Author

J. T. Sack

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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Biophysics· 5 Pharmacology & Toxicology· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 5 Assay:electrophysiology· 4 Approach:deep learning· 3 Research Focus:host-pathogen & immune response· 3 Approach:statistical model· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2

Frequent Co-Authors

P. Thapa· 4 shared K. Furutani· 3 shared V. Yarov-Yarovoy· 3 shared B. E. Cohen· 2 shared C. E. Clancy· 2 shared P. T. Nguyen· 2 shared R. J. Sepela· 2 shared R. Stewart· 2 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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4 shared papersBiophysics

P. Thapa

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Molecular Determinants of μ-Conotoxin KIIIA interaction with the Voltage-Gated Sodium Channel Nav1.7

I. H. Kimball, P. T. Nguyen, B. M. Olivera, J. T. Sack, V. Yarov-Yarovoy

The paper identifies molecular interactions between μ-conotoxin KIIIA and hNaV1.7 using computational modeling, experimental validation, and structural analysis.

bioRxiv · Feb 2, 2023 · PreprintBiophysics

Computational design of peptides to target Nav1.7 channel with high potency and selectivity for the treatment of pain

P. T. Nguyen, H. M. Nguyen, K. M. Wagner, R. Stewart, V. Singh, P. Thapa, Y.-J. Chen, M. W. Lillya, A. T. Ton, R. Kondo, A. Ghetti, M. W. Pennington, B. Hammock, T. N. Griffith, J. T. Sack, , V. Yarov-Yarovoy

The paper designs potent and selective peptide inhibitors of human NaV1.7 channels using Rosetta, with two peptides showing sub-nanomolar IC50 and high selectivity over other sodium channels.

bioRxiv · Jul 21, 2022Biophysics

Facilitation by a hERG blocker is induced by pore opening and operates by pore reopening

K. Furutani, R. Kawano, M. Ichiwara, R. Adachi, C. E. Clancy, J. T. Sack, S. Kita

This study investigates how nifekalant, a hERG blocker, facilitates hERG channel activation through pore opening rather than voltage sensors.

bioRxiv · May 26, 2022 · PreprintPharmacology & Toxicology

Structural modeling of the hERG potassium channel and associated drug interactions

J. Maly, A. M. Emigh, K. R. DeMarco, K. Furutani, J. T. Sack, C. E. Clancy, I. Vorobyov, V. Yarov-Yarovoy

This study uses Rosetta to model structural changes in hERG channels caused by mutations and drug interactions, revealing conformational shifts and binding mechanisms.

bioRxiv · Jul 8, 2021Biophysics

The AMIGO1 adhesion protein activates Kv2.1 voltage sensors

R. J. Sepela, R. G. Stewart, L. Valencia, P. Thapa, Z. Wang, B. E. Cohen, J. T. Sack

This study identifies how AMIGO1 modulates Kv2.1 voltage sensor movements and conductance activation by destabilizing the earliest resting state.

bioRxiv · Jun 20, 2021Biophysics

Optical measurement of voltage sensing by endogenous ion channel

P. Thapa, R. Stewart, R. J. Sepela, O. Vivas, L. K. Parajuli, M. Lillya, S. Fletcher-Taylor, B. E. Cohen, K. Zito, J. T. Sack

The paper introduces an imaging method to measure conformational changes of endogenous Kv2 voltage sensors in live tissue using a fluorophore-conjugated toxin and statistical modeling.

bioRxiv · Jan 13, 2021Biophysics

Facilitation of hERG channels by blockers: a mechanism predicted to reduce lethal cardiac arrhythmias

K. Furutani, K. Tsumoto, I.-S. Chen, K. Handa, Y. Yamakawa, J. T. Sack, Y. Kurachi

This paper proposes that hERG channel facilitation by blockers can reduce lethal cardiac arrhythmias by preventing early afterdepolarizations during repolarization.

bioRxiv · Jun 8, 2018Pharmacology & Toxicology

Organizing neuronal ER-PM junctions is a conserved nonconducting function of Kv2 plasma membrane ion channels

M. Kirmiz, S. Palacio, P. Thapa, A. N. King, J. T. Sack, J. Trimmer

The paper shows Kv2 ion channels organize ER-PM junctions independently of their ion-conducting function, conserved across species and distinct from their role in neuronal excitability.

bioRxiv · Apr 6, 2018Cell Biology