Author

L. Mach

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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Biochemistry· 1 Pharmacology & Toxicology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Organism:plant (other)· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. C. Rufer· 1 shared A. Mirazimi· 1 shared B. L. Hoare· 1 shared C. Gruenwald-Gruber· 1 shared C. Oostenbrink· 1 shared D. A. Sykes· 1 shared D. B. Veprintsev· 1 shared D. Maresch· 1 shared

Activity by Year

2021-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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1 shared paperPharmacology & Toxicology

A. C. Rufer

Mutual co-authors in cluster

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3 papers

Recent·Most cited

A universal cannabinoid CB1 and CB2 receptor TR-FRET kinetic ligand binding assay.

L. Borrega-Roman, B. L. Hoare, M. Kosar, R. C. Sarott, K. J. Patej, J. Bouma, M. Scott-Dennis, E. J. Koers, T. Gazzi, L. Mach, S. Barrondo, J. Salles, W. Guba, E. Kusznir, M. Nazare, , D. B. Veprintsev

This paper develops a TR-FRET-based assay to measure ligand binding kinetics for CB1R and CB2R, finding that D77 enables accurate determination of on- and off-rates for various agonists and antagonists.

bioRxiv · Jul 16, 2024Pharmacology & Toxicology

SBT5.2s are the major active extracellular subtilases processing IgG antibody 2F5 in the Nicotiana benthamiana apoplast

K. Beritza, P. Buscaill, S.-J. Song, P. V. Jutras, J. Huang, L. Mach, S. Dong, R. van der Hoorn

The paper shows that SBT5.2 subtilases degrade the IgG antibody 2F5 in Nicotiana benthamiana apoplast, and their knockout increases 2F5 accumulation without affecting plant growth.

bioRxiv · Apr 7, 2024 · PreprintPlant Biology

Structure-guided glyco-engineering of ACE2 for improved potency as soluble SARS-CoV-2 decoy receptor

T. Capraz, N. F. Kienzl, E. Laurent, J. W. Perthold, E. Foederl-Hoebenreich, C. Gruenwald-Gruber, D. Maresch, V. Monteil, J. Niederhoefer, G. Wirnsberger, A. Mirazimi, K. Zatloukal, L. Mach, J. M. Penninger, C. Oostenbrink, J. Stadlmann

This study engineers ACE2 glycosylation to enhance its binding to SARS-CoV-2 Spike protein, resulting in a more potent decoy receptor for COVID-19 treatment.

bioRxiv · Aug 31, 2021Biochemistry