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Information on EC 2.4.1.38 - beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase and Organism(s) Rattus norvegicus and UniProt Accession P80225
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EC Tree
2.4.1.38 beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferaseIUBMB Comments
Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by beta-1,6-links to galactose residues; lower activity towards residues linked to galactose by beta-1,3-links. A component of EC 2.4.1.22 (lactose synthase).
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Word Map
- 2.4.1.38
-
galts
-
galactosylate
- synthesis
- alpha-lactalbumin
-
p34cdc2-related
- beta4galts
- drug development
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
beta1,4gt1, beta1,4-gt 1, beta4galt-ii, galt v, beta1,4-galactosyltransferase 1, galti, galnact2, 4betagalt, betagalt, beta4-galt-ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyllactosamine synthetase
-
-
-
-
beta-1,4-galactosyltransferase
-
-
-
-
beta-N-acetyl-beta1-4-galactosyltransferase
-
-
-
-
beta-N-acetylglucosaminide beta1-4-galactosyltransferase
-
-
-
-
beta1,4-GT
-
-
-
-
beta1-4-galactosyltransferase
-
-
-
-
beta1-4GalT
-
-
-
-
Gal-T
-
-
-
-
galactosyltransferase, uridine diphosphogalactose-acetylglucosamine
-
-
-
-
GalTase
glycoprotein 4-beta-galactosyl-transferase
-
-
-
-
glycoprotein beta-galactosyltransferase
-
-
-
-
lactosamine synthase
-
-
-
-
lactosamine synthetase
-
-
-
-
lactose synthetase A protein
-
-
-
-
N-acetyllactosamine synthetase
-
-
-
-
NAL synthetase
-
-
-
-
thyroid galactosyltransferase
-
-
-
-
thyroid glycoprotein beta-galactosyltransferase
-
-
-
-
UDP-beta-1,4-galactosyltransferase
-
-
-
-
UDP-Gal:N-acetylglucosamine beta1-4-galactosyltransferase
-
-
-
-
UDP-galactose N-acetylglucosamine beta-4-galactosyltransferase
-
-
-
-
UDP-galactose-acetylglucosamine galactosyltransferase
-
-
-
-
UDP-galactose-N-acetylglucosamine beta-1,4-galactosyltransferase
-
-
-
-
UDP-galactose-N-acetylglucosamine galactosyltransferase
-
-
-
-
UDP-galactose:N-acetylglucosaminide beta1-4-galactosyltransferase
-
-
-
-
UDPgalactose-glycoprotein galactosyltransferase
-
-
-
-
UDPgalactose-N-acetylglucosamine beta-D-galactosyltransferase
-
-
-
-
UDPgalactose:N-acetyl-beta-D-glucosaminylglycopeptide beta-1,4-galactosyltransferase
-
-
-
-
UDPgalactose:N-acetylglucosaminyl(beta1-4)galactosyltransferase
-
-
-
-
uridine diphosphogalactose-acetylglucosamine galactosyltransferase
-
-
-
-
uridine diphosphogalactose-glycoprotein galactosyltransferase
-
-
-
-
additional information
GalTase
-
-
-
-
additional information
the enzyme belongs to the family of beta-1,4-galactosyltransferases, beta-1,4-GalTs
additional information
-
the enzyme belongs to the family of beta-1,4-galactosyltransferases, beta-1,4-GalTs
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:N-acetyl-beta-D-glucosaminylglycopeptide 4-beta-galactosyltransferase
Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. High activity is shown towards such residues in branched-chain polysaccharides when these are linked by beta-1,6-links to galactose residues; lower activity towards residues linked to galactose by beta-1,3-links. A component of EC 2.4.1.22 (lactose synthase).
CAS REGISTRY NUMBER
COMMENTARY
37237-43-7
-
9054-94-8
-
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
UDP-alpha-D-galactose + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
?
-
-
-
-
?
UDP-alpha-D-galactose + N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
?
-
-
-
-
?
