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Information on EC 2.5.1.6 - methionine adenosyltransferase and Organism(s) Rattus norvegicus and UniProt Accession P13444
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2.5.1.6 methionine adenosyltransferaseSpecify your search results
Word Map
- 2.5.1.6
- monolayers
-
self-assembled
- gold
-
film
- alkanethiols
-
photoelectron
-
infrared
-
fabric
-
electrode
-
electrochemical
-
tunnel
-
voltammetry
-
coverage
-
interfacial
-
ellipsometry
-
impedance
- s-adenosylhomocysteine
-
thiolate
-
silicon
-
photoemission
-
electrochemistry
-
well-ordered
-
photovoltaic
-
wafer
-
large-area
-
transistor
-
transmethylation
-
semiconductor
-
nanoscopic
-
field-effect
-
close-packed
-
stamp
-
photolithography
-
wettabl
-
nanopatterns
-
polycrystalline
-
electroless
-
thin-film
-
chemisorption
- drug development
-
lithography
-
microcontact
-
fermi
-
headgroups
-
wettability
- synthesis
- medicine
-
micropatterned
-
microbalance
-
silane
-
statin-associated
-
transsulfuration
- ferrocene
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
sams, mat2a, methionine adenosyltransferase, mat1a, s-adenosylmethionine synthetase, adomet synthetase, sam synthetase, mat ii, matalpha2, s-adenosyl-l-methionine synthetase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosylmethionine synthetase
-
-
-
-
AdoMet synthetase
-
-
-
-
ATP-methionine adenosyltransferase
-
-
-
-
MAT III
methionine adenosyltransferase
methionine S-adenosyltransferase
-
-
-
-
methionine-activating enzyme
-
-
-
-
S-adenosyl-L-methionine synthetase
-
-
-
-
S-adenosylmethionine synthase
-
-
-
-
S-adenosylmethionine synthetase
-
-
-
-
methionine adenosyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine
mechanism, key role of K182 in the correct positioning of the substrates, and D135 in stabilizing the sulfonium group formed in the product
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
adenosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:L-methionine S-adenosyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY
9012-52-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
3'-deoxy-ATP + L-methionine + H2O
?
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
mechanism
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
the product S-adenosylmethionine is important as a direct metabolic donor of methyl and alpha-amino-n-butyryl groups
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
two reaction steps: S-adenosylmethionine synthesis and tripolyphosphate hydrolysis. Tripolyphosphate hydrolysis is the rate determining reaction
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
MAT activity controls cellular glutathione levels, polyamine synthesis and folate cycling
-
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-methionine + H2O
phosphate + diphosphate + S-adenosyl-L-methionine
-
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
the product S-adenosylmethionine is important as a direct metabolic donor of methyl and alpha-amino-n-butyryl groups
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
two reaction steps: S-adenosylmethionine synthesis and tripolyphosphate hydrolysis. Tripolyphosphate hydrolysis is the rate determining reaction
-
-
?
ATP + L-methionine + H2O
S-adenosyl-L-methionine + phosphate + diphosphate
-
MAT activity controls cellular glutathione levels, polyamine synthesis and folate cycling
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-methionine
30% reduction in total activity is detected at 5 mM L-methionine
ATP
-
ATP and methionine act as a switch between two different MAT III isoforms
carbon tetrachloride
-
depletion of glutathione levels reduces MAT I/III activities in vivo
Cu2+
isozyme subunit MATalpha2 is inhibited by 0.25 mM Cu2+ in the presence or absence of dithiothreitol, strong reduction in MAT2B gene expression induced by Cu2+ (60%), copper effects can only be prevented by buthionine sulfoximine, whereas N-acetylcysteine and neocuproine are ineffective
p-chloromercuribenzoate
-
alpha and beta isoenzymes completely inhibited, gamma isoenzyme slightly inhibited
phosphate
-
individually a weak inhibitor, in combination with diphosphate there is a synergistic inhibitory effect
S-nitrosylated glutathione
-
rapid and dose-dependent loss of enzymatic activity of MAT I/III
tripolyphosphate
-
activation or inhibition, depending on isoenzyme, S-adenosylmethionine and tripolyphosphate concentration
additional information
-
MAT is inactivated after 6 h of incubation in hypoxia (3% O2) in rat hepatocytes, prevented by NG-monomethyl-L-arginine methyl ester. Hepatic MAT s a sensible target for free radicals in vivo
