A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-ATPase (AHA1 isoform): site and mechanism of action on H+-ATPase activity differ from those of 14-3-3 proteins. (Q44105230)

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scientific article published in August 2002

Language	Label	Description	Also known as
English	A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-ATPase (AHA1 isoform): site and mechanism of action on H+-ATPase activity differ from those of 14-3-3 proteins.	scientific article published in August 2002

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scholarly article

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12 November 2019

A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-ATPase (AHA1 isoform): site and mechanism of action on H+-ATPase activity differ from those of 14-3-3 proteins (English)

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12 November 2019

Arabidopsis thaliana

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Piero Morandini

1

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12 November 2019

Maria Cristina Bonza

4

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12 November 2019

Maria Ida De Michelis

9

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12 November 2019

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Marco Valera

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12 November 2019

Cristina Albumi

3

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12 November 2019

Sonia Giacometti

5

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12 November 2019

Giuseppe Ravera

6

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12 November 2019

Irene Murgia

7

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12 November 2019

Carlo Soave

8

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12 November 2019

publication date

1 August 2002

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12 November 2019

The Plant Journal

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12 November 2019

31

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12 November 2019

4

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12 November 2019

487-497

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12 November 2019

The 14-3-3 proteins associate with the plant plasma membrane H(+)-ATPase to generate a fusicoccin binding complex and a fusicoccin responsive system

1 reference

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Cloning and expression of human NF-YC

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21 January 2018

At-ACA8 encodes a plasma membrane-localized calcium-ATPase of Arabidopsis with a calmodulin-binding domain at the N terminus

1 reference

https://api.crossref.org/works/10.1046%2FJ.1365-313X.2002.01373.X

21 January 2018

Adenosine 5'-monophosphate inhibits the association of 14-3-3 proteins with the plant plasma membrane H(+)-ATPase

1 reference

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21 January 2018

The two major plant plasma membrane H+-ATPases display different regulatory properties

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The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit

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Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins

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Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947).

1 reference

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21 January 2018

Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure

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The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases

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High efficiency transformation of Escherichia coli with plasmids

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Post-translational modification of plant plasma membrane H(+)-ATPase as a requirement for functional complementation of a yeast transport mutant.

1 reference

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21 January 2018

Binding of regulatory 14-3-3 proteins to the C terminus of the plant plasma membrane H+ -ATPpase involves part of its autoinhibitory region

1 reference

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21 January 2018

A soluble auxin-binding protein, ABP57. Purification with anti-bovine serum albumin antibody and characterization of its mechanistic role in the auxin effect on plant plasma membrane H+-ATPase

1 reference

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21 January 2018

Blue light activates the plasma membrane H(+)-ATPase by phosphorylation of the C-terminus in stomatal guard cells

1 reference

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21 January 2018

Analysis of the phosphorylation level in guard-cell plasma membrane H+-ATPase in response to fusicoccin

1 reference

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

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A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples

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A plant plasma membrane H+-ATPase expressed in yeast is activated by phosphorylation at its penultimate residue and binding of 14-3-3 regulatory proteins in the absence of fusicoccin.

1 reference

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21 January 2018

PLANT PLASMA MEMBRANE H+-ATPases: Powerhouses for Nutrient Uptake

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H-pumping driven by the plasma membrane ATPase in membrane vesicles from radish: stimulation by fusicoccin.

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21 January 2018

Identifiers

10.1046/J.1365-313X.2002.01373.X

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12182706%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12182706%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

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