Results 21 to 30 of about 20,996 (256)

The Amyloid Forming Peptides Islet Amyloid Polypeptide and Amyloid β Interact at the Molecular Level

open access: yesInternational Journal of Molecular Sciences, 2021
Epidemiological studies support a connection between the two common disorders, type-2 diabetes and Alzheimer’s disease. Both conditions have local amyloid formation in their pathogenesis, and cross-seeding between islet amyloid polypeptide (IAPP) and ...
Ye Wang, G. Westermark
semanticscholar   +1 more source

Identification of transmissible proteotoxic oligomer-like fibrils that expand conformational diversity of amyloid assemblies

open access: yesCommunications Biology, 2021
Nguyen et al identified cytotoxic amyloid fibrils with oligomer-like characteristics, which were assembled from an islet amyloid polypeptide (IAPP) derivative containing an Asn-to-Gln substitution (N21Q). They presented evidence to show that these stable
Phuong Trang Nguyen   +5 more
doaj   +1 more source

An autophagy enhancer ameliorates diabetes of human IAPP-transgenic mice through clearance of amyloidogenic oligomer

open access: yesNature Communications, 2021
Islet amyloid polypeptide (IAPP) deposition is associated with islet cell loss in diabetes. Here the authors show that a small molecule autophagy enhancer reduces IAPP accumulation in vitro, and also improves glucose tolerance in hIAPP + mice fed high ...
Jinyoung Kim   +14 more
doaj   +1 more source

Heterologous Expression of Immature Forms of Human Islet Amyloid Polypeptide in Yeast Triggers Intracellular Aggregation and Cytotoxicity

open access: yesFrontiers in Microbiology, 2020
Diabetes is a major public health issue that has attained alarming levels worldwide. Pancreatic aggregates of human islet amyloid polypeptide (IAPP) represent a major histopathological hallmark of type 2 diabetes.
Ana F. Raimundo   +11 more
doaj   +1 more source

Amyloid formation reduces protein kinase B phosphorylation in primary islet β-cells which is improved by blocking IL-1β signaling. [PDF]

open access: yesPLoS ONE, 2018
Amyloid formation in the pancreatic islets due to aggregation of human islet amyloid polypeptide (hIAPP) contributes to reduced β-cell mass and function in type 2 diabetes (T2D) and islet transplantation. Protein kinase B (PKB) signaling plays a key role
Yun Zhang   +6 more
doaj   +1 more source

Facet-dependent interactions of islet amyloid polypeptide with gold nanoparticles: Implications for fibril formation and peptide-induced lipid membrane disruption [PDF]

open access: yes, 2017
A comprehensive understanding of the mechanisms of interaction between proteins or peptides and nanomaterials is crucial for the development of nanomaterial-based diagnostics and therapeutics.
Alison A. Edwards   +14 more
core   +8 more sources

Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils

open access: yesNature Structural & Molecular Biology, 2020
Amyloid deposits consisting of fibrillar islet amyloid polypeptide (IAPP) in pancreatic islets are associated with beta-cell loss and have been implicated in type 2 diabetes (T2D).
C. Röder   +8 more
semanticscholar   +1 more source

Dietary Supplementation with Curcumin Reduce Circulating Levels of Glycogen Synthase Kinase-3β and Islet Amyloid Polypeptide in Adults with High Risk of Type 2 Diabetes and Alzheimer’s Disease

open access: yesNutrients, 2020
Dietary supplementation with curcumin has been previously reported to have beneficial effects in people with insulin resistance, type 2 diabetes (T2D) and Alzheimer’s disease (AD).
R. Thota   +5 more
semanticscholar   +1 more source

Islet amyloid deposits preferentially in the highly functional and most blood-perfused islets

open access: yesEndocrine Connections, 2017
Islet amyloid and beta cell death in type 2 diabetes are heterogeneous events, where some islets are affected early in the disease process, whereas others remain visibly unaffected.
Sara Ullsten   +5 more
doaj   +1 more source

Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin

open access: yesNature Communications, 2022
Integrated kinetic and structural investigations reveal that the ubiquitous co-chaperonin prefoldin interacts with its coiled-coil helices on the islet amyloid polypeptide fibril surface and fibril ends to inhibit fibril elongation and secondary ...
Ricarda Törner   +10 more
doaj   +1 more source

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