Author

Hsiang-Ling Huang

The Ohio State UniversityORCID 0000-0002-5944-1252Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Research Focus:differential expression· 1 Assay:electrophysiology· 1 Organism:human· 1 Assay:imaging· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

Krishna ChinthalapudiiD· 2 shared Sarah M. HeissleriD· 2 shared Alex Williams· 1 shared Ana Laura López-SerranoiD· 1 shared Angelina Ramirez‐Navarro· 1 shared Apoorva PurohitiD· 1 shared Ashmita KciD· 1 shared Calum A. MacRaeiD· 1 shared

Activity by Year

2026-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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2 shared papersPhysiology

Krishna ChinthalapudiORCID

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2 papers

Recent·Most cited

Beyond Glycogen Storage: AMPKγ2 Regulates Cardiac Hypertrophy and Electrophysiology via Myosin Interaction

Qianyun Ge, Kusumika Saha, Micah L. Burch, Willow H. Battista, Ashmita Kc, Max Homilius, Rachelle A. Victorio, Dajun Quan, Hsiang-Ling Huang, Joseph M. Hazel, Alex Williams, Emily Pan, Krishna Chinthalapudi, Sarah M. Heissler, Calum A. MacRae, Wandi Zhu

This study shows PRKAG2 variants cause cardiac hypertrophy and electrical changes in zebrafish, independent of glycogen storage, through AMPKγ2-myosin interactions.

bioRxiv · Apr 23, 2026 · PreprintPhysiology

Structural and Functional Mechanisms Underlying Activation Gate Dynamics and IFM Motif Accessibility in Human Nav1.5

Rupam Biswas, Ana Laura López-Serrano, Apoorva Purohit, Angelina Ramirez‐Navarro, Hsiang-Ling Huang, Xiaolin Cheng, Sarah M. Heissler, Isabelle Deschênes, Krishna Chinthalapudi

This study presents a cryo-EM structure of human Nav1.5 in an intermediate open state, revealing a new Na+ binding site and showing ion binding modulates IFM motif docking and inactivation kinetics.

Nature Communications · Feb 16, 2026Peer-reviewedBiophysics