Shreya GhoshVitali TugarinovG. Marius CloreaLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, MD 20892-0520...
Date:
Proceedings of the National Academy of Sciences, Volume 120, Issue 21, May 2023. Read More
PNAS:
Number: 21
Volume: 120
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[NMR paper] Quantitative NMR analysis of the mechanism and kinetics of chaperone Hsp104 action on amyloid-?42 aggregation and fibril formation
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The chaperone Hsp104, a member of the Hsp100/Clp family of translocases, prevents fibril formation of a variety of amyloidogenic peptides in a paradoxically substoichiometric manner. To understand the mechanism whereby Hsp104 inhibits fibril formation, we probed the interaction of Hsp104 with the Alzheimer's amyloid-?42 (A?42) peptide using a variety of biophysical techniques. Hsp104 is highly effective at suppressing the formation of Thioflavin T (ThT)...
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The N-terminal region of the huntingtin protein, encoded by exon-1 (htt^(ex1)) and containing an expanded polyglutamine tract, forms fibrils that accumulate in neuronal inclusion bodies, resulting in Huntington's disease. We previously showed that reversible formation of a sparsely populated tetramer of the N-terminal amphiphilic domain, comprising a dimer of dimers in a four-helix bundle configuration, occurs on the microsecond timescale and is an essential...
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https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00342/20210803/images/medium/bi1c00342_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00342
http://feeds.feedburner.com/~r/acs/bichaw/~4/rYtDmRoWk6c
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[NMR paper] Understanding amyloid fibril formation using protein fragments: structural investigations via vibrational spectroscopy and solid-state NMR.
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Biophys Rev. 2018 May 31;:
Authors: Martial B, Lefèvre T, Auger M
Abstract
It is well established that amyloid proteins play a primary role in neurodegenerative diseases. Alzheimer's, Parkinson's, type II diabetes, and Creutzfeldt-Jakob's...
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Amyloid fibrils and soluble oligomers are two types of protein aggregates associated with neurodegeneration. Classic therapeutic strategies try to prevent the nucleation and spread of amyloid fibrils, whilst diffusible oligomers have emerged as promising drug targets affecting downstream pathogenic processes. We developed a generic protein aggregation model and validate it against measured compositions of fibrillar and non-fibrillar assemblies of ataxin-3, a protein implicated in Machado-Joseph disease....
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Biochemistry. 2000 Nov 14;39(45):13748-59
Authors: Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, Reed J, Tycko R
The seven-residue peptide N-acetyl-Lys-Leu-Val-Phe-Phe-Ala-Glu-NH(2), called A...
Quantitative NMR analysis of the mechanism and kinetics of chaperone Hsp104 action on amyloid-?42 aggregation and fibril formation
Linear Mode
