BRENDA - Enzyme Database show
show all sequences of 3.5.4.B9

Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G

Chelico, L.; Prochnow, C.; Erie, D.A.; Chen, X.S.; Goodman, M.F.; J. Biol. Chem. 285, 16195-16205 (2010)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
F126A/W127A
site-directed mutagenesis, the N-terminal CD1 domain mutant, that shows disrupted dimerization at the predicted CD1-CD1 dimer interface, predominantly converts Apo3G to a monomer that binds single-stranded DNA, Alu RNA, and catalyzes processive C to U deaminations with 3'-5' deamination polarity, similar to wild-type Apo3G. The mutation causes severe disruption in oligomer formation resulting in about 92% monomers and 8% dimers, with no larger oligomer forms detected
Homo sapiens
I314A/Y315A
site-directed mutagenesis, C-terminal CD2 domain mutant, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
Homo sapiens
additional information
comparison of Apo3G native and monomeric N-mutant F/W ssDNA substrate binding and catalysis, overview
Homo sapiens
R313A/D316A/D317A/Q318A
site-directed mutagenesis, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
Homo sapiens
Y124A/Y125A
site-directed mutagenesis, the N-terminal CD1 domain mutant is composed of roughly 47% monomers, 42% dimers, 10% tetramers, and 1% much larger molecular mass species of about 650 kDa
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
pre-steady state and steady state kinetics, stopped-flow fluorescence measurements, detailed overview
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2'-deoxycytidine + H2O
Homo sapiens
in ssDNA
2'-deoxyuridine + NH3
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2'-deoxycytidine + H2O
in ssDNA
712428
Homo sapiens
2'-deoxyuridine + NH3
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. Apo3G exists as monomers, dimers, tetramers, and higher order oligomers whose distributions depend on DNA substrate and salt
Homo sapiens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F126A/W127A
site-directed mutagenesis, the N-terminal CD1 domain mutant, that shows disrupted dimerization at the predicted CD1-CD1 dimer interface, predominantly converts Apo3G to a monomer that binds single-stranded DNA, Alu RNA, and catalyzes processive C to U deaminations with 3'-5' deamination polarity, similar to wild-type Apo3G. The mutation causes severe disruption in oligomer formation resulting in about 92% monomers and 8% dimers, with no larger oligomer forms detected
Homo sapiens
I314A/Y315A
site-directed mutagenesis, C-terminal CD2 domain mutant, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
Homo sapiens
additional information
comparison of Apo3G native and monomeric N-mutant F/W ssDNA substrate binding and catalysis, overview
Homo sapiens
R313A/D316A/D317A/Q318A
site-directed mutagenesis, C-terminal CD2 domain mutant, mutation at the Apo2 tetrameric interface and predicted CD1 oligomerization region, the mutant contains about 12% tetramers with no larger oligomeric forms
Homo sapiens
Y124A/Y125A
site-directed mutagenesis, the N-terminal CD1 domain mutant is composed of roughly 47% monomers, 42% dimers, 10% tetramers, and 1% much larger molecular mass species of about 650 kDa
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
pre-steady state and steady state kinetics, stopped-flow fluorescence measurements, detailed overview
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2'-deoxycytidine + H2O
Homo sapiens
in ssDNA
2'-deoxyuridine + NH3
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2'-deoxycytidine + H2O
in ssDNA
712428
Homo sapiens
2'-deoxyuridine + NH3
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. Apo3G exists as monomers, dimers, tetramers, and higher order oligomers whose distributions depend on DNA substrate and salt
Homo sapiens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.3
-
assay at
Homo sapiens
Other publictions for EC 3.5.4.B9
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
734319
Lu
Crystal structure of DNA cytid ...
Homo sapiens
J. Biol. Chem.
290
4010-4021
2015
-
-
1
1
12
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13
-
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1
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2
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1
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13
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12
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13
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1
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13
-
-
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12
12
735015
Zhu
Host APOBEC3G protein inhibits ...
