Author

John B. Cowgill

Stockholm UniversityORCID 0000-0002-7968-8359Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Biochemistry· 1 Biophysics· 1 Neuroscience· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Assay:cryo-EM· 2 Organism:human· 2 Research Focus:protein structure prediction· 2 Research Focus:cell type annotation· 1 Research Focus:drug response / drug discovery· 1 Assay:electrophysiology· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

Chen FaniD· 2 shared Erik R. LindahliD· 2 shared Rebecca J. HowardiD· 2 shared Alexander BlairiD· 1 shared Baron ChandaiD· 1 shared Claudia P. Alvarez-BaroniD· 1 shared Debanjan TewariiD· 1 shared Jan Steyaert· 1 shared

Activity by Year

2018-2026 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 16 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersBiochemistry

Chen FanORCID

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Structural basis for activation and potentiation in a human α5β3 GABAA receptor

John B. Cowgill, Chen Fan, Jan Steyaert, Rebecca J. Howard, Erik R. Lindahl

This paper reports cryo-EM structures of human α5β3 GABAARs with modulators, revealing activation mechanisms and differential responses to GABA and etomidate.

Diva portal (Dalarna University Library) · Jun 15, 2026Peer-reviewedBiochemistry

Cryo-EM structures of {rho}1 GABA(A) receptors with antagonist and agonist drugs

Chen Fan, John B. Cowgill, Rebecca J. Howard, Erik R. Lindahl

This study presents cryo-EM structures of human rho1 GABAA receptors bound to antagonist and agonist drugs, revealing distinct binding poses and conformational changes that explain their pharmacological effects.

Nature Communications · Aug 1, 2025Peer-reviewedBiophysics

Bipolar Switching by HCN Voltage Sensor Underlies Hyperpolarization Activation.

John B. Cowgill, Vadim A. Klenchin, Claudia P. Alvarez-Baron, Debanjan Tewari, Alexander Blair, Baron Chanda

The paper identifies how the HCN voltage sensor can drive pore opening in either direction, revealing a common principle in voltage-gated ion channels.

Proceedings of the National Academy of Sciences · Dec 26, 2018Peer-reviewedNeuroscience