Two hydrolase resistant analogues of diadenosine 5',5"'-P1,P3-triphosphate for studies with Fhit, the human fragile histidine triad protein

Nucleosides Nucleotides. Jan-Mar 1998;17(1-3):301-8. doi: 10.1080/07328319808005178.

Abstract

The design and synthesis of analogues of diadenosine 5',5"'-P1,P3-triphosphate that are resistant to pyrophosphate hydrolysis is described in relation to their rôle in signalling and tumorigenesis involving the Fhit protein, the human fragile histidine triad protein, which is a novel Ap3A binding/cleaving protein.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acid Anhydride Hydrolases / metabolism
  • Binding Sites / physiology
  • DNA-Binding Proteins / metabolism
  • Dinucleoside Phosphates / chemistry*
  • Humans
  • Hydrolysis
  • Molecular Structure
  • Neoplasm Proteins*
  • Polyphosphates / chemical synthesis*
  • Proteins / metabolism*
  • Stereoisomerism

Substances

  • DNA-Binding Proteins
  • Dinucleoside Phosphates
  • Neoplasm Proteins
  • Polyphosphates
  • Proteins
  • fragile histidine triad protein
  • diadenosine tetraphosphate
  • diadenosine triphosphate
  • Acid Anhydride Hydrolases