Author

U. Hegenbart

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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Approach:experimental assay· 2 Organism:human· 2 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1

Frequent Co-Authors

B. Reif· 2 shared M. Faendrich· 2 shared T. Pradhan· 2 shared B. P. C. Hazenberg· 1 shared C. Haupt· 1 shared J. Bijzet· 1 shared J. Schoenfelder· 1 shared K. Annamalai· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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2 shared papersBiochemistry

B. Reif

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2 papers

Recent·Most cited

Protease Resistance of ex vivo Amyloid Fibrils implies the proteolytic Selection of disease-associated Fibril Morphologies

J. Schoenfelder, P. B. Pfeiffer, T. Pradhan, J. Bijzet, B. P. C. Hazenberg, S. O. Schoenland, U. Hegenbart, B. Reif, C. Haupt, M. Faendrich

The paper shows ex vivo amyloid fibrils are more protease stable than in vitro fibrils, supporting the proteolytic selection hypothesis for disease-associated fibril morphologies.

bioRxiv · Jul 5, 2021Biochemistry

Amyloidogenic core of a human {lambda}-III immunoglobulin light chain fibril and their germline variants probed by MAS solid state NMR

T. Pradhan, K. Annamalai, R. Sarkar, S. Huhn, U. Hegenbart, S. Schoenland, M. Faendrich, B. Reif

This study uses MAS solid-state NMR to analyze the structure of amyloid fibrils from a human lambda-III immunoglobulin light chain and identifies a key mutation affecting fibril conformation.

bioRxiv · Oct 2, 2020 · PreprintBiophysics