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D136N
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
D39E
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
G122E
the mutant exhibits very low cleavage efficiency toward eukaryotic initiation factor 4G
L40F
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
S67F
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
V120M
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
Y89L
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
Y90L
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
D136N
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the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
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D39E
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the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
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G122E
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the mutant exhibits very low cleavage efficiency toward eukaryotic initiation factor 4G
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L40F
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the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
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S67F
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the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
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C110S
construction of catalytically inactive enzyme mutant EV71-2AC110S
D136N
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
D144A
the mutant shows increased activity compared to the wild type enzyme
D39E
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
E145A
the mutant shows strongly reduced activity compared to the wild type enzyme
G122E
the mutant exhibits very low cleavage efficiency toward eukaryotic initiation factor 4G
H21N/D39E/C110A
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site-directed mutagenesis, a EV-A71 2Apro deleted replicon plasmid is constructed by deletion mutagenesis of the wild-type EV-A71 replicon by mutation at three positions (mutations of H21N, D39E, and C110A) of the 2Apro coding sequence
L40F
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
R55A
the mutant shows reduced activity compared to the wild type enzyme
S67F
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
V120M
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
Y89L
the mutant shows wild type cleavage efficiency toward eukaryotic initiation factor 4G
Y90L
the mutant shows reduced cleavage efficiency toward eukaryotic initiation factor 4G
C110S
Enterovirus A71 BrCR
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construction of catalytically inactive enzyme mutant EV71-2AC110S
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G60R
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mutant is devoid of eIF4G cleavage activity
134Rstop
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
C101S
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intramolecular cleavage is reduced to 52% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 20% of that of the wild-type enzyme, cleavage of eIF4G is 75-100% of that of the wild-type enzyme
C106S
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
C112S
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intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G
C138A
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intramolecular cleavage is reduced to 90% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 200% of that of the wild-type enzyme, cleavage of eIF4G is 75-100% of that of the wild-type enzyme
C52A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G
C54A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G
C61A
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intramolecular cleavage is reduced to 54% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 40% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
D105N
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
D105T
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
D132R/R134D
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
D132T
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
D35A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
D35E
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intramolecular cleavage is reduced to 16% of the wild-type activity, cleavage of P8-P8' is completely abolished
D35T
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
DELTAG104
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
DELTAG107/108
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cleavage of P8-P8' is completely abolished
F130L
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intramolecular cleavage is completely abolished
F130S
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intramolecular cleavage is completely abolished
F130V
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
F136V
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intramolecular cleavage is reduced to 57% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 25% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
G115A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
G115S
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
G118A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
G118S
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
G123A
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intramolecular cleavage is reduced to 23% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 8% of that of the wild-type enzyme, cleavage of eIF4G is less than 10% of that of the wild-type enzyme
G123A/G124A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
G123S
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intramolecular cleavage is reduced to 20% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 10% of that of the wild-type enzyme, cleavage of eIF4G is below 10% of that of the wild-type enzyme
G124A
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intramolecular cleavage is reduced to 22% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 9% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
G124S
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intramolecular cleavage is reduced to 30% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 10% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
H114G
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intramolecular cleavage and cleavage of P8-P8' is completely abolished, no detectable cleavage of eIF5G
H135stop
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
H18A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
H18Y
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
K113P/H114A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
N16A
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
R134Q
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intramolecular cleavage and cleavage of P8-P8' is completely abolished, no cleavage of eIF4G is detected
T121Y
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
Y289R
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inactive, substitution of 2Apro A104 can partially restore self-processing on the mutant Y289R
Y289R/A104C
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substitution of 2Apro A104 can partially restore self-processing on the mutant Y289R
Y289R/A104S
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substitution of 2Apro A104 can partially restore self-processing on the mutant Y289R
Y85K
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intramolecular cleavage is reduced to 82% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 39% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme
Y86F
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intramolecular cleavage is reduced to 62% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 21% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme
Y86K
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intramolecular cleavage is reduced to 71% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 34% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme
V54A
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a BseRI fragment 4742-6148 is transferred from Se1-3C-02 DNA to pT7M, leads to defects in trans but not cis cleavage
Y88L
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the BstEII fragment of picornavirus DNA from nucleotide 3240-3930 is replaced with a PCR product containing the appropriate mutation, the growth of picornavirus mutant is similar to that of wild-type virus in untreated cells but is completely inhibited in IFN-alpha-treated cells
Y88S
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the BstEII fragment of picornavirus DNA from nucleotide 3240-3930 is replaced with a PCR product containing the appropriate mutation, the growth of picornavirus mutant is similar to that of wild-type virus in untreated cells but is completely inhibited in IFN-alpha-treated cells
R20D
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significant defect in self-cleavage activity
R20G
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significant defect in self-cleavage activity
R20P
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complete inactivation, no self-cleavage activity
R20V
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significant defect in self-cleavage activity
H114N
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mutant enzyme does not contain Zn2+
H114N
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intramolecular cleavage and cleavage of P8-P8' is completely abolished
L19S
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cleavage of P8-P8' is reduced to 42% of the wild-type activity
L19S
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intramolecular cleavage activity is reduced to 80% of that of the wild-type activity, cleavage of P8-P8' is reduced to 42% of the wild-type activity
Y85T
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intramolecular cleavage is reduced to 74% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 32% of that of the wild-type enzyme, cleavage of eIF4G is 25-50% of that of the wild-type enzyme
Y85T
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intramolecular cleavage is reduced to 27% of that of the wild-type enzyme and cleavage of P8-P8' is reduced to 8% of that of the wild-type enzyme, cleavage of eIF4G is 10-25% of that of the wild-type enzyme
additional information
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generation of inactive mutant 2A29K through site-directed mutagenesis
additional information
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overexpression of these DAP5 truncates (45 kDa N-terminal (DAP5-N) and 52 kDa C-terminal (DAP5-C) fragments) demonstrates that DAP5-N retains the capability of initiating IRES-driven translation of apoptosis-associated p53, but not the prosurvival Bcl-2 (B-cell lymphoma 2) when compared with the full-length DAP5
additional information
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generation of inactive mutant 2A29K through site-directed mutagenesis
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additional information
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stable expression of enzyme in HeLa cell lines. Expression of enzyme leads to apoptosis, indicated by nuclear fragmentation, DNA breakdown and phosphatidylserine translocation. Enzyme induces the cleavage of poly-ADP-ribose-polymerase, which is blocked by the caspase-3 inhibitor peptide Asp-Glu-Val-Asp
additional information
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recombinant protein with His-tag, no enzymic activity upon eukaryotic initiation factor 4G I
additional information
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the presence of an extensive C-terminal helix, in which Asp132, Arg134, Phe130 and Phe136 play important roles, explains why mutations in this region are generally detrimental to proteinase activity.The zinc-binding motif comprises Cys52, Cys54, Cys112 and His114. Exchange of these residues inactivates the enzyme
additional information
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modification of R20 to every amino acid possible
additional information
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substitution mutants of position R20 produce less severe disease
additional information
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substitution mutants of position R20 produce less severe disease
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