Mutagenesis of the C-terminal nucleotide-binding site of an anion-translocating ATPase.
Open Access
- 1 September 1992
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 267 (27) , 19272-19277
- https://doi.org/10.1016/s0021-9258(18)41771-1
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Structurally and catalytically important residues in the phosphate binding loop of adenylate kinase of Escherichia coliBiochemistry, 1990
- Identification of the Cystic Fibrosis Gene: Cloning and Characterization of Complementary DNAScience, 1989
- The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoproteinNature, 1989
- Site-directed mutagenesis of stable adenosine triphosphate synthaseBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
- NMR studies of the magnesium-ATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzymeBiochemistry, 1985
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- A plasmid-encoded arsenite pump produces arsenite resistance in Escherichia coliBiochemical and Biophysical Research Communications, 1984
- Direct and specific photochemical crosslinking of adenosine 5'-triphosphate to an aminoacyl-tRNA synthetaseBiochemistry, 1977
- ATPase of Escherichia coli: purification, dissociation, and reconstitution of the active complex from the isolated subunitsBiochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970