the Axin-APC complex provide a rationale for the evolutionary conservation seen in both proteins.

Indexed as

Repressor ProteinsSignal TransductionZebrafish ProteinsAdenomatous Polyposis Coli ProteinAmino Acid SequenceAnimalsAxin ProteinBinding SitesCytoskeletal ProteinsHumansMolecular Sequence DataMutagenesisProtein BindingProtein ConformationProteinsProto-Oncogene MasAdenomatous Polyposis Coli Proteinaxin1 protein, XenopusAxin ProteinCytoskeletal ProteinsMAS1 protein, humanProteinsProto-Oncogene MasProto-Oncogene ProteinsRepressor ProteinsWnt ProteinsXenopus ProteinsZebrafish Proteins

Identifiers

PMID10811618
PMCPMC384355
OpenAlexW1991756459

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.