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Random Circular Permutation of Genes and Expressed Polypeptide Chains: Application of the Method to the Catalytic Chains of Aspartate Transcarbamoylase

Proceedings of the National Academy of Sciences - PNAS, 1996-10, Vol.93 (21), p.11591-11596

1996

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Binding of Bisubstrate Analog Promotes Large Structural Changes in the Unregulated Catalytic Trimer of Aspartate Transcarbamoylase: Implications for Allosteric Regulation

Proceedings of the National Academy of Sciences - PNAS, 2000-05, Vol.97 (10), p.5077-5082

2000

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Assessment of the Allosteric Mechanism of Aspartate Transcarbamoylase Based on the Crystalline Structure of the Unregulated Catalytic Subunit

Proceedings of the National Academy of Sciences - PNAS, 1999-05, Vol.96 (10), p.5388-5393

1999

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Can a simple model account for the allosteric transition of aspartate transcarbamoylase?

The Journal of biological chemistry, 1988-12, Vol.263 (35), p.18583-18586

Schachman, H K

1988

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Aspartate Transcarbamoylase Containing Circularly Permuted Catalytic Polypeptide Chains

Proceedings of the National Academy of Sciences - PNAS, 1993-12, Vol.90 (24), p.11980-11984

1993

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STILL LOOKING FOR THE IVORY TOWER

Annual review of biochemistry, 2000-01, Vol.69 (1), p.1-29

Schachman, Howard K

2000

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Shared Active Sites in Oligomeric Enzymes: Model Studies with Defective Mutants of Aspartate Transcarbamoylase Produced by Site-Directed Mutagenesis

Proceedings of the National Academy of Sciences - PNAS, 1987-01, Vol.84 (1), p.31-35

1987

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Quantitative urea gradient gel electrophoresis for studies of dissociation and unfolding of oligomeric proteins

Biophysical chemistry, 2002-12, Vol.101, p.133-144

2002

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Analytical ultracentrifugation reborn

Nature (London), 1989-09, Vol.341 (6239), p.259-260

Schachman, H. K

1989

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Regeneration of Active Enzyme by Formation of Hybrids from Inactive Derivatives: Implications for Active Sites Shared between Polypeptide Chains of Aspartate Transcarbamoylase

Proceedings of the National Academy of Sciences - PNAS, 1985-01, Vol.82 (2), p.361-365

1985

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Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase

Biochemistry (Easton), 1990-04, Vol.29 (15), p.3724-3731

1990

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In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: Implications for protein folding and assembly

Protein science, 1996-07, Vol.5 (7), p.1290-1300

1996

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Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Characterization of the active site and evidence for an interdomain carboxy‐terminal helix in ornithine transcarbamoylase

Protein science, 1996-04, Vol.5 (4), p.709-718

1996

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Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions

The Journal of biological chemistry, 1992-02, Vol.267 (4), p.2443-2450

1992

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Homotropic effects in aspartate transcarbamoylase: What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl- l-aspartate?

Journal of molecular biology, 1985-11, Vol.186 (1), p.175-184

1985

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Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme

The Journal of biological chemistry, 1991-11, Vol.266 (31), p.20833-20839

1991

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Role of a Carboxyl-Terminal Helix in the Assembly, Interchain Interactions, and Stability of Aspartate Transcarbamoylase

Proceedings of the National Academy of Sciences - PNAS, 1991-01, Vol.88 (2), p.458-462

1991

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Changes in Stability and Allosteric Properties of Aspartate Transcarbamoylase Resulting from Amino Acid Substitutions in the Zinc-Binding Domain of the Regulatory Chains

Proceedings of the National Academy of Sciences - PNAS, 1989-05, Vol.86 (9), p.3094-3098

1989

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Application of Methyl-TROSY NMR to Test Allosteric Models Describing Effects of Nucleotide Binding to Aspartate Transcarbamoylase

Journal of molecular biology, 2009-04, Vol.387 (3), p.540-547

2009

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A 70-Amino Acid Zinc-Binding Polypeptide from the Regulatory Chain of Aspartate Transcarbamoylase Forms a Stable Complex with the Catalytic Subunit Leading to Markedly Altered Enzyme Activity

