Structure-function relation of phospholamban: modulation of channel activity as a potential regulator of SERCA activity. - Wikidata - awgldk - TriplyDB

Structure-function relation of phospholamban: modulation of channel activity as a potential regulator of SERCA activity.

Structure-function relation of phospholamban: modulation of channel activity as a potential regulator of SERCA activity.

http://www.wikidata.org/entity/Q34544548

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Structural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium Transport Engineered transmembrane pores.General rules for the arrangements and gating motions of pore-lining helices in homomeric ion channels.Acute inotropic and lusitropic effects of cardiomyopathic R9C mutation of phospholamban.Investigation of Pathogenic Genes in Chinese sporadic Hypertrophic Cardiomyopathy Patients by Whole Exome Sequencing Posttranslational modifications of calcium/calmodulin-dependent protein kinase IIδ and its downstream signaling in human failing hearts.Self-assembling study of sarcolipin and its mutants in multiple molecular dynamic simulations.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.

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P2860

Structure-function relation of phospholamban: modulation of channel activity as a potential regulator of SERCA activity.

http://www.wikidata.org/entity/Q34544548

description

2013 nî lūn-bûn

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2013 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հունվարին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

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Structure-function relation of ...... l regulator of SERCA activity.

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Andrea Saponaro

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Howard S Young

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Maria Rosa Moncelli

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P2860

Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy

Effects of phospholamban transmembrane mutants on the calcium affinity, maximal activity, and cooperativity of the sarcoplasmic reticulum calcium pump

NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles

Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method

The chloroplast protein import channel Toc75: pore properties and interaction with transit peptides.

Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy.

Förster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex.

The structure of phospholamban pentamer reveals a channel-like architecture in membranes

Phospholamban and cardiac contractile function.

Dilated cardiomyopathy and heart failure caused by a mutation in phospholamban.

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scholarly article

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10.1371/JOURNAL.PONE.0052744

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1

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Serena Smeazzetto

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