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An n.m.r. probe of succinyl-coenzyme A synthetase: subunit interactions and the mechanism of action

Biochem Soc Trans (1983) 11 (3): 315–323.

This article has been cited by the following articles in journals that are participating in CrossRef Cited-by Linking.

Probing the Nucleotide-Binding Site of Escherichia coli Succinyl-CoA Synthetase

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Marie E. Fraser
Edward R. Brownie
Michael N. G. James
William A. Bridger
William T. Wolodko

Biochemistry (1999) 38 (22): 7273.

Native-like intermediate on the folding pathway of Escherichia coli succinyl-CoA synthetase.

I A Khan
J S Nishimura

Journal of Biological Chemistry (1988) 263 (5): 2152.

Reaction of substrates with 35S-thiophosphorylated succinyl-CoA synthetase of pig heart. Similarities to the case of the Escherichia coli enzyme.

J S Nishimura
T Mitchell

Journal of Biological Chemistry (1985) 260 (4): 2077.

31P NMR chemical shifts of phosphate covalently bound to proteins

Günter Matheis
John R. Whitaker

International Journal of Biochemistry (1984) 16 (8): 867.

Thiophosphorylation as a probe for subunit interactions in Escherichia coli succinyl coenzyme A synthetase. Further evidence for catalytic cooperativity and substrate synergism.

W T Wolodko
E R Brownie
M D O'Connor
W A Bridger

Journal of Biological Chemistry (1983) 258 (23): 14116.

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