Author

R. Zalk

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· 4 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:cryo-EM· 4 Research Focus:protein structure prediction· 3 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:development & morphogenesis· 1

Frequent Co-Authors

A. Yaron· 2 shared J. Guez-Haddad· 2 shared M. Hons· 2 shared T. Khazma· 2 shared Y. Opatowsky· 2 shared A. Bernheim· 1 shared A. Grossman· 1 shared A. Plotnikov· 1 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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2 shared papersBiochemistry

A. Yaron

Mutual co-authors in cluster

Author profile →

6 papers

Recent·Most cited

A link between genotype and cellular architecture in microbiome members as revealed by cryo-EM

B. H. Wimmer, S. Morais, R. Zalk, I. Mizrahi, O. Medalia

The paper uses cryo-EM to analyze microbial cellular architecture and finds that structural similarity correlates with taxonomic distance within families but not above.

bioRxiv · Sep 8, 2022Microbiology

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

A Duplex Structure of SARM1 Octamers Induced by a New Inhibitor

T. Khazma, Y. Golan-Vaishenker, J. Guez-Haddad, A. Grossman, R. Sain, A. Plotnikov, R. Zalk, A. Yaron, M. Hons, Y. Opatowsky

The paper identifies a new inhibitor of SARM1 that stabilizes an octamer conformation and induces a meta-stable duplex structure, revealing an additional auto-inhibition mechanism.

bioRxiv · Mar 2, 2022 · PreprintBiochemistry

SAMase of bacteriophage T3 inactivates E. coli methionine S-adenosyltransferase by forming hetero-polymers

H. Simon-Baram, D. Kleiner, F. Shmulevich, R. Zarivach, R. Zalk, H. Tang, F. Ding, S. Bershtein

This paper shows that bacteriophage T3's SAMase degrades SAM and inhibits E. coli's MAT by forming hetero-polymers, leading to metabolic disruption.

bioRxiv · May 5, 2021Microbiology

Neutralization of the anthrax toxin by antibody-mediated stapling of its membrane penetrating loop

F. Hoelzgen, R. Zalk, R. Alcalay, S. Cohen Schwartz, G. Garau, A. Shahar, O. Mazor, G. A. Frank

This study determines the cryo-EM structure of anthrax toxin's protective antigen complexed with an antibody, revealing how the antibody neutralizes the toxin by preventing pore formation.

bioRxiv · Apr 18, 2021Biochemistry

The Structural Basis for SARM1 Inhibition, and Activation Under Energetic Stress

M. Sporny, J. Guez-Haddad, T. Khazma, A. Yaron, M. Dessau, C. Mim, M. N. Isupov, R. Zalk, M. Hons, Y. Opatowsky

This paper presents cryo-EM structures of SARM1 showing how NAD+ inhibits its NADase activity and how NAD+ depletion activates it, leading to cell death.

bioRxiv · Aug 5, 2020Biochemistry