Phillip James Stansfeld

The paper shows that two classes of myosins organize distinct membrane domains through active forces, enabling spatial segregation of nanoclusters and modulating information transduction.

This study investigates how cardiolipin modulates MmpL3 function in mycobacteria, revealing its role in regulating proton translocation and MA transport.

This study presents cryo-EM structures of ArnC, revealing its conformational changes and catalytic mechanism for aminoarabinose glycosylation in polymyxin resistance.

The paper uses cryo-EM and simulations to reveal how LptM and LptY facilitate LPS transport by modulating LptD conformational dynamics in the translocon complex.

The paper presents structures of the Tat core complex in resting and substrate-bound states, revealing how substrate proteins interact with the complex through their signal peptides and proposing a model for early transport steps.

This study reveals the conformational dynamics and membrane insertion mechanism of B4GALNT1 in ganglioside synthesis using crystal structures and molecular simulations.

This study identifies a direct interaction between TolB and cardiolipin, revealing a lipid-binding role for TolB in maintaining outer membrane homeostasis in E. coli.

The paper describes the structure and function of the YbbAP-TesA complex, a Type VII ABC transporter lipid-hydrolase in E. coli, revealing its role in substrate extraction and hydrolysis.

This study develops a computational model to simulate toroidal membranes and investigates their lipid properties and protein interactions during membrane fission processes.

The paper investigates how cardiolipin interacts with membrane proteins to stabilize them, using a model protein and simulations to identify key factors.

This study presents cryo-EM structures of AftB from Mycobacterium chubuense, revealing its architecture and mechanism for terminal arabinosylation in mycobacterial cell wall biosynthesis.

This study determines the cryo-EM structures of PimE from Mycobacterium abscessus and elucidates its mechanism of action, providing insights for anti-TB drug development.

The paper shows that lipid degradation via PDATs limits ER membrane expansion by converting phospholipids into storage lipids in yeast.

This study identifies a new inhibited conformation of KdpFABC, termed E1-P tight, resulting from KdpBS162 phosphorylation, which represents an off-cycle state in P-type ATPases.