Activation of PI3K/Akt pathway by PTEN reduction and PIK3CA mRNA amplification contributes to cisplatin resistance in an ovarian cancer cell line (Q27824833)

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English	Activation of PI3K/Akt pathway by PTEN reduction and PIK3CA mRNA amplification contributes to cisplatin resistance in an ovarian cancer cell line	scientific article

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scholarly article

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13 November 2016

Activation of PI3K/Akt pathway by PTEN reduction and PIK3CA mRNA amplification contributes to cisplatin resistance in an ovarian cancer cell line (English)

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13 November 2016

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based on heuristic

inferred from title

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based on heuristic

inferred from title

cancer cell line

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based on heuristic

inferred from title

2

object named as

Eui-Ju Choi

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author name string

Sooyong Lee

1

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Changbae Jin

3

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Dong-Hyun Kim

4

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language of work or name

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publication date

April 2005

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Gynecologic Oncology

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97

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26-34

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1

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High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Overexpression of metallothionein confers resistance to anticancer drugs.

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Acquired cisplatin resistance in human ovarian cancer cells is associated with enhanced repair of cisplatin-DNA lesions and reduced drug accumulation

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Cellular and molecular determinants of cisplatin resistance

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Cellular survival: a play in three Akts

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

The PI 3-kinase/Akt signaling pathway delivers an anti-apoptotic signal.

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

PIK3CA is implicated as an oncogene in ovarian cancer.

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Frequent loss of PTEN expression is linked to elevated phosphorylated Akt levels, but not associated with p27 and cyclin D1 expression, in primary epithelial ovarian carcinomas

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Apoptosis meets signal transduction: elimination of a BAD influence

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Bax-induced caspase activation and apoptosis via cytochrome c release from mitochondria is inhibitable by Bcl-xL.

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Akt/Protein kinase B inhibits cell death by preventing the release of cytochrome c from mitochondria

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Akt regulates cell survival and apoptosis at a postmitochondrial level

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

The phosphatidylinositol 3-kinase (PI3K)-Akt pathway suppresses Bax translocation to mitochondria

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

The lipid phosphatase activity of PTEN is critical for its tumor supressor function

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

The tumor-suppressor activity of PTEN is regulated by its carboxyl-terminal region

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Phosphorylation of the PTEN tail regulates protein stability and function

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex

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https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Mutation of the PTEN tumor suppressor gene is not a feature of ovarian cancers.

1 reference

https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Genomic gain of PIK3CA and increased expression of p110alpha are associated with progression of dysplasia into invasive squamous cell carcinoma.

1 reference

https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Frequent monoallelic deletion of PTEN and its reciprocal associatioin with PIK3CA amplification in gastric carcinoma.

1 reference

https://api.crossref.org/works/10.1016%2FJ.YGYNO.2004.11.051

7 January 2021

Identifiers

10.1016/J.YGYNO.2004.11.051

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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