Search Results - "Radford, Sheena"

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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Amyloid structures: much more than just a cross-β fold by Gallardo, Rodrigo, Ranson, Neil A, Radford, Sheena E

“…•New structures have shown that there is a remarkable diversity and complexity of the amyloid fold.•The same sequence forms different amyloid structures in…”
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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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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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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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Mass spectrometry-enabled structural biology of membrane proteins by Calabrese, Antonio N., Radford, Sheena E.

“…[Display omitted] •Mass spectrometry (MS) is an integral component of the structural biology toolkit.•Native MS and footprinting MS methods can be used to…”
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PyXlinkViewer: A flexible tool for visualization of protein chemical crosslinking data within the PyMOL molecular graphics system by Schiffrin, Bob, Radford, Sheena E., Brockwell, David J., Calabrese, Antonio N.

“…Chemical crosslinking‐mass spectrometry (XL‐MS) is a valuable technique for gaining insights into protein structure and the organization of macromolecular…”
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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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Taking Charge: Metal Ions Accelerate Amyloid Aggregation in Sequence Variants of α‑Synuclein by Byrd, Emily J., Wilkinson, Martin, Radford, Sheena E., Sobott, Frank

“…Αlpha-synuclein (αS) is an intrinsically disordered protein which exhibits a high degree of conformational heterogeneity. In vivo, αS experiences various…”
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Small molecule probes of protein aggregation by Young, Lydia M, Ashcroft, Alison E, Radford, Sheena E

“…[Display omitted] •A range of functionally and structurally unrelated proteins form amyloid.•Toxic intermediates remain elusive, making their targeting a…”
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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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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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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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Energy landscapes of functional proteins are inherently risky by Gershenson, Anne, Gierasch, Lila M, Pastore, Annalisa, Radford, Sheena E

“…Evolutionary pressure for protein function leads to unavoidable sampling of conformational states that are at risk of misfolding and aggregation. The resulting…”
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