Author

B. Reif

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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Biophysics· 3 Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 4 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 3 Research Focus:host-pathogen & immune response· 1 Assay:protein structure· 1 Organism:zebrafish· 1

Frequent Co-Authors

A. Ramamoorthy· 2 shared M. Faendrich· 2 shared T. Pradhan· 2 shared U. Hegenbart· 2 shared B. P. C. Hazenberg· 1 shared B. Sahoo· 1 shared C. Goebl· 1 shared C. Hartlmueller· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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2 shared papersBiophysics

A. Ramamoorthy

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Author profile →

5 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

Conformational Tuning of Amylin by Charged Styrene-maleic-acid Copolymers

B. Sahoo, C. Souders, T. Nakayama, Z. Deng, H. Linton, S. Suladze, M. Ivanova, B. Reif, T. Ando, C. Martyniuk, A. Ramamoorthy

This study shows that charged styrene-maleic-acid copolymers alter amylin aggregation and conformation, with SMAQA inhibiting fibrillation and SMAEA accelerating it.

bioRxiv · Apr 23, 2020Biophysics

Small Molecule Induced Toxic Human-IAPP Species Characterized by NMR

S. Cox, D. Rodriguez Camargo, Y.-H. Lee, M. I. Ivanova, V. Padmini, B. Reif, A. Ramamoorthy

This study shows CurDAc inhibits hIAPP aggregation and disaggregates fibers, producing a toxic oligomer.

bioRxiv · Nov 24, 2019Biophysics

Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A

C. Goebl, V. Morris, L. van Dam, M. Visscher, P. Polderman, C. Hartlmueller, H. de Ruiter, M. Hora, L. Liesinger, R. Birner-Gruenberger, H. Vos, B. Reif, T. Madl, T. Dansen

This study shows that cysteine oxidation in p16INK4A leads to amyloid fibril formation, which inactivates its tumor suppressor function.

bioRxiv · Jan 2, 2019Biochemistry