Author
H. Stahlberg
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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2017-2023 · peak 6/yrCo-Author Collaboration Network
10 top collaborators · 21 mutual co-author links22 papers
Recent·Most cited
- MicrobiologybioRxivPreprintDOI 10.1101/2023.07.18.549530
- MicrobiologybioRxiv
Structure of a membrane-bound menaquinol:organohalide oxidoreductase
L. Cimmino, A. G. Duarte, D. Ni…·J. Maillard
The paper presents the first cryo-EM structure of a functional menaquinol:organohalide oxidoreductase from Desulfitobacterium hafniense, revealing its mechanism of electron transfer and energy conservation during organohalide respiration.
DOI 10.1038/s41467-023-42927-7 - ImmunologybioRxiv
Cryo-EM structures and binding of mouse and human ACE2 to SARS-CoV-2 variants of concern indicate that mutations enabling immune escape could expand host range
D. Ni, P. Turelli, B. Beckert…·K. Lau
The paper reports cryo-EM structures of mouse ACE2 bound to SARS-CoV-2 VOC Spike proteins, showing mutations enabling immune escape may expand host range.
- BioengineeringbioRxivPreprint
De novo design of site-specific protein interactions with learned surface fingerprints
P. Gainza, S. Wehrle, A. Van Hall-Beauvais…·B. E. Correia
This paper designs novel protein interactions using geometric deep learning to generate surface fingerprints, achieving nanomolar affinity for four targets through computational and experimental methods.
DOI 10.1101/2022.06.16.496402 - ImmunologybioRxivPreprint
SARS-CoV-2 Omicron potently neutralized by a novel antibody with unique Spike binding properties
C. Fenwick, P. Turelli, D. Ni…·G. Pantaleo
This paper identifies a potent human monoclonal antibody, P2G3, that neutralizes multiple SARS-CoV-2 variants including Omicron, and demonstrates its protective efficacy in a monkey model.
DOI 10.1101/2022.03.18.484873 - ImmunologybioRxivPreprint
Structural analysis of the Spike of the Omicron SARS-COV-2 variant by cryo-EM and implications for immune evasion.
D. Ni, K. Lau, P. Turelli…·D. Trono
The paper reports cryo-EM structures of mouse ACE2 bound to Spike proteins of four SARS-CoV-2 variants, revealing mutations that enhance binding and immune evasion.
- MicrobiologybioRxiv
Structural and molecular determinants for the interaction of ExbB from Serratia marcescens and HasB, a TonB paralog
V. Biou, R. J. D. Adaixo, M. Chami…·P. Delepelaire
The paper determines the cryo-EM structures of ExbBSm and ExbB-ExbDSm complex, identifies key residues for function and interaction with TonB/HasB, and reveals the role of ExbBSm extension in heme acquisition.
DOI 10.1038/s42003-022-03306-y - BiochemistrybioRxivPreprint
Insight into Lipopolysaccharide Translocation by Cryo-EM structures of a LptDE Transporter in Complex with Pro-Macrobodies
M. Botte, D. Ni, S. Schenck…·M. Hennig
The paper uses cryo-EM to determine structures of the LptDE transporter complex with Pro-Macrobodies, revealing partially and fully opened states of the transporter during LPS translocation.
DOI 10.1101/2021.03.23.436624 - BiophysicsbioRxiv
Structures of ABCG2 under turnover conditions reveal a key step in drug transport mechanism
Q. Yu, D. Ni, J. Kowal…·K. P. Locher
This study presents cryo-EM structures of ABCG2 under turnover conditions, revealing conformational changes that elucidate the transport mechanism and substrate specificity.
- BiophysicsbioRxiv
Structural basis of drug recognition by the multidrug transporter ABCG2
J. Kowal, D. Ni, S. Jackson…·K. P. Locher
This study presents cryo-EM structures of ABCG2 bound to anticancer drugs, revealing how it recognizes and binds exogenous compounds and the structural basis for drug-induced ATPase activity.
