Author

S. A. Pless

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· 6

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:electrophysiology· 5 Organism:human· 4 Research Focus:protein folding & dynamics· 3 Organism:mouse· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1

Frequent Co-Authors

D. Sarkar· 2 shared I. Galleano· 2 shared K. K. Khoo· 2 shared S. A. Heusser· 2 shared S. Friis· 2 shared A. Hauser· 1 shared A. Sinz· 1 shared C. B. Borg· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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2 shared papersBiophysics

D. Sarkar

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Author profile →

6 papers

Recent·Most cited

Protein semisynthesis underscores role of a conserved lysine in activation and desensitization of acid-sensing ion channels

D. Sarkar, I. Galleano, S. A. Heusser, S. Y. Ou, G. R. Uzun, K. K. Khoo, G. J. v. d. H. van Noort, J. S. Harrison, S. A. Pless

This study uses semisynthesis to investigate the role of a conserved lysine in ASIC1a function, showing its importance in activation and desensitization.

bioRxiv · Jan 23, 2023Biophysics

Conformational decoupling in acid-sensing ion channels uncovers mechanism and stoichiometry of PcTx1-mediated inhibition

S. A. Heusser, C. B. Borg, J. Colding, S. A. Pless

This study investigates the mechanism and stoichiometry of PcTx1 inhibition of ASIC1a using voltage-clamp fluorometry and subunit concatenation, revealing multiple binding modes and conformational changes.

bioRxiv · Jun 21, 2021Biophysics

P2X2 receptor subunit interfaces are missense variant hotspots where mutations tend to increase apparent ATP affinity

F. Gasparri, D. Sarkar, S. Bielickaite, M. H. Poulsen, A. Hauser, S. A. Pless

This study maps missense variants in P2X2 receptor inter-subunit interfaces and shows mutations often increase apparent ATP affinity and show energetic coupling.

bioRxiv · Mar 26, 2021Biophysics

The M1 and pre-M1 segments contribute differently to ion selectivity in ASICs and ENaCs

Z. P. Sheikh, M. Wulf, S. Friis, M. Althaus, T. Lynagh, S. A. Pless

This study shows that the pre-M1 and M1 regions of ASICs and ENaCs differentially contribute to ion selectivity through structural and functional analyses.

bioRxiv · Feb 16, 2021Biophysics

Functional crosstalk between phosphorylation and disease-causing mutations in the cardiac sodium channel Nav1.5

I. Galleano, H. Harms, K. Choudhury, K. K. Khoo, L. Delemotte, S. A. Pless

This paper investigates how phosphorylation and disease-causing mutations interact in Nav1.5, showing that mutations can amplify phosphorylation's impact on channel function and drug sensitivity.

bioRxiv · Dec 11, 2020Biophysics

High-throughput characterization of photocrosslinker-bearing ion channel variants to map residues critical for function and pharmacology

N. Braun, S. Friis, C. Ihling, A. Sinz, J. Andersen, S. A. Pless

The paper develops a high-throughput method to study functional and pharmacological properties of ncAA-containing hASIC1a variants using automated patch-clamp.

bioRxiv · Nov 24, 2020Biophysics