BRENDA - Enzyme Database show
show all sequences of 2.7.4.8

Insights into open/closed conformations of the catalytically active human guanylate kinase as investigated by small-angle X-ray scattering

Jain, R.; Khan, N.; Menzel, A.; Rajkovic, I.; Konrad, M.; Techert, S.; Eur. Biophys. J. 45, 81-89 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant expression of the N-terminally His6-tagged and SUMO-tagged enzyme in Escherichia coli strain BL21-(DE3)-pLysS
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
P1 -(5'-adenosyl)-P5 -(5'-guanosyl)pentaphosphate
a non-hydrolysable bi-substrate analogue
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Homo sapiens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
22000
-
-
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + GMP
Homo sapiens
-
ADP + GDP
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q16774
gene GUK1
-
Purification (Commentary)
Commentary
Organism
recombinant N-terminally His6-tagged and SUMO-tagged enzyme from Escherichia coli strain BL21-(DE3)-pLysS by nickel affinity chromatography and gel filtration
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + GMP
-
738145
Homo sapiens
ADP + GDP
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 22000, recombinant His6-SUMO-tagged enzyme, SDS-PAGE
Homo sapiens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Homo sapiens
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant expression of the N-terminally His6-tagged and SUMO-tagged enzyme in Escherichia coli strain BL21-(DE3)-pLysS
Homo sapiens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
-
Homo sapiens
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
P1 -(5'-adenosyl)-P5 -(5'-guanosyl)pentaphosphate
a non-hydrolysable bi-substrate analogue
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Homo sapiens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
22000
-
-
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + GMP
Homo sapiens
-
ADP + GDP
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant N-terminally His6-tagged and SUMO-tagged enzyme from Escherichia coli strain BL21-(DE3)-pLysS by nickel affinity chromatography and gel filtration
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + GMP
-
738145
Homo sapiens
ADP + GDP
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 22000, recombinant His6-SUMO-tagged enzyme, SDS-PAGE
Homo sapiens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Homo sapiens
General Information
General Information
Commentary
Organism
evolution
GMPK is a member of the family of ATP:NMP phosphoryltransferases, nucleoside monophosphate kinases, NMP kinases, or NMPKs
Homo sapiens
additional information
size and shape of open and closed enzyme GMPK are tracked by SAXS. The binding of substrates GMP and AMPPNP, or Ap5G, or GMP and ADP, results in the compaction of size and shape of human enzyme GMPK. Determination of structural changes between open and completely closed hGMPK conformation, overview. Homology modelling of hGMPK by using the crystal structure of mGMPK's closed conformation, residues 5-194 of 197, as template, PDB ID 1LVG
Homo sapiens
physiological function
enzyme GMPK plays an important role in the recycling of the secondary messenger cGMP and thereby regulates the supply of guanine nucleotides to various signal transduction pathways. In addition to its physiological roles, GMPK is also required for the intracellular activation of numerous antiviral and anticancer purine nucleoside analog prodrugs
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
evolution
GMPK is a member of the family of ATP:NMP phosphoryltransferases, nucleoside monophosphate kinases, NMP kinases, or NMPKs
Homo sapiens
additional information
size and shape of open and closed enzyme GMPK are tracked by SAXS. The binding of substrates GMP and AMPPNP, or Ap5G, or GMP and ADP, results in the compaction of size and shape of human enzyme GMPK. Determination of structural changes between open and completely closed hGMPK conformation, overview. Homology modelling of hGMPK by using the crystal structure of mGMPK's closed conformation, residues 5-194 of 197, as template, PDB ID 1LVG
Homo sapiens
physiological function
enzyme GMPK plays an important role in the recycling of the secondary messenger cGMP and thereby regulates the supply of guanine nucleotides to various signal transduction pathways. In addition to its physiological roles, GMPK is also required for the intracellular activation of numerous antiviral and anticancer purine nucleoside analog prodrugs
Homo sapiens
Other publictions for EC 2.7.4.8
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)
738145
Jain
Insights into open/closed conf ...
Homo sapiens
Eur. Biophys. J.
45
81-89
2016
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1
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1
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1
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1
1
1
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1
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3
3
-
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739667
Zhang
Mechanistic insight into the f ...
Saccharomyces cerevisiae
Sci. Rep.
5
8405
2015
-
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-
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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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2
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1
1
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738614
Nomura
Diversity in guanosine 3,5-bis ...
