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solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase

Proceedings of the National Academy of Sciences - PNAS, 2007-05, Vol.104 (21), p.8815-8820

2007

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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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Random circular permutation leading to chain disruption within and near α helices in the catalytic chains of aspartate transcarbamoylase: Effects on assembly, stability, and function

Protein science, 2001-03, Vol.10 (3), p.528-537

2001

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Cooperative Interactions in Aspartate Transcarbamoylase. 1. Hybrids Composed of Native and Chemically Inactivated Catalytic Polypeptide Chains

Proceedings of the National Academy of Sciences - PNAS, 1974-11, Vol.71 (11), p.4452-4456

1974

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Ultrasonographic Characteristics of Cortical Sulcus Development in the Human Fetus between 18 and 41 Weeks of Gestation

Chinese medical journal, 2017-04, Vol.130 (8), p.920-928

2017

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Why cannot Maria be extinguished in Burkina Faso?

Journal of microbiology, immunology and infection, 2015-04, Vol.48 (2), p.S119-S119

2015

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Ligand-Promoted Weakening of Intersubunit Bonding Domains in Aspartate Transcarbamoylase

Proceedings of the National Academy of Sciences - PNAS, 1977-09, Vol.74 (9), p.3777-3781

1977

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Preparation of 125I-Catalytic Subunit of Aspartate Transcarbamylase and Its Use in Studies of the Regulatory Subunit

The Journal of biological chemistry, 1973-06, Vol.248 (11), p.3762-3768

1973

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In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains

Protein science, 1993-06, Vol.2 (6), p.1013-1023

1993

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A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: assembly, oligomers, and domains

Biophysical chemistry, 1996-04, Vol.59 (3), p.289-297

1996

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Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains

Protein science, 1993-06, Vol.2 (6), p.1001-1012

1993

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Negative complementation in aspartate transcarbamylase. Analysis of hybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunits

The Journal of biological chemistry, 1992-11, Vol.267 (31), p.22148-22155

1992

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Effect of Amino Acid Substitutions on the Catalytic and Regulatory Properties of Aspartate Transcarbamoylase

Proceedings of the National Academy of Sciences - PNAS, 1986-08, Vol.83 (16), p.5934-5938

1986

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Location of Amino Acid Alterations in Mutants of Aspartate Transcarbamoylase: Structural Aspects of Interallelic Complementation

Proceedings of the National Academy of Sciences - PNAS, 1984-01, Vol.81 (1), p.115-119

1984

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Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase

Analytical biochemistry, 1987-05, Vol.163 (1), p.188-195

1987

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Communication between Catalytic Subunits in Hybrid Asparta Transcarbamoylase Molecules: Effect of Ligand Binding to Active Chains on the Conformation of Unliganded, Inactive Chains

Proceedings of the National Academy of Sciences - PNAS, 1980-09, Vol.77 (9), p.5187-5191

1980

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Solvent effects on oxygen atom transfer reaction between manganese（V）-oxo corrole and alkene

中国化学快报：英文版, 2013 (6), p.447-449

Lan Yu Qi Wang Lu Dai Wei-Ying Li Rong Chen Mian HR Mahmood Hai-Yang Liu Chi-Kwong Chang

2013

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On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase

Journal of molecular biology, 1981-10, Vol.152 (1), p.131-152

1981

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[5] Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits

Methods in Enzymology, 1978, Vol.51, p.35-41

1978

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Aqueous Two‐Phase Emulsion Bioink‐Enabled 3D Bioprinting of Porous Hydrogels

Advanced materials (Weinheim), 2018-12, Vol.30 (50), p.e1805460-n/a

2018

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Interface Modification by Ionic Liquid: A Promising Candidate for Indoor Light Harvesting and Stability Improvement of Planar Perovskite Solar Cells

Advanced energy materials, 2018-08, Vol.8 (24), p.n/a

2018

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Proteogenomic analysis reveals alternative splicing and translation as part of the abscisic acid response in Arabidopsis seedlings

The Plant journal : for cell and molecular biology, 2017-08, Vol.91 (3), p.518-533

2017

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Vascular Risk and β‐Amyloid Are Synergistically Associated with Cortical Tau

Annals of neurology, 2019-02, Vol.85 (2), p.272-279

2019

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Development and Evaluation of an Attendance Tracking System Using Smartphones with GPS and NFC

Applied artificial intelligence, 2022-12, Vol.36 (1)

2022

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solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase

Aspartate Transcarbamoylase Containing Circularly Permuted Catalytic Polypeptide Chains

Random circular permutation leading to chain disruption within and near α helices in the catalytic chains of aspartate transcarbamoylase: Effects on assembly, stability, and function

Cooperative Interactions in Aspartate Transcarbamoylase. 1. Hybrids Composed of Native and Chemically Inactivated Catalytic Polypeptide Chains

Ultrasonographic Characteristics of Cortical Sulcus Development in the Human Fetus between 18 and 41 Weeks of Gestation

Why cannot Maria be extinguished in Burkina Faso?

Ligand-Promoted Weakening of Intersubunit Bonding Domains in Aspartate Transcarbamoylase

Preparation of 125I-Catalytic Subunit of Aspartate Transcarbamylase and Its Use in Studies of the Regulatory Subunit

In vivo formation of active aspartate transcarbamoylase from complementing fragments of the catalytic polypeptide chains

A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: assembly, oligomers, and domains

Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains

Negative complementation in aspartate transcarbamylase. Analysis of hybrid enzyme molecules containing different arrangements of polypeptide chains from wild-type and inactive mutant catalytic subunits

Effect of Amino Acid Substitutions on the Catalytic and Regulatory Properties of Aspartate Transcarbamoylase

Location of Amino Acid Alterations in Mutants of Aspartate Transcarbamoylase: Structural Aspects of Interallelic Complementation

Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase

Communication between Catalytic Subunits in Hybrid Asparta Transcarbamoylase Molecules: Effect of Ligand Binding to Active Chains on the Conformation of Unliganded, Inactive Chains

Solvent effects on oxygen atom transfer reaction between manganese（V）-oxo corrole and alkene

On the detection of homotropic effects in enzymes of low co-operativity. Application to modified aspartate transcarbamoylase

[5] Aspartate transcarbamoylase (Escherichia coli): Preparation of subunits

Aqueous Two‐Phase Emulsion Bioink‐Enabled 3D Bioprinting of Porous Hydrogels

Interface Modification by Ionic Liquid: A Promising Candidate for Indoor Light Harvesting and Stability Improvement of Planar Perovskite Solar Cells

Proteogenomic analysis reveals alternative splicing and translation as part of the abscisic acid response in Arabidopsis seedlings

Therapy-induced mutations drive the genomic landscape of relapsed acute lymphoblastic leukemia

Vascular Risk and β‐Amyloid Are Synergistically Associated with Cortical Tau

Development and Evaluation of an Attendance Tracking System Using Smartphones with GPS and NFC

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