Atomic-level mechanisms for phospholamban regulation of the calcium pump. - Test2 - elhamkhani - TriplyDB

Atomic-level mechanisms for phospholamban regulation of the calcium pump.

Atomic-level mechanisms for phospholamban regulation of the calcium pump.

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Structure of myosin filaments from relaxed Lethocerus flight muscle by cryo-EM at 6 Å resolution.The Ca2+-ATPase pump facilitates bidirectional proton transport across the sarco/endoplasmic reticulum.Sarcolipin and phospholamban inhibit the calcium pump by populating a similar metal ion-free intermediate state.Hide and Seek: Protein-coding Sequences Inside "Non-coding" RNAs.Sarcolipin Promotes Uncoupling of the SERCA Ca2+ Pump by Inducing a Structural Rearrangement in the Energy-Transduction Domain.Self-assembling study of sarcolipin and its mutants in multiple molecular dynamic simulations.Preexisting domain motions underlie protonation-dependent structural transitions of the P-type Ca2+-ATPase.

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Atomic-level mechanisms for phospholamban regulation of the calcium pump.

http://www.wikidata.org/entity/Q35333572

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2015 nî lūn-bûn

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2015 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի ապրիլին հրատարակված գիտական հոդված

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2015年の論文

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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2015年学术文章

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name

Atomic-level mechanisms for phospholamban regulation of the calcium pump.

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Atomic-level mechanisms for phospholamban regulation of the calcium pump.

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Atomic-level mechanisms for phospholamban regulation of the calcium pump.

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Atomic-level mechanisms for phospholamban regulation of the calcium pump.

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Atomic-level mechanisms for phospholamban regulation of the calcium pump.

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Atomic-level mechanisms for phospholamban regulation of the calcium pump.

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J.BPJ.2015.03.004

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Biophysical Journal

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Atomic-level mechanisms for phospholamban regulation of the calcium pump

@en

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G Lizbeth Ramírez-Salinas

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Joseph M Autry

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P2860

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

Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase.

Ion pathways in the sarcoplasmic reticulum Ca2+-ATPase

Very fast prediction and rationalization of pKa values for protein-ligand complexes

Exploring the conformational transitions of biomolecular systems using a simple two-state anisotropic network model

Structural changes in the calcium pump accompanying the dissociation of calcium

Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach

Structures of the Excited States of Phospholamban and Shifts in Their Populations upon Phosphorylation

The Structural Basis for Phospholamban Inhibition of the Calcium Pump in Sarcoplasmic Reticulum

SERCA mutant E309Q binds two Ca2+ions but adopts a catalytically incompetent conformation

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