L. M. Espinoza-Fonseca

The paper investigates the stoichiometry and structure of the NKA-PLM regulatory complex using fluorescence lifetime assays and simulations, revealing a (alpha-beta-PLM)2 composition.

This study combines computational and experimental methods to evaluate drug potency, efficacy, and safety for targeting membrane proteins, using SERCA2a as a model.

This paper identifies DWORF as a direct activator of SERCA, increasing its turnover rate and calcium reuptake, contrasting with the inhibitory effect of phospholamban.

The paper investigates sarcolamban peptides from invertebrates to determine their regulatory effects on SERCA1a, finding they act as super-inhibitors with phospholamban-like or sarcolipin-like characteristics.

This study uses multiscale simulations to show that SERCA facilitates passive proton transport through a transient water pore on the microsecond timescale.

This study uses simulations and experiments to show Ca2+ binding induces structural changes in the SERCA-PLB complex, pre-activating SERCA through dynamic allostery.

This study uses molecular dynamics simulations to show that the conserved C-terminal domain of sarcolipin dynamically controls interdomain communication, essential for its regulatory function.

This paper characterizes the interaction between sarcolipin (SLN) pentamer and monomer with SERCA, revealing structural and functional insights into SLN's regulation of calcium transport and thermogenesis.

The paper analyzes Ca2+ regulation in horse gluteus muscle, finding high SLN RNA but low SLN protein, suggesting a non-coding role, and enhanced SR Ca2+ transport.

This study uses MD simulations to show that nonannular lipid binding does not affect the stability of the E2 state of SERCA, but may be functionally important during the E2-to-E1 transition.

This paper shows that phospholamban pentamer interacts with SERCA in both crystal forms, playing structural and functional roles in its regulation.

This study uses molecular dynamics simulations to show that Ca2+ binding at saturating concentrations relieves SERCA inhibition by phospholamban through local structural changes, without altering PLB's overall conformation.