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show all sequences of 1.14.15.16

The novel purification and biochemical characterization of a reversible CYP24A1:adrenodoxin complex

Hartfield, K.A.; Stout, C.D.; Annalora, A.J.; J. Steroid Biochem. Mol. Biol. 136, 47-53 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene CYP24A1, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha F'IQ
Rattus norvegicus
Engineering
Amino acid exchange
Commentary
Organism
additional information
development of truncated expression constructs for rat DELTA51CYP24A1. Adrenodoxin binding enhances the stability of the enzyme-substrate complex, despite lowering the ligand binding affinity of the free enzyme for calcitriol over 9fold. Truncation of CYP24A1's flexible N-terminus (DELTA51) improves the enzyme's ability to recruit substrate, without altering adrenodoxin's ability to stabilize the ligand-bound form
Rattus norvegicus
S57D
site-directed mutagenesis
Rattus norvegicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
5-cyclohexylpentyl beta-D-maltoside
-
Rattus norvegicus
6-cyclohexylhexyl beta-D-maltoside
-
Rattus norvegicus
7-cyclohexylheptyl beta-D-maltoside
-
Rattus norvegicus
CHAPS
inhibits ligand binding to the CYP24A1:adrenodoxin complex at concentrations well below their reported critical micelle concentration (CMC) values
Rattus norvegicus
Facade-EM
-
Rattus norvegicus
Fos-choline-14
-
Rattus norvegicus
additional information
detergent inhibition properties of the purified enzyme-adrenodoxin cofactor complex bound to calcitriol, overview
Rattus norvegicus
n-dodecyl beta-D-maltoside
-
Rattus norvegicus
nonyl-beta-D-glucoside
-
Rattus norvegicus
octa ethylene glycol monododecyl ether
-
Rattus norvegicus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
x * 55000, about, recombinant His6-tagged enzyme, SDS-PAGE
Rattus norvegicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
calcitriol + 2 reduced adrenodoxin + 2 H+ + O2
Rattus norvegicus
-
calcitetrol + 2 oxidized adrenodoxin + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
gene CYP24A1
-
Purification (Commentary)
Commentary
Organism
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha F'IQ by nickel affinity chromatography and gel filtration, copurification with added recombinant bovine adrenodoxin for enzyme-cofctor complex preparation
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
calcitriol + 2 reduced adrenodoxin + 2 H+ + O2
-
736701
Rattus norvegicus
calcitetrol + 2 oxidized adrenodoxin + H2O
-
-
-
?
calcitriol + 2 reduced adrenodoxin + 2 H+ + O2
recombinant truncated DELTA108 adrenodoxin from Bos taurus is used
736701
Rattus norvegicus
calcitetrol + 2 oxidized adrenodoxin + H2O
-
-
-
?
additional information
detailed analysis of the reversible complex between recombinant truncated enzyme DELT51CYP24A1 and recombinant truncated DELTA108adrenodoxin, kinetics, overview. Adrenodoxin binding enhances the stability of the enzyme-substrate complex, despite lowering the ligand binding affinity of the free enzyme for calcitriol over 9fold
736701
Rattus norvegicus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 55000, about, recombinant His6-tagged enzyme, SDS-PAGE
Rattus norvegicus
Cofactor
Cofactor
Commentary
Organism
Structure
adrenodoxin
-
Rattus norvegicus
heme
-
Rattus norvegicus
NADPH
-
Rattus norvegicus
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.29
-
n-dodecyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
0.29
-
octa ethylene glycol monododecyl ether
pH and temperature not specified in the publication
Rattus norvegicus
0.37
-
Facade-EM
pH and temperature not specified in the publication
Rattus norvegicus
0.95
-
7-cyclohexylheptyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
1.05
-
5-cyclohexylpentyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
1.67
-
Fos-choline-14
pH and temperature not specified in the publication
Rattus norvegicus
1.88
-
6-cyclohexylhexyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
3.65
-
CHAPS
pH and temperature not specified in the publication
Rattus norvegicus
6.9
-
n-dodecyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene CYP24A1, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain DH5alpha F'IQ
Rattus norvegicus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
adrenodoxin
-
Rattus norvegicus
heme
-
Rattus norvegicus
NADPH
-
Rattus norvegicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
