Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents (Q40634835)

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scientific article published on 12 September 2003

Language	Label	Description	Also known as
English	Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents	scientific article published on 12 September 2003

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents (English)

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

author name string

Zhenhui Chen

1

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

David L Stokes

2

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

William J Rice

3

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Larry R Jones

4

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

language of work or name

0 references

publication date

12 September 2003

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

22 September 2017

278

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

48

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

48348-48356

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Phospholamban: a promising therapeutic target in heart failure?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Cardiac excitation-contraction coupling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Close proximity between residue 30 of phospholamban and cysteine 318 of the cardiac Ca2+ pump revealed by intermolecular thiol cross-linking.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Phospholamban inhibitory function is activated by depolymerization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

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.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Cooperative setting for long-range linkage of Ca(2+) binding and ATP synthesis in the Ca(2+) ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Structural changes in the calcium pump accompanying the dissociation of calcium

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Computational design of a water-soluble analog of phospholamban

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Structure and function of the calcium pump

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

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.M309545200

21 January 2018

Phospholamban reduces cardiac Ca-ATPase sensitivity to thapsigargin and cyclopiazonic acid

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Thapsigargin, a high affinity and global inhibitor of intracellular Ca2+ transport ATPases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Mapping of the dimer interface of the Escherichia coli mannitol permease by cysteine cross-linking

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Changing the lactose permease of Escherichia coli into a galactose-specific symporter

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Effects of various amino acid 256 mutations on sarcoplasmic/endoplasmic reticulum Ca2+ ATPase function and their role in the cellular adaptive response to thapsigargin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the Ca2+ transport activity of the Ca2+-ATPase expressed in COS-1 cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulers

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Chemical cross-linking and mass spectrometry for protein structural modeling.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

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.M309545200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

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.M309545200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Reexamination of the role of the leucine/isoleucine zipper residues of phospholamban in inhibition of the Ca2+ pump of cardiac sarcoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Characterisation of ATP binding inhibition to the sarcoplasmic reticulum Ca(2+)-ATPase by thapsigargin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M309545200

21 January 2018

Identifiers

10.1074/JBC.M309545200

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

ResearchGate publication ID

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