UDPgalactose + degalactosylated fetuin
UDP + fetuin containing beta-1,4-galactose linkages
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
UDPgalactose + N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
UDP + galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
-
-
galactose is transferred much faster to the N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-branch than to the N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-branch
?
UDPgalactose + ovomucoid
UDP + ovomucoid with beta-1,4-bound galactose
-
-
-
?
UDPgalactose + glucose
lactose + UDP
-
in presence of alpha-lactalbumin
-
?
UDPgalactose + glucose
lactose + UDP
-
in presence of alpha-lactalbumin
-
?
UDPgalactose + glucose
lactose + UDP
-
in presence of alpha-lactalbumin
-
?
UDPgalactose + N-acetylglucosamine
UDP + N-acetyllactosamine
-
-
-
-
?
UDPgalactose + N-acetylglucosamine
UDP + N-acetyllactosamine
-
-
-
?
UDPgalactose + N-acetylglucosamine
UDP + N-acetyllactosamine
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
the soluble enzyme form from the luminal fluid of the epididymis is suggested to play a role on sperm maturation
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
the enzyme may be involved in the synthesis of plasma glycoproteins by the liver during secretion, and may possibly be required for secretion of these proteins
-
-
?
additional information
?
-
-
beta-1,4-GalT I is a type II membrane-bound glycoprotein, which occurs the plasma membrane of different types of cells where it serves as a cell surface adhesion molecule mediating various cell-cell and cell-matrix interactions such as sperm-egg binding, cell spreading, migration, and neurite outgrowth
-
-
?
additional information
?
-
beta-1,4-GalT I is a type II membrane-bound glycoprotein, which occurs the plasma membrane of different types of cells where it serves as a cell surface adhesion molecule mediating various cell-cell and cell-matrix interactions such as sperm-egg binding, cell spreading, migration, and neurite outgrowth
-
-
?
additional information
?
-
-
beta-1,4-GalT-I plays a key role in the synthesis of selectin ligands such as sialy Lewis, sLex, and sulfated sLex, overview. beta-1,4-GalT-I may play an important role in the inflammation reaction
-
-
?
additional information
?
-
-
beta-1,4-GalT-I transfers galactose from UDP-galactose donors to terminal N-acetylglucosamine of carbohydrate chains in beta-1,4-linkage to form a Galbeta1->4GlcNAc structure
-
-
?
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
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
-
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
the soluble enzyme form from the luminal fluid of the epididymis is suggested to play a role on sperm maturation
-
-
?
UDPgalactose + N-acetylglucosaminyl at the non-reducing ends of protein-bound oligosaccharides
?
-
the enzyme may be involved in the synthesis of plasma glycoproteins by the liver during secretion, and may possibly be required for secretion of these proteins
-
-
?
additional information
?
-
-
beta-1,4-GalT I is a type II membrane-bound glycoprotein, which occurs the plasma membrane of different types of cells where it serves as a cell surface adhesion molecule mediating various cell-cell and cell-matrix interactions such as sperm-egg binding, cell spreading, migration, and neurite outgrowth
-
-
?
additional information
?
-
beta-1,4-GalT I is a type II membrane-bound glycoprotein, which occurs the plasma membrane of different types of cells where it serves as a cell surface adhesion molecule mediating various cell-cell and cell-matrix interactions such as sperm-egg binding, cell spreading, migration, and neurite outgrowth
-
-
?
additional information
?
