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

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.
Authors	G M Blackburn, X Liu, A Rösler, C Brenner
Journal	Nucleosides & nucleotides (Nucleosides Nucleotides) 1998 Jan-Mar Vol. 17 Issue 1-3 Pg. 301-8 ISSN: 0732-8311 [Print] United States
PMID	9708352 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
Chemical References	DNA-Binding Proteins Dinucleoside Phosphates Neoplasm Proteins Polyphosphates Proteins fragile histidine triad protein diadenosine tetraphosphate diadenosine triphosphate Acid Anhydride Hydrolases
Topics	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

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