Author

Marina Shenkman

Tel Aviv University

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· 2 Neuroscience· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:differential expression· 1 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Organism:mouse· 1 Approach:statistical model· 1

Frequent Co-Authors

Gerardo Zelmar LederkremeriD· 3 shared Haddas Saad· 2 shared Arun ThiruvalluvaniD· 1 shared Bella Groisman· 1 shared Brad J. Geddes· 1 shared Carlos SpichigeriD· 1 shared Chaitanya PateliD· 1 shared Christian Enrique González-BillaultiD· 1 shared

Activity by Year

2020-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 27 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

Gerardo Zelmar LederkremerORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Mannosidases IA, IB and IC are in segregated vesicular structures and involved in both glycoprotein quality control and maturation

Haddas Saad, Marina Shenkman, Edward Avezov, Isam Khalaila, Gerardo Zelmar Lederkremer

This study identifies that ManIA, ManIB, and ManIC localize to quality control vesicles and have distinct roles in glycoprotein maturation and ERAD, with different substrate preferences.

bioRxiv · Oct 22, 2026 · PreprintCell Biology

Oligosaccharyltransferase is involved in targeting to ER-associated degradation

Marina Shenkman, Navit Ogen‐Shtern, Chaitanya Patel, Haddas Saad, Bella Groisman, Metsada Pasmanik, Sonya M. Schermann, Roman Körner, Gerardo Zelmar Lederkremer

The paper identifies oligosaccharyltransferase (OST) subunits as key interactors in ER-associated degradation (ERAD), suggesting a role in late stages of quality control beyond N-glycosylation.

Cells · Oct 14, 2025Peer-reviewedCell Biology

Insulin-like growth factor 2 (IGF2) protects against Huntington's disease through the extracellular disposal of protein aggregates

Paula García-Huerta, Paulina Troncoso-Escudero, Di Wu, Arun Thiruvalluvan, Marisol Cisternas-Olmedo, Daniel R. Henríquez, Lars Plate, Pedro Chaná‐Cuevas, Cristian Saquel, Peter Thielen, Kenneth A. Longo, Brad J. Geddes, Gerardo Zelmar Lederkremer, Neeraj Sharma, Marina Shenkman, , Claudio A. Hetz

This study identifies IGF2 as a disease modifier that reduces intracellular protein aggregates by promoting their extracellular disposal in Huntington's disease models.

Acta Neuropathologica · Jul 8, 2020Peer-reviewedNeuroscience