Author

A. Upcher

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 Biophysics· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Research Focus:development & morphogenesis· 2 Approach:biophysical modeling· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Organism:human· 1

Frequent Co-Authors

A. Bernheim· 1 shared A. Wagner· 1 shared B. A. Palmer· 1 shared B. Junglas· 1 shared B. Rayan· 1 shared C. Sachse· 1 shared D. Nachmias· 1 shared E. Barnea· 1 shared

Activity by Year

2022-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperBiochemistry

A. Bernheim

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The Formation of Biogenic Guanine Crystals Closely Resembles Melanosome Morphogenesis

A. Wagner, A. Upcher, R. Maria, T. Magnesen, E. Zelinger, G. Raposa, B. A. Palmer

This study shows that the formation of biogenic guanine crystals in scallops resembles melanosome morphogenesis in vertebrates, revealing shared mechanisms in crystal template formation.

bioRxiv · Oct 1, 2022 · PreprintCell Biology

The Asgard archaeal ESCRT-III system forms helical filaments and remodels eukaryotic membranes, shedding light on the emergence of eukaryogenesis

N. Melnikov, B. Junglas, G. Halbi, D. Nachmias, E. Zerbib, A. Upcher, R. Zalk, C. Sachse, A. Bernheim, N. Elia

This study shows Asgard archaeal ESCRT-III proteins form helical filaments and remodel eukaryotic-like membranes, supporting their role in eukaryogenesis.

bioRxiv · Sep 7, 2022 · PreprintBiochemistry

Natural Antimicrobial Peptides Self-assemble as α/β Chameleon Amyloids

P. Ragonis-Bachar, B. Rayan, E. Barnea, Y. Engelberg, A. Upcher, M. Landau

The paper identifies 14 fibril-forming antimicrobial peptides (ffAMPs) that exhibit cross-β and α/β amyloid properties, suggesting a link between amyloid formation and antimicrobial activity.

bioRxiv · Jun 23, 2022Biophysics