Diadenosines as FHIT-ness instructors

Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit.

Alterations in the FHIT gene at 3p14.2 occur as early and frequent events in the development of several common human cancers. The ability of human Fhit-negative cells to form tumors in nude mice is suppressed by stable reexpression of Fhit protein. Fhit protein is a diadenosine P1,P3-triphosphate (ApppA) hydrolase whose fungal and animal homologs form a branch of the histidine triad (HIT) super...

Toric Kempf–Ness sets

In the theory of algebraic group actions on affine varieties, the concept of a Kempf– Ness set is used to replace the categorical quotient by the quotient with respect to a maximal compact subgroup. Using recent achievements of “toric topology,” we show that an appropriate notion of a Kempf–Ness set exists for a class of algebraic torus actions on quasiaffine varieties (coordinate subspace arra...

Structural Mad-ness

ammalian sex-determining factors with homology to DNA binding proteins are required for splicing, according to a study by Paolo SassoneCorsi and coworkers at the Université Louis Pasteur (Strasbourg, France). Examination of high mobility group (HMG) domain containing SRY and Sox proteins demonstrated a surprising but clear association with splicing complexes. SRY, the testis-determining factor ...

FHIT (fragile histidine triad)

Fhit protein is a tumor suppressor with reduced or no expression in many types of cancer. Fhit expression is more frequently lost in cancers of individuals with familial mutations causing deficiency in DNA repair genes such as BRCA1 and BRCA2 and MSH2. In vitro Fhit acts as a hydrolase that cleaves diadenosine triphosphate (Ap3A) to ADP and AMP. The Fhit-Ap3A enzyme-substrate complex appears to...

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