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uridine diphosphate and n-acetyllactosamine

uridine diphosphate has been researched along with n-acetyllactosamine in 3 studies

Research

Studies (3)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	3 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Dohmae, N; Seko, A; Takio, K; Yamashita, K	1
Ishiguro, M; Kajihara, Y; Kakuda, S; Kato, R; Kawasaki, T; Oka, S; Shiba, T; Tagawa, H; Wakatsuki, S	1
Ishiguro, M; Kakuda, S; Kato, R; Kawasaki, T; Oka, S; Shiba, T; Wakatsuki, S	1

Reviews

1 review(s) available for uridine diphosphate and n-acetyllactosamine

Article	Year
[Molecular mechanisms in acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1]. Seikagaku. The Journal of Japanese Biochemical Society, 2005, Volume: 77, Issue:2 Topics: Amino Sugars; Binding Sites; CD57 Antigens; Glucuronosyltransferase; Humans; Ions; Manganese; Protein Conformation; Substrate Specificity; Uridine Diphosphate	2005

Article

Year

[Molecular mechanisms in acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1].

Seikagaku. The Journal of Japanese Biochemical Society, 2005, Volume: 77, Issue:2

Topics: Amino Sugars; Binding Sites; CD57 Antigens; Glucuronosyltransferase; Humans; Ions; Manganese; Protein Conformation; Substrate Specificity; Uridine Diphosphate

2005

Other Studies

2 other study(ies) available for uridine diphosphate and n-acetyllactosamine

Article	Year
Beta 1,4-galactosyltransferase (beta 4GalT)-IV is specific for GlcNAc 6-O-sulfate. Beta 4GalT-IV acts on keratan sulfate-related glycans and a precursor glycan of 6-sulfosialyl-Lewis X. The Journal of biological chemistry, 2003, Mar-14, Volume: 278, Issue:11 Topics: Acetylglucosamine; Amines; Amino Acid Sequence; Amino Acids; Amino Sugars; Animals; Blotting, Northern; Carbohydrate Sequence; Chromatography; Cloning, Molecular; COS Cells; DNA, Complementary; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Galactosyltransferases; Gene Library; Humans; Keratan Sulfate; Lewis X Antigen; Lipids; Lymph Nodes; Models, Chemical; Molecular Sequence Data; Peptides; Polysaccharides; Protein Binding; Protein Structure, Tertiary; Sepharose; Sphingosine; Swine; Tissue Distribution; Transfection; Uridine Diphosphate	2003
Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1. The Journal of biological chemistry, 2004, May-21, Volume: 279, Issue:21 Topics: Amino Acid Motifs; Amino Acid Sequence; Amino Sugars; Binding Sites; Carbohydrates; Catalysis; CD57 Antigens; Cell Adhesion; Crystallography, X-Ray; Dimerization; Electrons; Epitopes; Escherichia coli; Glucuronosyltransferase; Humans; Manganese; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity; Uridine Diphosphate	2004

Article

Year

Beta 1,4-galactosyltransferase (beta 4GalT)-IV is specific for GlcNAc 6-O-sulfate. Beta 4GalT-IV acts on keratan sulfate-related glycans and a precursor glycan of 6-sulfosialyl-Lewis X.

The Journal of biological chemistry, 2003, Mar-14, Volume: 278, Issue:11

Topics: Acetylglucosamine; Amines; Amino Acid Sequence; Amino Acids; Amino Sugars; Animals; Blotting, Northern; Carbohydrate Sequence; Chromatography; Cloning, Molecular; COS Cells; DNA, Complementary; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Galactosyltransferases; Gene Library; Humans; Keratan Sulfate; Lewis X Antigen; Lipids; Lymph Nodes; Models, Chemical; Molecular Sequence Data; Peptides; Polysaccharides; Protein Binding; Protein Structure, Tertiary; Sepharose; Sphingosine; Swine; Tissue Distribution; Transfection; Uridine Diphosphate

2003

Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1.

The Journal of biological chemistry, 2004, May-21, Volume: 279, Issue:21

Topics: Amino Acid Motifs; Amino Acid Sequence; Amino Sugars; Binding Sites; Carbohydrates; Catalysis; CD57 Antigens; Cell Adhesion; Crystallography, X-Ray; Dimerization; Electrons; Epitopes; Escherichia coli; Glucuronosyltransferase; Humans; Manganese; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity; Uridine Diphosphate

2004