Author

S. H. Schmidt

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· 3

Signature Assays, Organisms & Methods

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Organism:human· 3 Research Focus:drug response / drug discovery· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:mechanistic / dynamical model· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

F. W. Herberg· 3 shared S. Knapp· 3 shared J.-H. Weng· 2 shared P. C. Aoto· 2 shared S. Mathea· 2 shared S. S. Taylor· 2 shared A. Kortholt· 1 shared A. Soliman· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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3 shared papersBiochemistry

F. W. Herberg

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Author profile →

3 papers

Recent·Most cited

Two helices control the dynamic crosstalk between the catalytic domains of LRRK2

J.-H. Weng, P. C. Aoto, R. Lorenz, J. Wu, S. H. Schmidt, J. T. Manschwetus, P. Kaila-Sharma, S. Mathea, S. Knapp, F. W. Herberg, S. S. Taylor

The paper identifies two helices that regulate the conformation and function of the kinase domain in LRRK2 through dynamic crosstalk.

bioRxiv · Sep 29, 2021 · PreprintBiochemistry

Nanobodies as allosteric modulators of Parkinson's disease-associated LRRK2

R. K. Singh, A. Soliman, G. Guaitoli, E. Störmer, F. von Zweydorf, T. Dal Maso, L. Van Rillaer, S. H. Schmidt, D. Chatterjee, E. Pardon, S. Knapp, E. J. Kennedy, J. Steyaert, F. W. Herberg, A. Kortholt, , W. Versees

This study identifies and characterizes Nanobodies that modulate LRRK2 activity through non-ATP-competitive mechanisms, offering new tools for Parkinson's disease research and therapy.

bioRxiv · Aug 30, 2021Biochemistry

Conformation and dynamics of the kinase domain drive subcellular location and activation of LRRK2

S. H. Schmidt, J.-H. Weng, P. C. Aoto, D. Boassa, S. Mathea, S. Silletti, J. Hu, M. Wallbott, E. A. Komives, S. Knapp, F. W. Herberg, S. S. Taylor

This study investigates how Parkinson's Disease mutations affect LRRK2 activation and subcellular localization through conformational changes and domain interactions.

bioRxiv · Jul 13, 2020Biochemistry