-
bacterial lipopolysaccharide
-
results in the accumulation of nitrites and nitrates in serum and in the inactivation of MAT I/III
-
diphosphate
-
individually a weak inhibitor, in combination with phosphate there is a marked synergistic effect
hydrogen peroxide
-
inactives CHO cells-MAT, prevented by desferoxamine. Time- and dose-dependent inactivation of MAT I/III, activity recovered by addition of glutathione
L-buthionine-(S,R)-sulfoximine
-
inhibits glutathione synthesis and this decreases MAT activity in vivo. Prevented by the administration of glutathione-ethyl ester
L-buthionine-(S,R)-sulfoximine
-
inactivates hepatic MAT, prevented by the administration of glutathione-ethyl ester
L-methionine
-
ATP and methionine act as a switch between two different MAT III isoforms
L-methionine
30% reduction in total activity is detected at 5 mM L-methionine
nitric oxide
-
two MAT III isoforms, one with low tripolyphosphatase activity that is insensitive to NO and another with high tripolyphosphatase activity that is inhibited by NO
S-adenosylmethionine
-
above 0.3 mM inhibits both high-MW and low-MW isoenzymes
S-adenosylmethionine
-
inhibition of rat kidney enzyme and rat liver MAT-II, weak inhibition of rat liver MAT-I
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
tripolyphosphatase activity stimulated by preincubation with ATP and methionine
dithiothreitol
-
required for alpha and beta isoenzymes activity, not required for gamma enzyme
E2F1
present continually in the MAT2A promoter during liver regeneration
-
E2F3
present continually in the MAT2A promoter during liver regeneration
-
E2F4
present continually in the MAT2A promoter during liver regeneration
-
L-methionine
17% increase of activity is observed at 60 mM L-methionine
methionine
-
stimulation of activity demonstrated in vivo. Tripolyphosphatase activity stimulated by preincubation with ATP and methionine
Sp1
binding of Sp1 to the MAT2A promoter is essential for the transcriptional up-regulation of the gene
-
tripolyphosphates
-
activation or inhibition, depending on isoenzyme, S-adenosylmethionine and tripolyphosphate concentration
additional information
-
no effect with ADP and methionine or S-adenosylmethionine
-
Dimethylsulfoxide
-
activates isoform from kidney and isoform MAT-III from liver
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.287
Cu2+
Rattus norvegicus
isozyme subunit MATalpha2, in the absence of dithiothreitol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
different values in refolding and purification process
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
recombinant enzyme, isoform MAT I, tetramer, and MAT III, dimer
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoforms MAT2AandMAT2beta are induced in culture-activated primary hepatic stellate cells and hepatic stellate cells from 10-day bile duct ligated rat livers. Hepatic stellate cell activation leads to a decline in intracellular S-adenosylmethionine and methyhthioadenosine levels, a drop in the S-adenosylmethionine/S-adenosylhomocysteine ratio, and global DNA hypomethylation. The decrease in S-adenosylmethionen levels is associated with lower MATII activity during activation
-
predominant expression of MAT1A, induction of MAT2A during periods of rapid growth and dedifferentiaition
-
predominant expression of MAT1A, induction of MAT2A during periods of rapid growth and dedifferentiation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
isoform MAT I, presence of two partially overlapping areas at the C-terminal end of the protein involved both in cytoplasmic retention and nuclear localization
-
isoform MAT I, in extrahepatic tissues, the protein colocalizes with nuclear matrix markers. Presence of two partially overlapping areas at the C-terminal end of the protein involved both in cytoplasmic retention and nuclear localization. Neither nuclear localization nor matrix binding requires activity. Nuclear accumulation of the active enzyme only correlates with histone H3K27 trimethylation among the epigenetic modifications evaluated
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
MAT2A silencing in primary heaptic stellate cells results in decreased collagen and alpha-smooth muscle actin expression and cell growth and increased apoptosis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). METK1_RAT
397
0
43698
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44300
110000
120000
200000
208000
210000
47000
48000
97000
44300
