Core Viewpoint - The research reveals the atomic structure of pathological human islet amyloid polypeptide (hIAPP) fibrils, providing a significant foundation for understanding the mechanisms of type 2 diabetes (T2D) and developing treatment strategies [7]. Group 1: Research Findings - The study analyzed hIAPP fibrils extracted from pancreatic tissues of three T2D patients using cryo-electron microscopy (cryo-EM) [4]. - The hIAPP fibrils exhibited a uniform morphology, consisting of two symmetrical protofibrils, containing amino acid residues 2-37, and forming an Ω-shaped spatial fold [4]. - Additional electron density observed in pancreatic hIAPP fibrils suggests potential ligand binding, which may significantly impact the pathogenesis of T2D [4][5]. Group 2: Structural Insights - The core findings include the atomic structure of hIAPP fibrils derived from T2D patients [5]. - The hIAPP fibrils display an unprecedented Ω-shaped folding structure with a conserved core region [5]. - Structural similarities were observed between pathological hIAPP fibrils and Aβ fibrils [5].

Core Insights - The article discusses the critical role of thyroid hormone transport to the brain for normal neural development, mediated by the transport proteins MCT8 and OATP1C1 [2][3]. Group 1: Research Findings - A recent study published in the journal Cell by researchers from Baylor College of Medicine and the National Institutes of Health provides structural insights into the transport mechanisms of thyroid hormones via MCT8 and OATP1C1 [4][5]. - The study utilized cryo-electron microscopy to analyze the structures of MCT8 and OATP1C1 in complex with active thyroid hormones T3 and its precursor T4, achieving resolutions of 2.9 Å and 2.3 Å respectively [7]. - Key findings include the high transport specificity of MCT8 for thyroid hormones, the selective transport mechanism of OATP1C1 for thyroxine, and the discovery of a conserved extracellular regulatory site in OATP1C1 that can be allosterically inhibited by E1G [9][11].