Jean-Pierre Morello

TL;DR: It is demonstrated that β2-adrenergic receptors do form SDS-resistant homodimers and that transmembrane domain VI of the receptor may represent part of an interface for receptor dimerization, which suggests that interconversion between monomeric and dimeric forms may be important for biological activity.

TL;DR: It is shown that by binding to newly synthesized mutant receptors, small ligands can act as pharmacological chaperones, promoting the proper folding and maturation of receptors and their targeting to the cell surface.

TL;DR: The advances described here are examples of "bedside physiology" and provide diagnostic tools for physicians caring for patients with congenital nephrogenic diabetes insipidus and the acquired form of NDI, which is much more common than the congenital form, and is associated with downregulation of AQP2.

TL;DR: It is demonstrated that membrane‐permeable opioid ligands facilitate maturation and ER export of the receptor, thus acting as pharmacological chaperones, and proposed that these ligands stabilize the newly synthesized receptor in the native or intermediate state of its folding pathway.

TL;DR: The discovery that ligands with pharmacological selectivity (pharmacological chaperones) can rescue the proper targeting and function of misfolded proteins, including receptors, might help to develop new treatments for 'conformational diseases'.