-
-
beta-1,4-GalT-I plays a key role in the synthesis of selectin ligands such as sialy Lewis, sLex, and sulfated sLex, overview. beta-1,4-GalT-I may play an important role in the inflammation reaction
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-lactalbumin
-
inhibits reaction with UDPgalactose and N-acetylglucosamine
-
additional information
-
TNF-alpha and its receptors affect the expression of beta-1,4 galactosyltransferase I mRNA by rat primary astrocytes, downregulation of beta-1,4-GalT I mRNA expression by TNF-alpha stimulation, overview
-
additional information
TNF-alpha and its receptors affect the expression of beta-1,4 galactosyltransferase I mRNA by rat primary astrocytes, downregulation of beta-1,4-GalT I mRNA expression by TNF-alpha stimulation, overview
-
additional information
-
bis(oxalate)oxovanadium(IV), bis(maltolato)oxovanadium(IV), bis(kojato)oxovanadium(IV) and bis(2,2'-bipyridine)oxovanadium(IV) act as anti-diabetic drugs affecting the Golgi complex morphology and the enzyme activity, overview
-
additional information
-
TNF-alpha and its receptors affect the expression of beta-1,4 galactosyltransferase V mRNA by rat primary astrocytes, overview
-
additional information
TNF-alpha and its receptors affect the expression of beta-1,4 galactosyltransferase V mRNA by rat primary astrocytes, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha-lactalbumin
-
stimulates transfer of galactose from UDPgalactose to N-acetylgalactosamine
-
additional information
-
lipopolysaccharide stimulation of astrocytes induces the enzyme expression, overview
-
additional information
lipopolysaccharide stimulation of astrocytes induces the enzyme expression, overview
-
additional information
-
intraperitoneal administration of lipopolysaccharide, a potent inducer of systemic inflammation, strongly induces beta-1,4-GalT-I mRNA expression in the lung, heart, liver, spleen, kidney, lymph node, hippocampus, and testis, as well as in the cerebral cortex. In the rat lung, liver and testis, LPS stimulation of beta-1,4-GalT-I mRNA expression is time-dependent and biphasic
-
additional information
-
lipopolysaccharide stimulation of astrocytes induces the enzyme expression, overview
-
additional information
lipopolysaccharide stimulation of astrocytes induces the enzyme expression, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.28
galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
-
-
0.43
N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(galactosyl-beta-1,4-N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
-
-
0.13
N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,6-(N-acetylglucosaminyl-beta-1,2-mannosyl-alpha-1,3-)mannosyl-beta-1,4-N-acetylglucosaminyl-beta-1,4-(fucosyl-alpha-1,6-)N-acetylglucosaminyl-asparagine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
very high enzyme concentration in Golgi apparatus of epididymal duct epithelium from initial segment to intermediate caput, although much lower amounts of enzyme are in efferent ducts, distal caput, corpus and cauda. Even in the initial segment and caput epididymis, only low levels of soluble enzyme form are detected in the fluid
-
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
beta-1,4-GalT I is a type II membrane-bound glycoprotein which occurs on the plasma membrane of different types of cells where it serves as a cell surface adhesion molecule
-
-
-
the enzyme from kidney appears to be an intrinsic membrane protein
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
knockdown of beta-1,4-GalT-I reduces the activation potentiation caused by the overexpression of CDK11p58, illustrating the function of CDK11p58 to promote astrocyte activation depends on beta-1,4-GalT-I
malfunction
-
overexpression of beta-1,4-GalT-I represses Schwann cell proliferation induced by low concentration of TNF-alpha via ERK1/2 signal pathway and TNFR2, while knocking down beta-1,4-GalT I expression inhibits Schwann cell apoptosis induced by high concentration of TNF-alpha via P38, JNK signal pathways, and TNFR1
malfunction
-
silencing of beta-1,4-GalT I suppresses TNF-alpha autocrine, while overexpression of beta-1,4-GalT I promotes TNF-alpha autocrine in TNF-alpha-treated Schwann cells
physiological function
-
beta-1,4-GalT-I may play an important role in adhesion and migration of Schwann cells during inflammation
physiological function
-
beta-1,4-GalT I plays a positive role in the regulation of TNF-alpha-induced TNF-alpha secretion. It promotes the activation of ERK, JNK, and P38 MAP kinase signal pathways which subsequently enhance TNF-alpha secretion in TNF-alpha-treated Schwann cells
physiological function
-
beta-1,4-GalT I plays an important role in Schwann cell proliferation and apoptosis induced by TNF-alpha via different signal pathways and TNF-alpha receptor
physiological function
-
beta1,4-GalT-I plays an important role in the inflammation process of rheumatoid arthritis synovial tissue
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). B4GT1_RAT
32
0
3137
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, partially purified enzyme stable for several weeks, purified enzyme stable for 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
anti-TNFR1 antibody suppresses the expression of beta-1,4-GalT I, and TNF-alpha autocrine
-
beta-1,4-GalT-I mRNA is significant increased 2 h after lipopolysaccharide stimulation with 0.001 mg/ml
-
CDK11p58 and beta-1,4-GalT-I are induced in lipopolysaccharide-challenged rat primary astrocytes in a affinis dose- and time-dependent manner. CDK11p58 regulates the expression of beta-1,4-GalT-I by interacting with it. The expression of beta-1,4-GalT-I increases, and astrocyte activation enhances due to the overexpression of CDK11p58
-
mRNA and protein expression of beta1,4-GalT-I increases in synovial tissue of a collagen-induced rat model of rheumatoid arthritis compared with the normal group at 10d and 15d after collagen-induced
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Paquet, M.R.; Moscarello, M.A.
