Author

G. Maksaev

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· 2 Cell Biology· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Organism:Arabidopsis· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Research Focus:development & morphogenesis· 1

Frequent Co-Authors

P. Yuan· 2 shared A. Stary-Weinzinger· 1 shared C. Nichols· 1 shared E. Haswell· 1 shared E. S. Haswell· 1 shared E.-M. Zangerl· 1 shared F. Ren· 1 shared H. Bernsteiner· 1 shared

Activity by Year

2018-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiophysics

P. Yuan

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Author profile →

4 papers

Recent·Most cited

OzTracs: Optical Osmolality Reporters Engineered from Mechanosensitive Ion Channels

T. J. Kleist, I. W. Lin, S. Xu, G. Maksaev, M. Sadoine, E. S. Haswell, W. B. Frommer, M. M. Wudick

This paper describes the engineering of osmolality sensors called OzTracs by fusing fluorescent proteins to mechanosensitive ion channels, showing they report osmolality changes through indirect mechanisms.

bioRxiv · Feb 10, 2022Cell Biology

Cryo-EM structures of the ATP release channel pannexin 1

Z. Deng, Z. He, G. Maksaev, R. M. Bitter, M. Rau, J. A. J. Fitzpatrick, P. Yuan

This study presents cryo-EM structures of pannexin 1 from Xenopus tropicalis and Homo sapiens, revealing its heptameric architecture and molecular sieve mechanism for ATP release.

bioRxiv · Jan 5, 2020Biophysics

Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels

E.-M. Zangerl, S. Lee, G. Maksaev, H. Bernsteiner, F. Ren, P. Yuan, A. Stary-Weinzinger, C. Nichols

The paper investigates the open conformation and K+ ion conduction mechanism in Kir2.2 channels using a forced open mutation and structural analysis.

bioRxiv · May 18, 2019Biophysics

Nonpolar Residues in the Presumptive Pore-Lining Helix of Mechanosensitive Channel MSL10 Influence Channel Behavior and Confirm a Non-Conducting Function

G. Maksaev, J. Shoots, S. Ohri, E. Haswell

This study identifies nonpolar residues in MSL10's pore-lining helix that influence conductance, gating tension, and cell death signaling, showing ion channel function is independent of cell death.

bioRxiv · Feb 12, 2018Plant Biology