Two hydrolase resistant analogues of diadenosine 5',5"'-P1,P3-triphosphate for studies with Fhit, the human fragile histidine triad protein.
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.
Department of Chemistry, Sheffield University, UK. g.m.blackburn@sheffield.ac.uk
G M
GM
Blackburn
X
X
Liu
A
A
Rösler
C
C
Brenner
D017766:Acid Anhydride Hydrolases / Q000378:metabolism; D001665:Binding Sites / Q000502:physiology; D004268:DNA-Binding Proteins / Q000378:metabolism; D015226:Dinucleoside Phosphates / Q000737:chemistry*; D006801:Humans; D006868:Hydrolysis; D015394:Molecular Structure; D009363:Neoplasm Proteins; D011122:Polyphosphates / Q000138:chemical synthesis*; D011506:Proteins / Q000378:metabolism*; D013237:Stereoisomerism; D000099170:Bis(5'-adenosyl)triphosphatase
D017766:Acid Anhydride Hydrolases; D004268:DNA-Binding Proteins; D015226:Dinucleoside Phosphates; D009363:Neoplasm Proteins; D011122:Polyphosphates; D011506:Proteins; D000099170:Bis(5'-adenosyl)triphosphatase; C020733:diadenosine tetraphosphate; C011440:diadenosine triphosphate