The phosphorylation site of the Kdp-ATPase of Escherichia coli: site-directed mutagenesis of the aspartic acid residues 300 and 307 of the KdpB subunit-Reference-Cited by-同舟云学术

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The phosphorylation site of the Kdp-ATPase of Escherichia coli: site-directed mutagenesis of the aspartic acid residues 300 and 307 of the KdpB subunit

Published:1992-12 Issue:23 Volume:6 Page:3511-3520
ISSN:0950-382X
Container-title:Molecular Microbiology
language:en
Short-container-title:Mol Microbiol

Author:

Puppe Wolfram,Siebers Annette,Altendorf Karlheinz

Publisher

Wiley

Subject

Molecular Biology,Microbiology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.1992.tb01786.x/fullpdf

Reference47 articles.

1. Transduction of chromosomal genes and episomes in Escherichia coli

2. An automated continuous assay of membrane-bound and soluble ATPases and related enzymes

3. A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots

4. Specific cesium transport via the Escherichia coli Kup (TrkD) K+ uptake system

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1. P-type ATPases: Many more enigmas left to solve;Journal of Biological Chemistry;2023-11

2. Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC;Nature Communications;2021-08-24

3. Molecular Mechanisms for Bacterial Potassium Homeostasis;Journal of Molecular Biology;2021-08

4. Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC;2021-05-18

5. The KdpFABC complex – K+transport against all odds;Molecular Membrane Biology;2019-01-01

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