BRENDA - Enzyme Database
show all sequences of 2.1.1.5

Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase

Szegedi, S.S.; Castro, C.C.; Koutmos, M.; Garrow, T.A.; J. Biol. Chem. 283, 8939-8945 (2008)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
AdoMet
weak inhibitor, at 2 mM: 24% inhibition
Homo sapiens
AdoMet
weak inhibitor, at 2.5 mM: 15% inhibition
Mus musculus
dimethylglycine
at 0.2 mM: 80% inhibition, at 2 mM: 97% inhibition; weak inhibitor, at 2 mM: 11% inhibition
Homo sapiens
dimethylglycine
at 0.25 mM: 64% inhibition, at 2.5 mM: 95% inhibition; weak inhibitor, at 2.5 mM: 19% inhibition
Mus musculus
dimethylsulfonioacetate
at 2 mM: 79% inhibition; weak inhibitor, at 2 mM: 20% inhibition
Homo sapiens
dimethylsulfonioacetate
at 0.25 mM: 29% inhibition, at 2.5 mM: 82% inhibition
Mus musculus
dimethylsulfoniopropionate
weak inhibitor, at 2 mM: 29% inhibition
Homo sapiens
dimethylsulfoniopropionate
weak inhibitor, at 2.5 mM: 11% inhibition; weak inhibitor, at 2.5 mM: 17% inhibition
Mus musculus
methionine
at 2 mM: 60% inhibition; weak inhibitor at 2 mM: 15% inhibition
Homo sapiens
methionine
at 2.5 mM: 38% inhibition; at 2.5 mM: 48% inhibition
Mus musculus
S-(delta-carboxybutyl)-L-homocysteine
at 0.05 mM: 97% inhibition, at 0.5 mM: total inhibition; weak inhibitor, at 0.5 mM: 26% inhibition
Homo sapiens
S-(delta-carboxybutyl)-L-homocysteine
at 0.025 mM: 22% inhibition, at 0.0625 mM: 36% inhibition, at 0.125 mM: 49% inhibition, at 0.5 mM: 81% inhibition; total inhibition
Mus musculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.76
-
S-methyl-L-methionine
-
Mus musculus
0.94
-
S-methyl-L-methionine
-
Homo sapiens
2.2
-
betaine
-
Homo sapiens
3
-
S-methyl-L-methionine
-
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn
BHMT-2 is a zinc metalloenzyme
Homo sapiens
Zn
BHMT-2 is a zinc metalloenzyme
Mus musculus
Zn2+
BHMT is a zinc metalloenzyme
Homo sapiens
Zn2+
BHMT-2 is a zinc metalloenzyme
Mus musculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Mus musculus
-
liver
-
Mus musculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-homocysteine + betaine
-
687808
Mus musculus
L-methionine + dimethylglycine
-
-
-
?
L-homocysteine + betaine
-
687808
Homo sapiens
L-methionine + dimethylglycine
-
-
-
?
L-homocysteine + S-methyl-L-methionine
-
687808
Mus musculus
?
-
-
-
?
L-homocysteine + S-methyl-L-methionine
-
687808
Homo sapiens
?
-
-
-
?
L-homocysteine + S-methyl-L-methionine
BHMT-2 uses S-methylmethionine as a methyl donor for the methylation of homocysteine. Unlike BHMT, BHMT-2 can not use betaine
687808
Homo sapiens
?
-
-
-
?
L-homocysteine + S-methylmethionine
BHMT-2 uses S-methylmethionine as a methyl donor for the methylation of homocysteine. Unlike BHMT, BHMT-2 can not use betaine
687808
Mus musculus
?
