The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit.
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Structural characterization of human histidine triad nucleotide-binding protein 2, a member of the histidine triad superfamilyStereochemistry of rHint1 hydrolase assisted cleavage of P-N bond in nucleoside 5'-O-phosphoramidothioates.Adenylylsulfate-ammonia adenylyltransferase activity is another inherent property of Fhit proteins.Disease-associated mutations inactivate AMP-lysine hydrolase activity of Aprataxin.Kinetic mechanism of human histidine triad nucleotide binding protein 1.Immunohistochemical characterization of FHIT expression in normal human tissuesFhit proteins can also recognize substrates other than dinucleoside polyphosphates.Lysyl-tRNA synthetase-generated lysyl-adenylate is a substrate for histidine triad nucleotide binding proteins.Crystal structure of HINT from Helicobacter pylori.Fhit
P2860
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P2860
The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit.
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2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
The mechanism of action of the ...... chemical rescue of H96G-Fhit.
@en
The mechanism of action of the ...... chemical rescue of H96G-Fhit.
@nl
type
label
The mechanism of action of the ...... chemical rescue of H96G-Fhit.
@en
The mechanism of action of the ...... chemical rescue of H96G-Fhit.
@nl
prefLabel
The mechanism of action of the ...... chemical rescue of H96G-Fhit.
@en
The mechanism of action of the ...... chemical rescue of H96G-Fhit.
@nl
P2093
P356
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The mechanism of action of the ...... chemical rescue of H96G-Fhit.
@en
P2093
Abolfazl Arabshahi
Kaisheng Huang
Perry A Frey
Yaoming Wei
P304
P356
10.1021/BI049762N
P407
P577
2004-06-01T00:00:00Z