A kinetic comparison of partially purified rat liver Golgi and rat serum galactosyltransferases
Biochem. J.
218
745-751
1984
Bos taurus, Rattus norvegicus
Schachter, H.; Jabbal, I.; Hudgin, R.L.; Pinteric, L.
Intracellular localization of liver sugar nucleotide glycoprotein glycosyltransferases in a Golgi-rich fraction
J. Biol. Chem.
245
1090-1100
1970
Rattus norvegicus
Deshmukh, D.S.; Bear, W.D.; Soifer, D.
Isolation and characterization of an enriched Golgi fraction from rat brain
Biochim. Biophys. Acta
542
284-295
1978
Rattus norvegicus
Kawano, J.i.; Oinuma, T.; Nakayama, T.; Suganuma, T.
Characterization of beta 1->4 galactosyltransferase purified from rat liver microsomes
J. Biochem.
111
568-572
1992
Rattus norvegicus
Bendiak, B.; Ward, L.D.; Simpson, R.J.
Proteins of the Golgi apparatus. Purification to homogeneity, N-terminal sequence, and unusually large Stokes radius of the membrane-bound form of UDP-galactose:N-acetylglucosamine beta 1-4galactosyltransferase from rat liver
Eur. J. Biochem.
216
405-417
1993
Rattus norvegicus
Weiser, M.M.; Majumdar, S.; Wilson, J.R.; Luther, R.
Distribution, purification and characterization of rat intestinal UDPgalactose: N-acetylglucosaminyl(beta 1->4)galactosyltransferase
Biochim. Biophys. Acta
924
323-331
1987
Rattus norvegicus
Clark, P.E.; Moscarello, M.A.
The modulating effects of lipids on purified rat liver Golgi galactosyltransferase
Biochim. Biophys. Acta
859
143-150
1986
Rattus norvegicus
Paquet, M.R.; Narasimhan, S.; Schachter, H.; Moscarello, M.A.
Branch specificity of purified rat liver Golgi UDP-galactose: N-acetylglucosamine beta-1,4-galactosyltransferase. Preferential transfer of of galactose on the GlcNAc beta 1,2-Man alpha 1,3-branch of a complex biantennary Asn-linked oligosaccharide
J. Biol. Chem.
259
4716-4721
1984
Rattus norvegicus
Fraser, I.H.; Wadden, P.; Mookerjea, S.
Purification and stabilization of galactosyltransferase from serum and lysolecithin extracted microsomes
Can. J. Biochem.
58
878-884
1980
Rattus norvegicus
Fleischer, B.; Smigel, M.
Solubilization and properties of galactosyltransferase and sulfotransferase activities of Golgi membranes in Triton X-100
J. Biol. Chem.
253
1632-1638
1978
Rattus norvegicus
Fraser, I.H.; Mookerjea, S.
Purification of membrane-bound galactosyltransferase from rat liver microsomal fractions
Biochem. J.
