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- [1] DEMONSTRATION OF COOPERATING ALPHA-SUBUNITS IN WORKING (NA+ + K+)-ATPASE BY THE USE OF THE MGATP-COMPLEX ANALOG COBALT TETRAMMINE ATP EUROPEAN JOURNAL OF BIOCHEMISTRY, 1987, 168 (01): : 123 - 131
- [2] SHIFT TO THE NA+ FORM OF NA+/K+-TRANSPORTING ATPASE DUE TO MODIFICATION OF THE LOW-AFFINITY ATP-BINDING SITE BY CO(NH3)4ATP EUROPEAN JOURNAL OF BIOCHEMISTRY, 1989, 183 (01): : 173 - 178
- [3] Nucleotides trigger the release of Co(NH3)4ATP tightly bound to inactivated Na,K-ATPase NA/K-ATPASE AND RELATED TRANSPORT ATPASES: STRUCTURE, MECHANISM, AND REGULATION, 1997, 834 : 432 - 434
- [4] Independent access of fluorescein isothiocyanate and Co(NH3)4ATP to their binding sites on the protomer of Na,K-ATPase NA,K-ATPASE AND RELATED CATION PUMPS: STRUCTURE, FUNCTION, AND REGULATORY MECHANISMS, 2003, 986 : 265 - 266