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. (Q40880128)

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English	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.	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

24 September 2017

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. (English)

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Europe PubMed Central

PubMed publication ID

24 September 2017

phosphorylation

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author name string

Asahi M

1

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Europe PubMed Central

PubMed publication ID

24 September 2017

McKenna E

2

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Europe PubMed Central

PubMed publication ID

24 September 2017

Kurzydlowski K

3

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Europe PubMed Central

PubMed publication ID

24 September 2017

Tada M

4

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24 September 2017

MacLennan DH

5

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24 September 2017

language of work or name

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publication date

1 May 2000

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24 September 2017

Journal of Biological Chemistry

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24 September 2017

275

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24 September 2017

20

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24 September 2017

15034-15038

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Europe PubMed Central

PubMed publication ID

24 September 2017

The Mechanism of Ca2+ Transport by Sarco(Endo)plasmic Reticulum Ca2+-ATPases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Phospholamban: a prominent regulator of myocardial contractility

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Phospholamban regulates the Ca2+-ATPase through intramembrane interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Phospholamban inhibitory function is activated by depolymerization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Characterization and quantitation of phospholamban and its phosphorylation state using antibodies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

The physical mechanism of calcium pump regulation in the heart

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Conformational transitions of the sarcoplasmic reticulum Ca-ATPase studied by time-resolved EPR and quenched-flow kinetics

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Location of high affinity Ca2+-binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Nature and site of phospholamban regulation of the Ca2+ pump of sarcoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.20.15034

21 January 2018

Identifiers

10.1074/JBC.275.20.15034

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

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