BRENDA - Enzyme Database show
show all sequences of 3.4.23.38

Expression and enzymatic characterization of the soluble recombinant plasmepsin I from Plasmodium falciparum

Xiao, H.; Tanaka, T.; Ogawa, M.; Yada, R.Y.; Protein Eng. Des. Sel. 20, 625-633 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P-Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography and is capable of autocatalytic activation at pH 4.05.5, which occurrs at Leu116P-Ser117P, seven residues upstream of the native cleavage site (Gly123P-Asn1)
Plasmodium falciparum
Inhibitors
Inhibitors
Commentary
Organism
Structure
pepstatin A
-
Plasmodium falciparum
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Plasmodium falciparum
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
proteolytic modification
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P-Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography and is capable of autocatalytic activation at pH 4.05.5, which occurrs at Leu116PSer117P, seven residues upstream of the native cleavage site (Gly123P-Asn1)
Plasmodium falciparum
Purification (Commentary)
Commentary
Organism
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77PLeu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography
Plasmodium falciparum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH + H2O
-
682637
Plasmodium falciparum
?
-
-
-
?
human hemoglobin + H2O
-
682637
Plasmodium falciparum
?
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.5
3
EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH, and a second optimum at pH 4.5-5.5, mature fusion enzyme
Plasmodium falciparum
2.8
4
human hemoglobin, mature fusion enzyme
Plasmodium falciparum
4.5
5.5
EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH, and a second optimum at pH 2.5-3.0, mature fusion enzyme
Plasmodium falciparum
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0000000117
-
pepstatin A
pH 2.8, mature fusion protein
Plasmodium falciparum
0.0000000699
-
pepstatin A
pH 5.0, mature fusion protein
Plasmodium falciparum
Cloned(Commentary) (protein specific)
Commentary
Organism
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P-Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography and is capable of autocatalytic activation at pH 4.05.5, which occurrs at Leu116P-Ser117P, seven residues upstream of the native cleavage site (Gly123P-Asn1)
Plasmodium falciparum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
pepstatin A
-
Plasmodium falciparum
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.0000000117
-
pepstatin A
pH 2.8, mature fusion protein
Plasmodium falciparum
0.0000000699
-
pepstatin A
pH 5.0, mature fusion protein
Plasmodium falciparum
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
proteolytic modification
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77P-Leu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography and is capable of autocatalytic activation at pH 4.05.5, which occurrs at Leu116PSer117P, seven residues upstream of the native cleavage site (Gly123P-Asn1)
Plasmodium falciparum
Purification (Commentary) (protein specific)
Commentary
Organism
expression and partial characterization of soluble recombinant PM I from Plasmodium falciparum in which a truncated form of PM I (Lys77PLeu329) (P indicates a propart residues) is fused to thioredoxin in the pET32b(1) vector, Trx-tPM I and expressed in Escherichia coli Rosetta-gami B (DE3)pLysS. pLysS. The soluble fusion protein is purified from cell culture using a combination of Ni21 affinity and gel filtration chromatography
Plasmodium falciparum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH + H2O
-
682637
Plasmodium falciparum
?
-
-
-
?
human hemoglobin + H2O
-
682637
Plasmodium falciparum
?
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.5
3
EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH, and a second optimum at pH 4.5-5.5, mature fusion enzyme
Plasmodium falciparum
2.8
4
human hemoglobin, mature fusion enzyme
Plasmodium falciparum
4.5
5.5
EDANS-CO-CH2-CH2-CO-Ala-Leu-Glu-Arg-Met-Phe-Leu-Ser-Phe-Pro-Dap-(DABCYL)-OH, and a second optimum at pH 2.5-3.0, mature fusion enzyme
Plasmodium falciparum
Other publictions for EC 3.4.23.38
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)
718040
Bhaumik
Crystal structures of the free ...
Plasmodium falciparum
J. Struct. Biol.
175
73-84
2011
-
-
1
1
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1
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1
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1
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2
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1
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1
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1
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1
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-
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696329
Liu
Recombinant plasmepsin 1 from ...
