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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acid Anhydride Hydrolases / metabolism
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Binding Sites / physiology
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DNA-Binding Proteins / metabolism
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Dinucleoside Phosphates / chemistry*
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Humans
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Hydrolysis
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Molecular Structure
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Neoplasm Proteins*
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Polyphosphates / chemical synthesis*
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Proteins / metabolism*
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Stereoisomerism
Substances
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DNA-Binding Proteins
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Dinucleoside Phosphates
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Neoplasm Proteins
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Polyphosphates
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Proteins
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fragile histidine triad protein
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diadenosine tetraphosphate
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diadenosine triphosphate
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Acid Anhydride Hydrolases