(Q44370255)

English

Importance of conserved N-domain residues Thr441, Glu442, Lys515, Arg560, and Leu562 of sarcoplasmic reticulum Ca2+-ATPase for MgATP binding and subsequent catalytic steps. Plasticity of the nucleotide-binding site

scientific article published on 20 March 2003

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Europe PubMed Central

PubMed publication ID

2 December 2017

Importance of conserved N-domain residues Thr441, Glu442, Lys515, Arg560, and Leu562 of sarcoplasmic reticulum Ca2+-ATPase for MgATP binding and subsequent catalytic steps. Plasticity of the nucleotide-binding site (English)

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

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author name string

Johannes D Clausen

1

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Europe PubMed Central

PubMed publication ID

2 December 2017

David B McIntosh

2

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Europe PubMed Central

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2 December 2017

Bente Vilsen

3

1 reference

Europe PubMed Central

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2 December 2017

David G Woolley

4

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Europe PubMed Central

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2 December 2017

Jens Peter Andersen

5

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Europe PubMed Central

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2 December 2017

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publication date

20 March 2003

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Europe PubMed Central

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2 December 2017

Journal of Biological Chemistry

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2 December 2017

278

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Europe PubMed Central

PubMed publication ID

2 December 2017

22

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Europe PubMed Central

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2 December 2017

20245-20258

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Evolution of substrate specificities in the P-type ATPase superfamily.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Characterization of the ATP-binding domain of the sarco(endo)plasmic reticulum Ca(2+)-ATPase: probing nucleotide binding by multidimensional NMR.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

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.M301122200

21 January 2018

Functional role of "N" (nucleotide) and "P" (phosphorylation) domain interactions in the sarcoplasmic reticulum (SERCA) ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

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.M301122200

21 January 2018

High-efficiency transformation of mammalian cells by plasmid DNA

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Interaction of nucleotides with Asp(351) and the conserved phosphorylation loop of sarcoplasmic reticulum Ca(2+)-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Affinity labeling of the active site of the Ca2+-ATPase of sarcoplasmic reticulum.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Fe(2+)-catalyzed oxidation and cleavage of sarcoplasmic reticulum ATPase reveals Mg(2+) and Mg(2+)-ATP sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

The ATP-Mg2+ binding site and cytoplasmic domain interactions of Na+,K+-ATPase investigated with Fe2+-catalyzed oxidative cleavage and molecular modeling

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Importance of Na,K-ATPase residue alpha 1-Arg544 in the segment Arg544-Asp567 for high-affinity binding of ATP, ADP, or MgATP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Stability of "salt bridges" in membrane proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

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.M301122200

21 January 2018

Structural changes in the calcium pump accompanying the dissociation of calcium

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Kinetic evidence for two nucleotide binding sites on the calcium ATPase of sarcoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Mechanism of allosteric regulation of the Ca,Mg-ATPase of sarcoplasmic reticulum: studies with 5'-adenylyl methylenediphosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Modeling a dehalogenase fold into the 8-A density map for Ca(2+)-ATPase defines a new domain structure

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Simultaneous binding of phosphate and TNP-ADP to FITC-modified NA+,K(+)-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Replacement of several single amino acid side chains exposed to the inside of the ATP-binding pocket induces different extents of affinity change in the high and low affinity ATP-binding sites of rat Na/K-ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Kinetics and Regulation of Sarcoplasmic Reticulum ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Structure of the calcium pump from sarcoplasmic reticulum at 8-Å resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M301122200

21 January 2018

Identifiers

10.1074/JBC.M301122200

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 December 2017

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