Author

P. Y. Wang

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

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Biochemistry· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:cell signaling & trafficking· 2 Assay:cryo-EM· 2 Research Focus:protein structure prediction· 2 Approach:biophysical modeling· 1 Assay:bulk RNA-seq· 1 Research Focus:chromatin & epigenetic regulation· 1 Organism:E. coli· 1

Frequent Co-Authors

C. Ramakrishnan· 2 shared E. F. X. Byrne· 2 shared H. E. Kato· 2 shared J. M. Paggi· 2 shared K. Deisseroth· 2 shared K. E. Kishi· 2 shared K. Inoue· 2 shared K. Yamashita· 2 shared

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2019-2023 · peak 1/yr

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10 top collaborators · 45 mutual co-author links

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2 shared papersBiophysics

C. Ramakrishnan

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4 papers

Recent·Most cited

The guide RNA sequence dictates the slicing kinetics and conformational dynamics of the Argonaute silencing complex

P. Y. Wang, D. P. Bartel

The paper shows guide RNA sequence affects slicing rates and conformational dynamics of the Argonaute complex, with sequence variations influencing slicing efficiency and 3'-mismatch tolerance.

bioRxiv · Oct 15, 2023Biochemistry

Structural basis for ion selectivity in potassium-selective channelrhodopsins

S. Tajima, Y. S. Kim, M. Fukuda, E. F. X. Byrne, P. Y. Wang, J. M. Paggi, K. E. Kishi, C. Ramakrishnan, S. Takaramoto, T. Nagata, M. Konno, M. Sugiura, K. Katayama, T. E. Matsui, K. Yamashita, , H. E. Kato

The paper determines the cryo-EM structures of two K+-selective channelrhodopsins, revealing a unique mechanism for K+ selectivity distinct from canonical K+ channels.

bioRxiv · Oct 30, 2022Biophysics

Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine

K. E. Kishi, Y. S. Kim, M. Fukuda, T. Kusakizako, E. Thadhani, E. F. X. Byrne, J. M. Paggi, C. Ramakrishnan, T. E. Matsui, K. Yamashita, T. Nagata, M. Konno, P. Y. Wang, M. Inoue, T. Benster, , H. E. Kato

The paper presents the cryo-EM structure of ChRmine, revealing unique architectural features and provides insights into its conduction mechanism and potential for optogenetic applications.

bioRxiv · Aug 15, 2021Biophysics

Secondary motifs enable concentration-dependent regulation by Rbfox family proteins

B. E. Begg, M. Jens, P. Y. Wang, C. B. Burge

This study identifies secondary RNA motifs that enable Rbfox proteins to regulate splicing at lower concentrations, expanding beyond the canonical GCAUG motif.

bioRxiv · Nov 12, 2019 · PreprintBiochemistry