BRENDA - Enzyme Database
show all sequences of 3.1.31.1

Penaeus monodon Tudor staphylococcal nuclease preferentially interacts with N-terminal domain of Argonaute-1

Phetrungnapha, A.; Panyim, S.; Ongvarrasopone, C.; Fish Shellfish Immunol. 34, 875-884 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression and interaction analysis of the enzyme fused to a GAL4-DNA-binding domain and the three Argonaute proteins in the Saccharomyces cerevisiae strain Y187 two-hybrid system, expression of N-terminally GST-tagged enzyme constructs comprising amino acid residues 1-889, 1-660, and residues 320-889, in Escherichia coli strain Rossetta (DE3)
Penaeus monodon
Engineering
Amino acid exchange
Commentary
Organism
additional information
knockdown of the enzyme by dsRNA
Penaeus monodon
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
calcium-dependent nuclease activity
Penaeus monodon
additional information
the enzyme activity is not affected by Mg2+ and Mn2+
Penaeus monodon
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
120000
-
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
Penaeus monodon
126000
-
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
Penaeus monodon
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Penaeus monodon
the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Penaeus monodon
G1ARD5
-
-
Purification (Commentary)
Commentary
Organism
recombinant GST-tagged enzyme constructs from Escherichia coli strain Rossetta (DE3) by glutathione affinity chromatography, and anion or cation exchange chromatography, followed by dialysis
Penaeus monodon
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA
729764
Penaeus monodon
?
-
-
-
-
additional information
substrates are double-stranded RNA targeting PAZ domain of PmAgo1, PmRab7, and gfp. The enzyme shows calcium-dependent RNase activity, overview
729764
Penaeus monodon
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
Penaeus monodon
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Penaeus monodon
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Penaeus monodon
Cloned(Commentary) (protein specific)
Commentary
Organism
expression and interaction analysis of the enzyme fused to a GAL4-DNA-binding domain and the three Argonaute proteins in the Saccharomyces cerevisiae strain Y187 two-hybrid system, expression of N-terminally GST-tagged enzyme constructs comprising amino acid residues 1-889, 1-660, and residues 320-889, in Escherichia coli strain Rossetta (DE3)
Penaeus monodon
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
knockdown of the enzyme by dsRNA
Penaeus monodon
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
calcium-dependent nuclease activity
Penaeus monodon
additional information
the enzyme activity is not affected by Mg2+ and Mn2+
Penaeus monodon
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
120000
-
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
Penaeus monodon
126000
-
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
Penaeus monodon
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Penaeus monodon
the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant GST-tagged enzyme constructs from Escherichia coli strain Rossetta (DE3) by glutathione affinity chromatography, and anion or cation exchange chromatography, followed by dialysis
Penaeus monodon
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA
729764
Penaeus monodon
?
-
-
-
-
additional information
substrates are double-stranded RNA targeting PAZ domain of PmAgo1, PmRab7, and gfp. The enzyme shows calcium-dependent RNase activity, overview
729764
Penaeus monodon
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
Penaeus monodon
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
assay at
Penaeus monodon
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Penaeus monodon
General Information
General Information
Commentary
Organism
malfunction
suppression of Penaeus monodon Tudor staphylococcal nuclease by double-stranded RNA results in decreasing dsRNA-mediated gene silencing activity. Knockdown of Argonaute protein PmAgo1 and the enzyme diminishes the ability of dsRNA-Rab7 to knockdown PmRab7 expression
Penaeus monodon
additional information
the enzyme interacts with Argonaute protein PmAgo1, but not with PmAgo2 or PmAgo3. Interaction between PmAgo and the enzyme is mediated through the N-terminal domain of PmAgo1 and the SN1-2 domains of the enzyme, interaction analysis and mapping using the two-hybrid system for different protein constructs, overview
Penaeus monodon
physiological function
involvement of PmAgo1 and the enzyme in shrimp RNAi pathway, RNAi-based mechanism in shrimp, overview
Penaeus monodon
General Information (protein specific)
General Information
Commentary
Organism
malfunction
suppression of Penaeus monodon Tudor staphylococcal nuclease by double-stranded RNA results in decreasing dsRNA-mediated gene silencing activity. Knockdown of Argonaute protein PmAgo1 and the enzyme diminishes the ability of dsRNA-Rab7 to knockdown PmRab7 expression
Penaeus monodon
additional information
the enzyme interacts with Argonaute protein PmAgo1, but not with PmAgo2 or PmAgo3. Interaction between PmAgo and the enzyme is mediated through the N-terminal domain of PmAgo1 and the SN1-2 domains of the enzyme, interaction analysis and mapping using the two-hybrid system for different protein constructs, overview
Penaeus monodon
physiological function
involvement of PmAgo1 and the enzyme in shrimp RNAi pathway, RNAi-based mechanism in shrimp, overview
Penaeus monodon
Other publictions for EC 3.1.31.1
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)
751764
Zhang
Tudor-staphylococcal nuclease ...
