Author

H. Wille

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:mouse· 3 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

A. M. Sevillano· 1 shared A. Sriraman· 1 shared C. Kim· 1 shared D. A. Kramer· 1 shared D. McKenzie· 1 shared E. Biasini· 1 shared E. Chimal-Juarez· 1 shared E. Monleon· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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1 shared paperBiochemistry

A. M. Sevillano

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Author profile →

3 papers

Recent·Most cited

Fibronectin: a natural barrier against prion infection

M. C. Garza, S. G. Kang, C. Kim, E. Monleon, J. van der Merwe, D. A. Kramer, R. Fahlman, V. Sim, J. Aiken, D. McKenzie, L. M. Cortez, H. Wille

This study identifies fibronectin as a natural barrier against prion infection by showing its association with PrPSc and its ability to reduce prion infectivity in vitro and in tissues.

bioRxiv · Aug 31, 2023 · PreprintBiochemistry

Rational design of structure-based vaccines targeting misfolded alpha-synuclein conformers of Parkinson's disease and related disorders

J. M. Flores-Fernandez, V. Pesch, A. Sriraman, E. Chimal-Juarez, S. Amidian, X. Wang, S. Reithofer, L. Ma, G. Tamgueney, H. Wille

This paper designs vaccines targeting misfolded alpha-synuclein by mimicking its fibril structure, inducing antibodies that recognize pathological forms without reacting to native protein.

bioRxiv · Jun 30, 2023Biochemistry

Full Atomistic Model Of Prion Structure And Conversion

G. Spagnolli, M. Rigoli, S. Orioli, A. M. Sevillano, P. Faccioli, H. Wille, E. Biasini, J. R. Requena

The paper builds the first atomic-resolution model of mouse PrPSc using experimental data and computational methods, simulating the conversion of PrPC to PrPSc and providing a physically-coherent mechanism for prion propagation.

bioRxiv · Dec 22, 2018Biochemistry