Results 131 to 140 of about 20,996 (256)

Small molecule probes of protein aggregation [PDF]

open access: yes, 2017
Understanding the mechanisms of amyloid formation and toxicity remain major challenges. Whilst substantial progress has been made in the development of methods able to identify the species formed during self-assembly and to describe the kinetic ...
Abedini   +139 more
core   +1 more source

Folded Small Molecule Manipulation of Islet Amyloid Polypeptide

open access: yesChemistry & Biology, 2014
Islet amyloid polypeptide (IAPP) is a hormone cosecreted with insulin by pancreatic β cells. Upon contact with lipid bilayers, it is stabilized into a heterogeneous ensemble of structural states. These processes are associated with gains of function, including catalysis of β sheet-rich amyloid formation, cell membrane penetration, loss of membrane ...
Kumar, Sunil   +3 more
openaire   +2 more sources

Inhibitory Activities of Antioxidant Flavonoids from Tamarix gallica on Amyloid Aggregation Related to Alzheimer\u27s and Type 2 Diabetes Diseases [PDF]

open access: yes, 2017
The prevention of amyloid aggregation is promising for the treatment of age-related diseases such as Alzheimer’s (AD) and type 2 diabetes (T2D). Ten antioxidant flavonoids isolated from the medicinal halophyte Tamarix gallica were tested for their ...
Hanaki Mizuho   +7 more
core   +1 more source

Cell-to-cell transmission of IAPP aggregates in T2DM induces neuronal death by triggering oxidative stress and ferroptosis

open access: yesNeurobiology of Disease
Type 2 diabetes mellitus (T2DM) is associated with an elevated risk of neurodegenerative diseases, yet the underlying mechanisms remain elusive. A hallmark feature of T2DM is the amyloid deposition of islet amyloid polypeptide (IAPP) in the pancreas ...
Honglin Zheng   +11 more
doaj   +1 more source

Conformation-Dependent Manipulation of Human Islet Amyloid Polypeptide Fibrillation by Shiitake-Derived Lentinan.

open access: yesACS Applied Materials and Interfaces, 2018
Misfolding and aggregation of human islet amyloid polypeptide (hIAPP) into fibrils are important contributions to the pathology of type 2 diabetes. Developing effective inhibitors of protein aggregation and fibrillation has been considered a promising ...
Yanru Xin   +3 more
semanticscholar   +1 more source

Expression of neurogenin3 reveals an islet cell precursor population in the pancreas [PDF]

open access: yes, 2000
Differentiation of early gut endoderm cells into the endocrine cells forming the pancreatic islets of Langerhans depends on a cascade of gene activation events controlled by transcription factors including the basic helix-loop-helix (bHLH) proteins.
Anderson, David J.   +8 more
core  

Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils

open access: yesACS Nano, 2017
Determining the structural origins of amyloid fibrillation is essential for understanding both the pathology of amyloidosis and the rational design of inhibitors to prevent or reverse amyloid formation.
Shih-Ting Wang   +14 more
semanticscholar   +1 more source

Polyphenol Interactions with Amyloid Fibrils: A Molecular Docking Study

open access: yesEast European Journal of Physics
Polyphenols, a versatile group of naturally occurring compounds with many favorable biological properties currently attract increasing research interest in the context of their ability to inhibit the formation and to destabilize special protein ...
Uliana Malovytsia   +5 more
doaj   +1 more source

Common fibrillar spines of amyloid-β and human islet amyloid polypeptide revealed by microelectron diffraction and structure-based inhibitors

open access: yesJournal of Biological Chemistry, 2017
Amyloid-β (Aβ) and human islet amyloid polypeptide (hIAPP) aggregate to form amyloid fibrils that deposit in tissues and are associated with Alzheimer's disease (AD) and type II diabetes (T2D), respectively. Individuals with T2D have an increased risk of
P. Krotee   +14 more
semanticscholar   +1 more source

Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity. [PDF]

open access: yes, 2012
The amyloid protein aggregation associated with diseases such as Alzheimer's, Parkinson's and type II diabetes (among many others) features a bewildering variety of β-sheet-rich structures in transition from native proteins to ordered oligomers and ...
Cheng, Pin-Nan   +4 more
core  

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