Search Results - "Cawood, Emma E."

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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Modulation of Amyloidogenic Protein Self-Assembly Using Tethered Small Molecules by Cawood, Emma E, Guthertz, Nicolas, Ebo, Jessica S, Karamanos, Theodoros K, Radford, Sheena E, Wilson, Andrew J

“…Protein–protein interactions (PPIs) are involved in many of life’s essential biological functions yet are also an underlying cause of several human diseases,…”
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Structural mapping of oligomeric intermediates in an amyloid assembly pathway by Karamanos, Theodoros K, Jackson, Matthew P, Calabrese, Antonio N, Goodchild, Sophia C, Cawood, Emma E, Thompson, Gary S, Kalverda, Arnout P, Hewitt, Eric W, Radford, Sheena E

“…Transient oligomers are commonly formed in the early stages of amyloid assembly. Determining the structure(s) of these species and defining their role(s) in…”
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Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone by Cawood, Emma E., Clore, G. Marius, Karamanos, Theodoros K.

“…DNAJB6 is a prime example of an anti‐aggregation chaperone that functions as an oligomer. DNAJB6 oligomers are dynamic and subunit exchange is critical for…”
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Understanding β-strand mediated protein-protein interactions: tuning binding behaviour of intrinsically disordered sequences by backbone modification by Cawood, Emma E, Baker, Emily, Edwards, Thomas A, Woolfson, Derek N, Karamanos, Theodoros K, Wilson, Andrew J

“…A significant challenge in chemical biology is to understand and modulate protein-protein interactions (PPIs). Given that many PPIs involve a folded protein…”
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The role of the IT-state in D76N β2-microglobulin amyloid assembly: A crucial intermediate or an innocuous bystander? by Smith, Hugh I., Guthertz, Nicolas, Cawood, Emma E., Maya-Martinez, Roberto, Breeze, Alexander L., Radford, Sheena E.

“…The D76N variant of human β2-microglobulin (β2m) is the causative agent of a hereditary amyloid disease. Interestingly, D76N-associated amyloidosis has a…”
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Bioorthogonal, Bifunctional Linker for Engineering Synthetic Glycoproteins by McBerney, Ryan, Dolan, Jonathan P., Cawood, Emma E., Webb, Michael E., Turnbull, W. Bruce

“…Post-translational glycosylation of proteins results in complex mixtures of heterogeneous protein glycoforms. Glycoproteins have many potential applications…”
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Microsecond Backbone Motions Modulate the Oligomerization of the DNAJB6 Chaperone by Cawood, Emma E., Clore, G. Marius, Karamanos, Theodoros K.

“…DNAJB6 is a prime example of an anti‐aggregation chaperone that functions as an oligomer. DNAJB6 oligomers are dynamic and subunit exchange is critical for…”
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Towards optimizing peptide-based inhibitors of protein-protein interactions: predictive saturation variation scanning (PreSaVS) by Hetherington, Kristina, Dutt, Som, Ibarra, Amaurys A, Cawood, Emma E, Hobor, Fruzsina, Woolfson, Derek N, Edwards, Thomas A, Nelson, Adam, Sessions, Richard B, Wilson, Andrew J

“…A simple-to-implement and experimentally validated computational workflow for sequence modification of peptide inhibitors of protein-protein interactions…”
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The role of the I T -state in D76N β 2 -microglobulin amyloid assembly: A crucial intermediate or an innocuous bystander? by Smith, Hugh I, Guthertz, Nicolas, Cawood, Emma E, Maya-Martinez, Roberto, Breeze, Alexander L, Radford, Sheena E

“…The D76N variant of human β -microglobulin (β m) is the causative agent of a hereditary amyloid disease. Interestingly, D76N-associated amyloidosis has a…”
Get full text