2 * 44300, analysis of association/dissociation between dimer and tetramer by gel filtration and MALDI-TOF MS
44300
4 * 44300, analysis of association/dissociation between dimer and tetramer by gel filtration and MALDI-TOF MS
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 44300, analysis of association/dissociation between dimer and tetramer by gel filtration and MALDI-TOF MS
tetramer
dimer
tetramer
additional information
-
study of thermal unfolding, implications for structure and oligomerization pathway
tetramer
4 * 44300, analysis of association/dissociation between dimer and tetramer by gel filtration and MALDI-TOF MS
dimer
-
recombinant enzyme is present in two different oligomeric forms that can be separated by hydrophobic chromatography and DMSO elution
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F251D
-
inactive, but displays correct nuclear localization and matrix binding
additional information
-
MAT1A knockout mice, spontaneous steatohepatitis develops by 8 months, hepatocellular carcinoma develops by 18 months
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
significant decrease during the interval from 0-8 hr at 23ºC after decapitation. From here up to 72 hs post-mortem at 4ºC the activity remains at 60% of the initial value
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 50 mM Tris/HCl, pH 7.8, 20% v/v glycerol, 0.2 mM DTT, 0.1 mM EDTA, 10 mM MgCl2, 0.1 M KCl, partially purified liver enzymes stable for at least 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
method that includes DEAE-Sephacel chromatography and phenyl Sepharose CL-4B chromatography
-
method that includes DEAE-Sepharose, phenyl-Sepharose and blue-Sepharose chromatographies and ultrafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dithiothreitol-refolding in the presence or absence of 250 mM CuSO4
dithiothreitol-refolding in the presence or absence of 250 mM CuSO4
refolding by direct dialysis or by dilution after treatment with urea under several conditions
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
animals fed ethanol intragastrically for 9 weeks switch hepatic MAT expression from MAT1A to MAT2A followed by decrease in S-adenosylmethionine levels, hypomethylation of c-myc, increase in c-myc expression and increased DNA strand break accumulation
medicine
-
MAT1A knockout mice, spontaneous steatohepatitis develops by 8 months, hepatocellular carcinoma develops by 18 months
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Geller, A.M.; Kotb, M.Y.S.; Jernigan, H.M.; Kredich, N.M.
Purification and properties of rat lens methionine adenosyltransferase
Exp. Eye Res.
43
997-1008
1986
Rattus norvegicus
Tallan, H.H.; Cohen, P.A.
Methionine adenosyltransferase: kinetic properties of human and rat liver enzymes
Biochem. Med.
16
234-250
1976
Homo sapiens, Rattus norvegicus
Liau, M.C.; Lin, G.W.; Hurlbert, R.B.
Partial purification and characterization of tumor and liver S-adenosylmethionine synthetases
Cancer Res.
37
427-435
1977
Rattus norvegicus
Sullivan, D.M.; Hoffman, J.L.
Fractionation and kinetic properties of rat liver and kidney methionine adenosyltransferase isozymes
Biochemistry
22
1636-1641
1983
Rattus norvegicus
Hoffman, J.L.
Fractionation of methionine adenosyltransferase isozymes (rat liver)
Methods Enzymol.
94
223-228
1983
Rattus norvegicus
Cabrero, C.; Puerta, J.; Alemany, S.
Purification and comparison of two forms of S-adenosyl-L-methionine synthetase from rat liver
Eur. J. Biochem.
170
299-304
1987
Rattus norvegicus
Okada, G.; Teraoka, H.; Tsukada, K.
Multiple species of mammalian S-adenosylmethionine synthetase. Partial purification and characterization
Biochemistry
20
934-940
1981
Rattus norvegicus
Suman, Y.; Shimizu, K.; Tsukada, K.
Isozymes of S-adenosylmethionine synthetase from rat liver: isolation and characterization
J. Biochem.
100
67-75
1986
Rattus norvegicus
Mingorance, J.; Alvarez, L.; Pajares, M.A.; Mato, J.M.
Recombinant rat liver S-adenosyl-L-methionine synthetase tetramers and dimers are in equilibrium
Int. J. Biochem. Cell Biol.
29
485-491
1997
Rattus norvegicus
Avila, M.A.; Corrales, F.J.; Ruiz, F.; Sanchez-Gongora, E.; Mingorance, J.; Carretero, M.V.; Mato, J.M.
Specific interaction of methionine adenosyltransferase with free radicals
Biofactors
8
27-32
1998
Rattus norvegicus
del Pino, M.M.; Corrales, F.J.; Mato, J.M.
Hysteretic behavior of methionine adenosyltransferase III. Methionine switches between two conformations of the enzyme with different specific activity
J. Biol. Chem.
275
23476-23482
2000
Rattus norvegicus
Ekegren, T.; Aquilonius, S.M.; Gomes-Trolin, C.