Proceedings of the National Academy of Sciences - PNAS, 1991-12, Vol.88 (23), p.10568-10572

1991

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Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Implications for domain switching

Protein science, 1996-04, Vol.5 (4), p.719-728

1996

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Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase: Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments

Journal of molecular biology, 1989-03, Vol.206 (1), p.221-230

1989

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Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP

The Journal of biological chemistry, 1989-02, Vol.264 (5), p.2476-2481

1989

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Site-specific mutagenesis of aspartate transcarbamoylase. Replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activity

The Journal of biological chemistry, 1984-09, Vol.259 (18), p.11180-11183

1984

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Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine

Biochemistry (Easton), 1992-07, Vol.31 (28), p.6585-6591

1992

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Random Circular Permutation of Genes and Expressed Polypeptide Chains: Application of the Method to the Catalytic Chains of Aspartate Transcarbamoylase

Binding of Bisubstrate Analog Promotes Large Structural Changes in the Unregulated Catalytic Trimer of Aspartate Transcarbamoylase: Implications for Allosteric Regulation

Assessment of the Allosteric Mechanism of Aspartate Transcarbamoylase Based on the Crystalline Structure of the Unregulated Catalytic Subunit

Can a simple model account for the allosteric transition of aspartate transcarbamoylase?

Aspartate Transcarbamoylase Containing Circularly Permuted Catalytic Polypeptide Chains

STILL LOOKING FOR THE IVORY TOWER

Shared Active Sites in Oligomeric Enzymes: Model Studies with Defective Mutants of Aspartate Transcarbamoylase Produced by Site-Directed Mutagenesis

Quantitative urea gradient gel electrophoresis for studies of dissociation and unfolding of oligomeric proteins

Analytical ultracentrifugation reborn

Regeneration of Active Enzyme by Formation of Hybrids from Inactive Derivatives: Implications for Active Sites Shared between Polypeptide Chains of Aspartate Transcarbamoylase

Heterotropic effectors promote a global conformational change in aspartate transcarbamoylase

In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: Implications for protein folding and assembly

Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Characterization of the active site and evidence for an interdomain carboxy‐terminal helix in ornithine transcarbamoylase

Long range effects of amino acid substitutions in the catalytic chain of aspartate transcarbamoylase. Localized replacements in the carboxyl-terminal alpha-helix cause marked alterations in allosteric properties and intersubunit interactions

Homotropic effects in aspartate transcarbamoylase: What happens when the enzyme binds a single molecule of the bisubstrate analog N-phosphonacetyl- l-aspartate?

Different amino acid substitutions at the same position in the nucleotide-binding site of aspartate transcarbamoylase have diverse effects on the allosteric properties of the enzyme

Role of a Carboxyl-Terminal Helix in the Assembly, Interchain Interactions, and Stability of Aspartate Transcarbamoylase

Changes in Stability and Allosteric Properties of Aspartate Transcarbamoylase Resulting from Amino Acid Substitutions in the Zinc-Binding Domain of the Regulatory Chains

Application of Methyl-TROSY NMR to Test Allosteric Models Describing Effects of Nucleotide Binding to Aspartate Transcarbamoylase

A 70-Amino Acid Zinc-Binding Polypeptide from the Regulatory Chain of Aspartate Transcarbamoylase Forms a Stable Complex with the Catalytic Subunit Leading to Markedly Altered Enzyme Activity

Structural similarity between ornithine and aspartate transcarbamoylases of Escherichia coli: Implications for domain switching

Analysis of the ligand-promoted global conformational change in aspartate transcarbamoylase: Evidence for a two-state transition from boundary spreading in sedimentation velocity experiments

Cooperative binding of the bisubstrate analog N-(phosphonacetyl)-L-aspartate to aspartate transcarbamoylase and the heterotropic effects of ATP and CTP

Site-specific mutagenesis of aspartate transcarbamoylase. Replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activity

Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine

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