Cross interactions between Apolipoprotein E and amyloid proteins in neurodegenerative diseases.

Three common Apolipoprotein E isoforms, ApoE2, ApoE3, and ApoE4, are key regulators of lipid homeostasis, among other functions. Apolipoprotein E can interact with amyloid proteins. The isoforms differ by one or two residues at positions 112 and 158, and possess distinct structural conformations and functions, leading to isoform-specific roles in amyloid-based neurodegenerative diseases.

Repeat Eustachian Tube Balloon Dilation Outcomes in Adults With Chronic Eustachian Tube Dysfunction.

Objective: With increased focus on surgical management of the eustachian tube, clarifying management decisions benefits patients and surgeons. In this study, we examine the value of repeating the balloon dilation of the eustachian tube (BDET) procedure in patients who did not improve after the initial BDET.

Study Design: Level IV retrospective review of 145 BDETs performed on 86 patients between January 1, 2014, and May 1, 2019, identified 10 patients who underwent BDET more than once.

ATP Impedes the Inhibitory Effect of Hsp90 on Aβ Fibrillation.

Heat shock protein 90 (Hsp90) is a molecular chaperone that assists protein folding in an Adenosine triphosphate (ATP)-dependent way. Hsp90 has been reported to interact with Alzheimeŕs disease associated amyloid-β (Aβ) peptides and to suppress toxic oligomer- and fibril formation. However, the mechanism remains largely unclear.

Single-molecule studies of amyloid proteins: from biophysical properties to diagnostic perspectives.

In neurodegenerative diseases, a wide range of amyloid proteins or peptides such as amyloid-beta and α-synuclein fail to keep native functional conformations, followed by misfolding and self-assembling into a diverse array of aggregates. The aggregates further exert toxicity leading to the dysfunction, degeneration and loss of cells in the affected organs. Due to the disordered structure of the amyloid proteins, endogenous molecules, such as lipids, are prone to interact with amyloid proteins at a low concentration and influence amyloid cytotoxicity.