Families of Soft-Metal-Ion-Transporting ATPases
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, Michigan 48201
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JB.181.19.5891-5897.1999
Reference64 articles.
1. Evolution of substrate specificities in the P-type ATPase superfamily;Axelsen K. B.;J. Mol. Evol.,1998
2. Zinc(II) tolerance in Escherichia coli K-12: evidence that the zntA gene (o732) encodes a cation transport ATPase;Beard S. J.;Mol. Microbiol.,1997
3. Role of cysteinyl residues in metalloactivation of the oxyanion-translocating ArsA ATPase;Bhattacharjee H.;J. Biol. Chem.,1995
4. Spatial proximity of Cys113, Cys172, and Cys422 in the metalloactivation domain of the ArsA ATPase;Bhattacharjee H.;J. Biol. Chem.,1996
5. ZntR is a Zn(II)-responsive MerR-like transcriptional regulator of zntA in Escherichia coli
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