Mark Batchelor
University College London
20 Papers
326 Citations
Mark Batchelor is an academic researcher from University College London. The author has contributed to research in topics: Protein structure & Molten globule. The author has an hindex of 12, co-authored 20 publications. Previous affiliations of Mark Batchelor include Vertex Pharmaceuticals & UCL Institute of Neurology.
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Papers
Recombinant prion protein does not possess SOD-1 activity
Samantha Jones,Mark Batchelor,Daljit Bhelt,Anthony R. Clarke,John Collinge,Graham S. Jackson +5 more
TL;DR: It is found that PrP exhibits no detectable dismutase activity above baseline levels measured for copper (II) ions in water when assayed using a reliable procedure with a detection limit of at least 2 units of activity/mg of protein.
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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.
Laszlo L. P. Hosszu,Laszlo L. P. Hosszu,Graham S. Jackson,Clare R. Trevitt,Samantha Jones,Mark Batchelor,Daljit Bhelt,Kanella Prodromidou,Anthony R. Clarke,Jonathan P. Waltho,John Collinge +10 more
TL;DR: The data indicate that the 129M/V polymorphism does not affect prion propagation through its effect on PrPC; rather, its influence is likely to be downstream in the disease mechanism.
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Definable Equilibrium States in the Folding of Human Prion Protein
Laszlo L. P. Hosszu,Mark A Wells,Graham S. Jackson,Samantha Jones,Mark Batchelor,Anthony R. Clarke,C. Jeremy Craven,Jonathan P. Waltho,John Collinge +8 more
TL;DR: Analysis of NMR chemical shift and intensity changes shows that there is persistent structure in the molecule well beyond this major cooperative unfolding transition, and in aqueous solution the native and locally unfolded conformations are both significantly populated.
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Codon 129 polymorphism of the human prion protein influences the kinetics of amyloid formation.
Patrick A. Lewis,M. Howard Tattum,Samantha Jones,Daljit Bhelt,Mark Batchelor,Anthony R. Clarke,John Collinge,Graham S. Jackson +7 more
TL;DR: This work has shown that in a partially denatured conformation, the polymorphic variation has a profound influence on the ability of the protein to form amyloid fibrils spontaneously.
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Conformational Properties of -PrP *
Laszlo L. P. Hosszu,Clare R. Trevitt,Samantha Jones,Mark Batchelor,David J. Scott,Graham S. Jackson,John Collinge,Jonathan P. Waltho,Anthony R. Clarke +8 more
- 01 Jan 2009
TL;DR: It is found that a disulfide-reduced fragment of human PrP spanning residues 91–231 under acidic conditions, which similarly to PrPSc, is a potent inhibitor of the 26 S proteasome, assembles into soluble oligomers that have significant β-sheet content.
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