H
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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Journal ArticleDOI
Enhancement of bound-state residual dipolar couplings: Conformational analysis of lactose bound to Galectin-3
TL;DR: This work has added a propyl chain to the C terminus of the carbohydrate recognition domain of the protein, Galectin‐3, and report enhanced RDCs that prove consistent with known bound‐ligand geometries for this protein.
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Structure determination of blood group type glycolipids of cat small intestine by mass fragmentography
Michael E. Breimer,Gunnar C. Hansson,Karl-Anders Karlsson,Hakon Leffler,Weston Pimlott,Bo E. Samuelsson +5 more
TL;DR: The present work is an application of a novel technique of mass frag- mentography on a glycolipid mixture from an individ- ual cat small intestine that opens a unique possibility to test the postulated role of cell-surface carbohydrates in differentiation and regulation.
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Galectin-3 type-C self-association on neutrophil surfaces; The carbohydrate recognition domain regulates cell function.
Martina Sundqvist,Amanda Welin,Jonas Elmwall,Veronica Osla,Ulf J. Nilsson,Hakon Leffler,Johan Bylund,Anna Karlsson +7 more
TL;DR: Galectin‐3C enhances galectin'3 binding to neutrophils by nonactivating type‐C self‐association, in parallel to inhibiting neutrophil activation by galectIn‐3 (induced by type‐N self‐Association), which implicates type‐ C self‐ASSociation as a termination system for galect in‐3‐induced cell activation, with the purpose of avoiding oxidant‐dependent tissue damage.
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Arene–Anion Based Arginine-Binding Motif on a Galactose Scaffold: Structure–Activity Relationships of Interactions with Arginine-Rich Galectins
TL;DR: The electron-donating capacity of the 4-substituent of the C3-benzamides correlated positively with the magnitude of the affinity enhancement by the 2O-sulfate and the influence of the O2-anion substituent correlated negatively with the oxygen charge density in case of galectin-1, -3, and -9N.