Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy - Wikidata - awgldk - TriplyDB

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

http://www.wikidata.org/entity/Q34176103

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Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy Systems biology and the virtual physiological human Phospholamban C-terminal residues are critical determinants of the structure and function of the calcium ATPase regulatory complex.Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump Regulation of the sarcoplasmic reticulum calcium pump by divergent phospholamban isoforms in zebrafish.Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A.Sarco(endo)plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail.Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.Phosphorylated phospholamban stabilizes a compact conformation of the cardiac calcium-ATPase.Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban Phospholamban modulates the functional coupling between nucleotide domains in Ca-ATPase oligomeric complexes in cardiac sarcoplasmic reticulum.Sarcoplasmic reticulum function in smooth muscle.The FRET signatures of noninteracting proteins in membranes: simulations and experiments.Fourier-Bessel reconstruction of helical assemblies.Lipid-mediated folding/unfolding of phospholamban as a regulatory mechanism for the sarcoplasmic reticulum Ca2+-ATPase Cardiac Calcium ATPase Dimerization Measured by Cross-Linking and Fluorescence Energy Transfer.Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents.On the function of pentameric phospholamban: ion channel or storage form?Conformational memory in the association of the transmembrane protein phospholamban with the sarcoplasmic reticulum calcium pump SERCA.Solid-state NMR reveals structural changes in phospholamban accompanying the functional regulation of Ca2+-ATPase

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Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

http://www.wikidata.org/entity/Q34176103

description

2001 nî lūn-bûn

@nan

2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2001 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2001年の論文

@ja

2001年論文

@yue

2001年論文

@zh-hant

2001年論文

@zh-hk

2001年論文

@zh-mo

2001年論文

@zh-tw

2001年论文

@wuu

name

Locating phospholamban in co-crystals with Ca

@nl

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

@ast

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

@en

type

label

Locating phospholamban in co-crystals with Ca

@nl

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

@ast

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

@en

prefLabel

Locating phospholamban in co-crystals with Ca

@nl

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

@ast

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

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P1433

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P356

S0006-3495(01)75748-7

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Biophysical Journal

P1476

Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy

@en

P2093

D L Stokes

http://www.w3.org/2001/XMLSchema#string

H S Young

http://www.w3.org/2001/XMLSchema#string

L R Jones

http://www.w3.org/2001/XMLSchema#string

P2860

Protein measurement with the Folin phenol reagent

Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution

Solution structure of the cytoplasmic domain of phopholamban: phosphorylation leads to a local perturbation in secondary structure

Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites

Chronic phospholamban-sarcoplasmic reticulum calcium ATPase interaction is the critical calcium cycling defect in dilated cardiomyopathy

Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation

A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples

Phospholamban: protein structure, mechanism of action, and role in cardiac function.

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

Functional reconstitution of recombinant phospholamban with rabbit skeletal Ca(2+)-ATPase.

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884-894

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scholarly article

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10.1016/S0006-3495(01)75748-7

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2

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1301560

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