Author

H. Shaykhalishahi

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

Biology Disciplines

Click to filter author papers

Bioengineering· 1 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Organism:Drosophila· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Organism:mouse· 1

Frequent Co-Authors

A. K. Buell· 2 shared D. Willbold· 2 shared W. Hoyer· 2 shared A. Nagpal· 1 shared A. Voigt· 1 shared B. H. Falkenburger· 1 shared B. Strodel· 1 shared B. Uluca· 1 shared

Activity by Year

2017-2019 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBioengineering

A. K. Buell

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

An engineered monomer binding-protein for α-synucleinefficiently inhibits the proliferation of amyloid fibrils

E. D. Agerschou, T. Saridaki, P. Flagmeier, C. Galvagnion, D. Komnig, A. Nagpal, N. Gasterich, L. Heid, V. Prasad, H. Shaykhalishahi, A. Voigt, D. Willbold, C. M. Dobson, B. H. Falkenburger, W. Hoyer, A. K. Buell

The paper engineers a monomer-binding protein that inhibits α-synuclein fibril proliferation in vitro and in vivo, showing it reduces aggregates and related pathologies.

bioRxiv · Mar 5, 2019Bioengineering

A structural and kinetic link between membrane association and amyloid fibril formation of α-Synuclein

T. Viennet, M. M. Wördehoff, B. Uluca, C. Poojari, H. Shaykhalishahi, D. Willbold, B. Strodel, H. Heise, A. K. Buell, W. Hoyer, M. Etzkorn

This study investigates how α-Synuclein interacts with membrane surfaces and how these interactions influence its aggregation into amyloid fibrils.

bioRxiv · Aug 8, 2017Biophysics