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

Aberration of the enzymatic activity of Fhit tumor suppressor protein enhances cancer cell death upon photodynamic therapy similarly to that driven by wild-type Fhit.

Cancer letters - 18 Jul 2009

Ferens Bartosz, Kawiak Anna, Banecki Bogdan, Bielawski Krzysztof P, Zawacka-Pankau Joanna

Abstract excerpt

The tumor suppressor Fhit protein lost in many human pre-malignant tissues, possesses diadenosine triphosphate activity regulated by a photosensitizer, protoporphyrin IX (PpIX) in vitro. Interestingly, when exogenously restored, the protein suppresses the growth of human cervical carcinoma HeLa cells which is further enhanced by PpIX. Additionally, Fhit production enhances the overall response of cells to...

Read the complete abstract on PubMed

Topics

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

Share to Acid Anhydride Hydrolases
Share to Caspase 3

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrolysis

Share to Photochemotherapy

Share to Photosensitizing Agents

Share to Protoporphyrins

Share to Tetrazolium Salts

Share to Thiazoles

Source

Identifiers

PMID: 19286306
DOI: 10.1016/j.canlet.2009.02.014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Aberration of the enzymatic activity of Fhit tumor suppressor protein enhances cancer cell death upon photodynamic therapy similarly to that driven by wild-type Fhit.PMID 19286306Read ↗

Tumor suppressor Fhit protein interacts with protoporphyrin IX in vitro and enhances the response of HeLa cells to photodynamic therapy.Semantic proximity Read ↗

Designed FHIT alleles establish that Fhit-induced apoptosis in cancer cells is limited by substrate binding.Semantic proximity Read ↗

Expression and simple, one-step purification of fragile histidine triad (Fhit) tumor suppressor mutant forms in Escherichia coli and their interaction with protoporphyrin IX.Semantic proximity Read ↗

FHIT alterations in breast cancer.Semantic proximity Read ↗

Fragile histidine triad protein: structure, function, and its association with tumorogenesis.Semantic proximity Read ↗

Restoration of fragile histidine triad ( <i>FHIT</i> ) expression induces apoptosis and suppresses tumorigenicity in lung and cervical cancer cell linesSemantic proximity Read ↗

Fhit-deficient normal and cancer cells are mitomycin C and UVC resistant.Semantic proximity Read ↗

Replacement of Fhit in cancer cells suppresses tumorigenicity.Semantic proximity Read ↗

Selective Killing of Tumors Deficient in Methylthioadenosine Phosphorylase: A Novel StrategySemantic proximity Read ↗

The tumor suppressor Fhit acts as a repressor of β-catenin transcriptional activitySemantic proximity Read ↗

Correlation of fragile histidine triad (Fhit) protein structural features with effector interactions and biological functions.Semantic proximity Read ↗

Fhit modulates the DNA damage checkpoint response.Semantic proximity Read ↗

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