Author

I. Nehlmeier

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Microbiology· 3 Immunology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 4 Organism:human· 2 Organism:mouse· 1 Assay:proteomics· 1

Frequent Co-Authors

M. Hoffmann· 2 shared S. Pöhlmann· 2 shared A. Cossmann· 1 shared A. Dopfer-Jablonka· 1 shared A. Kempf· 1 shared A. Klippert· 1 shared A. M. Kempf· 1 shared A. Stevaert· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersImmunology

M. Hoffmann

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Macrophage- and CD4+ T cell-derived SIV differ in glycosylation, infectivity and neutralization sensitivity

C. B. Karsten, F. F. R. Buttner, S. Cajic, I. Nehlmeier, B. Roshani, A. Klippert, U. Sauermann, N. Stolte-Leeb, U. Reichl, R. Gerardy-Schahn, E. Rapp, C. Stahl-Hennig, S. Pohlmann

This study compares glycosylation, infectivity, and neutralization sensitivity of SIV produced in macrophages versus CD4+ T cells, revealing differences in glycan profiles and their impact on viral spread and antibody neutralization.

bioRxiv · Jan 2, 2024Microbiology

TMPRSS2 is essential for SARS-CoV-2 Beta and Omicron infection

K. Metzdorf, H. Jacobsen, M. C. Greweling-Pils, M. Hoffmann, T. Lueddecke, F. Miller, L. Melcher, A. M. Kempf, I. Nehlmeier, D. Bruder, M. Widera, S. Ciesek, S. Poehlmann, L. Cicin-Sain

The paper shows TMPRSS2 is essential for SARS-CoV-2 Beta and Omicron infection in mice, highlighting its role as an antiviral target.

bioRxiv · Dec 9, 2022Immunology

The Omicron variant is highly resistant against antibody-mediated neutralization - implications for control of the COVID-19 pandemic

M. Hoffmann, N. Krüger, S. Schulz, A. Cossmann, C. Rocha, A. Kempf, I. Nehlmeier, L. Graichen, A.-S. Moldenhauer, M. S. Winkler, M. Lier, A. Dopfer-Jablonka, H.-M. Jäck, G. Behrens, S. Pöhlmann

This study shows the Omicron variant is highly resistant to antibody neutralization, reducing effectiveness of current therapies and vaccines.

bioRxiv · Dec 12, 2021Microbiology

Evidence for influenza B virus hemagglutinin adaptation to the human host: high cleavability, acid-stability and preference for cool temperature

M. Laporte, A. Stevaert, V. Raeymaekers, T. Boogaerts, I. Nehlmeier, W. Chiu, M. Benkheil, B. Vanaudenaerde, S. Pöhlmann, L. M. Naesens

This study compares influenza B virus (IBV) and influenza A virus (IAV) hemagglutinin (HA) adaptation to human airways, finding IBV HA is more cleavable, acid-stable, and temperature-preferred for human upper airways.

bioRxiv · Aug 23, 2019 · PreprintMicrobiology