Author

C. Yoshioka

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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Biochemistry· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:cryo-EM· 3 Research Focus:protein structure prediction· 3 Organism:human· 1

Frequent Co-Authors

G. M. Martin· 3 shared S.-L. Shyng· 3 shared B. Kandasamy· 2 shared E. A. Rex· 1 shared E. Gouaux· 1 shared F. DiMaio· 1 shared F. Jalali-Yazdi· 1 shared J. F. Fay· 1 shared

Activity by Year

2016-2019 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiochemistry

G. M. Martin

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Author profile →

4 papers

Recent·Most cited

Mechanism of pharmacochaperoning in KATP channels revealed by cryo-EM

G. M. Martin, M. W. Sung, Z. Yang, L. M. Innes, B. Kandasamy, L. David, C. Yoshioka, S.-L. Shyng

This study reveals how pharmacochaperones stabilize KATP channels by binding to SUR1 and supporting Kir6.2 N-terminus insertion, enabling mutant channel assembly.

bioRxiv · Mar 8, 2019 · PreprintBiophysics

Mechanisms for zinc and proton inhibition of the GluN1/GluN2A NMDA receptor

F. Jalali-Yazdi, S. Chowdhury, C. Yoshioka, E. Gouaux

This study uses cryo-EM to determine the structure of the GluN1/GluN2A NMDAR under varying zinc and proton concentrations, revealing how zinc binding affects channel gating.

bioRxiv · Jul 26, 2018Biophysics

Anti-diabetic drug binding site in KATP channels revealed by Cryo-EM

G. M. Martin, B. Kandasamy, F. DiMaio, C. Yoshioka, S.-L. Shyng

The paper presents a cryo-EM structure of KATP channels bound to glibenclamide and ATP, revealing the drug's binding site and its interaction with the channel.

bioRxiv · Aug 5, 2017Biochemistry

Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating

G. M. Martin, C. Yoshioka, E. A. Rex, J. F. Fay, Q. Xie, M. R. Whorton, J. Z. Chen, S.-L. Shyng

The paper presents a cryo-EM structure of the KATP channel, revealing assembly and gating mechanisms involving SUR1 and Kir6.2 interactions with ATP and PIP2.

bioRxiv · Dec 16, 2016Biochemistry