Search bioRxiv⌕ Search

bioRxiv · 10.64898/2026.10.13.756866

Retinal Resistivity Mapped by Electrical Resistance Tomography

Abstract

Retinal resistivity is a key parameter for modeling both the electric field in tissue and the resulting neural response - a crucial step in designing retinal prostheses, especially since both depend on resistivity nonlinearly. Previous studies using penetrating microelectrodes reported vastly different values, varying by as much as two orders of magnitude, likely due to parasitic capacitance in microelectrodes, compression of tissue and its rupture by the inserted probe, allowing the conductive medium to seep in and alter the measurement. To measure retinal resistivity without compression or rupture, we applied electrical resistance tomography using a planar multielectrode array with a 30 m pitch. Voltage waveforms generated in response to current injected from one electrode were measured on other electrodes in the array, at distances ranging from 30 to 600 m. Data from wild-type and degenerated rat retinas were analyzed using two methods: a commercial inversion software, Res2DInv, and a custom machine learning-based decoder, with healthy retina approximated as a 4-layer structure and degenerated retina - as a 3-layer one.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Kochnev Goldstein, A., Zaman, M. A., Sommeling, M. A., Shah, S. V., Lotlikar, A., Bhuckory, M. B., Pham-Howard, D., Chen, Z. C., Vasireddy, P., Phillips, A. J., Sharon, A., Chichilnisky, E. J., Palanker, D.. 2026-10-20. Retinal Resistivity Mapped by Electrical Resistance Tomography. https://doi.org/10.64898/2026.10.13.756866

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Cancers relax selection on charge at the mitochondrial complex I quinone cavity

Mitochondrial complex I translocates protons through hydrated channels whose connectivity and electrostatics are both defined by structure, but whether they are distinctly constrained is unknown. From a 2.39 cryo-EM structure modelling 2,945 ordered waters, we built the proton wire of the seven mtDNA-encoded ND subunits and scored all 40,166 missense substitutions on two near-orthogonal axes (r = 0.17): electrostatic shift at proton-loading sites, and topological disruption of the wire. Across 858 germline variant sites, loading sites (0.51) and cut vertices (0.67) are both depleted. In tumours only loading sites are enriched (1.42 TCGA, 1.67 PCAWG, 1.29 MSK-IMPACT), a 3.06-fold difference tested as a wire class tissue-type interaction (P = 3.6 10-). It survives adjustment for conservation, burial and coverage, and is concentrated in ND1 within 15 of the quinone cavity, not spread along the proton path. Selection separates charge from connectivity, without establishing a fitness benefit.

biophysics↗

Rugnux: from diffraction images to structure at synchrotrons and XFELs in one program

Rising data rates in macromolecular crystallography outpace multi-program pipelines on computing clusters. Rugnux, a single GPU-accelerated program, turns rotation or serial still diffraction images into merged data and an initial structure. At synchrotrons, results arrive seconds after the last image; on one workstation, 207 public datasets from 36 sources took a median of 15 s each, with deposition-quality. Serial XFEL data were processed faster than the collection rate, enabling real-time structure determination.

biophysics↗

Phase Separation of Intracellular Proteins Influences Synaptic Bistability

Synaptic bistability at the post synaptic density has been proposed to be the result of the nucleation and evaporation of receptor clusters. The exact biophysical mechanism underlying these inter-receptor attractions that can trigger nucleation remains to be elucidated. Emerging evidence demonstrates that numerous postsynaptic density submembrane proteins, that interact with various membrane receptors, can undergo phase separation, necessitating a revised conceptual model. By employing Langevin dynamics simulations of coarse-grained scaffold proteins and interacting membrane receptors, we study how phase transitions of scaffold proteins alter receptor clustering at the membrane. In our model, scaffold macromolecules can undergo phase separation and interact with receptor molecules at the model membranes. We observed that the presence of scaffold polymers across the membrane creates an attractive interaction between otherwise purely repulsive receptors. By systematically varying the number of receptors at the membrane, we dissected the coupling between receptor clustering and the phase behavior of scaffold macromolecules. We show that the propensity for receptor clustering is enhanced by the condensation of scaffold proteins. We then used two different scaffolds and systematically varied the interaction between them, to change the spatial organization of two condensed phases w.r.t. one another. Interestingly, we observed that receptor clustering can be reduced by co-phase separation of scaffold macromolecules, indicating the role of competing interactions in receptor clustering. Our work advances understanding of receptor-mediated signaling and phase separation, providing insights into cellular compartmentalization and biochemical regulation at the synapse.

biophysics↗