Homo sapiens
Oncol. Lett.
15
9553-9558
2018
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1
1
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752163
Li
Tudor staphylococcal nuclease ...
Caenorhabditis elegans
RNA
24
739-748
2018
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1
1
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3
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1
1
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1
1
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1
1
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728958
Peng
-
Label-free and sensitive detec ...
Staphylococcus aureus
Anal. Methods
6
4090-4094
2014
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1
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1
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1
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1
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729738
Gao
Human Tudor staphylococcal nuc ...
Homo sapiens
FEBS Lett.
588
2154-2161
2014
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1
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1
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2
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2
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1
1
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729749
Santhekadur
Staphylococcal nuclease domain ...
Homo sapiens
FEBS open bio
4
353-361
2014
-
-
1
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1
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2
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3
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1
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1
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3
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1
1
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730113
Schaumburg
Characterization of a novel th ...
Staphylococcus sp., Staphylococcus sp. FS-A084, Staphylococcus sp. FS-A096, Staphylococcus sp. FS-Cb1b
J. Clin. Microbiol.
52
4036-4038
2014
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6
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1
3
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730556
Erlkamp
Crowding effects on the temper ...
Staphylococcus aureus
Phys. Chem. Chem. Phys.
16
5965-5976
2014
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1
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1
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2
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1
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730786
Kiedrowski
Staphylococcus aureus Nuc2 is ...
Staphylococcus aureus, Staphylococcus aureus N315
PLoS ONE
9
e95574
2014
-
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1
-
1
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1
1
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6
-
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1
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2
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1
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2
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2
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1
1
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1
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2
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2
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2
3
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729335
Talla
The fluorescence detected guan ...
Staphylococcus aureus
Biochimie
95
1386-1393
2013
-
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1
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1
1
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729399
Spencer
The pH dependence of staphyloc ...
Staphylococcus aureus
Biophys. Chem.
180-181
86-94
2013
-
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9
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1
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1
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9
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1
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729448
He
An ultra-high sensitive platfo ...
Staphylococcus aureus, Staphylococcus aureus CCTCC AB91093
Biosens. Bioelectron.
42
467-473
2013
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1
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1
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3
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1
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729764
Phetrungnapha
Penaeus monodon Tudor staphylo ...
Penaeus monodon
Fish Shellfish Immunol.
34
875-884
2013
-
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1
-
1
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2
2
1
-
4
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1
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2
1
1
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1
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1
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1
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2
2
1
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1
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2
1
1
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1
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3
3
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729821
Olson
Staphylococcus aureus nuclease ...
Staphylococcus aureus
Infect. Immun.
81
1316-1324
2013
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1
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3
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1
1
1
1
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730213
Nikitina
Combined micrococcal nuclease ...
Staphylococcus aureus
J. Mol. Biol.
425
1946-1960
2013
-
2
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1
1
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730338
Hu
Characterization and comparati ...
Staphylococcus aureus, Staphylococcus aureus N315
Microbiol. Res.
168
174-182
2013
6
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1
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1
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6
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1
5
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7
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3
1
2
1
1
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2
1
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9
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2
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2
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9
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2
5
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3
2
2
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2
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2
2
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730723
Mino
Gene- and protein-delivered zi ...
Staphylococcus aureus
PLoS ONE
8
e56633
2013
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1
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1
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5
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1
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730910
Roche
Structural, energetic, and dyn ...
Staphylococcus aureus
Proteins
81
1069-1080
2013
-
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1
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11
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1
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1
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1
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11
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1
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1
1
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729277
Wang
Protein crowding impedes press ...
Staphylococcus aureus
Biochim. Biophys. Acta
1820
957-961
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
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1
1
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729819
Beenken
Impact of extracellular nuclea ...
Staphylococcus aureus, Staphylococcus aureus N315
Infect. Immun.
80
1634-1638
2012
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1
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5
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1
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1
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2
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2
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2
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3
6
-
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729981
Santhekadur
Multifunction protein staphylo ...
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2012
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730207
Allan
Micrococcal nuclease does not ...
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J. Mol. Biol.
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2012
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730894
Pais
Mannosylglycerate stabilizes s ...
Staphylococcus aureus
Protein Sci.
