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Hakon Leffler

Researcher at Lund University

Publications -  296
Citations -  22579

Hakon Leffler is an academic researcher from Lund University. The author has contributed to research in topics: Galectin & Receptor. The author has an hindex of 80, co-authored 281 publications receiving 20756 citations. Previous affiliations of Hakon Leffler include University of Waterloo & University of Edinburgh.

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Arginine binding motifs: design and synthesis of galactose-derived arginine tweezers as galectin-3 inhibitors.

TL;DR: Modeling revealed arginine-144 being pinched by the C3 benzamide and O2 anionic substituents in that the benzamide stacked face-to-face and the anionic O2 substituent ion-paired with the guanidinium moiety.
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Galectin-1-Binding Glycoforms of Haptoglobin with Altered Intracellular Trafficking, and Increase in Metastatic Breast Cancer Patients

TL;DR: Galectin-1 detects a new type of functional biomarker for cancer: a specific type of glycoform of haptoglobin, and possibly other serum glycoproteins, with a different function after uptake into tissue cells as discussed by the authors.
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Low or No Inhibitory Potency of the Canonical Galectin Carbohydrate-binding Site by Pectins and Galactomannans *

TL;DR: The physiological effects of these plant polysaccharides are not due to inhibition of the canonical galectin carbohydrate-binding site, as suggested by a well established fluorescence anisotropy assay.

The Anti-angiogenic Peptide Anginex Greatly Enhances Galectin-1 Binding Affinity for

TL;DR: Galectin-1, a β-galactoside binding lectin, is up-regulated in the endothelium of tumors of different origin and has been shown to be the target for anginex, a powerful anti-angiogenic peptide with anti-tumor activity.
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Protein identification by in-gel digestion, high-performance liquid chromatography, and mass spectrometry: peptide analysis by complementary ionization techniques.

TL;DR: The resolution afforded by the QqTOF instrument permitted charge state determination for the fragment ions while preserving the high detection sensitivity that was essential in obtaining the composition of this mixture of proteins.