Results 71 to 80 of about 20,996 (256)
Self-assembling dipeptide antibacterial nanostructures with membrane disrupting activity. [PDF]
, 2017 Peptide-based supramolecular assemblies are a promising class of nanomaterials with important biomedical applications, specifically in drug delivery and tissue regeneration.
Adler-Abramovich, Lihi +10 more
core +3 more sources
Membrane-mediated amyloid deposition of human islet amyloid polypeptide [PDF]
Biophysical Reviews, 2017 Amyloid deposition of human islet amyloid polypeptide (hIAPP) within the islet of Langerhans is closely associated with type II diabetes mellitus. Accumulating evidence indicates that the membrane-mediated aggregation and subsequent deposition of hIAPP are linked to the dysfunction and death of insulin-producing pancreatic β-cells, but the molecular ...
openaire +2 more sources
The Journal of Physiology, EarlyView.Abstract figure legend Overview of multiscale cardiac remodelling in type 2 diabetes and how to model and simulate these changes using a human‐based, multiscale computational framework. Cardiac remodelling in type 2 diabetes occurs at ionic channel, protein, cellular, tissue and whole‐organ level, affecting the electrophysiological function, mechanical
Ambre Bertrand +2 more
wiley +1 more source
Journal of Diabetes Research, 2016 Human islet amyloid polypeptide (hIAPP) is the major component of the amyloid deposits found in the pancreatic islets of patients with type 2 diabetes mellitus (T2DM).
Lucie Caillon +3 more
doaj +1 more source
Biochemistry and Biophysics Reports, 2021 Islet amyloid polypeptide (IAPP) is a neuroendocrine hormone from pancreatic β-cells. Misfolded, aggregated IAPP is believed to be toxic to islet cells and amyloid deposits in the pancreas are pathological hallmarks of type 2 diabetes.
Madison Q. Ferguson, Maria C. DeRosa
doaj +1 more source
Amylin in the periphery II: An updated mini-review [PDF]
, 2006 Amylin is a polypeptide that is cosecreted with insulin from the beta cells of the pancreas. Therefore, in states of diabetes in which the beta-cell mass is largely depleted or dysfunctional, insulin and amylin secretion are also lost or dysregulated ...
Andrikopoulos, S +2 more
core +1 more source
Amyloid Formation in Heterogeneous Environments: Islet Amyloid Polypeptide Glycosaminoglycan Interactions [PDF]
Journal of Molecular Biology, 2013 Amyloid formation plays an important role in a broad range of diseases, and the search for amyloid inhibitors is an active area of research. Amyloid formation takes places in a heterogeneous environment in vivo with the potential for interactions with membranes and with components of the extracellular matrix.
Wang, Hui, Cao, Ping, Raleigh, Daniel P
openaire +5 more sources
Comprehensive Physiology, Volume 16, Issue 2, April 2026.Vagus nerve stimulation (VNS) effects span central and peripheral organ systems through diverse mechanistic pathways. This comprehensive review provides a unified synthesis of these mechanisms across neurological, cardiovascular, immunological, metabolic, and gastrointestinal domains, filling a critical gap and serving as a foundational resource for ...
Yifeng Bu +11 more
wiley +1 more source
Nature Communications, 2018 Toxic gain-of-function by islet amyloid polypeptide (IAPP) is thought to be mediated by membrane poration. Here the authors develop diluted-FRET to show that changes in pore structure correlate with onset of toxicity inside insulin secreting cells.
Melissa Birol +3 more
doaj +1 more source
β-Hairpin Peptide Mimics Decrease Human Islet Amyloid Polypeptide (hIAPP) Aggregation
Frontiers in Cell and Developmental Biology, 2021 Amyloid diseases are degenerative pathologies, highly prevalent today because they are closely related to aging, that have in common the erroneous folding of intrinsically disordered proteins (IDPs) which aggregate and lead to cell death. Type 2 Diabetes
Jacopo Lesma +13 more
doaj +1 more source