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The Journal of Biological Chemistry|July 31, 2014
Phospholamban C-terminal residues are critical determinants of the structure and function of the calcium ATPase regulatory complexNeha Abrol, Nikolai Smolin, Gareth Armanious, et al.
Biophysical Journal|December 21, 2019
Interaction of a Sarcolipin Pentamer and Monomer with the Sarcoplasmic Reticulum Calcium Pump, SERCAJohn Paul Glaves, Joseph O Primeau, Przemek A Gorski, et al.
The Journal of Biological Chemistry|March 18, 2009
Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPaseMette Laursen, Maike Bublitz, Karine Moncoq, et al.
Biorxiv : the Preprint Server for Biology|February 12, 2026
Supercharging the calcium pump: Identification of an activation hotspot on SERCA by cryo-EMVinh H Nguyen, Carlos Cruz-Cortés, Joseph O Primeau, et al.
Biological Chemistry|April 13, 2016
Probing catalytic rate enhancement during intramembrane proteolysisElena Arutyunova, Cameron C Smithers, Valentina Corradi, et al.
Scientific Reports|November 14, 2018
Intrinsic disorder in the regulatory N-terminal domain of diacylglycerol acyltransferase 1 from Brassica napusRashmi Panigrahi, Tsutomu Matsui, Andrew H Song, et al.
Biological Chemistry|July 26, 2018
An internally quenched peptide as a new model substrate for rhomboid intramembrane proteasesElena Arutyunova, Zhenze Jiang, Jian Yang, et al.
The Journal of Biological Chemistry|October 31, 2017
Conformational memory in the association of the transmembrane protein phospholamban with the sarcoplasmic reticulum calcium pump SERCASerena Smeazzetto, Gareth P Armanious, Maria Rosa Moncelli, et al.
Peptides|December 25, 2012
Distinct morphological and electrophysiological properties of an elk prion peptideJohn Paul Glaves, Przemek A Gorski, Kwai Alier, et al.
International Journal of Molecular Sciences|August 27, 2021
Nothing Regular about the Regulins: Distinct Functional Properties of SERCA Transmembrane Peptide Regulatory SubunitsNishadh Rathod, Jessi J Bak, Joseph O Primeau, et al.
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