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

Author:

Berbís M. Álvaro,André Sabine,Cañada F. Javier,Pipkorn Rüdiger,Ippel Hans,Mayo Kevin H.,Kübler DieterORCID,Gabius Hans-Joachim,Jiménez-Barbero Jesús

Funder

MINECO

Comunidad de Madrid

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference29 articles.

1. Dynamics of galectin-3 in the nucleus and cytoplasm;Haudek;Biochim. Biophys. Acta,1800

2. From lectin structure to functional glycomics: principles of the sugar code;Gabius;Trends Biochem. Sci.,2011

3. Context-dependent multifunctionality of galectin-1: a challenge for defining the lectin as therapeutic target;Smetana;Expert Opin. Ther. Targets,2013

4. Galectins: a family of animal lectins that decipher glycocodes;Kasai;J. Biochem.,1996

5. Galectinomics: finding themes in complexity;Cooper;Biochim. Biophys. Acta,2002

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