Search Results - "Viles, John H."

A Comparison of Three Fluorophores for the Detection of Amyloid Fibers and Prefibrillar Oligomeric Assemblies. ThT (Thioflavin T); ANS (1-Anilinonaphthalene-8-sulfonic Acid); and bisANS (4,4′-Dianilino-1,1′-binaphthyl-5,5′-disulfonic Acid) by Younan, Nadine D, Viles, John H

“…Amyloid fiber formation is a key event in many misfolding disorders. The ability to monitor the kinetics of fiber formation and other prefibrillar assemblies…”
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Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease by Viles, John H.

“…The accumulation of the amyloid‐β peptides (Aβ) is central to the development of Alzheimer's disease. The mechanism by which Aβ triggers a cascade of events…”
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Copper(II) Can Kinetically Trap Arctic and Italian Amyloid‑β40 as Toxic Oligomers, Mimicking Cu(II) Binding to Wild-Type Amyloid‑β42: Implications for Familial Alzheimer’s Disease by Tian, Yao, Shang, Qi, Liang, Ruina, Viles, John H.

“…The self-association of amyloid-β (Aβ) peptide into neurotoxic oligomers is believed to be central to Alzheimer’s disease (AD). Copper is known to impact Aβ…”
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Developing predictive rules for coordination geometry from visible circular dichroism of copper(II) and nickel(II) ions in histidine and amide main‐chain complexes by Stanyon, Helen F., Cong, Xiaojing, Chen, Yan, Shahidullah, Nabeela, Rossetti, Giulia, Dreyer, Jens, Papamokos, George, Carloni, Paolo, Viles, John H.

“…Circular dichroism (CD) spectroscopy in the visible region (vis‐CD) is a powerful technique to study metal–protein interactions. It can resolve individual d–d…”
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Copper and the structural biology of the prion protein by Viles, John H, Klewpatinond, Mark, Nadal, Rebecca C

“…PrP (prion-related protein) is a cell-surface Cu(2+)-binding glycoprotein which, when misfolded, is responsible for a number of transmissible spongiform…”
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Manganese Binding to the Prion Protein by Brazier, Marcus W., Davies, Paul, Player, Esmie, Marken, Frank, Viles, John H., Brown, David R.

“…There is considerable evidence that the prion protein binds copper. However, there have also been suggestions that prion protein (PrP) binds manganese. We used…”
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Deconvoluting the Cu2+ Binding Modes of Full-length Prion Protein by Klewpatinond, Mark, Davies, Paul, Bowen, Suzanne, Brown, David R., Viles, John H.

“…The prion protein (PrP) is a cell-surface Cu2+-binding glycoprotein that when misfolded is responsible for a number of transmissible spongiform…”
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pH Dependence of Amyloid‐β Fibril Assembly Kinetics: Unravelling the Microscopic Molecular Processes by Tian, Yao, Viles, John H.

“…Central to Alzheimer's disease (AD) is the assembly of the amyloid‐beta peptide (Aβ) into fibrils. A reduction in pH accompanying inflammation or subcellular…”
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Impact of Membrane Phospholipids and Exosomes on the Kinetics of Amyloid-β Fibril Assembly by Khursheed, Anum, Viles, John H

“…[Display omitted] •Amyloid assembly in Alzheimer's disease may be influenced by the lipid rich brain.•Anionic phospholipids accelerate fibril assembly by…”
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Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy by Bode, David C., Freeley, Mark, Nield, Jon, Palma, Matteo, Viles, John H.

“…The ability of amyloid-β peptide (Aβ) to disrupt membrane integrity and cellular homeostasis is believed to be central to Alzheimer’s disease pathology. Aβ is…”
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Cross-seeding of WT amyloid-β with Arctic but not Italian familial mutants accelerates fibril formation in Alzheimer's disease by Liang, Ruina, Tian, Yao, Viles, John H.

