Understanding the rules governing NCX1 palmitoylation

по Plain, Fiona, Turnbull, Dionne, Fraser, Niall J., Fuller, William
Опубликовано в: Channels (Austin) (2017)

Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods

по Hurst, Charlotte H., Turnbull, Dionne, Plain, Fiona, Fuller, William, Hemsley, Piers A.
Опубликовано в: Biotechniques (2017)

Dynamic Palmitoylation of the Sodium-Calcium Exchanger Modulates Its Structure, Affinity for Lipid-Ordered Domains, and Inhibition by XIP

по Gök, Caglar, Plain, Fiona, Robertson, Alan D., Howie, Jacqueline, Baillie, George S., Fraser, Niall J., Fuller, William
Опубликовано в: Cell Rep (2020)

Control of protein palmitoylation by regulating substrate recruitment to a zDHHC-protein acyltransferase

по Plain, Fiona, Howie, Jacqueline, Kennedy, Jennifer, Brown, Elaine, Shattock, Michael J., Fraser, Niall J., Fuller, William
Опубликовано в: Commun Biol (2020)

An amphipathic α-helix directs palmitoylation of the large intracellular loop of the sodium/calcium exchanger

по Plain, Fiona, Congreve, Samitha Dilini, Yee, Rachel Sue Zhen, Kennedy, Jennifer, Howie, Jacqueline, Kuo, Chien-Wen, Fraser, Niall J., Fuller, William
Опубликовано в: J Biol Chem (2017)

Insights into the molecular basis of the palmitoylation and depalmitoylation of NCX1

по Gök, Caglar, Main, Alice, Gao, Xing, Kerekes, Zsombor, Plain, Fiona, Kuo, Chien-Wen, Robertson, Alan D., Fraser, Niall J., Fuller, William
Опубликовано в: Cell Calcium (2021)