Author

R. Rosenzweig

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· 2 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 3 Approach:biophysical modeling· 2 Research Focus:cell signaling & trafficking· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Assay:protein structure· 2 Assay:proteomics· 2

Frequent Co-Authors

G. Zoltsman· 2 shared O. Faust· 2 shared A. S. Wentink· 1 shared B. Bukau· 1 shared C. Sizun· 1 shared C.-A. Richard· 1 shared H. Hofmann· 1 shared I. Petrovic· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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2 shared papersBiochemistry

G. Zoltsman

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A unique chaperoning mechanism in Class A JDPs recognizes and stabilizes mutant p53.

G. Zoltsman, T. L. Dang, M. Kuchersky, O. Faust, M. S. Silva, T. Ilani, A. S. Wentink, B. Bukau, R. Rosenzweig

This study identifies a unique chaperoning mechanism in class-A JDPs that recognizes and stabilizes mutant p53, promoting cancer progression by preventing its degradation.

bioRxiv · Nov 28, 2023Biochemistry

Structural study of UFL1-UFC1 interaction uncovers the importance of UFL1 N-terminal helix for ufmylation

S. Banerjee, J. K. Varga, M. Kumar, G. Zoltsman, M. N. Isupov, R. Rosenzweig, O. Schueler-Furman, R. Wiener

This study reveals the role of UFL1's N-terminal helix in binding UFC1 and ufmylation, uncovering a helix-mediated regulatory mechanism in the E1-E2-E3 cascade.

bioRxiv · Sep 15, 2022 · PreprintBiochemistry

Hsp40s display class-specific binding profiles, serving complementary roles in the prevention of tau amyloid formation

R. Irwin, O. Faust, I. Petrovic, S. G. Wolf, H. Hofmann, R. Rosenzweig

This study shows DNAJA2 and DNAJB1 prevent tau amyloid formation by binding distinct tau species, while HSPB1 only binds monomers, revealing complementary roles of Hsp40 chaperones in tau aggregation prevention.

bioRxiv · Apr 11, 2021 · PreprintBiophysics

Tetramerization of Phosphoprotein is essential for Respiratory Syncytial virus budding while its N terminal region mediates direct interactions with the Matrix protein.

M. Bajorek, M. Galloux, C.-A. Richard, O. Szekely, R. Rosenzweig, C. Sizun, J.-F. Elcouët

This paper identifies the tetrameric structure of the Phosphoprotein (P) as essential for RSV budding and shows its direct interaction with the Matrix (M) protein during assembly.

bioRxiv · Nov 17, 2020Microbiology