Structural bases for N-glycan processing by mannoside phosphorylase.
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Characterization and crystal structure determination of β-1,2-mannobiose phosphorylase from Listeria innocuaStructural insights into the difference in substrate recognition of two mannoside phosphorylases from two GH130 subfamiliesDiversity of phosphorylases in glycoside hydrolase families.Functions, structures, and applications of cellobiose 2-epimerase and glycoside hydrolase family 130 mannoside phosphorylases.Mannoside recognition and degradation by bacteria.Sites for Dynamic Protein-Carbohydrate Interactions of O- and C-Linked Mannosides on the E. coli FimH Adhesin.The GH130 Family of Mannoside Phosphorylases Contains Glycoside Hydrolases That Target β-1,2-Mannosidic Linkages in Candida Mannan.An inverting β-1,2-mannosidase belonging to glycoside hydrolase family 130 fromDyadobacter fermentans
P2860
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P2860
Structural bases for N-glycan processing by mannoside phosphorylase.
description
2015 nî lūn-bûn
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2015年の論文
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2015年論文
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2015年論文
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name
Structural bases for N-glycan processing by mannoside phosphorylase.
@ast
Structural bases for N-glycan processing by mannoside phosphorylase.
@en
type
label
Structural bases for N-glycan processing by mannoside phosphorylase.
@ast
Structural bases for N-glycan processing by mannoside phosphorylase.
@en
prefLabel
Structural bases for N-glycan processing by mannoside phosphorylase.
@ast
Structural bases for N-glycan processing by mannoside phosphorylase.
@en
P2093
P2860
P1476
Structural bases for N-glycan processing by mannoside phosphorylase.
@en
P2093
Gabrielle Potocki-Véronèse
Gianluca Cioci
Lionel Mourey
Pierre Roblin
Simon Ladevèze
P2860
P304
P356
10.1107/S1399004715006604
P50
P577
2015-05-14T00:00:00Z