164
541-547
1977
Rattus norvegicus
Nelson, J.D.; Jato-Rodriguez, J.J.; Mookerjea, S.
The occurrence and properties of soluble UDP-galactose:glycoprotein galactosyltransferase in human amniotic fluid
Can. J. Biochem.
52
42-50
1974
Homo sapiens, Rattus norvegicus
Wagner, R.R.; Cynkin, M.A.
Glycoprotein metabolism: a UDP-galactose-glycoprotein galactosyltransferase of rat serum
Biochem. Biophys. Res. Commun.
45
57-62
1971
Rattus norvegicus
Fraser, I.H.; Mookerjea, S.
Studies on the purification and properties of UDP-galactose glycoprotein galactosyltransferase from rat liver and serum
Biochem. J.
156
347-355
1976
Rattus norvegicus
Kawano, J.I.; Ide, S.; Oinuma, T.; Suganuma, T.
Regional distribution of beta1-4 galactosyltransferase in rat epididymis
Acta Histochem. Cytochem.
30
491-495
1997
Rattus norvegicus
-
Dabros, W.; Kordowiak, A.
Comparison of bipyridyl, maltol and kojic acid action as organic vanadium ligands on activity of galactosyltransferase (EC 2.4.1.38), some physiological parameters and ultrastructure of Golgi complexes in rat hepatocytes
Folia Histochem. Cytobiol.
45
239-244
2007
Rattus norvegicus
Qian, J.; Cheng, C.; Liu, H.; Chen, J.; Yan, M.; Niu, S.; Qin, J.; Sun, L.; Liu, L.; Gu, J.; Shen, A.
Expression of beta-1,4-galactosyltransferase-I in rat during inflammation
Inflammation
30
59-68
2007
Rattus norvegicus
Yan, M.; Xia, C.; Niu, S.; Shao, X.; Cheng, C.; Zhao, J.; Shen, A.
The role of TNF-alpha and its receptors in the production of beta-1,4 galactosyltransferase I and V mRNAs by rat primary astrocytes
J. Mol. Neurosci.
33
155-162
2007
Rattus norvegicus, Rattus norvegicus (P80225)
Yang, H.; Hu, L.; Chen, J.; Zhu, J.; Tao, T.; Zhang, F.; Li, X.; He, X.; Shen, A.; Cheng, C.
Lipopolysaccharide induced upregulation of beta-1,4-galactosyltransferase-I in Schwann cell
Inflammation
32
279-286
2009
Rattus norvegicus
Wang, H.; Xu, D.; Tao, R.; Ni, X.; Shen, A.; Wang, Y.
Beta-1,4-galactosyltransferase-I in synovial tissue of collagen-induced rat model of rheumatoid arthritis
Clin. Exp. Med.
11
147-154
2011
Rattus norvegicus
Liu, X.; Cheng, C.; Shao, B.; Wu, X.; Ji, Y.; Lu, X.; Shen, A.
The functional interaction between CDK11p58 and beta-1,4-galactosyltransferase I involved in astrocyte activation caused by lipopolysaccharide
Inflammation
35
1365-1377
2012
Rattus norvegicus
Yang, H.; Yuan, Q.; Chen, Q.; Li, C.; Wu, X.; Peng, C.; Kang, L.; Lu, X.; Sun, H.; Zhou, Z.; Shen, A.; Cheng, C.
beta-1,4-galactosyltransferase I promotes tumor necrosis factor-alpha autocrine via the activation of MAP kinase signal pathways in Schwann cells
J. Mol. Neurosci.
45
269-276
2011
Rattus norvegicus
Yuan, Q.; Yang, H.; Cheng, C.; Li, C.; Wu, X.; Huan, W.; Sun, H.; Zhou, Z.; Wang, Y.; Zhao, Y.; Lu, X.; Shen, A.
beta-1,4-Galactosyltransferase I involved in Schwann cells proliferation and apoptosis induced by tumor necrosis factor-alpha via the activation of MAP kinases signal pathways
Mol. Cell. Biochem.
365
149-158
2012
Rattus norvegicus
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