(Q44259022)

English

Val200 residue in Lys189-Lys205 outermost loop on the A domain of sarcoplasmic reticulum Ca2+-ATPase is critical for rapid processing of phosphoenzyme intermediate after loss of ADP sensitivity

scientific article

In more languages

default for all languages

No label defined

No description defined

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Val200 residue in Lys189-Lys205 outermost loop on the A domain of sarcoplasmic reticulum Ca2+-ATPase is critical for rapid processing of phosphoenzyme intermediate after loss of ADP sensitivity (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

author name string

Sanae Kato

1

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Mika Kamidochi

2

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Takashi Daiho

3

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Kazuo Yamasaki

4

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Wang Gouli

5

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Hiroshi Suzuki

6

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

language of work or name

0 references

publication date

19 December 2002

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

278

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

11

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

9624-9629

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

ADENOSINE TRIPHOSPHATE-LINKED CONCENTRATION OF CALCIUM IONS IN A PARTICULATE FRACTION OF RABBIT MUSCLE

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Structural organization, ion transport, and energy transduction of P-type ATPases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

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.M208861200

21 January 2018

Energy Interconversion by the Ca2+-Dependent ATPase of the Sarcoplasmic Reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Mechanism of calcium transport

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

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.M208861200

21 January 2018

Structural changes in the calcium pump accompanying the dissociation of calcium

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

ADP-insensitive phosphoenzyme intermediate of sarcoplasmic reticulum Ca(2+)-ATPase has a compact conformation resistant to proteinase K, V8 protease and trypsin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Organization of cytoplasmic domains of sarcoplasmic reticulum Ca(2+)-ATPase in E(1)P and E(1)ATP states: a limited proteolysis study

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

The complex ATP-Fe(2+) serves as a specific affinity cleavage reagent in ATP-Mg(2+) sites of Na,K-ATPase: altered ligation of Fe(2+) (Mg(2+)) ions accompanies the E(1)-->E(2) conformational change

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

The phosphorylation state of eucaryotic initiation factor 2 alters translational efficiency of specific mRNAs

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

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.M208861200

21 January 2018

Formation and decomposition of a phosphorylated intermediate in the reaction of Na plus-K plus dependent ATPase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Kinetic and equilibrium characterization of an energy-transducing enzyme and its partial reactions.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Evaluation of H2O activity in the free or phosphorylated catalytic site of Ca2+-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Transient-state kinetics of the ADP-insensitive phosphoenzyme in sarcoplasmic reticulum: implications for transient-state calcium translocation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Modification of Arginine-198 in Sarcoplasmic Reticulum Ca2+-ATPase by 1,2-Cyclohexanedione Causes Inhibition of Formation of the Phosphoenzyme Intermediate from Inorganic Phosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Mutations of Arg198 in sarcoplasmic reticulum Ca2+-ATPase cause inhibition of hydrolysis of the phosphoenzyme intermediate formed from inorganic phosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Deletions or specific substitutions of a few residues in the NH(2)-terminal region (Ala(3) to Thr(9)) of sarcoplasmic reticulum Ca(2+)-ATPase cause inactivation and rapid degradation of the enzyme expressed in COS-1 cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Role of water in the energy of hydrolysis of phosphate compounds--energy transduction in biological membranes.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M208861200

21 January 2018

Identifiers

10.1074/JBC.M208861200

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 December 2017

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q44259022&oldid=2108956564"