Original paper
Galectin-3 N-terminal tail prolines modulate cell activity and glycan-mediated oligomerization/phase separation
Abstract
Galectin-3 (Gal-3) has a long, aperiodic, and dynamic proline-rich N-terminal tail (NT). The functional role of the NT with its numerous prolines has remained enigmatic since its discovery. To provide some resolution to this puzzle, we individually mutated all 14 NT prolines over the first 68 residues and assessed their effects on various Gal-3-mediated functions. Our findings show that mutation of any single proline (especially P37A, P55A,...
Paper Details
Title
Galectin-3 N-terminal tail prolines modulate cell activity and glycan-mediated oligomerization/phase separation
Published Date
May 5, 2021
Volume
118
Issue
19
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Notes
History