Evidence map›Paper›PMID 26110608›Full record

ReviewPrion2015

Targeting prion protein interactions in cancer.

Tiago G Santos, Marilene H Lopes, Vilma R Martins

Open access · goldAbstract readReview
In one paragraph

Review in Prion, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Emerging roles of the cellular prion protein (PrPCellular and molecular life sciences : CMLS · 2023
    Review
  7. Review
  8. Article
  9. Review
  10. Human RAD51 Protein Forms Amyloid-like AggregatesInternational journal of molecular sciences · 2022
    Article
  11. Article
  12. Article
  13. Review
  14. The Cellular Prion Protein: A Promising Therapeutic Target for Cancer.International journal of molecular sciences · 2020
    Review
  15. A New Take on Prion Protein Dynamics in Cellular Trafficking.International journal of molecular sciences · 2020
    Review
  16. Prion Protein at the Leading Edge: Its Role in Cell Motility.International journal of molecular sciences · 2020
    Review
  17. Article
  18. Review
  19. Article
  20. Article
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 3 institutions in 2 countries.

Tiago G Santosa International Research Center; AC Camargo Cancer Center ; São Paulo , Brazil ;
Marilene H Lopes
Vilma R Martins
AC Camargo Hospital · BRInstitute of Biomedical Science · GBNational Council for Scientific and Technological Development · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years, prion protein (PrP(C)) has been considered as a promising target molecule for cancer therapies, due its direct or indirect participation in tumor growth, metastasis, and resistance to cell death induced by chemotherapy. PrP(C) functions as a scaffold protein, forming multiprotein complexes on the plasma membrane, which elicits distinct signaling pathways involved in diverse biological phenomena and could be modulated depending on the cell type, complex composition, and organization. In addition, PrP(C) and its partners participate in self-renewal of embryonic, tissue-specific stem cells and cancer stem cells, which are suggested to be responsible for the origin, maintenance, relapse, and dissemination of tumors. Interference with protein-protein interaction has been recognized as an important therapeutic strategy in cancer; indeed, the possible interference in PrP(C) engagement with specific partners is a novel strategy. Recently, our group successfully used that approach to interfere with the interaction between PrP(C) and HSP-90/70 organizing protein (HOP, also known as stress-inducible protein 1 - STI1) to control the growth of human glioblastoma in animal models. Thus, PrP(C)-organized multicomplexes have emerged as feasible candidates for anti-tumor therapy, warranting further exploration.

Indexed as

AnimalsHumansLigandsNeoplasmsNeoplastic Stem CellsPrionsProtein BindingSignal TransductionLigandsPrionsBBB, blood brain barriercancercancer stem cellcell signalingCSC, cancer stem cellGBM, glioblastoma multiformeHSP, heat shock proteinsligandpeptideprion proteintherapy

Identifiers

PMID26110608
PMCPMC4601254
OpenAlexW2137903361

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.