21
1126-1137
2012
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1
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730986
Chen
Micrococcal nuclease detection ...
Staphylococcus aureus
Talanta
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533-538
2012
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717383
Wang
Inhibitor binding increases th ...
Staphylococcus aureus
Biophys. J.
100
1094-1099
2011
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718378
Kitahara
Structural plasticity of staph ...
Staphylococcus sp.
Proteins
79
1293-1305
2011
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1
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718396
Tang
The staphylococcal nuclease pr ...
Staphylococcus aureus, Staphylococcus aureus RN4220
Sci. China Life Sci.
54
863-869
2011
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2
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702379
Karp
Conformational consequences of ...
Staphylococcus sp.
Biochemistry
49
4138-4146
2010
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7
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702709
Kato
Nonlocal interactions are resp ...
Staphylococcus sp.
Biophys. J.
98
678-686
2010
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705421
Zhou
Inhibition of replication of c ...
Staphylococcus aureus
J. Virol. Methods
167
79-83
2010
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717245
Wang
Importance of the C-terminal l ...
Staphylococcus sp.
Biochemistry
49
4318-4326
2010
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717382
Hu
The role of tryptophan in stap ...
Staphylococcus sp.
Biophys. Chem.
151
170-177
2010
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717620
Li
Fine mapping of chromatin stru ...
Staphylococcus aureus
Fly
4
213-215
2010
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1
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717951
Berends
Nuclease expression by Staphyl ...
Staphylococcus aureus, Staphylococcus aureus USA 300 LAC
J. Innate Immun.
2
576-586
2010
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718081
Tremillon
Production and purification of ...
Staphylococcus aureus
Microb. Cell Fact.
9
37
2010
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697993
Chouayekh
Highly efficient production of ...
Staphylococcus aureus
FEMS Microbiol. Lett.
293
232-239
2009
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699892
Volkening
Purification of DNA from the c ...
Staphylococcus aureus
J. Virol. Methods
157
55-61
2009
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700123
Kwon
Generation of Vibrio anguillar ...
Staphylococcus aureus, Staphylococcus aureus KCCM 11335
Mol. Biotechnol.
42
154-159
2009
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1
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7
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701613
Kuruma
Staphylococcal nuclease domain ...
Homo sapiens
Am. J. Pathol.
174
2044-2050
2009
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3
1
1
3
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702789
Balasundaram
Step change in the efficiency ...
Staphylococcus sp.
Biotechnol. Bioeng.
104
134-142
2009
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1
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1
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705338
Liu
Subdomain-specific collapse of ...
Staphylococcus sp.
J. Phys. Chem. B
113
12030-12036
2009
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705843
Sundstroem
Tudor staphylococcal nuclease ...
Arabidopsis thaliana, Homo sapiens, Picea abies
Nat. Cell Biol.
11
1347-1354
2009
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2
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2
3
3
2
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706658
Schlessman
Molecular determinants of the ...
Staphylococcus sp.
Proteins
77
570-588
2009
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1
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680252
Hossain
Tudor domain proteins in proto ...
Plasmodium falciparum
Int. J. Parasitol.
38
513-526
2008
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1
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682744
Fitzkee
Electrostatic effects in unfol ...
Staphylococcus aureus
Protein Sci.
17
216-227
2008
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682777
Onitsuka
Mechanism of induced folding: ...
Staphylococcus aureus
Proteins
72
837-847
2008
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2
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1
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682778
Chow
Compact dimension of denatured ...
Staphylococcus aureus
Proteins
72
901-909
2008
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1
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3
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695997
Sunil
Transient silencing of Plasmod ...
Plasmodium falciparum
Biochem. Biophys. Res. Commun.
372
373-378
2008
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696005
Ishii
Probing force-induced unfoldin ...
Staphylococcus sp.
Biochem. Biophys. Res. Commun.
375
586-591
2008
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1
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1
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Baran
Electrostatic effects in a net ...
Staphylococcus sp.
J. Mol. Biol.
379
1045-1062
2008
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1
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1
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699852
Patel
A shorter peptide model from s ...
Staphylococcus sp.
J. Struct. Biol.
164
60-74
2008
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Restricted backbone conformati ...
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Folding kinetics of staphyloco ...
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Complementation of the Lactoco ...
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Local stability identification ...
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Local stability identification ...
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Elucidation of information enc ...
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Neural network-based predictio ...
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Development of cell lines stab ...
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Perchlorate-induced conformati ...
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Feng
The effects of amino acid repl ...
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Biochimie
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Pressure denaturation of staph ...
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Fluorometric study of the acid ...
