Author

N. Landeck

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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Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Assay:metabolomics· 1

Frequent Co-Authors

A. Beilina· 2 shared A. Mamais· 2 shared J. H. Kluss· 2 shared L. Bonet-Ponce· 2 shared M. R. Cookson· 2 shared R. Kumaran· 2 shared A. Kaganovich· 1 shared C. K. E. Bleck· 1 shared

Activity by Year

2020-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 41 mutual co-author links

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2 shared papersCell Biology

A. Beilina

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2 papers

Recent·Most cited

Pathogenic mutations in LRRK2 sequester Rab8a to damaged lysosomes and regulate transferrin-mediated iron uptake in microglia

A. Mamais, N. Landeck, R. G. Langston, L. Bonet-Ponce, N. Smith, A. Beilina, A. Kaganovich, M. C. Ghosh, L. Pellegrini, J. H. Kluss, R. Kumaran, I. Papazoglou, N. Maio, C. Kim, D. C. Gershlick, M. R. Cookson

This study shows that LRRK2 mutations sequester Rab8a into lysosomes and disrupt transferrin-mediated iron uptake in microglia, linking LRRK2 dysfunction to iron dysregulation in Parkinson's disease.

bioRxiv · Jul 27, 2020 · PreprintCell Biology

LRRK2 mediates tubulation and vesicle sorting from membrane damaged lysosomes

L. Bonet-Ponce, A. Beilina, C. Williamson, E. Lindberg, J. H. Kluss, S. Saez-Atienzar, N. Landeck, R. Kumaran, A. Mamais, C. K. E. Bleck, Y. Li, M. R. Cookson

This study identifies LRRK2's role in lysosomal tubulation and vesicle sorting from damaged lysosomes, introducing the process LYTL.

bioRxiv · Jan 23, 2020Cell Biology