Author

C. G. Vanoye

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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Signature Assays, Organisms & Methods

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Organism:human· 4 Approach:deep learning· 2 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Assay:electrophysiology· 1 Approach:experimental assay· 1 Approach:mechanistic / dynamical model· 1 Assay:protein sequence· 1

Frequent Co-Authors

A. L. George· 4 shared G. Kuenze· 4 shared J. Meiler· 4 shared C. R. Sanders· 3 shared A. M. Duran· 1 shared C. Sanders· 1 shared E. F. McDonald· 1 shared H. Huang· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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4 shared papersBiophysics

A. L. George

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4 papers

Recent·Most cited

Molecular simulations reveal a mechanism for enhanced allosteric coupling between voltage-sensor and pore domains in KCNQ1 explaining its activation by ML277

G. Kuenze, C. G. Vanoye, M. C. Wilkinson, R. R. Desai, S. Adusumilli, C. R. Sanders, A. L. George, J. Meiler

bioRxiv · May 31, 2022 · PreprintBiophysics

Predicting the Functional Impact of KCNQ1 Variants with Artificial Neural Networks

S. Phul, G. Kuenze, C. G. Vanoye, C. R. Sanders, A. L. George, J. Meiler

This paper develops ANN models to predict the functional impact of KCNQ1 variants using biophysical features, outperforming models based solely on evolutionary features.

bioRxiv · Dec 6, 2021Biophysics

Disease-Linked Super-Trafficking of a Mutant Potassium Channel

H. Huang, L. M. Chamness, C. G. Vanoye, G. Kuenze, J. Meiler, A. L. George, J. P. Schlebach, C. Sanders

The paper investigates whether gain-of-function mutations in KCNQ1 cause super-trafficking of the potassium channel to the plasma membrane, finding increased surface levels and altered channel activity.

bioRxiv · Jul 29, 2020Biophysics

Upgraded molecular models of the human KCNQ1 potassium channel

G. Kuenze, A. M. Duran, H. Woods, K. R. Brewer, E. F. McDonald, C. G. Vanoye, A. L. George, C. R. Sanders, J. Meiler

This paper develops and validates structural models of human KCNQ1 potassium channels to understand mutation-induced dysfunction and guide drug design.

bioRxiv · May 24, 2019Biophysics