“…Alzheimer’s disease (AD) involves the neurotoxic self-assembly of a 40 and 42 residue peptide, Amyloid-β (Aβ). Inherited early-onset AD can be caused by single…”
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Ion Channel Formation by Amyloid-β42 Oligomers but Not Amyloid-β40 in Cellular Membranes by Bode, David C., Baker, Mark D., Viles, John H.

“…A central hallmark of Alzheimer’s disease is the presence of extracellular amyloid plaques chiefly consisting of amyloid-β (Aβ) peptides in the brain…”
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3D-visualization of amyloid-β oligomer interactions with lipid membranes by cryo-electron tomography by Tian, Yao, Liang, Ruina, Kumar, Amit, Szwedziak, Piotr, Viles, John H

“…Amyloid-β (Aβ) assemblies have been shown to bind to lipid bilayers. This can disrupt membrane integrity and cause a loss of cellular homeostasis, that…”
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Copper Binding to the Prion Protein: Structural Implications of Four Identical Cooperative Binding Sites by Viles, John H., Cohen, Fred E., Prusiner, Stanely B., Goodin, David B., Wright, Peter E., Dyson, H. Jane

“…Evidence is growing to support a functional role for the prion protein (PrP) in copper metabolism. Copper ions appear to bind to the protein in a highly…”
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Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: implications for Alzheimer disease by Stanyon, Helen F, Viles, John H

“…Alzheimer disease is a neurodegenerative disorder characterized by extracellular accumulation of amyloid-β peptide (Aβ) in the brain interstitium. Human serum…”
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Copper Redox Cycling Inhibits Aβ Fibre Formation and Promotes Fibre Fragmentation, while Generating a Dityrosine Aβ Dimer by Gu, Miao, Bode, David C., Viles, John H.

“…Oxidative stress and the formation of plaques which contain amyloid-β (Aβ) peptides are two key hallmarks of Alzheimer’s disease (AD). Dityrosine is found in…”
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Structure of the Recombinant Full-Length Hamster Prion Protein PrP(29-231): The N Terminus is Highly Flexible by Donne, David G., Viles, John H., Groth, Darlene, Mehlhorn, Ingrid, James, Thomas L., Cohen, Fred E., Prusiner, Stanley B., Wright, Peter E., Dyson, H. Jane

“…The prion diseases seem to be caused by a conformational change of the prion protein (PrP) from the benign cellular from PrPCto the infectious scrapie form…”
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Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies by Nasica-Labouze, Jessica, Nguyen, Phuong H, Sterpone, Fabio, Berthoumieu, Olivia, Buchete, Nicolae-Viorel, Coté, Sébastien, De Simone, Alfonso, Doig, Andrew J, Faller, Peter, Garcia, Angel, Laio, Alessandro, Li, Mai Suan, Melchionna, Simone, Mousseau, Normand, Mu, Yuguang, Paravastu, Anant, Pasquali, Samuela, Rosenman, David J, Strodel, Birgit, Tarus, Bogdan, Viles, John H, Zhang, Tong, Wang, Chunyu, Derreumaux, Philippe

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Truncated Amyloid-β(11–40/42) from Alzheimer Disease Binds Cu2+ with a Femtomolar Affinity and Influences Fiber Assembly by Barritt, Joseph D., Viles, John H.

“…Alzheimer disease coincides with the formation of extracellular amyloid plaques composed of the amyloid-β (Aβ) peptide. Aβ is typically 40 residues long…”
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Therapeutic potential for amyloid surface inhibitor: only amyloid‐β oligomers formed by secondary nucleation disrupt lipid membrane integrity by Tian, Yao, Liu, Jianbo, Yang, Fadeng, Lian, Chenshan, Zhang, Huawei, Viles, John H., Li, Zigang

“…Inhibition of amyloid‐β peptide (Aβ) aggregation is a promising therapeutic strategy for Alzheimer's disease (AD), as Aβ aggregation is generally believed to…”
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