Exendin-4 (3-39) truncates the extreme N-terminus while preserving the central helical core and C-terminal extension. The fragment is widely used to analyze structural elements necessary for receptor engagement. Researchers compare its behavior with full-length exendin-4 to identify activation motifs. Its sequence supports biophysical, binding, and conformation studies.
3. Cationic cell-penetrating peptides are potent furin inhibitors
5. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs
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