Evidence map›Paper›PMID 12360406›Full record

ArticleOncogene2002

Hp95 promotes anoikis and inhibits tumorigenicity of HeLa cells.

Ying Wu, Shujuan Pan, Weiping Luo, Sue-Hwa Lin, Jian Kuang

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  11. The helicase protein DHX29 promotes translation initiation, cell proliferation, and tumorigenesis.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
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  13. Review
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  16. Alternative polyadenylation produces two major transcripts of Alix.Archives of biochemistry and biophysics · 2007
    Article
  17. Article
  18. 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

5 authors at 1 institution in 1 country.

Ying WuDepartment of Experimental Therapeutics, The University of Texas, M.D. Anderson Cancer Center, Houston, Texas, TX 77030, USA.
Shujuan Pan
Weiping Luo
Sue-Hwa Lin
Jian Kuang
The University of Texas MD Anderson Cancer Center · US

Funding

Tumor Evolution and Metastasis ProgramP30CA016672 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Scott Kopetz · 1985 to 2026
$290.8M
NCI NIH HHS CA16672
6 · The paper itself

Abstract

p95 is a putative signal transduction protein of approximately 95 kDa that contains multiple tyrosine residues that are conserved from yeast to human, a Src phosphorylation consensus sequence and a proline-rich C-terminus that binds SH3-domains. Previous studies have established that mammalian p95 is physically associated with proteins that regulate apoptotic induction and cell transformation; however, it is unclear whether p95 is a positive or negative regulator in these processes. Moreover, a p95 partner protein has been localized at both focal adhesions and actin-cytoskeletons in rat astrocytes. However, there is no evidence that mammalian p95 has roles in regulating cell adhesion or morphology. In this study, we examined the effects of p95 on the anchorage-independent growth and tumorigenicity of malignant HeLa cells, and on the growth and morphology of non-transformed NIH3T3 cells. In HeLa cells, p95 overexpression promoted detachment-induced apoptosis (anoikis), inhibited detachment of viable cells from substratum and reduced tumorigenicity. In NIH3T3 cells, p95 overexpression promoted flat cell morphology and slowed cell proliferation, whereas p95 downregulation had opposite effects. These findings indicate that the mammalian p95 is a positive regulator in apoptotic signaling and a negative regulator in cell transformation. They also suggest that p95 has roles in regulating cell adhesion and morphology.

Indexed as

Anoikis3T3 CellsAnimalsApoptosisCalcium-Binding ProteinsCarrier ProteinsCell AdhesionCell Cycle ProteinsCell DivisionEndosomal Sorting Complexes Required for TransportG1 PhaseHeLa CellsHumansMiceMice, NudeNeoplasms, ExperimentalCalcium-Binding ProteinsCarrier ProteinsCell Cycle ProteinsEndosomal Sorting Complexes Required for TransportPDCD6IP protein, humanPhosphoproteins

Identifiers

PMID12360406
OpenAlexW2322016361

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.