Author

I. Riera-Tur

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Cell Biology· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Approach:microscopy & imaging analysis· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell-cell communication· 1 Assay:cryo-EM· 1

Frequent Co-Authors

I. Dudanova· 3 shared F. U. Hartl· 2 shared M. S. Hipp· 2 shared R. Fernandez-Busnadiego· 2 shared V. A. Trinkaus· 2 shared W. Baumeister· 2 shared A. Bracher· 1 shared A. Martinez-Sanchez· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 32 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersCell Biology

I. Dudanova

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Cell BiologybioRxivJul 16, 2021

The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model

P. Yuste-Checa, V. A. Trinkaus, I. Riera-Tur…·F. U. Hartl

This study shows that Clusterin enhances Tau aggregate seeding in a cellular model by stabilizing soluble seed species and facilitating their transfer to recipient cells.

DOI 10.1038/s41467-021-25060-1

proteomicsexperimental assay

𝕏 PostBluesky

Cell BiologyNature CommunicationsPeer-reviewedApr 14, 2021

In situ architecture of neuronal alpha-Synuclein inclusions

V. A. Trinkaus, I. Riera-Tur, A. Martinez-Sanchez…·R. Fernandez-Busnadiego

This study uses cryo-ET to show that neuronal alpha-Synuclein inclusions contain fibrils intermixed with cellular membranes and are nucleated by oligomers.

DOI 10.1038/s41467-021-22108-0

humancryo-EM

𝕏 PostBluesky

Cell BiologybioRxivPreprintDec 16, 2019

Amyloid-like aggregates cause lysosomal defects in neurons via gain-of-function toxicity

I. Riera-Tur, T. Schaefer, D. Hornburg…·I. Dudanova

This study shows that amyloid-like aggregates impair lysosomal function in neurons by sequestering AP-31, leading to neurotoxicity.

DOI 10.1101/2019.12.16.877431

proteomicsimaging

𝕏 PostBluesky