development of truncated expression constructs for rat DELTA51CYP24A1. Adrenodoxin binding enhances the stability of the enzyme-substrate complex, despite lowering the ligand binding affinity of the free enzyme for calcitriol over 9fold. Truncation of CYP24A1's flexible N-terminus (DELTA51) improves the enzyme's ability to recruit substrate, without altering adrenodoxin's ability to stabilize the ligand-bound form
Rattus norvegicus
S57D
site-directed mutagenesis
Rattus norvegicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
5-cyclohexylpentyl beta-D-maltoside
-
Rattus norvegicus
6-cyclohexylhexyl beta-D-maltoside
-
Rattus norvegicus
7-cyclohexylheptyl beta-D-maltoside
-
Rattus norvegicus
CHAPS
inhibits ligand binding to the CYP24A1:adrenodoxin complex at concentrations well below their reported critical micelle concentration (CMC) values
Rattus norvegicus
Facade-EM
-
Rattus norvegicus
Fos-choline-14
-
Rattus norvegicus
additional information
detergent inhibition properties of the purified enzyme-adrenodoxin cofactor complex bound to calcitriol, overview
Rattus norvegicus
n-dodecyl beta-D-maltoside
-
Rattus norvegicus
nonyl-beta-D-glucoside
-
Rattus norvegicus
octa ethylene glycol monododecyl ether
-
Rattus norvegicus
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.29
-
n-dodecyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
0.29
-
octa ethylene glycol monododecyl ether
pH and temperature not specified in the publication
Rattus norvegicus
0.37
-
Facade-EM
pH and temperature not specified in the publication
Rattus norvegicus
0.95
-
7-cyclohexylheptyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
1.05
-
5-cyclohexylpentyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
1.67
-
Fos-choline-14
pH and temperature not specified in the publication
Rattus norvegicus
1.88
-
6-cyclohexylhexyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
3.65
-
CHAPS
pH and temperature not specified in the publication
Rattus norvegicus
6.9
-
n-dodecyl beta-D-maltoside
pH and temperature not specified in the publication
Rattus norvegicus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
x * 55000, about, recombinant His6-tagged enzyme, SDS-PAGE
Rattus norvegicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
calcitriol + 2 reduced adrenodoxin + 2 H+ + O2
Rattus norvegicus
-
calcitetrol + 2 oxidized adrenodoxin + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain DH5alpha F'IQ by nickel affinity chromatography and gel filtration, copurification with added recombinant bovine adrenodoxin for enzyme-cofctor complex preparation
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
calcitriol + 2 reduced adrenodoxin + 2 H+ + O2
-
736701
Rattus norvegicus
calcitetrol + 2 oxidized adrenodoxin + H2O
-
-
-
?
calcitriol + 2 reduced adrenodoxin + 2 H+ + O2
recombinant truncated DELTA108 adrenodoxin from Bos taurus is used
736701
Rattus norvegicus
calcitetrol + 2 oxidized adrenodoxin + H2O
-
-
-
?
additional information
detailed analysis of the reversible complex between recombinant truncated enzyme DELT51CYP24A1 and recombinant truncated DELTA108adrenodoxin, kinetics, overview. Adrenodoxin binding enhances the stability of the enzyme-substrate complex, despite lowering the ligand binding affinity of the free enzyme for calcitriol over 9fold
736701
Rattus norvegicus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 55000, about, recombinant His6-tagged enzyme, SDS-PAGE
Rattus norvegicus
Other publictions for EC 1.14.15.16
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)
736557
Mugg
Quantitation of CYP24A1 enzyma ...
Homo sapiens
J. Clin. Endocrinol. Metab.
100
684-688
2015
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-
1
-
11
-
-
2
1
-
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4
-
2
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3
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5
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3
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1
3
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11
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2
1
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4
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3
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5
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1
1
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736056
Ferla
Novel styryl-indoles as small ...