Homo sapiens
PLoS ONE
10
e0121608
2015
-
-
-
-
-
-
-
-
-
-
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1
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1
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1
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1
1
-
-
-
721999
Jaszczur
AID and Apobec3G haphazard dea ...
Homo sapiens
Cell. Mol. Life Sci.
70
3089-3108
2013
-
-
-
-
1
-
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1
1
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3
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2
1
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1
1
-
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-
734795
Holtz
APOBEC3G cytosine deamination ...
Homo sapiens
Nucleic Acids Res.
41
6139-6148
2013
-
-
-
-
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1
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1
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718465
Li
First-in-class small molecule ...
Homo sapiens
ACS Chem. Biol.
7
506-517
2012
-
-
-
1
-
-
34
-
-
-
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1
-
5
-
-
1
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1
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1
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34
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1
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34
34
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1
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1
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1
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1
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720014
Senavirathne
Single-stranded DNA scanning a ...
Homo sapiens
J. Biol. Chem.
287
15826-15835
2012
1
-
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2
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1
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2
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1
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1
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2
1
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-
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1
1
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-
-
721668
Shlyakhtenko
Nanoscale structure and dynami ...
Homo sapiens
Biochemistry
51
6432-6440
2012
-
-
-
-
-
-
-
-
-
-
-
1
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1
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1
1
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1
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1
1
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1
1
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-
722064
Olson
Small-molecule APOBEC3G DNA cy ...
Homo sapiens
ChemMedChem
8
112-117
2012
-
-
-
-
2
-
5
-
-
1
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1
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1
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1
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1
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4
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2
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4
5
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1
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1
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1
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1
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1
1
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723071
Sadler
APOBEC3G contributes to HIV-1 ...
Homo sapiens
J. Virol.
84
7396-7404
2012
-
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1
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1
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1
1
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723754
Monajemi
Emerging complexities of APOBE ...
Homo sapiens
Retrovirology
9
35
2012
-
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1
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1
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1
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1
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1
1
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719945
Demorest
Phosphorylation directly regul ...
Homo sapiens, Mus musculus
J. Biol. Chem.
286
26568-26575
2011
-
-
2
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7
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2
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5
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2
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2
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7
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721103
Li
Functional analysis of the two ...
Homo sapiens
Virology
414
130-136
2011
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1
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1
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1
1
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722698
Feng
Intensity of deoxycytidine dea ...
Homo sapiens
J. Biol. Chem.
286
11415-11426
2011
-
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1
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2
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2
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2
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1
1
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712428
Chelico
Structural model for deoxycyti ...
Homo sapiens
J. Biol. Chem.
285
16195-16205
2010
-
-
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5
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1
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1
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2
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1
1
1
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1
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719342
Carpenter
Determinants of sequence-speci ...
Homo sapiens
DNA Repair
9
579-587
2010
-
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1
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1
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1
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722114
Furukawa
Structure, interaction and rea ...
Homo sapiens
EMBO J.
28
440-451
2009
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1
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10
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10
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1
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722665
Rausch
Dissecting APOBEC3G substrate ...
Homo sapiens
J. Biol. Chem.
284
7047-7058
2009
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1
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1
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1
2
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1
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1
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723261
Holden
Crystal structure of the anti- ...
Homo sapiens
Nature
456
121-124
2008
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1
1
10
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10
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722104
Pham
DNA deaminases AID and APOBEC3 ...
Homo sapiens
DNA Repair
6
689-692
2007
-
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1
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722103
Coker
The nuclear DNA deaminase AID ...
Homo sapiens
DNA Repair
6
235-243
2006
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1
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1
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1
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1
1
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723256
Chelico
APOBEC3G DNA deaminase acts pr ...
Homo sapiens
Nat. Struct. Mol. Biol.
13
392-399
2006
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1
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1
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1
2
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2
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1
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Suspene
APOBEC3G is a single-stranded ...
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723260
Zhang
The cytidine deaminase CEM15 i ...
Homo sapiens
Nature
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94-98
2003
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