Evidence map›Paper›PMID 18523588›Full record

ArticlePloS one2008

Identification of nucleolin as new ErbB receptors- interacting protein.

Ayelet Di Segni, Keren Farin, Ronit Pinkas-Kramarski

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 62 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Nucleolin: a cell portal for viruses, bacteria, and toxins.Cellular and molecular life sciences : CMLS · 2022
    Review
  5. Overexpression of Nucleolin and Associated Genes in Prostate Cancer.International journal of molecular sciences · 2022
    Article
  6. Article
  7. Article
  8. Cell surface Nucleolin represents a novel cellular target for neuroblastoma therapy.Journal of experimental & clinical cancer research : CR · 2021
    Article
  9. Cancer Stem Cells and Nucleolin as Drivers of Carcinogenesis.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  10. Frontiers in cell and developmental biology · 2021
    Article
  11. Article
  12. Altered immunoreactivity of ErbB4, a causative gene product for ALS19, in the spinal cord of patients with sporadic ALS.Neuropathology : official journal of the Japanese Society of Neuropathology · 2019
    Article
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  14. Article
  15. Article
  16. Article
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  19. Article
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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 1 institution in 1 country.

Ayelet Di SegniDepartment of Neurobiology, Tel-Aviv University, Ramat-Aviv, Israel.
Keren Farin
Ronit Pinkas-Kramarski
Tel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe ErbB receptor tyrosine kinases are major contributors to malignant transformation. These receptors are frequently overexpressed in a variety of human carcinomas. The role of the ErbB receptors and their ligands in carcinomas and the mechanism by which their overexpression leads to cancer development is still unclear. Ligand binding to specific ErbB receptor is followed by receptor dimerization, phosphorylation and recruitment of SH2 containing cytoplasmic proteins, which initiate the cascade of signaling events. Nevertheless, increasing data suggest that there are non-phosphorylated receptor-substrate interactions that may affect ErbB-mediated responses. METHODOLOGY/PRINCIPAL

findingsIn the present study, using GST-ErbB4 fusion protein pull down assay and mass spectroscopic analysis, we have found the ErbB receptors interact with nucleolin via their cytoplasmic tail. Nucleolin is a ubiquitous, nonhistone, nucleolar, multifunctional phosphoprotein that is also overexpressed in cancer cells. Our results demonstrate that overexpression of ErbB1 and nucleolin may lead to receptor dimerization, phosphorylation and to anchorage independent growth. CONCLUSIONS/SIGNIFICANCE: The oncogenic potential of ErbB depends on receptor levels and activation. Our results suggest that nucleolin may affect ErbB dimerization and activation leading to enhanced cell growth.

Indexed as

AnimalsBase SequenceCell DivisionCell LineDimerizationDNA PrimersHumansNucleolinPhosphoproteinsPhosphorylationProtein BindingRatsReceptor Protein-Tyrosine KinasesRNA-Binding ProteinsSignal TransductionDNA PrimersNucleolinPhosphoproteinsReceptor Protein-Tyrosine KinasesRNA-Binding Proteins

Identifiers

PMID18523588
PMCPMC2390759
OpenAlexW2069296806

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.