Author

D. Susan-Resiga

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· 3 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:proteomics· 3 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Organism:mouse· 1

Frequent Co-Authors

N. G. Seidah· 4 shared R. Essalmani· 4 shared A. Evagelidis· 3 shared A. Delpal· 2 shared B. Coutard· 2 shared C. Mapa· 2 shared D. Huynh· 2 shared E. A. Cohen· 2 shared

Activity by Year

2020-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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4 shared papersBiochemistry

N. G. Seidah

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Implications of Spike-glycoprotein processing at S1/S2 by Furin, at S2' by Furin and/or TMPRSS2 and shedding of ACE2: cell-to-cell fusion, cell entry and infectivity of SARS-CoV-2

R. Essalmani, J. Jain, D. Susan-Resiga, U. Andreo, A. Evagelidis, M. Derbali, D. Huynh, F. Dallaire, M. Laporte, A. Delpal, P. Sutto-Ortiz, B. Coutard, C. Mapa, K. Wilcoxen, E. Decroly, , N. G. Seidah

The paper discusses the implications of spike-glycoprotein processing by Furin and TMPRSS2 on SARS-CoV-2 infectivity and cell entry, but the manuscript has been withdrawn.

bioRxiv · Jul 2, 2021 · PreprintBiochemistry

Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLRthat is shed by Furin

D. Susan-Resiga, E. Girard, R. Essalmani, A. Roubtsova, J. Marcinkiewicz, R. M. Derbali, A. Evagelidis, J. H. Byun, P. F. Lebeau, R. C. Austin, N. G. Seidah

This paper identifies ASGR1 as a novel PCSK9-independent ligand of liver LDLR that is shed by Furin, leading to reduced LDLR levels and LDL uptake.

bioRxiv · Apr 11, 2021Biochemistry

In vivo analysis of the contribution of proprotein convertases to the processing of FGF23

O. Al Rifai, D. Susan-Resiga, R. Essalmani, J. Creemers, N. G. Seidah, M. Ferron

This study investigates the role of proprotein convertases in FGF23 processing in vivo, finding that furin contributes to cleavage under specific conditions but not universally.

bioRxiv · Jan 15, 2021Physiology

SARS-CoV-2 spike-glycoprotein processing at S1/S2 and S2' and shedding of the ACE2 viral receptor: roles of Furin and TMPRSS2 and implications for viral infectivity and cell-to-cell fusion

R. Essalmani, J. Jain, D. Susan-Resiga, U. Andreo, A. Evagelidis, R. M. Derbali, D. Huynh, F. Dallaire, M. Laporte, A. Delpal, P. Sutto-Ortiz, B. Coutard, C. Mapa, K. Wilcoxen, E. Decroly, , N. G. Seidah

This study investigates the roles of Furin and TMPRSS2 in SARS-CoV-2 spike protein processing and viral entry, showing their synergistic effects and suggesting combined inhibitors as antivirals.

bioRxiv · Dec 18, 2020 · PreprintBiochemistry