Author

S. Mathea

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· 8 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 9 Organism:human· 8 Research Focus:protein folding & dynamics· 6 Assay:proteomics· 5 Research Focus:cell signaling & trafficking· 3 Research Focus:drug response / drug discovery· 3 Research Focus:cell type annotation· 2 Assay:cryo-EM· 2

Frequent Co-Authors

S. Knapp· 8 shared D. Chatterjee· 5 shared A. E. Leschziner· 4 shared S. L. Reck-Peterson· 3 shared V. Dederer· 3 shared A. Karapetsas· 2 shared A. U. Malik· 2 shared D. R. Alessi· 2 shared

Activity by Year

2020-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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8 shared papersBiochemistry

S. Knapp

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Author profile →

10 papers

Recent·Most cited

Mechanism of human PINK1 activation at the TOM complex in a reconstituted system

O. Raimi, H. Ojha, K. Ehses, V. Dederer, S. Lange, C. P. Rivera, T. Deegan, Y. Chen, M. Wightman, R. Toth, K. Labib, S. Mathea, N. Ranson, R. Fernandez-Busnadiego, M. Muqit

This study identifies TOM20, TOM70, TOM40, and associated subunits as critical for PINK1 activation in a reconstituted yeast system, providing insights for PINK1 activator development.

bioRxiv · Dec 23, 2023Biochemistry

Development of LRRK2 designed ankyrin-repeat proteins

V. Dederer, M. Sanz Murillo, E. P. Karasmanis, K. S. Hatch, D. Chatterjee, F. Preuss, K. R. Abdul Azeez, L. V. Nguyen, C. Galicia, B. Dreier, A. Pluckthun, W. Versees, S. Mathea, A. E. Leschziner, S. L. Reck-Peterson, S. Knapp

This study develops a high-affinity DARPin that binds to LRRK2's WD40 domain, improving structural analysis and revealing its role in disrupting LRRK2 filaments and Rab8A phosphorylation.

bioRxiv · Nov 14, 2023Biochemistry

Inhibition of Parkinsons Disease-related LRRK2 by type-I and type-II kinase inhibitors: activity and structures

A. E. Leschziner, M. Sanz Murillo, A. V. Suarez, V. Dederer, D. Chatterjee, J. A. Louro, S. Knapp, S. Mathea

This study presents cryo-EM structures of LRRK2 bound to type-I and type-II inhibitors, revealing conformational changes and providing a basis for inhibitor design.

bioRxiv · Sep 7, 2023Biophysics

Structure of LRRK1 and mechanisms of autoinhibition and activation

J. M. Reimer, A. M. Dickey, Y. X. Lin, R. G. Abrisch, S. Mathea, D. Chatterjee, E. J. Fay, M. D. Daugherty, S. L. Reck-Peterson, A. E. Leschziner

This study solves cryo-EM structures of LRRK1 in monomeric and dimeric forms, revealing distinct autoinhibition mechanisms compared to LRRK2 and their evolutionary context.

bioRxiv · Nov 22, 2022Biochemistry

PKC isoforms activate LRRK1 kinase by phosphorylating conserved residues (Ser1064, Ser1074 and Thr1075) within the CORB GTPase domain

A. U. Malik, A. Karapetsas, R. S. Nirujogi, D. Chatterjee, T. K. Phung, M. Wightman, R. Gourlay, N. Morrice, S. Mathea, S. Knapp, D. R. Alessi

This study identifies that PKC isoforms activate LRRK1 by phosphorylating specific residues in the CORB GTPase domain, enhancing kinase activity.

bioRxiv · Jun 9, 2022Biochemistry

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

Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

A. U. Malik, A. Karapetsas, R. S. Nirujogi, S. Mathea, P. Pal, P. Lis, M. Taylor, E. Purlyte, R. Gourlay, M. Dorward, S. Weidlich, R. Toth, N. K. Polinski, S. Knapp, F. Tonelli, D. R. Alessi

This study identifies distinct Rab proteins phosphorylated by LRRK1 and LRRK2, showing they are regulated by different mechanisms and respond differently to inhibitors.

bioRxiv · Nov 25, 2020Biochemistry

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

Nucleotide binding, evolutionary insights and interaction partners of the pseudokinase Unc-51-like kinase 4

F. Preuss, D. Chatterjee, S. Mathea, S. Shrestha, J. St-Germain, M. Saha, N. Kannan, B. Raught, R. Rottapel, S. Knapp

This study presents the structure of ULK4-ATPγS complex, identifies disease mutations affecting ATP binding, and reveals ULK4's interaction partners and evolutionary adaptations.

bioRxiv · Jun 18, 2020Biochemistry

Parkinson's Disease-linked LRRK2 structure and model for microtubule interaction

C. K. Deniston, J. Salogiannis, S. Mathea, D. M. Snead, I. Lahiri, O. Donosa, R. Watanabe, J. Böhning, A. K. Shiau, S. Knapp, E. Villa, S. L. Reck-Peterson, A. E. Leschziner

This study reports the structure of LRRK2 and its interaction with microtubules, showing that its conformation regulates binding and affects motor protein function.

bioRxiv · Jan 6, 2020Biophysics