Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer (Q40140151)

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scientific article published on April 1999

Language	Label	Description	Also known as
English	Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer	scientific article published on April 1999

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer (English)

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

author name string

Pollesello P

1

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

Annila A

2

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

Ovaska M

3

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

language of work or name

0 references

publication date

1 April 1999

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

Biophysical Journal

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

76

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

4

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

1784-1795

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

Using experimental information to produce a model of the transmembrane domain of the ion channel phospholamban

1 reference

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AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR

1 reference

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The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?

1 reference

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Temperature coefficients of amide proton NMR resonance frequencies in trifluoroethanol: a monitor of intramolecular hydrogen bonds in helical peptides.

1 reference

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Fourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban

1 reference

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22 September 2017

Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban.

1 reference

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Total synthesis and functional properties of the membrane-intrinsic protein phospholamban

1 reference

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

1 reference

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

1 reference

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

1 reference

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1 reference

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Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban

1 reference

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Three-dimensional structure of proteins determined by molecular dynamics with interproton distance restraints: application to crambin

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Regulation of the Ca2+ pump ATPase by cAMP-dependent phosphorylation of phospholamban

1 reference

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Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin

1 reference

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1 reference

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Mechanism by which cyclic adenosine 3':5'-monophosphate-dependent protein kinase stimulates calcium transport in cardiac sarcoplasmic reticulum

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Control of calcium transport in the myocardium by the cyclic AMP-Protein kinase system

1 reference

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Phospholamban: a regulatory protein of the cardiac sarcoplasmic reticulum

1 reference

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Phospholamban inhibitory function is activated by depolymerization

1 reference

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Phospholamban regulates the Ca2+-ATPase through intramembrane interactions

1 reference

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Structure and functions of channel-forming peptides: magainins, cecropins, melittin and alamethicin

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Phospholamban forms Ca2+-selective channels in lipid bilayers.

1 reference

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Cysteine reactivity and oligomeric structures of phospholamban and its mutants.

1 reference

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Functional Co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation

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The hydrophilic domain of phospholamban inhibits the Ca2+ transport step of the Ca(2+)-ATPase

1 reference

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Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum

1 reference

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Identification of a calmodulin-dependent protein kinase in the cardiac cytosol, which phosphorylates phospholamban in the sarcoplasmic reticulum

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Secondary structure of detergent-solubilized phospholamban, a phosphorylatable, oligomeric protein of cardiac sarcoplasmic reticulum

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Regulation of the calcium ion pump of sarcoplasmic reticulum: Reversible inhibition by phospholamban and by the calmodulin binding domain of the plasma membrane calcium pump

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An investigation of the mechanism of inhibition of the Ca(2+)-ATPase by phospholamban

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Translation of Ser16 and Thr17 phosphorylation of phospholamban into Ca 2+-pump stimulation

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Computational searching and mutagenesis suggest a structure for the pentameric transmembrane domain of phospholamban

1 reference

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Two‐dimensional spectroscopy. Application to nuclear magnetic resonance

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Temperature dependence of 1H chemical shifts in proteins

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Complete assignment of the 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Application of an integrated approach to spin system identification in proteins

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Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers

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Interaction of calmodulin with phospholamban and caldesmon: comparative studies by 1H-NMR spectroscopy

1 reference

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The effect of 17O on the relaxation of an amide proton within a hydrogen bond

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Conformation of the cytoplasmic domain of phospholamban by NMR and CD

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Mechanism of inhibition of the Ca(2+)-ATPase by spermine and other polycationic compounds

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Subunit structure and multiple phosphorylation sites of phospholamban

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The Secondary Structure of Phospholamban: A Two-Dimensional NMR Study

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Alterations of Sarcoplasmic Reticulum Proteins in Failing Human Dilated Cardiomyopathy

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Conformational effects of serine phosphorylation in phospholamban peptides

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A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure

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The effect of N-terminal acetylation on Ca(2+)-ATPase inhibition by phospholamban

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Evidence for a phosphorylation-induced conformational change in phospholamban cytoplasmic domain by CD analysis

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1 reference

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Residues 2-25 of phospholamban are insufficient to inhibit Ca2+ transport ATPase of cardiac sarcoplasmic reticulum

1 reference

https://pubmed.ncbi.nlm.nih.gov/10096878

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban.

1 reference

https://pubmed.ncbi.nlm.nih.gov/10096878

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains

1 reference

https://pubmed.ncbi.nlm.nih.gov/10096878

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Isoproterenol induces both cAMP- and calcium-dependent phosphorylation of phospholamban in canine heart in vivo

1 reference

https://pubmed.ncbi.nlm.nih.gov/10096878

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1016/S0006-3495(99)77339-X

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

17 September 2017

ResearchGate publication ID

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