Author

I. I. Serysheva

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· 3 Physiology· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 3 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

G. Fan· 4 shared M. R. Baker· 3 shared D. I. Yule· 2 shared L. E. Terry· 2 shared M. Chen· 2 shared M. L. Baker· 2 shared S. J. Ludtke· 2 shared V. Arige· 2 shared

Activity by Year

2018-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 38 mutual co-author links

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4 shared papersBiophysics

G. Fan

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4 papers

Recent·Most cited

Structural dynamics underlying gating and regulation in IP3R channel

G. Fan, M. R. Baker, L. E. Terry, V. Arige, M. Chen, A. Seryshev, M. L. Baker, S. J. Ludtke, D. I. Yule, I. I. Serysheva

The paper determines 3D structures of IP3R1 in two ligand-bound states using cryo-EM and identifies dynamic properties of key domains involved in ligand binding and channel gating.

bioRxiv · May 27, 2022Biophysics

Functional Determination of Calcium Binding Sites Required for the Activation of Inositol 1,4,5-trisphosphate receptors.

V. Arige, L. E. Terry, L. E. Wagner, M. R. Baker, G. Fan, I. I. Serysheva, D. I. Yule

This study identifies acidic residues in IP3Rs critical for Ca2+ binding and activation, showing their role in modulating channel activity and Ca2+ sensitivity.

bioRxiv · Mar 7, 2022Physiology

In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution

M. Chen, X. Shi, Z. Yu, G. Fan, I. I. Serysheva, M. Baker, B. Luisi, S. Ludtke, Z. Wang

The paper uses cryo-ET to determine the 7 Å structure of the AcrAB-TolC efflux pump in Escherichia coli, revealing its activation mechanism through interprotein interactions.

bioRxiv · Jun 10, 2020Biophysics

Cryo-EM Reveals Ligand Induced Allostery Underlying InsP3R Channel Gating

G. Fan, M. R. Baker, Z. Wang, A. B. Serysheva, S. J. Ludtke, M. L. Baker, I. I. Serysheva

The paper presents cryo-EM structures of InsP3R1 in activated and apo-states, revealing ligand-induced conformational changes that underlie channel gating.

bioRxiv · Jul 23, 2018Biophysics