Articles with "amyloid formation" as a keyword



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The role of amyloidogenic proteins as a meeting point of type 2 diabetes and Parkinson's disease pathways

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Published in 2017 at "Movement Disorders"

DOI: 10.1002/mds.26897

Abstract: The impairment of amyloid formation is associated with Parkinson disease (PD) and type 2 diabetes (T2D) in which the primary pathological characteristics are assembly of asynuclein into amyloid fiber and islet amyloid polypeptide (IAPP) formation… read more here.

Keywords: aggregation; disease; formation; pro iapp ... See more keywords
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Polyphenol‐solubility alters amyloid fibril formation of α‐synuclein

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Published in 2021 at "Protein Science"

DOI: 10.1002/pro.4130

Abstract: Amyloid fibril formation is associated with various amyloidoses, including neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Amyloid fibrils form above the solubility of amyloidogenic proteins or peptides upon breaking supersaturation, followed by a nucleation… read more here.

Keywords: formation synuclein; formation; fibril formation; solubility ... See more keywords
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Mechanism of rutin mediated inhibition of insulin amyloid formation and protection of Neuro-2a cells from fibril-induced apoptosis

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Published in 2020 at "Molecular Biology Reports"

DOI: 10.1007/s11033-020-05393-8

Abstract: Many metabolic and neurodegenerative diseases are associated with protein misfolding and aggregation. Insulin a key hormone, under certain conditions aggregates and forms pathological amyloid fibrils. Several polyphenols have been studied extensively to elucidate their inhibitory… read more here.

Keywords: insulin; fibril induced; insulin amyloid; rutin ... See more keywords
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Shear-induced amyloid formation of IDPs in the brain.

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Published in 2019 at "Progress in molecular biology and translational science"

DOI: 10.1016/bs.pmbts.2019.05.008

Abstract: The IDP amyloid β-protein (Aβ) has been both the prime causative suspect and drug development target in the fight against Alzheimer's disease (AD). Unfortunately, all clinical trials against Aβ based on this assumption have failed.… read more here.

Keywords: induced amyloid; shear induced; induced aggregation; amyloid formation ... See more keywords
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Thioflavin T fluorescence to analyse amyloid formation kinetics: Measurement frequency as a factor explaining irreproducibility.

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Published in 2017 at "Analytical biochemistry"

DOI: 10.1016/j.ab.2017.06.007

Abstract: The most frequent method to monitor amyloid formation relies on the fluorescence of thioflavin T (ThT). The present study reports a novel factor of irreproducibility in ThT kinetic assays performed in microplate. Discrepancies among kinetics… read more here.

Keywords: fluorescence; frequency; irreproducibility; factor ... See more keywords
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Cross-Reactivity of Alpha-Synuclein with Other Cellular Components Can Dramatically Modulate Amyloid Formation

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Published in 2017 at "Biophysical Journal"

DOI: 10.1016/j.bpj.2016.11.1980

Abstract: The aggregation process, going from monomers to amyloid fibers, of the protein α-synuclein (αS) somehow causes degeneration of dopaminergic neurons in Parkinson's disease patients. The exact activities of αS are not yet identified, but synapse… read more here.

Keywords: cross reactivity; modulate amyloid; formation; parkinson disease ... See more keywords
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Ribosylation induced structural changes in Bovine Serum Albumin: understanding high dietary sugar induced protein aggregation and amyloid formation

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Published in 2020 at "Heliyon"

DOI: 10.1016/j.heliyon.2020.e05053

Abstract: Non-enzymatic glycation of proteins is believed to be the root cause of high dietary sugar associated pathophysiological maladies. We investigated the structural changes in protein during progression of glycation using ribosylated Bovine Serum Albumin (BSA).… read more here.

Keywords: formation; ribosylation; glycation; dietary sugar ... See more keywords
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The Process of Amyloid Formation due to Monoclonal Immunoglobulins.

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Published in 2020 at "Hematology/oncology clinics of North America"

DOI: 10.1016/j.hoc.2020.07.003

Abstract: Monoclonal antibodies secreted by clonally expanded plasma cells can form a range of pathologic aggregates including amyloid fibrils. The enormous diversity in the sequences of the involved light chains may be responsible for complexity of… read more here.

Keywords: process amyloid; formation due; amyloid fibrils; monoclonal immunoglobulins ... See more keywords
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Correct partner makes the difference: Septin G-interface plays a critical role in amyloid formation.

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Published in 2019 at "International journal of biological macromolecules"

DOI: 10.1016/j.ijbiomac.2019.04.105

Abstract: Septins are members of a group of GTP-binding proteins highly conserved in eukaryotes, being linked to diverse cell processes, such as cytokinesis and membrane association. On the other hand, the malfunction of septins is linked… read more here.

Keywords: critical role; formation; interface; amyloid formation ... See more keywords
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Likelihood of amyloid formation in COVID-19-induced ARDS

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Published in 2021 at "Trends in Microbiology"

DOI: 10.1016/j.tim.2021.03.008

Abstract: Severe coronavirus disease 2019 (COVID-19) infection leads to multifactorial acute respiratory distress syndrome (ARDS), with little therapeutic success. The pathophysiology associated with ARDS or post-ARDS is not yet well understood. We hypothesize that amyloid formation… read more here.

Keywords: induced ards; likelihood amyloid; covid; amyloid formation ... See more keywords
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Differential Effects of Aromatic Residues on Amyloid Formation and Cytotoxicity of Human IAPP.

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Published in 2022 at "Biochemistry"

DOI: 10.1021/acs.biochem.2c00267

Abstract: Islet amyloid polypeptide (IAPP) is a 37-residue polypeptide hormone secreted by the pancreatic β-cells. IAPP plays a role in glycemic regulation, but in the pre-type-2 diabetic state, it aggregates to form an islet amyloid. The… read more here.

Keywords: amyloid formation; aromatic residues; role; formation cytotoxicity ... See more keywords