(Q24311415)

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Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain

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Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain (English)

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GOA release 2020-03-11

carbohydrate binding

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GOA release 2020-03-11

Soichi Wakatsuki

6

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author name string

Masamichi Nagae

1

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Nozomu Nishi

2

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Takeomi Murata

3

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Taichi Usui

4

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Takanori Nakamura

5

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Ryuichi Kato

7

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language of work or name

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publication date

February 2009

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19

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2

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112-7

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Purification and characterization of a chitinase from Amycolatopsis orientalis with N-acetyllactosamine-repeating unit releasing activity

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Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding

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Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue

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Processing of X-ray diffraction data collected in oscillation mode

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Binding and cross-linking properties of galectins

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Structural basis for the recognition of carbohydrates by human galectin-7

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Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease

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Enzymatic synthesis of natural and 13C enriched linear poly-N-acetyllactosamines as ligands for galectin-1.

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Human galectin-1 recognition of poly-N-acetyllactosamine and chimeric polysaccharides

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10.1093/GLYCOB/CWN121

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