Research graph
References from A hallmark of phospholamban functional divergence is located in the N-terminal phosphorylation domain. Local targets link to admitted publications; unresolved targets remain external evidence.
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Sarcolipin promotes uncoupling of the SERCA Ca2+ pump by inducing a structural rearrangement in the energy-transduction domain
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Physical interactions between phospholamban and sarco(endo)plasmic reticulum Ca2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP
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Ablation of sarcolipin decreases the energy requirements for Ca2+ transport by sarco(endo)plasmic reticulum Ca2+-ATPases in resting skeletal muscle
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Structure and orientation of sarcolipin in lipid environments
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Functional reconstitution of recombinant phospholamban with rabbit skeletal Ca(2+)-ATPase
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Structural basis for relief of phospholamban-mediated inhibition of the sarcoplasmic reticulum Ca(2+)-ATPase at saturating Ca(2+) conditions
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Microsecond molecular simulations reveal a transient proton pathway in the calcium pump
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Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box size
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Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomes
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Phospholamban inhibitory function is activated by depolymerization
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Effects of phospholamban transmembrane mutants on the calcium affinity, maximal activity, and cooperativity of the sarcoplasmic reticulum calcium pump
10.1021/bi900852m · 2009 · External reference
Defining the molecular components of calcium transport regulation in a reconstituted membrane system
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Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
10.1006/jmbi.1996.0114 · 1996 · External reference
Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum
10.1074/jbc.273.23.14238 · 1998 · External reference
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Ca2+ occlusion and gating function of Glu309 in the ADP-fluoroaluminate analog of the Ca2+-ATPase phosphoenzyme intermediate
10.1074/jbc.m403211200 · 2004 · External reference
10.1038/emboj.2013.250
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Thermodynamics of cation binding to the sarcoendoplasmic reticulum calcium atpase pump and impacts on enzyme function
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Effects of pseudophosphorylation mutants on the structural dynamics of smooth muscle myosin regulatory light chain
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Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin
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The phospholamban pentamer alters function of the sarcoplasmic reticulum calcium pump SERCA
10.1016/j.bpj.2019.01.013 · 2019 · External reference
Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban
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Regulatory Role of Phospholamban in the Efficiency of Cardiac Sarcoplasmic Reticulum Ca2+ Transport
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Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPase
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Phospholamban domain I/cytochrome b5 transmembrane sequence chimeras do not inhibit SERCA2a
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Phospholamban regulates the Ca2+-ATPase through intramembrane interactions
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Residues 2-25 of phospholamban are insufficient to inhibit Ca2+ transport ATPase of cardiac sarcoplasmic reticulum
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