Author

A. Titz

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 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:bacteria (other)· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Research Focus:protein structure prediction· 1 Approach:statistical model· 1

Frequent Co-Authors

C. Mayer· 2 shared K. Balbuchta· 2 shared M. Borisova· 2 shared A. Engelbrecht· 1 shared A. Imberty· 1 shared A. L. Lovering· 1 shared A. Varrot· 1 shared E. Paci· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersMicrobiology

C. Mayer

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The Glycan-Specificity of the Pineapple Lectin AcmJRL and its Carbohydrate-Dependent Binding of the SARS-CoV-2 Spike Protein

J. Meiers, J. Dastbaz, S. Adam, S. Rasheed, S. H. Kirsch, P. Meiser, P. Gross, R. Mueller, A. Titz

This study identifies high-mannose glycans as the preferred ligands for AcmJRL and shows its carbohydrate-dependent binding to the SARS-CoV-2 spike protein with a low micromolar KD.

bioRxiv · May 27, 2022 · PreprintBiophysics

NamZ1 and NamZ2 from the oral pathogen Tannerella forsythia are peptidoglycan processing exo-β-N-acetylmuramidases with distinct substrate specificity

M. Borisova, K. Balbuchta, A. L. Lovering, A. Titz, C. Mayer

This study identifies two exo-β-N-acetylmuramidases from Tannerella forsythia with distinct substrate specificities, revealing functional diversity in PGN degradation.

bioRxiv · Dec 2, 2021Microbiology

Exo-beta-N-acetylmuramidase NamZ of Bacillus subtilis is the founding member of a family of exo-lytic peptidoglycan hexosaminidases

M. Müller, M. Calvert, I. Hottmann, R. M. Kluj, T. Teufel, K. Balbuchta, A. Engelbrecht, K. A. Selim, Q. Xu, M. Borisova, A. Titz, C. Mayer

The paper identifies NamZ as an exo-{beta}-N-acetylmuramidase in Bacillus subtilis, showing its role in peptidoglycan degradation and proposing it as a founding member of a new family of hexosaminidases.

bioRxiv · Jan 10, 2021Microbiology

Induction of Rare Conformation of Oligosaccharide by Binding to Calcium-dependent Bacterial Lectin: X-ray Crystallography and Modelling Study

M. Lepsik, R. Sommer, S. Kuhaudomlarp, M. Lelimousin, E. Paci, A. Varrot, A. Titz, A. Imberty

The paper uses X-ray crystallography and theoretical chemistry to study how a bacterial lectin stabilizes an unusual oligosaccharide conformation, with implications for designing carbohydrate-based drugs.

bioRxiv · Apr 18, 2019Biophysics