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Protein stabilization by osmol ...
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Early events during folding of ...
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X-ray and thermodynamic studie ...
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Schwehm
Changes in stability upon char ...
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Biochemistry
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2003
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Nishimura
Effect of salts on the stabili ...
Staphylococcus sp.
Biochemistry
40
2113-2128
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Significance of local electros ...
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Whitten
pH dependence of stability of ...
Staphylococcus sp.
Biochemistry
39
14292-14304
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Tryptophan 140 is important, b ...
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Double point mutant F34W/W140F ...
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Uversky
Structural properties of staph ...
Staphylococcus aureus
Biochemistry
63
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1998
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Uversky
Anion-induced folding of staph ...
Staphylococcus aureus
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Wall
Three-dimensional diffuse x-ra ...
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Yuanhe
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Overexpression, purification o ...
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135041
Eftink
Thermodynamics of the unfoldin ...
Staphylococcus aureus
Biochemistry
35
8084-8094
1996
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135046
Hinck
Engineered disulfide bonds in ...
Staphylococcus aureus
Biochemistry
35
10328-10338
1996
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135039
Libson
Crystal structures of the bina ...
Staphylococcus aureus
Biochemistry
33
8007-8016
1994
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135040
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Thermodynamic characterization ...
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Protein Sci.
3
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Hynes
Engineering alternative beta-t ...
Staphylococcus aureus
Biochemistry
33
5021-5030
1994
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3
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135045
Creighton
Electrophoretic characterizati ...
Staphylococcus aureus, Staphylococcus aureus Foggi Worthington
J. Mol. Biol.
242
670-682
1994
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1
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135038
Fink
Characterization of the stable ...
Staphylococcus aureus
Protein Sci.
2
1155-1160
1993
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1
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135037
Wang
Substrate masking: binding of ...
Staphylococcus aureus
Nucleic Acids Res.
18
6625-6631
1990
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1
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1
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2
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135036
Shortle
Effects of denaturants at low ...
Escherichia coli
Arch. Biochem. Biophys.
272
103-113
1989
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1
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1
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135035
Cecchini
Staphylococcal nuclease high-p ...
Escherichia coli, Escherichia coli pFOG, Staphylococcus aureus
J. Chromatogr.
444
97-106
1988
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1
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4
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135034
Calderon
Thermal denaturation of staphy ...
Escherichia coli
Biochemistry
24
6044-6049
1985
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1
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1
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135033
Vakil
Identification of a heat-labil ...
Staphylococcus aureus
Arch. Microbiol.
139
240-244
1984
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1
1
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2
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2
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1
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135032
Cozzone
-
Staphylococcal nuclease and it ...
Staphylococcus aureus
FEBS Lett.
155
55-60
1983
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1
1
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1
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135031
Guisan
-
Hydrolysis of nucleic acids by ...
Staphylococcus aureus
Enzyme Microb. Technol.
3
313-320
1981
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1
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1
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4
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1
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2
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4
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135029
Okabayashi
Surface-bound nuclease of Stap ...
Staphylococcus aureus 209P, Staphylococcus aureus
J. Bacteriol.
117
215-221
1974
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1
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135030
Wilchek
Purification of nucleases ...
Staphylococcus aureus
Methods Enzymol.
34
492-496
1974
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1
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2
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135027
Cotton
-
Staphylococcal nuclease x-ray ...
Staphylococcus aureus
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
153-175
1971
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1
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1
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1
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1
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135028
Anfinsen
-
Staphylococcal nuclease chemic ...
Staphylococcus aureus, Staphylococcus aureus Foggi Worthington, Staphylococcus aureus V8
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
177-204
1971
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6
1
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4
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16
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1
1
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23
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1
1
1
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6
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1
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4
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1
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23
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1
1
1
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135024
Reddi
-
Micrococcal nuclease ...
Staphylococcus aureus
Methods Enzymol.
12
257-262
1967
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-
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1
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1
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3
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1
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135025
Sulkowski
Phosphatase-free crystalline m ...
Staphylococcus aureus, Staphylococcus aureus Foggi Worthington
J. Biol. Chem.
241
4386-4388
1966
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1
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4
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135026
Taniuchi
The amino acid sequence of an ...
Staphylococcus aureus, Staphylococcus aureus V8
J. Biol. Chem.
241
4366-4385
1966
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13
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4
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4
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135023
Alexander
The purification and propertie ...
Staphylococcus aureus
J. Biol. Chem.
236
3014-3019
1961
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1
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1
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1
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1
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6
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3
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3
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1
1
1
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1
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1
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6
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3
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3
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