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Journal of Molecular Biology|June 30, 2000
Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetaseM E Fraser, M N James, W A Bridger, et al.The Journal of Biological Chemistry|December 10, 1983
Thiophosphorylation as a probe for subunit interactions in Escherichia coli succinyl coenzyme A synthetase. Further evidence for catalytic cooperativity and substrate synergismW T Wolodko, E R Brownie, M D O'Connor, et al.The Journal of Biological Chemistry|August 22, 1997
Mutually exclusive splicing generates two distinct isoforms of pig heart succinyl-CoA synthetaseD G Ryan, T Lin, E Brownie, et al.Biochemical Society Symposium|January 1, 1987
The subunits of succinyl-coenzyme A synthetase--function and assemblyW A Bridger, W T Wolodko, W Henning, et al.Biochemistry|January 8, 2000
ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallographyM A Joyce, M E Fraser, M N James, et al.Journal of Molecular Biology|January 26, 1999
A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesisD L Bailey, M E Fraser, W A Bridger, et al.Biochemistry|July 22, 1997
Productive interactions between the two domains of pig heart CoA transferase during folding and assemblyJ C Rochet, K Oikawa, L D Hicks, et al.Biochemistry|June 3, 1999
Probing the nucleotide-binding site of Escherichia coli succinyl-CoA synthetaseM A Joyce, M E Fraser, E R Brownie, et al.Biochemistry|September 14, 2000
Pig heart CoA transferase exists as two oligomeric forms separated by a large kinetic barrierJ C Rochet, E R Brownie, K Oikawa, et al.Pageof 4