Results 171 to 180 of about 7,626 (203)
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Journal of Bacteriology, 1974
The specific activity of uridine diphosphate N -acetylglucosamine-4-epimerase increases during spherulation of Physarum polycephalum , a process that involves the synthesis of galactosamine walls. This increase is prevented by the addition of cycloheximide.
W R, Hiatt, H R, Whiteley
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The specific activity of uridine diphosphate N -acetylglucosamine-4-epimerase increases during spherulation of Physarum polycephalum , a process that involves the synthesis of galactosamine walls. This increase is prevented by the addition of cycloheximide.
W R, Hiatt, H R, Whiteley
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Canadian Journal of Microbiology, 1979
Uridine diphosphate N-acetylglucosamine pyrophosphorylase (EC. 2.7.7.23) of Neurospora crassa has been purified approximately 210-fold with dithiothreitol as the stabilizing agent by use of chromatographic techniques. The enzyme preparation appeared to be homogeneous when subjected to electrophoresis.
K, Yamamoto +3 more
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Uridine diphosphate N-acetylglucosamine pyrophosphorylase (EC. 2.7.7.23) of Neurospora crassa has been purified approximately 210-fold with dithiothreitol as the stabilizing agent by use of chromatographic techniques. The enzyme preparation appeared to be homogeneous when subjected to electrophoresis.
K, Yamamoto +3 more
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European Journal of Biochemistry, 1994
Uptake and metabolism of uridine diphosphate N‐acetylglucosamine (UDP‐GlcNAc) by rough‐endoplasmic‐reticulum (rER)‐derived vesicles was studied. Analysis of the molecular species, double‐label experiments, cis‐inhibition and trans‐stimulation experiments revealed that uptake represented entry of intact UDP‐GlcNAc into the microsomal lumen.
X, Bossuyt, N, Blanckaert
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Uptake and metabolism of uridine diphosphate N‐acetylglucosamine (UDP‐GlcNAc) by rough‐endoplasmic‐reticulum (rER)‐derived vesicles was studied. Analysis of the molecular species, double‐label experiments, cis‐inhibition and trans‐stimulation experiments revealed that uptake represented entry of intact UDP‐GlcNAc into the microsomal lumen.
X, Bossuyt, N, Blanckaert
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Journal of Mass Spectrometry, 2005
AbstractUridine 5′‐diphospho‐N‐acetylglucosamine (UDP‐GlcNAc) is the final product of hexosamine biosynthetic pathway (HSP) and the donor substrate for the modification of nucleocytoplasmic proteins at serine and threonine residues with N‐acetylglucosamine (GlcNAc) catalyzed by O‐GlcNAc transferase (OGT).
Hua-Dong, Liu +4 more
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AbstractUridine 5′‐diphospho‐N‐acetylglucosamine (UDP‐GlcNAc) is the final product of hexosamine biosynthetic pathway (HSP) and the donor substrate for the modification of nucleocytoplasmic proteins at serine and threonine residues with N‐acetylglucosamine (GlcNAc) catalyzed by O‐GlcNAc transferase (OGT).
Hua-Dong, Liu +4 more
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Isolation of uridine diphosphate N-acetylglucosamine-6-fucose from hen oviduct
Biochimica et Biophysica Acta, 1962N, TAKAHASHI, S, SUZUKI
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Journal of the American Chemical Society, 1957
J. Solms, D. S. Feingold, W. Z. Hassid
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J. Solms, D. S. Feingold, W. Z. Hassid
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Mechanism of action of uridine diphosphate N-acetylglucosamine 2-epimerase
Biochemistry, 1970Wilmar L. Salo, Hewitt G. Fletcher
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Integrative oncology: Addressing the global challenges of cancer prevention and treatment
Ca-A Cancer Journal for Clinicians, 2022Jun J Mao,, Msce +2 more
exaly
Uridine diphosphate-N-acetylglucosamine-4-epimerase from Bacillus subtilus
Biochimica et Biophysica Acta, 1959openaire +2 more sources