A comparative study of methionine adenosyltransferase activity and regional distribution in mammalian spinal cord
Biochem. Pharmacol.
60
441-445
2000
Bos taurus, Felis catus, Macaca mulatta, Rattus norvegicus, Sus scrofa
Lopez-Vara, M.C.; Gasset, M.; Pajares, M.A.
Refolding and characterization of rat liver methionine adenosyltransferase from Escherichia coli inclusion bodies
Protein Expr. Purif.
19
219-226
2000
Rattus norvegicus
Corrales, F.J.; Perez-Mato, I.; Sanchez Del Pino, M.M.; Ruiz, F.; Castro, C.; Garcia-Trevijano, E.R.; Latasa, U.; Martinez-Chantar, M.L.; Martinez-Cruz, A.; Avila, M.A.; Mato, J.M.
Regulation of mammalian liver methionine adenosyltransferase
J. Nutr.
132
2377S-2381S
2002
Escherichia coli, Homo sapiens, Rattus norvegicus
Lu, S.C.; Mato, J.M.
Role of methionine adenosyltransferase and S-adenosylmethionine in alcohol-associated liver cancer
Alcohol
35
227-234
2005
Homo sapiens, Rattus norvegicus
Iloro, I.; Chehin, R.; Goni, F.M.; Pajares, M.A.; Arrondo, J.L.
Methionine adenosyltransferase alpha-helix structure unfolds at lower temperatures than beta-sheet: a 2D-IR study
Biophys. J.
86
3951-3958
2004
Rattus norvegicus
Sanchez-Perez, G.F.; Gasset, M.; Calvete, J.J.; Pajares, M.A.
Role of an intrasubunit disulfide in the association state of the cytosolic homo-oligomer methionine adenosyltransferase
J. Biol. Chem.
278
7285-7293
2003
Rattus norvegicus (P13444)
Kim, J.S.; Coon, S.L.; Blackshaw, S.; Cepko, C.L.; Moller, M.; Mukda, S.; Zhao, W.Q.; Charlton, C.G.; Klein, D.C.
Methionine adenosyltransferase:adrenergic-cAMP mechanism regulates a daily rhythm in pineal expression
J. Biol. Chem.
280
677-684
2005
Rattus norvegicus
Gonzalez, B.; Pajares, M.A.; Hermoso, J.A.; Guillerm, D.; Guillerm, G.; Sanz-Aparicio, J.
Crystal structures of methionine adenosyltransferase complexed with substrates and products reveal the methionine-ATP recognition and give insights into the catalytic mechanism
J. Mol. Biol.
331
407-416
2003
Rattus norvegicus (P13444)
Delgado, M.; Perez-Miguelsanz, J.; Garrido, F.; Rodriguez-Tarduchy, G.; Perez-Sala, D.; Pajares, M.A.
Early effects of copper accumulation on methionine metabolism
Cell. Mol. Life Sci.
65
2080-2090
2008
Rattus norvegicus, Rattus norvegicus (P13444), Rattus norvegicus (P18298)
Rodriguez, J.L.; Boukaba, A.; Sandoval, J.; Georgieva, E.I.; Latasa, M.U.; Garcia-Trevijano, E.R.; Serviddio, G.; Nakamura, T.; Avila, M.A.; Sastre, J.; Torres, L.; Mato, J.M.; Lopez-Rodas, G.
Transcription of the MAT2A gene, coding for methionine adenosyltransferase, is up-regulated by E2F and Sp1 at a chromatin level during proliferation of liver cells
Int. J. Biochem. Cell Biol.
39
842-850
2007
Rattus norvegicus (P18298)
Reytor, E.; Perez-Miguelsanz, J.; Alvarez, L.; Perez-Sala, D.; Pajares, M.A.
Conformational signals in the C-terminal domain of methionine adenosyltransferase I/III determine its nucleocytoplasmic distribution
FASEB J.
23
3347-3360
2009
Rattus norvegicus
Ramani, K.; Yang, H.; Kuhlenkamp, J.; Tomasi, L.; Tsukamoto, H.; Mato, J.M.; Lu, S.C.
Changes in the expression of methionine adenosyltransferase genes and S-adenosylmethionine homeostasis during hepatic stellate cell activation
Hepatology
51
986-995
2010
Homo sapiens, Rattus norvegicus
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