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
24
-
S-methyl-L-methionine
-
Homo sapiens
38
-
S-methyl-L-methionine
-
Homo sapiens
88
-
betaine
-
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Mus musculus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
AdoMet
weak inhibitor, at 2 mM: 24% inhibition
Homo sapiens
AdoMet
weak inhibitor, at 2.5 mM: 15% inhibition
Mus musculus
dimethylglycine
at 0.2 mM: 80% inhibition, at 2 mM: 97% inhibition; weak inhibitor, at 2 mM: 11% inhibition
Homo sapiens
dimethylglycine
at 0.25 mM: 64% inhibition, at 2.5 mM: 95% inhibition; weak inhibitor, at 2.5 mM: 19% inhibition
Mus musculus
dimethylsulfonioacetate
at 2 mM: 79% inhibition; weak inhibitor, at 2 mM: 20% inhibition
Homo sapiens
dimethylsulfonioacetate
at 0.25 mM: 29% inhibition, at 2.5 mM: 82% inhibition
Mus musculus
dimethylsulfoniopropionate
weak inhibitor, at 2 mM: 29% inhibition
Homo sapiens
dimethylsulfoniopropionate
weak inhibitor, at 2.5 mM: 11% inhibition; weak inhibitor, at 2.5 mM: 17% inhibition
Mus musculus
methionine
at 2 mM: 60% inhibition; weak inhibitor at 2 mM: 15% inhibition
Homo sapiens
methionine
at 2.5 mM: 38% inhibition; at 2.5 mM: 48% inhibition
Mus musculus
S-(delta-carboxybutyl)-L-homocysteine
at 0.05 mM: 97% inhibition, at 0.5 mM: total inhibition; weak inhibitor, at 0.5 mM: 26% inhibition
Homo sapiens
S-(delta-carboxybutyl)-L-homocysteine
at 0.025 mM: 22% inhibition, at 0.0625 mM: 36% inhibition, at 0.125 mM: 49% inhibition, at 0.5 mM: 81% inhibition; total inhibition
Mus musculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.76
-
S-methyl-L-methionine
-
Mus musculus
0.94
-
S-methyl-L-methionine
-
Homo sapiens
2.2
-
betaine
-
Homo sapiens
3
-
S-methyl-L-methionine
-
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn
BHMT-2 is a zinc metalloenzyme
Homo sapiens
Zn
BHMT-2 is a zinc metalloenzyme
Mus musculus
Zn2+
BHMT is a zinc metalloenzyme
Homo sapiens
Zn2+
BHMT-2 is a zinc metalloenzyme
Mus musculus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Mus musculus
-
liver
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-homocysteine + betaine
-
687808
Mus musculus
L-methionine + dimethylglycine
-
-
-
?
L-homocysteine + betaine
-
687808
Homo sapiens
L-methionine + dimethylglycine
-
-
-
?
L-homocysteine + S-methyl-L-methionine
-
687808
Mus musculus
?
-
-
-
?
L-homocysteine + S-methyl-L-methionine
-
687808
Homo sapiens
?
-
-
-
?
L-homocysteine + S-methyl-L-methionine
BHMT-2 uses S-methylmethionine as a methyl donor for the methylation of homocysteine. Unlike BHMT, BHMT-2 can not use betaine
687808
Homo sapiens
?
-
-
-
?
L-homocysteine + S-methylmethionine
BHMT-2 uses S-methylmethionine as a methyl donor for the methylation of homocysteine. Unlike BHMT, BHMT-2 can not use betaine
687808
Mus musculus
?
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
24
-
S-methyl-L-methionine
-
Homo sapiens
38
-
S-methyl-L-methionine
-
Homo sapiens
88
-
betaine
-
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Mus musculus
Other publictions for EC 2.1.1.5
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)
733821
Zhang
Both the folate cycle and beta ...
Mus musculus
FASEB J.
29
1069-1079
2015
-
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2
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1
1
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-
733463
Ma
Betaine homocysteine methyltra ...
Homo sapiens
Biomarkers
19
578-584
2014
-
1
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-
-
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-
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2
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1
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1
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1
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735230
Mladkova
Specific potassium ion interac ...
Homo sapiens
Proteins
82
2552-2564
2014
-
-
1
1
5
-
-
6
-
1
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2
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5
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2
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6
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1
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1
5
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6
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1
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5
-
2
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-
-
6
-
-
-
-
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4
4
719035
Korinek
Quantification of homocysteine ...
Homo sapiens
Biomed. Chromatogr.
27
111-121
2013
-
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1
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1
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1
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1
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733401
Selicharova
Effects of hyperhomocysteinemi ...
Homo sapiens
Biochim. Biophys. Acta
1834
1596-1606
2013
-
1
-
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-
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2
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1
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1
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1
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733781
Picha
The development of a new class ...
Homo sapiens
Eur. J. Med. Chem.
65
256-275
2013
-
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3
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2
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3
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3
3
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733936
Ganu
Splicing variants of the porci ...
