Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F1‐ATPase

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1. 1Identification of a tyrosine residue at a nucleotide binding site in the beta subunit of the mitochondrial ATPase with p-fluorosulfonyl[14C]-benzoyl-5'-adenosine.1978 · 208 citations
2. 2Effect of dicyclohexylcarbodiimide on unisite and multisite catalytic activities of the adenosine triphosphatase of Escherichia coli1985 · 49 citations
3. 3The Mechanism and Regulation of ATP Synthesis by F1-ATPases1981 · 311 citations
4. 4Replacement of arginine 246 by histidine in the beta subunit of Escherichia coli H+-ATPase resulted in loss of multi-site ATPase activity.1986 · 101 citations
5. 5Identification of the lysine residue to which the 4-nitrobenzofurazan group migrates after the bovine mitochondrial F1-ATPase is inactivated with 7-chloro-4-nitro[14C]benzofurazan.1984 · 84 citations