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Although studies determining the structure of GLP-1 bound to the N-terminal, extracellular domain of the receptor showed that the residues 13-33 of the GLP-1 peptide analogs form a helical structure (PDB ID 3iol, Underwood et al., 2010), recent EM structures of the whole receptor bound to the GLP-1 protein (PDB ID 6x18, Zhang et al., 2020) shows that the entire GLP-1 peptide forms a long helix as it binds to its receptor

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Key point: There is nothing GLP-1-specific about how creatine works

The clinical trial data behind the projections The projections for each medication are based on the landmark registration trials published in the New England Journal of Medicine