Plasmodium falciparum
Biochemistry
48
4086-99
2009
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1
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8
3
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4
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1
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3
1
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8
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8
8
3
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1
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4
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3
1
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707169
Moura
Role of Plasmodium falciparum ...
Plasmodium falciparum
Antimicrob. Agents Chemother.
53
4968-4978
2009
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1
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1
1
-
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-
708121
Friedman
Discovery of plasmepsin inhibi ...
Plasmodium falciparum
ChemMedChem
4
1317-1326
2009
-
-
-
-
-
-
14
-
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1
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1
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14
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14
14
-
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1
-
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680251
Bonilla
Effects on growth, hemoglobin ...
Plasmodium falciparum
Int. J. Parasitol.
37
317-327
2007
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1
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2
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1
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682004
Bonilla
Critical roles for the digesti ...
Plasmodium falciparum
Mol. Microbiol.
65
64-75
2007
-
-
-
-
-
-
-
-
3
-
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-
3
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682637
Xiao
Expression and enzymatic chara ...
Plasmodium falciparum
Protein Eng. Des. Sel.
20
625-633
2007
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1
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1
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4
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1
1
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2
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3
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2
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1
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1
2
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1
1
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2
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3
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667927
Ersmark
Macrocyclic inhibitors of the ...
Plasmodium falciparum
Bioorg. Med. Chem.
14
2197-2208
2006
-
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-
4
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3
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4
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4
4
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670126
Ersmark
Plasmepsins as potential targe ...
Plasmodium falciparum
Med. Res. Rev.
26
626-666
2006
-
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29
-
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5
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29
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29
29
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677552
Hof
Starving the malaria parasite: ...
Plasmodium falciparum
Angew. Chem.
45
2138-2141
2006
-
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4
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1
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4
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4
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679228
Boss
Achiral, cheap, and potent inh ...
Plasmodium falciparum
ChemMedChem
1
1341-1345
2006
-
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13
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1
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13
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13
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681296
DellAgli
High antiplasmodial activity o ...
Plasmodium falciparum
J. Med. Chem.
49
7440-7449
2006
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11
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3
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1
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10
11
10
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1
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669779
Johansson
Design and synthesis of potent ...
Plasmodium falciparum
J. Med. Chem.
48
4400-4409
2005
-
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17
-
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3
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16
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16
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648181
Ersmark
Potent inhibitors of the Plasm ...
Plasmodium falciparum
J. Med. Chem.
47
110-122
2004
-
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17
-
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3
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1
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15
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17
15
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1
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669770
Johansson
Design and synthesis of potent ...
Plasmodium falciparum
J. Med. Chem.
47
3353-3366
2004
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22
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3
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21
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21
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648183
Dahlgren
New inhibitors of the malaria ...
Plasmodium falciparum
Bioorg. Med. Chem.
11
3423-3437
2003
-
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12
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2
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12
3
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648186
Noteberg
Design and synthesis of plasme ...
Plasmodium falciparum
J. Med. Chem.
46
734-746
2003
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12
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3
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3
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1
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12
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12
12
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3
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1
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648187
Siripurkpong
Active Site Contribution to Sp ...
Plasmodium falciparum
J. Biol. Chem.
277
41009-41013
2002
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2
1
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1
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1
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1
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2
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1
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1
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1
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1
2
1
1
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1
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1
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2
-
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1
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648182
Berry
Plasmepsins as antimalarial ta ...
Plasmodium falciparum
Curr. Opin. Drug Discov. Devel.
3
624-629
2000
-
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3
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1
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2
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2
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1
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648188
Tyas
Naturally-occurring and recomb ...
Plasmodium falciparum
FEBS Lett.
454
210-214
1999
-
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3
10
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3
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5
-
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9
-
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5
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3
5
10
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5
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648189
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3
3
2
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1
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648190
Moon
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4
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4
2
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1
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648179
Francis
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1994
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Gluzman
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Goldberg
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2
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