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Exploring the In situ pairing of human galectins toward synthetic O-mannosylated core M1 glycopeptides of α-dystroglycan.
Sci Rep
October 2022
Frontier Research Center for Advanced Material and Life Science, Graduate School of Life Science and Faculty of Advanced Life Science, Hokkaido University, N21, W11, Sapporo, 001-0021, Japan.
Dystroglycan (DG), which constitutes a part of the dystrophin-glycoprotein complex, connects the extracellular matrix to the cytoskeleton. The matriglycans presented by the extracellular α-DG serve as a contact point with extracellular matrix proteins (ECM) containing laminin G-like domains, providing cellular stability. However, it remains unknown whether core M1 (GlcNAcβ1-2Man) structures can serve as ligands among the various O-Mannosylated glycans.
View Article and Find Full Text PDFThe marriage of chemokines and galectins as functional heterodimers.
Cell Mol Life Sci
December 2021
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota Health Sciences Center, Minneapolis, MN, 55455, USA.
Trafficking of leukocytes and their local activity profile are of pivotal importance for many (patho)physiological processes. Fittingly, microenvironments are complex by nature, with multiple mediators originating from diverse cell types and playing roles in an intimately regulated manner. To dissect aspects of this complexity, effectors are initially identified and structurally characterized, thus prompting familial classification and establishing foci of research activity.
View Article and Find Full Text PDFSimulating cellular galectin networks by mixing galectins in vitro reveals synergistic activity.
Biochem Biophys Rep
December 2021
Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, Minneapolis, MN, 55455, USA.
Background: Even though members of the family of adhesion/growth-regulatory galectins are increasingly detected to be co-expressed, they are still being routinely tested separately. The recent discovery of heterodimer formation among galectins-1, -3, and -7 in mixtures prompts further study of their functional activities in mixtures.
Methods: Cell agglutination, galectin binding to cells, as well as effects on cell proliferation, onset of apoptosis and migration were determined in assays using various cell types and mixtures of galectins-1, -3, and -7.
Imitating evolution's tinkering by protein engineering reveals extension of human galectin-7 activity.
Histochem Cell Biol
September 2021
Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, 80539, Munich, Germany.
Wild-type lectins have distinct types of modular design. As a step to explain the physiological importance of their special status, hypothesis-driven protein engineering is used to generate variants. Concerning adhesion/growth-regulatory galectins, non-covalently associated homodimers are commonly encountered in vertebrates.
View Article and Find Full Text PDFCharacterizing ligand-induced conformational changes in clinically relevant galectin-1 by H/HO (DO) exchange.
Biochimie
August 2021
Institute of Physiological Chemistry, Faculty of Veterinary Medicine, Ludwig-Maximilians-University Munich, Veterinärstr. 13, 80539, Munich, Germany. Electronic address:
Glycans of cellular glycoconjugates serve as biochemical signals for a multitude of (patho)physiological processes via binding to their receptors (e.g. lectins).
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