Author

L. Winter

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· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Organism:E. coli· 1 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

A. Vogt· 1 shared C. J. Day· 1 shared C. Siligan· 1 shared D. G. Knyazev· 1 shared H.-G. Koch· 1 shared J. M. Atack· 1 shared J. Poole· 1 shared J. R. L. Timms· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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1 shared paperBiophysics

A. Vogt

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2 papers

Recent·Most cited

YidC from Escherichia coli forms an ion-conducting pore upon activation by ribosomes.

D. G. Knyazev, L. Winter, A. Vogt, S. Posch, C. Siligan, N. Goessweiner-Mohr, N. Hagleitner-Ertugrul, H.-G. Koch, P. Pohl

The paper shows that E. coli YidC forms an ion-conducting pore when bound to a ribosome or ribosome-nascent chain complex, suggesting an alternative mechanism for membrane protein insertion.

bioRxiv · May 10, 2023Biophysics

The non-typeable Haemophilus influenzae major adhesin Hia is a dual function lectin that binds to human-specific respiratory tract sialic acid glycan receptors.

J. M. Atack, C. J. Day, J. Poole, K. Brockman, J. R. L. Timms, L. Winter, T. Haselhorst, L. O. Bakaletz, S. J. Barenkamp, M. P. Jennings

This paper identifies Hia, a major adhesin in NTHi, as a dual-function lectin that binds to human-specific sialic acid glycans, mimicking the combined activity of HMW1 and HMW2 adhesins.

bioRxiv · May 8, 2020Microbiology