Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR-Reference-Cited by-同舟云学术

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Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR

Published:2016-02-23 Issue:8 Volume:26 Page:888-903
ISSN:0959-6658
Container-title:Glycobiology
language:en
Short-container-title:Glycobiology

Author:

Ippel Hans,Miller Michelle C,Vértesy Sabine,Zheng Yi,Cañada F Javier,Suylen Dennis,Umemoto Kimiko,Romanò Cecilia,Hackeng Tilman,Tai Guihua,Leffler Hakon,Kopitz Jürgen,André Sabine,Kübler Dieter,Jiménez-Barbero Jesús,Oscarson Stefan,Gabius Hans-Joachim,Mayo Kevin H

Funder

Office of the Vice President for Research

Medical School

College of Biological Sciences

NIH

, NSF

Minnesota Medical Foundation

Kunst and Alice Wallenberg Foundation, Sweden

Verein zur Förderung des biologisch-technologischen Fortschritts in der Medizin e.V. (Heidelberg, Germany)

ITN network GLYCOPHARM

Publisher

Oxford University Press (OUP)

Subject

Biochemistry

Link

http://academic.oup.com/glycob/article-pdf/26/8/888/17488231/cww021.pdf

Reference68 articles.

1. Carbohydrate-binding protein 35. I. Properties of the recombinant polypeptide and the individuality of the domains;Agrwal;J Biol Chem,1993

2. Galectin-3 Precipitates as a Pentamer with Synthetic Multivalent Carbohydrates and Forms Heterogeneous Cross-linked Complexes

3. Thermodynamic binding studies of cell surface carbohydrate epitopes to galectins-1, -3, and -7: Evidence for differential binding specificities

4. Molecular modeling and mutagenesis studies of the N-terminal domains of galectin-3: evidence for participation with the C-terminal carbohydrate recognition domain in oligosaccharide binding

5. Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner

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