Author

Joel A. Hirsch

Tel Aviv UniversityORCID 0000-0001-7544-8668Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Physiology· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Assay:electrophysiology· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1 Organism:Xenopus· 1

Frequent Co-Authors

Boris ShalomoviD· 2 shared Enno KlußmanniD· 2 shared Kerstin Zühlke· 2 shared Nathan DascaliD· 2 shared Tal Keren Raifman· 2 shared Abdussalam AzemiD· 1 shared Adi Gali-Sayag· 1 shared Alberto G. BerruezoiD· 1 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersPhysiology

Boris ShalomovORCID

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3 papers

Recent·Most cited

PhysiologybioRxivPreprintSep 21, 2026

Gβγ dually regulates the M current via increased channel surface expression and PIP2 sensitivity

Boris Shalomov, Iiulia Papa-Dmitrieva, Tal Keren Raifman…·Nathan Dascal

This study shows Gβγ enhances M-current by increasing channel surface expression and stabilizing PIP2 coupling in Xenopus laevis oocytes.

DOI 10.64898/2026.09.15.751787

experimental assay

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PhysiologyNature CommunicationsPeer-reviewedNov 24, 2025

Live-cell quantitative monitoring reveals distinct, high-affinity Gβγ regulations of GIRK2 and GIRK1/2 channels

Reem Handklo‐Jamal, Tal Keren Raifman, Boris Shalomov…·Nathan Dascal

The paper shows Gβγ interacts with GIRK2 and GIRK1/2 channels with affinities in the microM range, with GIRK1/2 having higher apparent affinity due to a unique Gβγ docking site.

DOI 10.1038/s41467-025-66730-8

Xenopuselectrophysiology

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BiophysicsbioRxivPreprintOct 4, 2025

Structural basis for ATP-driven double-ring assembly of the human mitochondrial Hsp60 chaperonin

Igor Tascón, Jorge Pedro López-Alonso, Yoel Shkolnisky…·Iban Ubarretxena‐Belandia

The paper presents cryo-EM structures of human mitochondrial Hsp60 chaperonin in different states to elucidate the structural basis of ATP-driven double-ring assembly.

3 citations

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