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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 18 Feb 2003

Trapasso Francesco, Krakowiak Agnieszka, Cesari Rossano, Arkles Jeffrey, Yendamuri Sai, Ishii Hideshi, Vecchione Andrea, Kuroki Tamotsu, Bieganowski Pawel, Pace Helen C, Huebner Kay, Croce Carlo M, Brenner Charles

Abstract excerpt

The FHIT gene is inactivated early in the development of many human tumors, and Fhit-deficient mice have increased cancer incidence. Viral reexpression of Fhit kills Fhit-deficient cells by induction of apoptosis. Fhit, a member of branch 2 of the histidine-triad superfamily of nucleoside monophosphate hydrolases and transferases, is a diadenosine polyphosphate hydrolase, the active-site histidine of which is not...

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Share to Acid Anhydride Hydrolases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 12574506
DOI: 10.1073/pnas.0437915100
PMCID: PMC149877

Genes

FHIT

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.

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Designed FHIT alleles establish that Fhit-induced apoptosis in cancer cells is limited by substrate binding.PMID 12574506Read ↗

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

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