Arabidopsis thaliana, Bacillus subtilis, Escherichia coli, Oryza sativa Japonica Group, Oryza sativa Japonica Group Nipponbare, Pisum sativum, Saccharomyces cerevisiae, Synechococcus elongatus
J. Biol. Chem.
289
15631-15641
2014
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7
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9
4
9
7
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11
-
20
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7
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3
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11
-
7
-
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4
7
-
-
7
1
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1
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-
9
9
-
-
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1
9
1
4
9
9
-
11
-
-
-
9
-
5
-
-
11
-
9
-
-
4
9
-
-
-
-
10
14
-
4
4
739240
Gupta
Purification and characterizat ...
Brugia malayi
Parasitology
141
1341-1352
2014
-
-
1
-
-
-
8
2
-
2
2
1
-
3
-
-
1
1
-
-
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6
2
1
1
-
2
1
1
-
1
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-
1
1
-
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-
-
8
-
2
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2
2
1
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-
1
-
-
-
-
6
2
1
1
-
2
1
1
-
-
-
1
1
-
2
2
737590
Mori
Crystal structure of the guany ...
Homo sapiens
Biochem. Biophys. Res. Commun.
435
334-338
2013
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1
1
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-
-
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2
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3
-
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1
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1
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1
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3
3
-
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-
723031
Dembowski
Alternative splicing of a nove ...
Homo sapiens
J. Nucleic Acids
2012
816237
2012
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1
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3
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1
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721551
Mertlikova-Kaiserova
Point mutations in human guany ...
Homo sapiens
Biochem. Pharmacol.
82
131-138
2011
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1
-
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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1
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2
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1
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2
-
-
1
1
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-
-
-
-
-
1
1
1
1
-
-
722117
Zhu
Guanylate kinase domains of th ...
Homo sapiens, Rattus norvegicus
EMBO J.
30
4986-4997
2011
-
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2
2
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-
-
-
2
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2
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2
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2
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2
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2
2
-
-
-
723014
Kandeel
Binding dynamics and energetic ...
Plasmodium falciparum
J. Mol. Recognit.
24
322-332
2011
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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
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700079
Kandeel
Molecular cloning, expression, ...
Plasmodium falciparum
Mol. Biochem. Parasitol.
159
130-133
2008
-
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1
-
4
-
8
11
-
-
-
1
-
2
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2
-
4
-
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-
-
10
1
1
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2
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1
-
-
4
-
-
8
2
11
-
-
-
1
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-
-
-
2
-
4
-
-
-
-
10
1
1
-
-
-
-
-
-
-
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700475
Gardoni
Postsynaptic density-membrane ...
Homo sapiens, Mus musculus, Rattus norvegicus
Neuroscience
158
324-333
2008
-
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1
-
1
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-
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4
-
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4
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3
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3
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6
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5
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1
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1
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1
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4
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4
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3
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6
-
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5
-
1
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-
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-
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-
-
-
-
700950
Gonzalez-Gutierrez
The guanylate kinase domain of ...
Rattus norvegicus
Proc. Natl. Acad. Sci. USA
105
14198-14203
2008
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1
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1
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3
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1
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2
2
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2
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2
2
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672643
Choi
Guanylate kinase, induced fit, ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Biophys. J.
92
1651-1658
2007
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1
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1
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2
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3
-
1
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1
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7
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1
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1
1
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1
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2
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1
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7
-
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675510
Sumita
Synaptic scaffolding molecule ...
Rattus norvegicus
J. Neurochem.
100
154-166
2007
-
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1
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3
-
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1
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2
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5
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1
1
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1
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3
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1
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5
-
-
1
1
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-
-
-
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-
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-
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676138
Reese
The guanylate kinase domain of ...
Rattus norvegicus
Nat. Struct. Mol. Biol.
14
155-163
2007
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1
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1
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1
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1
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700744
Sugimoto
The rice nuclear gene, VIRESCE ...
Oryza sativa
Plant J.
52
512-527
2007
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1
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6
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3
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5
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671155
El Omari
Structure of Staphylococcus au ...
Staphylococcus aureus
Acta Crystallogr. Sect. F
F62
949-953
2006
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1
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2
1
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672440
Hible
Crystal structures of GMP kina ...
Escherichia coli
Biochimie
88
1157-1164
2006
-
1
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1
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1
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2
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3
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2
2
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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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2
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-
-
-
2
2
-
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673847
Willmon
A guanylate kinase/HSV-1 thymi ...
Homo sapiens, Mus musculus
Gene Ther.
13
1309-1312
2006
-
-
-
-
-
-
-
2
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6
-
2
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6
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2
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6
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6
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675894
Abergel
Impact of the excision of an a ...
Rickettsia conorii
Mol. Biol. Evol.
23
2112-2122
2006
-
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-
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2
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1
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7
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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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662657
Hible
Calorimetric and crystallograp ...
Escherichia coli
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Guanylate kinase from Escheric ...
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Hiraga
Nucleoside monophosphokinases ...
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Griffith
The partial purification of de ...
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