Author

T. Kupreichyk

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· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Approach:experimental assay· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1

Frequent Co-Authors

D. Willbold· 2 shared L. Gremer· 2 shared W. Hoyer· 2 shared C. Roeder· 1 shared D. Fenel· 1 shared E. Colas Debled· 1 shared G. F. Schroeder· 1 shared G. Schoehn· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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2 shared papersBiophysics

D. Willbold

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Author profile →

2 papers

Recent·Most cited

Structural Basis for the Inhibition of IAPP Fibril Formation by the Hsp60 Co-Chaperonin Prefoldin

R. Toerner, T. Kupreichyk, L. Gremer, E. Colas Debled, D. Fenel, P. Gans, D. Willbold, G. Schoehn, W. Hoyer, J. Boisbouvier

This study shows how prefoldin inhibits IAPP fibril formation by binding to the N-terminal segment of IAPP on fibril surfaces and ends, reducing aggregate size and number.

bioRxiv · Oct 20, 2021Biophysics

Amyloid fibril structure of islet amyloid polypeptide by cryo-electron microscopy reveals similarities with amyloid beta

C. Roeder, T. Kupreichyk, L. Gremer, L. U. Schaefer, K. R. Pothula, R. B. Ravelli, D. Willbold, W. Hoyer, G. F. Schroeder

This study uses cryo-EM to reveal the structure of IAPP fibrils, showing similarities with Aβ polymorphs and linking genetic mutations to amyloid formation.

bioRxiv · Feb 11, 2020Biochemistry