Author

Emily Furlong

Australian National UniversityORCID 0000-0002-9086-2979Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

Meghna SobtiiD· 2 shared Simon H. J. BrowniD· 2 shared Alastair G. StewartiD· 1 shared Alastair G. StewartiD· 1 shared Hiroshi UenoiD· 1 shared Hiroyuki NojiiD· 1 shared Ian-Blaine P. Reininger-Chatzigiannakis· 1 shared Jiayi Pan· 1 shared

Activity by Year

2024-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiophysics

Meghna SobtiORCID

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3 papers

Recent·Most cited

The Lower γ Region Ensures Unidirectional Rotation and Torque Generation in the Latter Half of the 80° Substep of F1-ATPase

Tomo Uchiyama, Hiroshi Ueno, Meghna Sobti, Emily Furlong, Simon H. J. Brown, Alastair G. Stewart, Hiroyuki Noji

This paper investigates the role of the lower γ region in F1-ATPase rotation, finding it contributes to unidirectional rotation and torque generation specifically in the latter half of the 0-80° step.

bioRxiv · May 12, 2026 · PreprintBiophysics

Molecular structure and nickel binding capacity of Proteus mirabilis UreE

Jiayi Pan, Sarah L. Mueller, Nuren Tasneem, Yang Wu, Emily Furlong

This study determines the structure of P. mirabilis UreE and shows it binds five nickel ions per dimer, with the C-terminus critical for full binding capacity.

Acta Crystallographica Section D Structural Biology · Mar 10, 2026Peer-reviewedBiochemistry

The molecular structure of an axle-less F1-ATPase

Emily Furlong, Ian-Blaine P. Reininger-Chatzigiannakis, Yi Cheng Zeng, Simon H. J. Brown, Meghna Sobti, Alastair G. Stewart

The paper solves the cryo-EM structure of an axle-less F1-ATPase and shows that the complete γ subunit is important for efficient ATP binding.

Biochimica et Biophysica Acta (BBA) - Bioenergetics · Oct 18, 2024Peer-reviewedBiochemistry