Search Results - "Radford, Sheena E."

A Diversity of Assembly Mechanisms of a Generic Amyloid Fold by Eichner, Timo, Radford, Sheena E.

“…Protein misfolding and amyloid assembly have long been recognized as being responsible for many devastating human diseases. Recent findings indicate that…”
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Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria by Horne, Jim E., Brockwell, David J., Radford, Sheena E.

“…β-Barrel outer membrane proteins (OMPs) represent the major proteinaceous component of the outer membrane (OM) of Gram-negative bacteria. These proteins…”
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A new era for understanding amyloid structures and disease by Iadanza, Matthew G., Jackson, Matthew P., Hewitt, Eric W., Ranson, Neil A., Radford, Sheena E.

“…The aggregation of proteins into amyloid fibrils and their deposition into plaques and intracellular inclusions is the hallmark of amyloid disease. The…”
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Proteostasis of Islet Amyloid Polypeptide: A Molecular Perspective of Risk Factors and Protective Strategies for Type II Diabetes by Milardi, Danilo, Gazit, Ehud, Radford, Sheena E, Xu, Yong, Gallardo, Rodrigo U, Caflisch, Amedeo, Westermark, Gunilla T, Westermark, Per, Rosa, Carmelo La, Ramamoorthy, Ayyalusamy

“…The possible link between hIAPP accumulation and β-cell death in diabetic patients has inspired numerous studies focusing on amyloid structures and aggregation…”
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Visualizing and trapping transient oligomers in amyloid assembly pathways by Cawood, Emma E., Karamanos, Theodoros K., Wilson, Andrew J., Radford, Sheena E.

“…Oligomers which form during amyloid fibril assembly are considered to be key contributors towards amyloid disease. However, understanding how such…”
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Macromolecular Crowding Enhances the Detection of DNA and Proteins by a Solid-State Nanopore by Chau, Chalmers C, Radford, Sheena E, Hewitt, Eric W, Actis, Paolo

“…Nanopore analysis of nucleic acid is now routine, but detection of proteins remains challenging. Here, we report the systematic characterization of the effect…”
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Looking Beyond the Core: The Role of Flanking Regions in the Aggregation of Amyloidogenic Peptides and Proteins by Ulamec, Sabine M, Brockwell, David J, Radford, Sheena E

“…Amyloid proteins are involved in many neurodegenerative disorders such as Alzheimer's disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein…”
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Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly by Xue, Wei-Feng, Homans, Steve W, Radford, Sheena E

“…Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid results in numerous human diseases. Despite an increasing number of…”
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An Imaging and Systems Modeling Approach to Fibril Breakage Enables Prediction of Amyloid Behavior by Xue, Wei-Feng, Radford, Sheena E.

“…Delineating the nanoscale properties and the dynamic assembly and disassembly behaviors of amyloid fibrils is key for technological applications that use the…”
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Ion Mobility Spectrometry–Mass Spectrometry Defines the Oligomeric Intermediates in Amylin Amyloid Formation and the Mode of Action of Inhibitors by Young, Lydia M, Cao, Ping, Raleigh, Daniel P, Ashcroft, Alison E, Radford, Sheena E

“…The molecular mechanisms by which different proteins assemble into highly ordered fibrillar deposits and cause disease remain topics of debate. Human amylin…”
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Folding versus aggregation: Polypeptide conformations on competing pathways by Jahn, Thomas R., Radford, Sheena E.

“…Protein aggregation has now become recognised as an important and generic aspect of protein energy landscapes. Since the discovery that numerous human diseases…”
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Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM by Iadanza, Matthew G., Higgins, Anna J., Schiffrin, Bob, Calabrese, Antonio N., Brockwell, David J., Ashcroft, Alison E., Radford, Sheena E., Ranson, Neil A.

“…The β-barrel assembly machinery (BAM) is a ∼203 kDa complex of five proteins (BamA–E), which is essential for viability in E. coli . BAM promotes the folding…”
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The structure of a β2-microglobulin fibril suggests a molecular basis for its amyloid polymorphism by Iadanza, Matthew G., Silvers, Robert, Boardman, Joshua, Smith, Hugh I., Karamanos, Theodoros K., Debelouchina, Galia T., Su, Yongchao, Griffin, Robert G., Ranson, Neil A., Radford, Sheena E.

“…All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from proteins associated with different diseases remains unclear…”
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Understanding the complex mechanisms of β2‐microglobulin amyloid assembly by Eichner, Timo, Radford, Sheena E.

“…Several protein misfolding diseases are associated with the conversion of native proteins into ordered protein aggregates known as amyloid. Studies of amyloid…”
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Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry–mass spectrometry by Young, Lydia M., Saunders, Janet C., Mahood, Rachel A., Revill, Charlotte H., Foster, Richard J., Tu, Ling-Hsien, Raleigh, Daniel P., Radford, Sheena E., Ashcroft, Alison E.

“…The search for therapeutic agents that bind specifically to precursor protein conformations and inhibit amyloid assembly is an important challenge. Identifying…”
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Modulation of β-Amyloid Fibril Formation in Alzheimer's Disease by Microglia and Infection by Brown, Madeleine R, Radford, Sheena E, Hewitt, Eric W

“…Amyloid plaques are a pathological hallmark of Alzheimer's disease. The major component of these plaques are highly ordered amyloid fibrils formed by amyloid-β…”
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Tuning the rate of aggregation of hIAPP into amyloid using small-molecule modulators of assembly by Xu, Yong, Maya-Martinez, Roberto, Guthertz, Nicolas, Heath, George R., Manfield, Iain W., Breeze, Alexander L., Sobott, Frank, Foster, Richard, Radford, Sheena E.

“…Human islet amyloid polypeptide (hIAPP) self-assembles into amyloid fibrils which deposit in pancreatic islets of type 2 diabetes (T2D) patients. Here, we…”
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Controlling amyloid formation of intrinsically disordered proteins and peptides: slowing down or speeding up? by Xu, Yong, Maya-Martinez, Roberto, Radford, Sheena E

“…The pathological assembly of intrinsically disordered proteins/peptides (IDPs) into amyloid fibrils is associated with a range of human pathologies, including…”
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Outer membrane protein folding from an energy landscape perspective by Schiffrin, Bob, Brockwell, David J, Radford, Sheena E

“…The cell envelope is essential for the survival of Gram-negative bacteria. This specialised membrane is densely packed with outer membrane proteins (OMPs),…”
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Nucleation of protein fibrillation by nanoparticles by Linse, Sara, Cabaleiro-Lago, Celia, Xue, Wei-Feng, Lynch, Iseult, Lindman, Stina, Thulin, Eva, Radford, Sheena E, Dawson, Kenneth A

“…Nanoparticles present enormous surface areas and are found to enhance the rate of protein fibrillation by decreasing the lag time for nucleation. Protein…”
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