- Molecular BiologybioRxivPreprint
Cryo-EM structural studies of the agonist complexed human TRPV4 ion-channel reveals novel structural rearrangements resulting in an open-conformation
M. Botte, A. K. C. Ulrich, R. Adaixo…·S. J. Holton
This paper reports the cryo-EM structure of hTRPV4 in an open conformation induced by 4-PDD agonist, revealing molecular mechanisms of activation and providing a template for inhibitor design.
DOI 10.1101/2020.10.13.334797 - BiophysicsbioRxivPreprint
Structural investigation of ACE2 dependent disassembly of the trimeric SARS-CoV-2 Spike glycoprotein
D. Ni, K. Lau, F. Lehmann…·H. Stahlberg
This study uses cryo-EM to show that hACE2 binding causes SARS-CoV-2 Spike trimer disassembly and S1 domain rearrangement, suggesting a mechanism for soluble hACE2's therapeutic effect.
- Cell BiologybioRxiv
The architecture of the centriole cartwheel-containing region revealed by cryo-electron tomography
N. Klena, M. Le Guennec, A.-M. Tassin…·P. Guichard
This study uses cryo-electron tomography to reveal the architectural diversity of the centriole cartwheel region across four species, showing structural variations in periodicity and organization.
- BiochemistrybioRxivPreprint
Determinants for forming a supramolecular myelin-like proteolipid lattice
S. Ruskamo, O. C. Krokengen, J. Kowal…·P. Kursula
This study uses structural and functional analyses to reveal how myelin protein P2 forms a supramolecular lattice between lipid bilayers, identifying key residues and interactions involved in membrane binding.
- BiophysicsbioRxiv
Retrieving High-Resolution Information from Disordered 2D Crystals by Single Particle Cryo-EM
R. Righetto, N. Biyani, J. Kowal…·H. Stahlberg
The paper develops a method to improve resolution and resolve conformational heterogeneity in 2D crystals using single-particle refinement, achieving 4 Å resolution for the MloK1 potassium channel.
DOI 10.1038/s41467-019-09661-5 - BiophysicsbioRxiv
Microfluidic protein isolation and sample preparation for high resolution cryo-EM
C. Schmidli, S. Albiez, L. Rima…·T. Braun
This paper introduces a microfluidic method for isolating and preparing proteins for cryo-EM, enabling high-resolution structure determination from minimal cell lysate.
- BiochemistrybioRxiv
Cryo-EM structure of the rhodopsin-Gαi-βγ complex reveals binding of the rhodopsin C-terminal tail to the Gβ subunit
C.-J. Tsai, J. Marino, R. J. Adaixo…·G. F. Schertler
The paper presents a cryo-EM structure of the rhodopsin-Gαi-βγ complex, revealing the C-terminal tail of rhodopsin bound to the Gβ subunit and identifying common anchoring points across G protein-subtype interactions.
DOI 10.7554/elife.46041 - BiochemistrybioRxiv
Molecular structure and function of myelin protein P0 in membrane stacking
A. Raasakka, S. Ruskamo, J. Kowal…·P. Kursula
This study characterizes the molecular structure and function of myelin protein P0, showing how its extracellular domains stack lipid membranes and stabilize the intraperiod line in peripheral myelin.
DOI 10.1038/s41598-018-37009-4 - BiophysicsbioRxiv
Focus: The interface between data collection and data processing in cryo-EM
N. Biyani, R. D. Righetto, R. McLeod…·H. Stahlberg
Focus is a software package that streamlines cryo-EM data collection and processing by integrating data import, management, and real-time monitoring in a user-friendly environment.
DOI 10.1016/j.jsb.2017.03.007 - BiophysicsbioRxiv
Image processing techniques for high-resolution structure determination from badly ordered 2D crystals
N. Biyani, S. Scherer, R. D. Righetto…·H. Stahlberg
The paper develops image-processing algorithms to improve 3D structure determination from badly ordered 2D crystals, achieving resolution improvements to approximately 5 Å.
DOI 10.1016/j.jsb.2018.03.013