Author

C. J. Gloeckner

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· 4 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 3 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1

Frequent Co-Authors

G. Guaitoli· 5 shared A. Kortholt· 3 shared F. von Zweydorf· 3 shared F. Raimondi· 2 shared F. Y. Ho· 2 shared W. Versees· 2 shared X. Zhang· 2 shared A. A. Skodras· 1 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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5 shared papersBiochemistry

G. Guaitoli

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Author profile →

6 papers

Recent·Most cited

Structural insights in the GTP-driven monomerization and activation of a bacterial LRRK2 homologue using allosteric nanobodies

C. Galicia, G. Guaitoli, M. Fislage, C. J. Gloeckner, W. Versees

This paper solves the structure of a bacterial Roco protein in its GTP-bound state using cryo-EM and nanobodies, revealing conformational changes and allosteric activation mechanisms.

bioRxiv · Nov 13, 2023 · PreprintBiochemistry

Biophysical analysis reveals autophosphorylation as an important negative regulator of LRRK2 dimerization

G. Guaitoli, X. Zhang, F. Saitta, P. Miglionico, L. M. Silbermann, F. Y. Ho, F. von Zweydorf, M. Signorelli, K. Tych, D. Fessas, F. Raimondi, A. Kortholt, C. J. Gloeckner

This study uses biophysical methods to show that autophosphorylation inhibits LRRK2 dimerization, suggesting it as a negative regulator with implications for Parkinson's disease.

bioRxiv · Aug 11, 2023 · PreprintBiochemistry

Intramolecular feedback regulation of the LRRK2 Roc G domain by a LRRK2 kinase dependent mechanism

B. K. Gilsbach, F. Y. Ho, B. Riebenbauer, X. Zhang, G. Guaitoli, A. Kortholt, C. J. Gloeckner

This study identifies a kinase-dependent negative feedback mechanism regulating LRRK2 Roc G domain activity through autophosphorylation of T1343, affecting GTP hydrolysis kinetics.

bioRxiv · Jul 31, 2023 · 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

Sirtuin-1 Sensitive Lysine-136 Acetylation Drives Phase Separation and Pathological Aggregation of TDP-43

J. Garcia Morato, F. Hans, F. von Zweydorf, R. Feederle, S. J. Elsaesser, A. A. Skodras, C. J. Gloeckner, E. Buratti, M. Neumann, P. J. Kahle

This study identifies K136 acetylation as a key modifier of TDP-43's RNA binding and phase separation, leading to pathological aggregation, and shows SIRT1's role in deacetylating and reducing this aggregation.

bioRxiv · May 26, 2020 · PreprintCell Biology

Allosteric structural alterations and auto-regulation of Rab5 GEF activity in Rabex5

J. Lauer, A. Cezanne, G. Guaitoli, F. Raimondi, M. Gentzel, V. Alva, M. Habeck, M. Ueffing, A. N. Lupas, C. J. Gloeckner, M. Zerial

This study reevaluates the autoinhibition mechanism of Rabex5 by analyzing structural changes and nucleotide exchange activity, revealing new regulatory roles for Ubiquitin binding domains.

bioRxiv · Feb 27, 2019 · PreprintBiophysics