Sus scrofa
Gene
529
228-237
2013
-
-
-
1
-
-
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-
-
-
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5
-
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-
11
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1
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11
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1
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1
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735112
Zhang
Homocysteine homeostasis and b ...
Myotis ricketti
PLoS ONE
8
e85632
2013
-
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4
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4
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4
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1
1
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720040
Lee
Betaine homocysteine methyltra ...
Mus musculus
J. Biol. Chem.
287
33094-33103
2012
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720080
Fridman
Corticoadrenal activity in rat ...
Rattus norvegicus
J. Biosci.
37
115-123
2012
-
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3
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4
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4
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1
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2
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2
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720202
Mladkova
Double-headed sulfur-linked am ...
Homo sapiens
J. Med. Chem.
55
6822-6831
2012
-
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1
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5
-
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1
1
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3
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1
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2
-
1
1
1
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1
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1
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5
1
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1
1
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1
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2
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1
1
1
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733673
Van den Bergh
Betaine homocysteine methyl tr ...
Homo sapiens
Clin. Chim. Acta
413
105-108
2012
-
1
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3
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703877
Liu
An integrative genomic analysi ...
Mus musculus
Genome Res.
20
28-35
2010
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3
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704793
Xu
All-trans-retinoic acid intens ...
Homo sapiens
J. Cell. Biochem.
109
468-477
2010
-
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2
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2
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2
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1
1
1
1
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702044
Kharbanda
Proteomics reveal a concerted ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
381
523-527
2009
-
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3
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1
1
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1
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705038
Vanek
Structure-activity study of ne ...
Homo sapiens
J. Med. Chem.
52
3652-3665
2009
-
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17
-
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-
-
-
2
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-
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1
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5
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5
17
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1
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705295
Ohuchi
Hepatic cystathionine beta-syn ...
Rattus norvegicus
J. Nutr. Sci. Vitaminol.
55
178-185
2009
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2
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1
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1
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1
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705297
Brosnan
Creatine synthesis is a major ...
Sus scrofa
J. Nutr.
139
1292-1297
2009
-
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1
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10
2
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1
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-
10
2
-
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-
-
-
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1
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-
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684264
Ji
Effect of transgenic extrahepa ...
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Alcohol. Clin. Exp. Res.
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2008
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1
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1
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1
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1
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684710
Castro
Liver betaine-homocysteine S-m ...
Homo sapiens, Mus musculus
Arch. Biochem. Biophys.
472
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2008
1
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6
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1
1
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1
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-
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1
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-
1
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-
4
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-
-
-
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-
1
-
-
-
-
6
-
-
1
-
1
-
1
-
-
-
-
-
1
-
1
-
-
4
-
-
-
-
-
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687808
Szegedi
Betaine-homocysteine S-methylt ...
Homo sapiens, Mus musculus
J. Biol. Chem.
283
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2008
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-
2
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-
6
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12
-
4
-
4
-
-
-
-
-
-
-
2
-
-
6
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
689024
Li
Human betaine-homocysteine met ...
Homo sapiens
Mol. Genet. Metab.
94
326-335
2008
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1
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8
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9
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3
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-
-
1
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-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
8
-
-
-
-
9
-
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
701995
Mercer
Macroautophagy-dependent, intr ...
Homo sapiens
Autophagy
4
185-194
2008
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
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-
-
-
-
-
1
1
-
-
-
-
-
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-
1
1
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671242
Schaefer
Osmotic regulation of betaine ...
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Am. J. Physiol. Gastrointest. Liver Physiol.
292
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2007
1
3
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5
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4
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1
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1
3
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-
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3
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4
-
-
1
-
-
-
-
-
-
-
-
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-
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671886
Ou
Inhibition of human betaine-ho ...
Homo sapiens
Biochem. J.
401
87-96
2007
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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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-
-
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-
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-
2
1
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-
1
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-
1
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-
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-
-
1
-
-
-
-
-
-
-
-
-
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-
-
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687005
Ji
Mechanisms of protection by th ...
Homo sapiens
Hepatology
46
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2007
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1
1
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1
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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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-
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-
-
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689005
Ananth
Polymorphisms in methionine sy ...
Homo sapiens
Mol. Genet. Metab.
