Author

B. Caughey

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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Biochemistry· 3 Biophysics· 2 Pathology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:mouse· 4 Assay:cryo-EM· 3 Research Focus:protein structure prediction· 3 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Approach:deep learning· 1

Frequent Co-Authors

a. kraus· 4 shared A. G. Hughson· 3 shared E. Artikis· 3 shared F. Hoyt· 3 shared B. Hansen· 2 shared B. Race· 2 shared C. L. Schwartz· 2 shared G. J. Raymond· 2 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 44 mutual co-author links

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4 shared papersBiochemistry

a. kraus

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

Neuronal Ndst1 depletion accelerates prion protein clearance and slows neurodegeneration in prion infection

P. Aguilar Calvo, A. Malik, D. Sandoval, C. Barback, C. Orru, H. Standke, O. Thomas, C. Dwyer, D. Pizzo, J. Bapat, K. Soldau, R. Ogawa, M. Riley, P. Nilsson, a. kraus, , C. J. Sigurdson

This study shows that reducing HS sulfation in neurons slows prion disease progression by enhancing prion protein clearance and reducing plaque formation.

bioRxiv · Jun 19, 2023 · PreprintPathology

Cryo-EM of prion strains from the same genotype of host identifies conformational determinants

F. Hoyt, P. Alam, E. Artikis, C. L. Schwartz, A. G. Hughson, B. Race, C. Baune, G. J. Raymond, G. S. Baron, A. Kraus, B. Caughey

The paper determines the near-atomic structure of two prion strains from the same host genotype, revealing conformational differences that underlie strain-specific characteristics.

bioRxiv · Sep 19, 2022Biophysics

Structure of anchorless RML prion reveals motif variation between strains

F. Hoyt, H. G. Standke, E. Artikis, C. L. Schwartz, B. Hansen, K. Li, A. G. Hughson, M. Manca, O. R. Thomas, G. J. Raymond, G. S. Baron, B. Caughey, A. Kraus

Cryo-electron microscopy reveals a near-atomic structure of an infectious, brain-derived murine prion fibril and strain differences.

bioRxiv · Dec 22, 2021 · PreprintBiochemistry

Discovery of Potent Inhibitors of α-Synuclein Aggregation Using Structure-Based Iterative Learning

R. I. Horne, E. Andrzejewska, P. Alam, Z. F. Brotzakis, A. Srivastava, A. Aubert, M. Nowinska, R. C. Gregory, R. Staats, A. Possenti, S. Chia, P. Sormanni, B. Ghetti, B. Caughey, T. P. J. Knowles, M. Vendruscolo

This paper uses structure-based machine learning to identify potent small molecule inhibitors of α-synuclein aggregation, achieving compounds two orders of magnitude more potent than previous reports.

bioRxiv · Nov 10, 2021Biophysics

Structure of an infectious mammalian prion

A. Kraus, F. Hoyt, C. Schwartz, B. Hansen, A. G. Hughson, E. Artikis, B. Race, B. Caughey

This paper determines the structure of an infectious mammalian prion using cryo-electron microscopy, revealing its fibril architecture and molecular features involved in propagation.

bioRxiv · Feb 14, 2021Biochemistry

Brazilin Removes Toxic alpha-Synuclein and Seeding Competent Assemblies from Parkinson Brain by Altering Conformational Equilibrium

G. R. Nahass, Y. Sun, Y. Xu, M. Batchelor, M. Reilly, I. Benilova, N. Kedia, K. Spehar, F. Sobott, R. B. Sessions, B. Caughey, S. E. Radford, P. Jat, J. Collinge, J. Bieschke

This paper shows Brazilin inhibits alpha-synuclein fibril formation and reduces toxicity in Parkinson's disease by altering conformational equilibrium.

bioRxiv · Sep 29, 2020Biochemistry