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

Click to filter author papers

Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

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

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 papersBiophysics

D. Willbold

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

BiophysicsbioRxivOct 20, 2021

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

R. Toerner, T. Kupreichyk, L. Gremer…·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.

DOI 10.1038/s41467-022-30042-y

structural biologyexperimental assay

𝕏 PostBluesky

BiochemistrybioRxivFeb 11, 2020

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

C. Roeder, T. Kupreichyk, L. Gremer…·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.

DOI 10.1038/s41594-020-0442-4

humancryo-EM

𝕏 PostBluesky