91
104-110
2007
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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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671232
Ratnam
Effects of diabetes and insuli ...
Rattus norvegicus
Am. J. Physiol. Endocrinol. Metab.
290
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2006
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3
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-
1
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-
2
1
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-
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-
1
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-
3
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-
1
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-
-
-
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-
-
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671233
Nieman
Folate status modulates the in ...
Rattus norvegicus
Am. J. Physiol. Endocrinol. Metab.
291
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2006
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1
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2
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1
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-
1
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-
-
-
-
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-
-
-
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-
-
1
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-
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-
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-
1
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-
1
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671855
Sparks
Hepatic very-low-density lipop ...
Rattus norvegicus
Biochem. J.
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363-371
2006
1
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1
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673003
Pajares
Betaine homocysteine S-methylt ...
Cavia porcellus, Homo sapiens, Macaca mulatta, Mesocricetus auratus, Mus musculus, Mus musculus C57/BL6J, Ovis aries, Rattus norvegicus, Sus scrofa
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13
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2
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5
1
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3
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18
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2
1
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675300
Jiracek
S-alkylated homocysteine deriv ...
Homo sapiens
J. Med. Chem.
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2006
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1
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1
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6
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1
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6
18
1
2
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-
1
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675562
Collinsova
Inhibition of betaine-homocyst ...
Mus musculus
J. Nutr.
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2006
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-
1
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2
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-
1
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-
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-
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675565
Slow
Liver choline dehydrogenase an ...
Rattus norvegicus
J. Nutr.
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2006
3
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4
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676758
Pillai
Homocysteine remethylation in ...
Gallus gallus
Poult. Sci.
85
90-95
2006
2
1
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-
1
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2
1
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1
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1
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657520
Delgado-Reyes
High sodium chloride intake de ...
Sus scrofa
Am. J. Physiol.
288
R182-187
2005
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5
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-
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657874
Garrido
Rat liver betaine homocysteine ...
Rattus norvegicus
Biochem. J.
391
589-599
2005
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1
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2
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1
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2
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657875
Miller
Conformation-dependent inactiv ...
Homo sapiens
Biochem. J.
392
443-448
2005
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-
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2
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-
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1
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657666
Szegedi
Oligomerization is required fo ...
Homo sapiens
Arch. Biochem. Biophys.
426
32-42
2004
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11
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2
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11
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2
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658928
Ichikawa
In vitro modification of betai ...
Sus scrofa
Int. J. Biochem. Cell Biol.
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2004
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1
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-
1
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-
1
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2
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-
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659712
Gonzalez
Crystal structure of rat liver ...
Rattus norvegicus
J. Mol. Biol.
338
771-782
2004
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1
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2
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
1
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-
1
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-
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2
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-
-
-
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-
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657817
Gonzalez
Active-site-mutagenesis study ...
Rattus norvegicus
Biochem. J.
370
945-952
2003
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13
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20
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2
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1
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26
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13
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20
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2
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1
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26
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-
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658186
Forestier
Betaine homocysteine methyltra ...
Rattus norvegicus
Biochim. Biophys. Acta
1638
29-34
2003
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-
1
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2
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1
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-
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-
1
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-
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-
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-
-
1
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-
-
-
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2
-
-
1
-
-
-
-
-
-
-
-
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-
658422
Collinsova
Combining combinatorial chemis ...
Homo sapiens
Chem. Biol.
10
113-122
2003
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7
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1
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7
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-
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-
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-
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1
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-
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441239
Gonzalez
Crystallization and preliminar ...
Rattus norvegicus
Acta Crystallogr. Sect. D
58
1507-1510
2002
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1
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1
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1
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-
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
441248
Bose
Expression of recombinant huma ...
Homo sapiens
Protein Expr. Purif.
25
73-80
2002
-
-
-
-
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-
1
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-
-
1
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3
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1
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-
-
-
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-
-
-
-
-
-
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-
1
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-
1
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-
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-
-
-
-
-
-
1
-
-
-
-
-
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-
441250
Breksa
Random mutagenesis of the zinc ...
Homo sapiens
Arch. Biochem. Biophys.
399
73-80
2002
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1
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4
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-
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-
-
1
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-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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441240
Bose
Crystallization and preliminar ...
Homo sapiens
Acta Crystallogr. Sect. D
57
431-433
2001
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1
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2
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