Reversible Conversion of Monomeric Human Prion Protein between Native and Fibrilogenic Conformations von Jackson, G. S., Hosszu, L. L. P., Power, A., Hill, A. F., Kenney, J., Saibil, H., Craven, C. J., Waltho, J. P., Clarke, A. R., Collinge, J.

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High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin von Milanesi, Lilia, Trevitt, Clare R, Whitehead, Brian, Hounslow, Andrea M, Tomas, Salvador, Hosszu, Laszlo L P, Hunter, Christopher A, Waltho, Jonathan P

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A reassessment of copper(II) binding in the full-length prion protein von Wells, Mark A, Jackson, Graham S, Jones, Samantha, Hosszu, Laszlo L P, Craven, C Jeremy, Clarke, Anthony R, Collinge, John, Waltho, Jonathan P

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Multiple forms of copper (II) co-ordination occur throughout the disordered N-terminal region of the prion protein at pH 7.4 von Wells, Mark A, Jelinska, Clare, Hosszu, Laszlo L P, Craven, C Jeremy, Clarke, Anthony R, Collinge, John, Waltho, Jonathan P, Jackson, Graham S

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Folding kinetics of the human prion protein probed by temperature jump von Hart, Tanya, Hosszu, Laszlo L.P, Trevitt, Clare R, Jackson, Graham S, Waltho, Jonathan P, Collinge, John, Clarke, Anthony R

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Location and Properties of Metal-Binding Sites on the Human Prion Protein von Jackson, G S, Murray, I, Hosszu, L L, Gibbs, N, Waltho, J P, Clarke, A R, Collinge, J

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Characterization of Prion Disease Associated with a Two-Octapeptide Repeat Insertion von Brennecke, Nicholas, Cali, Ignazio, Mok, Tze How, Speedy, Helen, Genomics England Research Consortium, Hosszu, Laszlo L P, Stehmann, Christiane, Cracco, Laura, Puoti, Gianfranco, Prior, Thomas W, Cohen, Mark L, Collins, Steven J, Mead, Simon, Appleby, Brian S

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Ex vivo mammalian prions are formed of paired double helical prion protein fibrils von Terry, Cassandra, Wenborn, Adam, Gros, Nathalie, Sells, Jessica, Joiner, Susan, Hosszu, Laszlo L. P., Tattum, M. Howard, Panico, Silvia, Clare, Daniel K., Collinge, John, Saibil, Helen R., Wadsworth, Jonathan D. F.

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N-terminal Domain of Prion Protein Directs Its Oligomeric Association von Trevitt, Clare R., Hosszu, Laszlo L.P., Batchelor, Mark, Panico, Silvia, Terry, Cassandra, Nicoll, Andrew J., Risse, Emmanuel, Taylor, William A., Sandberg, Malin K., Al-Doujaily, Huda, Linehan, Jacqueline M., Saibil, Helen R., Scott, David J., Collinge, John, Waltho, Jonathan P., Clarke, Anthony R.

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A systematic investigation of production of synthetic prions from recombinant prion protein von Schmidt, Christian, Fizet, Jeremie, Properzi, Francesca, Batchelor, Mark, Sandberg, Malin K., Edgeworth, Julie A., Afran, Louise, Ho, Sammy, Badhan, Anjna, Klier, Steffi, Linehan, Jacqueline M., Brandner, Sebastian, Hosszu, Laszlo L. P., Tattum, M. Howard, Jat, Parmjit, Clarke, Anthony R., Klöhn, Peter C., Wadsworth, Jonathan D. F., Jackson, Graham S., Collinge, John

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Structural effects of the highly protective V127 polymorphism on human prion protein von Hosszu, Laszlo L. P., Conners, Rebecca, Sangar, Daljit, Batchelor, Mark, Sawyer, Elizabeth B., Fisher, Stuart, Cliff, Matthew J., Hounslow, Andrea M., McAuley, Katherine, Leo Brady, R., Jackson, Graham S., Bieschke, Jan, Waltho, Jonathan P., Collinge, John

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Evaluating the causality of novel sequence variants in the prion protein gene by example von Mok, Tze How, Koriath, Carolin, Jaunmuktane, Zane, Campbell, Tracy, Joiner, Susan, Wadsworth, Jonathan D.F., Hosszu, Laszlo L.P., Brandner, Sebastian, Parvez, Ambereen, Truelsen, Thomas Clement, Lund, Eva Løbner, Saha, Romi, Collinge, John, Mead, Simon

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Definable Equilibrium States in the Folding of Human Prion Protein von Hosszu, Laszlo L. P, Wells, Mark A, Jackson, Graham S, Jones, Samantha, Batchelor, Mark, Clarke, Anthony R, Craven, C. Jeremy, Waltho, Jonathan P, Collinge, John

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Conformational Properties of β-PrP von Hosszu, Laszlo L.P., Trevitt, Clare R., Jones, Samantha, Batchelor, Mark, Scott, David J., Jackson, Graham S., Collinge, John, Waltho, Jonathan P., Clarke, Anthony R.

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The H187R Mutation of the Human Prion Protein Induces Conversion of Recombinant Prion Protein to the PrPSc-like Form von Hosszu, Laszlo L. P, Tattum, M. Howard, Jones, Samantha, Trevitt, Clare R, Wells, Mark A, Waltho, Jonathan P, Collinge, John, Jackson, Graham S, Clarke, Anthony R

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Loss of Residues 119–136, Including the First β-strand of Human Prion Protein, Generates an Aggregation-competent Partially “Open” Form von Hosszu, Laszlo L.P., Sangar, Daljit, Batchelor, Mark, Risse, Emmanuel, Hounslow, Andrea M., Collinge, John, Waltho, Jonathan P., Bieschke, Jan

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Domain Behavior during the Folding of a Thermostable Phosphoglycerate Kinase von Parker, Martin J, Spencer, James, Jackson, Graham S, Burston, Steven G, Hosszu, Laszlo L. P, Craven, C. Jeremy, Waltho, Jonathan P, Clarke, Anthony R

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Structural mobility of the human prion protein probed by backbone hydrogen exchange von Clarke, Anthony R, Hosszu, Laszlo L. P, Baxter, Nicola J, Jackson, Graham S, Power, Aisling, Waltho, Jonathan P, Craven, C. Jeremy, Collinge, John

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The Residue 129 Polymorphism in Human Prion Protein Does Not Confer Susceptibility to Creutzfeldt-Jakob Disease by Altering the Structure or Global Stability of PrPC von Hosszu, Laszlo L P, Jackson, Graham S, Trevitt, Clare R, Jones, Samantha, Batchelor, Mark, Bhelt, Daljit, Prodromidou, Kanella, Clarke, Anthony R, Waltho, Jonathan P, Collinge, John

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Structure of a kinetic protein folding intermediate by equilibrium amide exchange von Hosszu, Laszlo L. P, Craven, C. Jeremy, Parker, Martin J, Lorch, Mark, Spencer, James, Clarke, Anthony R, Waltho, Jonathan P

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