Author

C. R. Sanders

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· 4 Biochemistry· 1

Signature Assays, Organisms & Methods

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Organism:human· 4 Approach:deep learning· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1

Frequent Co-Authors

A. L. George· 3 shared C. G. Vanoye· 3 shared G. Kuenze· 3 shared J. Meiler· 3 shared A. Hadziselimovic· 1 shared A. K. Kenworthy· 1 shared A. M. Duran· 1 shared D. D. Luu· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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3 shared papersBiophysics

A. L. George

Mutual co-authors in cluster

Author profile →

5 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

Delivery of recombinant SARS-CoV-2 envelope protein into human cells

J. M. Hutchison, R. Capone, D. D. Luu, A. Hadziselimovic, W. D. Van Horn, C. R. Sanders

This paper describes the delivery of SARS-CoV-2 envelope protein into human cells using amphipols, enabling membrane integration and retrograde trafficking to ERGIC and Golgi regions.

bioRxiv · Feb 18, 2021Biochemistry

Peripheral Myelin Protein 22 Preferentially Partitions into Ordered Phase Membrane Domains

J. T. Marinko, G. C. Li, A. K. Kenworthy, C. R. Sanders

This paper shows that PMP22 preferentially partitions into ordered membrane domains, and disease mutations disrupt this preference.

bioRxiv · Jan 28, 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