Exo- and endoglycosidases revisited. - Wikidata - thesis-toulmin - TriplyDB

Exo- and endoglycosidases revisited.

Exo- and endoglycosidases revisited.

http://www.wikidata.org/entity/Q38087861

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Endo-β-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells PslG, a self-produced glycosyl hydrolase, triggers biofilm disassembly by disrupting exopolysaccharide matrix Lacto-N-biosidase encoded by a novel gene of Bifidobacterium longum subspecies longum shows unique substrate specificity and requires a designated chaperone for its active expression

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P2860

Exo- and endoglycosidases revisited.

http://www.wikidata.org/entity/Q38087861

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Exo- and endoglycosidases revisited.

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Exo- and endoglycosidases revisited.

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Exo- and endoglycosidases revisited.

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Proceedings of the Japan Academy, Series B

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Exo- and endoglycosidases revisited.

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Akira Kobata

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P2860

Structural and thermodynamic analyses of solute-binding Protein from Bifidobacterium longum specific for core 1 disaccharide and lacto-N-biose I

Endo-beta-N-acetylglucosaminidase acting on carbohydrate moieties of glycoproteins. Purification and properties of the enzyme from Diplococcus pneumoniae

Structural studies of two ovalbumin glycopeptides in relation to the endo-beta-N-acetylglucosaminidase specificity

Primary structure of four human milk octa-, nona-, and undeca-saccharides established by 1H- and 13C-nuclear magnetic resonance spectroscopy

Oligosaccharides of human milk: structural studies of di-and trifucosyl derivatives of lacto-N-octaose and lacto-N-neoctaose

Oligosaccharides of human milk. Structural studies of two new octasaccharides, difucosyl derivatives of para-lacto-N-hexaose and para-lacto-N-neohexaose

The predominance of type I oligosaccharides is a feature specific to human breast milk

Human milk oligosaccharides are resistant to enzymatic hydrolysis in the upper gastrointestinal tract.

A clostridial endo-beta-galactosidase that cleaves both blood group A and B glycotopes: the first member of a new glycoside hydrolase family, GH98.

Novel putative galactose operon involving lacto-N-biose phosphorylase in Bifidobacterium longum.

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97-117

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scholarly article

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10.2183/PJAB.89.97

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3

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89

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2013-01-01T00:00:00Z

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235895454

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23474886

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3647078

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