Author

B. M. Hällberg

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· 2 Biochemistry· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell type annotation· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

B. Murrell· 2 shared D. J. Sheward· 2 shared G. M. McInerney· 2 shared H. Das· 2 shared L. Hanke· 2 shared A. Gruzinov· 1 shared A. Motso· 1 shared A. Rising· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersImmunology

B. Murrell

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

BiophysicsbioRxivSep 28, 2022

Mass spectrometry of RNA-binding proteins during liquid-liquid phase separation reveals distinct assembly mechanisms and droplet architectures

C. Sahin, A. Motso, X. Gu…·M. Landreh

The paper uses mass spectrometry and simulations to study phase separation of RNA-binding proteins, revealing distinct assembly mechanisms and droplet structures.

DOI 10.1021/jacs.3c00932

proteomicsexperimental assay

𝕏 PostBluesky

ImmunologybioRxivPreprintJan 3, 2022

Structural basis of Omicron neutralization by affinity-matured public antibodies

D. J. Sheward, P. Pushparaj, H. Das…·B. M. Hällberg

The paper identifies affinity-matured antibodies that neutralize SARS-CoV-2 Omicron with high potency and resolves their structure to explain cross-neutralization.

DOI 10.1101/2022.01.03.474825

humanproteomics

𝕏 PostBluesky

BiochemistrybioRxivPreprintJun 9, 2021

A dual allosteric pathway drives human mitochondrial Lon

G. Valentin Gese, S. Shahzad, C. Pardo-Hernandez…·B. M. Hällberg

This study reveals the dual allosteric mechanism of human mitochondrial Lon protease through cryo-EM and biochemistry, showing how coordinated ATP hydrolysis and substrate translocation occur.

DOI 10.1101/2021.06.09.447696

humancryo-EM

𝕏 PostBluesky

BiophysicsbioRxivJun 23, 2020

Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2

T. F. Custodio, H. Das, D. J. Sheward…·C. Löw

This study isolates and characterizes synthetic nanobodies that neutralize SARS-CoV-2, identifying Sb23 with high affinity and neutralization activity.

DOI 10.1038/s41467-020-19204-y

virusprotein structure

𝕏 PostBluesky