Author

J. Salogiannis

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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Biophysics· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Organism:Arabidopsis· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:gene regulatory network inference· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

S. L. Reck-Peterson· 3 shared A. Aguilar-Maldonado· 1 shared A. E. Leschziner· 1 shared A. K. Shiau· 1 shared A. P. Ryan· 1 shared B. Cao· 1 shared B. V. Tsu· 1 shared C. Beierschmitt· 1 shared

Activity by Year

2020-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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Curved chords = mutual co-authorship

3 shared papersMicrobiology

S. L. Reck-Peterson

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

MicrobiologybioRxivJul 11, 2022

Antiviral function and viral antagonism of the rapidly evolving dynein activating adapter NINL

D. A. Stevens, C. Beierschmitt, S. Mahesula…·M. D. Daugherty

This study identifies NINL as an antiviral innate immune component targeted by viruses through proteolytic cleavage, revealing its role in interferon response and viral antagonism.

DOI 10.7554/elife.81606

humanproteomics

𝕏 PostBluesky

Cell BiologybioRxivPreprintFeb 3, 2020

PxdA interacts with the DipA phosphatase to regulate endosomal hitchhiking of peroxisomes

J. Salogiannis, J. R. Christensen, A. Aguilar-Maldonado…·S. L. Reck-Peterson

The paper identifies PxdA as a specific molecular linker for peroxisome hitchhiking on early endosomes in A. nidulans and reveals DipA as a regulator of this process.

DOI 10.1101/2020.02.03.932616

Arabidopsisgenetic perturbation / CRISPR

𝕏 PostBluesky

BiophysicsbioRxivJan 6, 2020

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

C. K. Deniston, J. Salogiannis, S. Mathea…·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.

DOI 10.1038/s41586-020-2673-2

humanprotein structure

𝕏 PostBluesky