Homo sapiens
Eur. J. Med. Chem.
87
39-51
2014
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1
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17
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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
15
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15
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1
1
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15
17
15
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1
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1
-
1
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1
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736086
Tieu
Kinetic analysis of human CYP2 ...
Homo sapiens, Rattus norvegicus
FEBS J.
281
3280-3296
2014
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-
1
-
1
-
-
1
3
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1
15
-
2
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1
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16
1
1
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1
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6
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1
6
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1
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-
1
3
-
1
15
-
-
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1
-
-
-
-
16
1
1
-
-
-
1
-
-
-
-
2
2
-
-
-
736616
Ferla
Small-molecule inhibitors of 2 ...
Homo sapiens
J. Med. Chem.
57
7702-7715
2014
-
-
-
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1
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1
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1
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-
1
1
-
-
-
724907
Urbschat
Vitamin D hydroxylases CYP2R1, ...
Homo sapiens
Eur. J. Clin. Invest.
43
1282-1290
2013
-
-
-
-
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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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2
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1
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1
1
1
1
-
-
728214
Luo
24-Hydroxylase in cancer: impa ...
Homo sapiens
J. Steroid Biochem. Mol. Biol.
136
252-257
2013
-
1
-
-
-
-
6
-
1
-
-
2
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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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1
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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1
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1
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728215
Hoebaus
Epigenetic regulation of the 1 ...
Homo sapiens
J. Steroid Biochem. Mol. Biol.
136
296-299
2013
-
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1
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5
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5
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1
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1
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736545
Rhieu
Metabolic stability of 3-epi-1 ...
Rattus norvegicus
J. Cell. Biochem.
114
2293-2305
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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12
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2
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2
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1
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11
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1
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12
-
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-
-
-
-
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1
2
2
1
-
-
736701
Hartfield
The novel purification and bio ...
Rattus norvegicus
J. Steroid Biochem. Mol. Biol.
136
47-53
2013
-
-
1
-
2
-
10
-
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-
1
1
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1
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1
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3
1
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3
9
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1
3
-
2
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10
9
-
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1
1
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1
-
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-
-
3
1
-
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-
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726809
Jones
25-Hydroxyvitamin D-24-hydroxy ...
Rattus norvegicus
Arch. Biochem. Biophys.
523
9-18
2012
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2
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1
1
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717838
Kaufmann
Bioengineering anabolic vitami ...
Homo sapiens
J. Biol. Chem.
286
28729-28737
2011
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1
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3
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1
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3
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1
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3
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1
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3
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714178
Zhu
Screening of selective inhibit ...
Homo sapiens
Biochemistry
49
10403-10411
2010
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1
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8
4
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1
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4
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1
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4
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4
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2
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1
2
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8
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4
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1
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1
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4
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4
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4
4
716740
Prosser
Single A326G mutation converts ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
104
12673-12678
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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3
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714302
Masuda
Evidence for the activation of ...
Homo sapiens, Mus musculus
Biochim. Biophys. Acta
1761
221-234
2006
-
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5
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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
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716274
Hamamoto
Structure-function analysis of ...
Homo sapiens, Rattus norvegicus
Mol. Pharmacol.
70
120-128
2006
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1
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10
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9
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4
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5
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7
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2
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1
2
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10
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9
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5
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7
-
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8
8
715091
Sakaki
Metabolism of vitamin D3 by cy ...
Homo sapiens, Rattus norvegicus
Front. Biosci.
10
119-134
2005
-
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2
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6
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2
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2
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C-25 hydroxylation of 1alpha,2 ...
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10
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2
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2
2
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1
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Enzymes involved in the activa ...
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714836
Akeno
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714138
Beckman
Human 25-hydroxyvitamin D3-24- ...
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Biochemistry
35
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Patel
Effect of vitamin D metabolite ...
Rattus norvegicus
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45
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1994
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714835
Tenenhouse
Effect of the X-linked Hyp mut ...
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120
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Danan
Presence of 25-hydroxyvitamin ...
Rattus norvegicus
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1982
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1
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