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- W2912668316 abstract "Significance Glycan-lectin recognition is vital to embryogenesis, and progression in common diseases such as cancer and osteoarthritis. However, the rules governing specificity for the functional pairing and postbinding events are not yet understood, even though human lectins have been thoroughly characterized structurally. Herein, we employ protein engineering to produce new types of variants via redesign of modular lectin architecture. Comparative assays with cells (for growth regulation) and surface-programmable nanovesicles (for bridging) revealed qualitative effector/antagonist changes caused by topological switching, using human galectins-1 and -3 as a test case. In addition to identifying galectin-3’s unique chimera-type design as a means to enable functional antagonism between galectins, this approach generates new promising tools for imaging studies on lattices and for innovative therapeutic approaches." @default.
- W2912668316 created "2019-02-21" @default.
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- W2912668316 date "2019-02-04" @default.
- W2912668316 modified "2023-10-18" @default.
- W2912668316 title "Design–functionality relationships for adhesion/growth-regulatory galectins" @default.
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