Evidence for the participation of histidine residues located in the 56 kDa C-terminal polypeptide domain of ADP-ribosyl transferase in its catalytic activity.
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Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functionsChemical modification and irreversible inhibition of striatal A2a adenosine receptors.Destabilization of Zn2+ coordination in ADP-ribose transferase (polymerizing) by 6-nitroso-1,2-benzopyrone coincidental with inactivation of the polymerase but not the DNA binding function.Dependence of trans-ADP-ribosylation and nuclear glycolysis on the Arg 34-ATP complex of Zn2+ finger I of poly-ADP-ribose polymerase-1.Coenzymatic activity of randomly broken or intact double-stranded DNAs in auto and histone H1 trans-poly(ADP-ribosylation), catalyzed by poly(ADP-ribose) polymerase (PARP I).Peptidyl beta-homo-aspartals (3-amino-4-carboxybutyraldehydes): new specific inhibitors of caspases.
P2860
Evidence for the participation of histidine residues located in the 56 kDa C-terminal polypeptide domain of ADP-ribosyl transferase in its catalytic activity.
description
1990 nî lūn-bûn
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1990年の論文
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1990年学术文章
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name
Evidence for the participation ...... ase in its catalytic activity.
@en
Evidence for the participation ...... ase in its catalytic activity.
@nl
type
label
Evidence for the participation ...... ase in its catalytic activity.
@en
Evidence for the participation ...... ase in its catalytic activity.
@nl
prefLabel
Evidence for the participation ...... ase in its catalytic activity.
@en
Evidence for the participation ...... ase in its catalytic activity.
@nl
P2093
P2860
P1433
P1476
Evidence for the participation ...... ase in its catalytic activity.
@en
P2093
P2860
P356
10.1016/0014-5793(90)81038-P
P407
P577
1990-10-01T00:00:00Z