Author

D. Sangar

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Assay:protein structure· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Organism:mouse· 1

Frequent Co-Authors

J. Bieschke· 3 shared J. Collinge· 2 shared K. Jack· 2 shared M. Batchelor· 2 shared A. M. Hounslow· 1 shared B. Mistry· 1 shared E. Hill· 1 shared E. Risse· 1 shared

Activity by Year

2022-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersBiophysics

J. Bieschke

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Author profile →

3 papers

Recent·Most cited

Loss of the first β-strand of human prion protein generates an aggregation-competent partially "open" form

L. L. P. Hosszu, D. Sangar, M. Batchelor, E. Risse, A. M. Hounslow, J. P. Waltho, J. Collinge, J. Bieschke

This study examines the structural and functional changes in a truncated form of human prion protein lacking a conserved membrane region, showing it forms fibrils more readily than the native form.

bioRxiv · Sep 20, 2022 · PreprintBiophysics

Syntaxin 6 delays prion protein fibril formation and prolongs presence of toxic aggregation intermediates

D. Sangar, E. Hill, K. Jack, M. Batchelor, B. Mistry, J. M. Ribes, G. S. Jackson, S. Mead, J. Bieschke

This study shows syntaxin-6 inhibits PrP fibril formation but prolongs toxic intermediate aggregates, suggesting it acts as an anti-chaperone in prion disease.

bioRxiv · Aug 25, 2022Biochemistry

Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics

Y. Sun, K. Jack, T. Ercolani, D. Sangar, L. L. Hosszu, J. Collinge, J. Bieschke

This study uses super-resolution microscopy to observe competing prion protein fibril populations with distinct structures and kinetics, revealing their quasi-species behavior.

bioRxiv · Aug 10, 2022Biophysics