Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway. - Wikidata - wikimedia - TriplyDB

Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway.

Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway.

http://www.wikidata.org/entity/Q33597188

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Apoptosis in pancreatic β-islet cells in Type 2 diabetes Neuroendocrine hormone amylin in diabetes Mechanisms of islet amyloidosis toxicity in type 2 diabetes The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP Amylin at the interface between metabolic and neurodegenerative disorders On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides Hsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes Treatment UCHL1 deficiency exacerbates human islet amyloid polypeptide toxicity in β-cells: evidence of interplay between the ubiquitin/proteasome system and autophagy Early amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.Membrane Curvature-sensing and Curvature-inducing Activity of Islet Amyloid Polypeptide and Its Implications for Membrane Disruption.Calcium-activated calpain-2 is a mediator of beta cell dysfunction and apoptosis in type 2 diabetes.Drosophila melanogaster as a model system for studies of islet amyloid polypeptide aggregation.Autophagy defends pancreatic β cells from human islet amyloid polypeptide-induced toxicity Neuroinflammation and neurologic deficits in diabetes linked to brain accumulation of amylin.Lipid interaction and membrane perturbation of human islet amyloid polypeptide monomer and dimer by molecular dynamics simulations.Amylin deposition in the brain: A second amyloid in Alzheimer disease?β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency.The Mitochondrial Peptidase Pitrilysin Degrades Islet Amyloid Polypeptide in Beta-Cells.Cyclin-dependent kinase 5 promotes pancreatic β-cell survival via Fak-Akt signaling pathways.Age related changes in pancreatic beta cells: A putative extra-cerebral site of Alzheimer's pathology.Structural similarities and differences between amyloidogenic and non-amyloidogenic islet amyloid polypeptide (IAPP) sequences and implications for the dual physiological and pathological activities of these peptides.Cardioprotection by controlling hyperamylinemia in a "humanized" diabetic rat model Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease.β-cell loss and β-cell apoptosis in human type 2 diabetes are related to islet amyloid deposition.Human-IAPP disrupts the autophagy/lysosomal pathway in pancreatic β-cells: protective role of p62-positive cytoplasmic inclusions Islet amyloid polypeptide is a target antigen for diabetogenic CD4+ T cells.Structure-Based Small Molecule Modulation of a Pre-Amyloid State: Pharmacological Enhancement of IAPP Membrane-Binding and Toxicity.Concentration-dependent transitions govern the subcellular localization of islet amyloid polypeptide Type 2 diabetes as a protein misfolding disease.X-ray Crystallographic Structures of Oligomers of Peptides Derived from β2-Microglobulin Kisspeptin prevention of amyloid-β peptide neurotoxicity in vitro.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Human islet amyloid polypeptide at the air-aqueous interface: a Langmuir monolayer approach.β-Cell failure in type 2 diabetes: a case of asking too much of too few?Islet β cell mass in diabetes and how it relates to function, birth, and death.CHOP Contributes to, But Is Not the Only Mediator of, IAPP Induced β-Cell Apoptosis Adsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated Aggregation Degradation of islet amyloid polypeptide by neprilysin.β-Cell Deficit in Obese Type 2 Diabetes, a Minor Role of β-Cell Dedifferentiation and Degranulation.A common landscape for membrane-active peptides.

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P2860

Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway.

http://www.wikidata.org/entity/Q33597188

description

2009 nî lūn-bûn

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2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Evidence for proteotoxicity in ...... arly in the secretory pathway.

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Evidence for proteotoxicity in ...... arly in the secretory pathway.

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Evidence for proteotoxicity in ...... arly in the secretory pathway.

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Evidence for proteotoxicity in ...... arly in the secretory pathway.

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The American Journal of Pathology

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Evidence for proteotoxicity in ...... arly in the secretory pathway.

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Chang-jiang Huang

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Charles G Glabe

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Howard A Reber

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Michael W Yeh

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O Joe Hines

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Sergey Ryazantsev

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Tatyana Gurlo

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Timothy D O'Brien

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P2860

Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis

Protein homeostasis and aging: taking care of proteins from the cradle to the grave

Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging

Beta-cell deficit and increased beta-cell apoptosis in humans with type 2 diabetes

The natural history of insulin secretory dysfunction and insulin resistance in the pathogenesis of type 2 diabetes mellitus.

Effects of meal ingestion on plasma amylin concentration in NIDDM and nondiabetic humans.

Mitochondrial function in normal and diabetic beta-cells.

Toxic human islet amyloid polypeptide (h-IAPP) oligomers are intracellular, and vaccination to induce anti-toxic oligomer antibodies does not prevent h-IAPP-induced beta-cell apoptosis in h-IAPP transgenic mice.

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861-869

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20042670

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type-2 diabetes

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