Author

Y. A. Hannun

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· 1 Cell Biology· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1 Assay:proteomics· 1

Frequent Co-Authors

L. M. Obeid· 2 shared A. Budillon· 1 shared A. J. Snider· 1 shared A. Luini· 1 shared A. Nakano· 1 shared A. Vocat· 1 shared B. Lombardi· 1 shared C. Mao· 1 shared

Activity by Year

2018-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersImmunology

L. M. Obeid

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Neutral sphingomyelinase 2 regulates inflammatory responses in monocytes/macrophages induced by TNF-α

F. Al-Rashed, Z. Ahmad, R. Thomas, M. Melhem, A. J. Snider, L. M. Obeid, F. Al-Mulla, Y. A. Hannun, R. Ahmad

This study shows that nSMase2 regulates TNF-α-induced inflammatory responses in monocytes/macrophages by affecting CD11c expression and inflammatory mediator secretion.

bioRxiv · May 6, 2020Immunology

The Glyco-enzyme adaptor GOLPH3 Links Intra-Golgi Transport Dynamics to Glycosylation Patterns and Cell Proliferation

R. Rizzo, D. Russo, K. Kurokawa, P. Sahu, B. Lombardi, D. Supino, M. Zhukovsky, A. Vocat, P. Pothukuchi, V. Kunnathully, L. Capolupo, G. Boncompain, C. Vitagliano, F. Zito Marino, G. Aquino, , A. Luini

This study shows GOLPH3 regulates glycosylation and cell proliferation by controlling glyco-enzyme recycling and lysosomal degradation.

bioRxiv · Dec 23, 2019 · PreprintCell Biology

Alkaline ceramidase catalyzes the hydrolysis of ceramides via a catalytic mechanism shared by Zn2+-dependent amidases

J. K. Yi, R. Xu, L. M. Obeid, Y. A. Hannun, M. V. Airola, C. Mao

This study investigates the catalytic mechanism of ACER3, identifying key residues and demonstrating its Zn2+-dependent activity similar to other Zn-based amidases.

bioRxiv · Oct 13, 2018Biochemistry