Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Regulation of mammalian target of rapamycin activity in PTEN-inactive prostate cancer cells by I kappa B kinase alpha.

Cancer research - 1 Jul 2007

Dan Han C, Adli Mazhar, Baldwin Albert S

Abstract excerpt

The mammalian target of rapamycin (mTOR) is a mediator of cell growth, survival, and energy metabolism at least partly through its ability to regulate mRNA translation. mTOR is activated downstream of growth factors, insulin, and Akt-dependent signaling associated with oncoprotein expression or l...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Gene Expression Regulation, Neoplastic
Share to HeLa Cells
Share to I-kappa B Kinase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Prostatic Neoplasms

Share to Protein Kinases

Share to PTEN Phosphohydrolase

Share to RNA Interference

Share to TOR Serine-Threonine Kinases

Source

Identifiers

PMID: 17616684
DOI: 10.1158/0008-5472.CAN-07-1232

Genes

PTEN

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17616684-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of mammalian target of rapamycin activity in PTEN-inactive prostate cancer cells by I kappa B kinase alpha.PMID 17616684Read ↗

Akt-dependent activation of mTORC1 complex involves phosphorylation of mTOR (mammalian target of rapamycin) by IκB kinase α (IKKα).Semantic proximity Read ↗

Differential IKK/NF-κB Activity Is Mediated by TSC2 through mTORC1 in PTEN-Null Prostate Cancer and Tuberous Sclerosis Complex Tumor Cells.Semantic proximity Read ↗

Cytosolic phospholipase A2α sustains pAKT, pERK and AR levels in PTEN-null/mutated prostate cancer cells.Semantic proximity Read ↗

Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase.Semantic proximity Read ↗

PTEN regulated PI3K-p110 and AKT isoform plasticity controls metastatic prostate cancer progressionSemantic proximity Read ↗

The p85beta regulatory subunit of PI3K serves as a substrate for PTEN protein phosphatase activity during insulin mediated signaling.Semantic proximity Read ↗

mTOR inhibition reverses Akt-dependent prostate intraepithelial neoplasia through regulation of apoptotic and HIF-1-dependent pathways.Semantic proximity Read ↗

A constitutively activated form of the p110β isoform of PI3-kinase induces prostatic intraepithelial neoplasia in miceSemantic proximity Read ↗

Novel roles of Akt and mTOR in suppressing TGF-beta/ALK5-mediated Smad3 activation.Semantic proximity Read ↗

4E-BP1, a repressor of mRNA translation, is phosphorylated and inactivated by the Akt(PKB) signaling pathway.Semantic proximity Read ↗

PI3K-Akt signaling is involved in the regulation of p21WAF/CIP expression and androgen-independent growth in prostate cancer cellsSemantic proximity Read ↗

Inhibition of ILK in PTEN-mutant human glioblastomas inhibits PKB/Akt activation, induces apoptosis, and delays tumor growth.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.