Author

R. Ishmukhametov

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:chromatin & epigenetic regulation· 2 Assay:cryo-EM· 2 Organism:E. coli· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

A. G. Stewart· 2 shared J. L. Walshe· 2 shared M. Sobti· 2 shared C. v. d. Does· 1 shared F. Braun· 1 shared N. Mikami· 1 shared R. M. Berry· 1 shared S.-V. Albers· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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2 shared papersBiophysics

A. G. Stewart

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3 papers

Recent·Most cited

Motile ghosts of the halophilic archaeon, Haloferax volcanii

Y. Kinosita, N. Mikami, Z. Li, F. Braun, T. E. Quax, C. v. d. Does, R. Ishmukhametov, S.-V. Albers, R. M. Berry

This study presents a membrane-permeabilized ghost system for Haloferax volcanii to investigate archaellum motility, revealing ATP selectivity, negative cooperativity, and a torque-speed curve with characteristics of both bacterial flagellar motors and F1-ATPase.

Proceedings of the National Academy of Sciences · Oct 13, 2020Peer-reviewedBiophysics

Subunit epsilon of E. coli F1Fo ATP synthase attenuates enzyme activity by modulating central stalk flexibility

M. Sobti, J. L. Walshe, Y. C. Zeng, R. Ishmukhametov, A. G. Stewart

This study presents cryo-EM structures of E. coli ATP synthase showing how the ε subunit modulates central stalk flexibility to regulate enzyme activity.

bioRxiv · Sep 30, 2020 · PreprintBiophysics

Visualizing movements in E. coli F1Fo ATP synthase indicates how the F1 and Fo motors are coupled

M. Sobti, J. L. Walshe, R. Ishmukhametov, A. G. Stewart

The paper presents high-resolution cryo-EM structures of E. coli F1Fo ATP synthase and describes a rotational sub-step of the Fo motor that explains how the F1 and Fo motors are coupled with minimal energy loss.

bioRxiv · Apr 29, 2019 · PreprintBiophysics