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The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution

The Journal of biological chemistry, 1994-04, Vol.269 (14), p.10883-10890

1994

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Pig Heart CoA Transferase Exists as Two Oligomeric Forms Separated by a Large Kinetic Barrier

Biochemistry (Easton), 2000-09, Vol.39 (37), p.11291-11302

2000

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A detailed structural description of Escherichia coli succinyl-CoA synthetase

Journal of molecular biology, 1999-01, Vol.285 (4), p.1633-1653

1999

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Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase

Journal of molecular biology, 2000-06, Vol.299 (5), p.1325-1339

2000

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The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-angstrom resolution

The Journal of biological chemistry, 1994-04, Vol.269 (14), p.10883-10890

1994

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Cloning, characterization, and expression of the β subunit of pig heart succinyl‐CoA synthetase

Protein science, 1993-08, Vol.2 (8), p.1255-1262

1993

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ADP-Binding Site of Escherichia coli Succinyl-CoA Synthetase Revealed by X-ray Crystallography

Biochemistry (Easton), 2000-01, Vol.39 (1), p.17-25

2000

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

Biochemistry (Easton), 1999-06, Vol.38 (22), p.7273-7283

1999

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Crystallization of succinyl-CoA synthetase from Escherichia coli

The Journal of biological chemistry, 1984-04, Vol.259 (8), p.5316-5320

1984

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

The Journal of biological chemistry, 1983-12, Vol.258 (23), p.14116-14119

1983

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Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli

Biochemistry (Easton), 1986-09, Vol.25 (19), p.5420-5425

1986

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Capacity for Alternating Sites Cooperativity in Catalysis by Succinyl-Coenzyme a Synthetase

Proceedings of the National Academy of Sciences - PNAS, 1981-04, Vol.78 (4), p.2140-2144

1981

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A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesis

Journal of molecular biology, 1999-01, Vol.285 (4), p.1655

1999

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Subunits of succinyl-coenzyme A synthetase: coordination of production in Escherichia coli and discovery of a factor that precludes refolding

Journal of Bacteriology, 1980-07, Vol.143 (1), p.231-237

1980

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Mutually Exclusive Splicing Generates Two Distinct Isoforms of Pig Heart Succinyl-CoA Synthetase

The Journal of biological chemistry, 1997-08, Vol.272 (34), p.21151-21159

1997

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Productive Interactions between the Two Domains of Pig Heart CoA Transferase during Folding and Assembly

Biochemistry (Easton), 1997-07, Vol.36 (29), p.8807-8820

1997

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A detailed structural description of Escherichia coli succinly-CoA synthetase

Journal of molecular biology, 1999-05, Vol.288 (3), p.501-501

1999

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The subunits of succinyl-coenzyme A synthetase--function and assembly

Biochemical Society Symposia, 1987, Vol.54, p.103

1987

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Studies of the process of renaturation and assembly of Escherichia coli succinyl-CoA synthetase from its alpha and beta subunits

Biochemistry and cell biology, 1987-05, Vol.65 (5), p.452-457

1987

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Structure of the Mammalian CoA Transferase from Pig Heart

Biochemistry (Easton), 2002-12, Vol.41 (49), p.14455-14462

2002

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Two Glutamate Residues, Glu 208α and Glu 197β, Are Crucial for Phosphorylation and Dephosphorylation of the Active-Site Histidine Residue in Succinyl-CoA Synthetase

Biochemistry (Easton), 2002-01, Vol.41 (2), p.537-546

2002

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Mechanism of succinyl-CoA synthetase

Acta crystallographica. Section A, Foundations of crystallography, 2002-08, Vol.58 (s1), p.c13-c13

2002

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Rabbit cardiac myosin. I. Physical and chemical characterization of the native molecule

Canadian journal of biochemistry, 1975-02, Vol.53 (2), p.164-174

1975

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Rabbit cardiac myosin. II. Proteolytic fragmentation with insolubilized papain

Canadian journal of biochemistry, 1975-02, Vol.53 (2), p.175-188

1975

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Observations on damage development in fibre reinforced polymer laminates under cyclic loading

International journal of fatigue, 2003-05, Vol.25 (5), p.437-446

2003

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The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution

Pig Heart CoA Transferase Exists as Two Oligomeric Forms Separated by a Large Kinetic Barrier

A detailed structural description of Escherichia coli succinyl-CoA synthetase

Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase

The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-angstrom resolution

Cloning, characterization, and expression of the β subunit of pig heart succinyl‐CoA synthetase

ADP-Binding Site of Escherichia coli Succinyl-CoA Synthetase Revealed by X-ray Crystallography

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

Crystallization of succinyl-CoA synthetase from Escherichia coli

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

Active enzyme sedimentation, sedimentation velocity, and sedimentation equilibrium studies of succinyl-CoA synthetases of porcine heart and Escherichia coli

Capacity for Alternating Sites Cooperativity in Catalysis by Succinyl-Coenzyme a Synthetase

A dimeric form of Escherichia coli succinyl-CoA synthetase produced by site-directed mutagenesis

Subunits of succinyl-coenzyme A synthetase: coordination of production in Escherichia coli and discovery of a factor that precludes refolding

Mutually Exclusive Splicing Generates Two Distinct Isoforms of Pig Heart Succinyl-CoA Synthetase

Productive Interactions between the Two Domains of Pig Heart CoA Transferase during Folding and Assembly

A detailed structural description of Escherichia coli succinly-CoA synthetase

The subunits of succinyl-coenzyme A synthetase--function and assembly

Studies of the process of renaturation and assembly of Escherichia coli succinyl-CoA synthetase from its alpha and beta subunits

Structure of the Mammalian CoA Transferase from Pig Heart

Two Glutamate Residues, Glu 208α and Glu 197β, Are Crucial for Phosphorylation and Dephosphorylation of the Active-Site Histidine Residue in Succinyl-CoA Synthetase

Mechanism of succinyl-CoA synthetase

Rabbit cardiac myosin. I. Physical and chemical characterization of the native molecule

Rabbit cardiac myosin. II. Proteolytic fragmentation with insolubilized papain

Observations on damage development in fibre reinforced polymer laminates under cyclic loading

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