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The evolution of function within the Nudix homology clan

Proteins, structure, function, and bioinformatics, 2017-05, Vol.85 (5), p.775-811

2017

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PYRIDOXAL PHOSPHATE ENZYMES: Mechanistic, Structural, and Evolutionary Considerations

Annual review of biochemistry, 2004-01, Vol.73 (1), p.383-415

2004

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Autoinhibition of Human Dicer by Its Internal Helicase Domain

Journal of molecular biology, 2008-06, Vol.380 (1), p.237-243

2008

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Active site prediction using evolutionary and structural information

Bioinformatics, 2010-03, Vol.26 (5), p.617-624

2010

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Substrate specificity characterization for eight putative nudix hydrolases. Evaluation of criteria for substrate identification within the Nudix family

Proteins, structure, function, and bioinformatics, 2016-12, Vol.84 (12), p.1810-1822

2016

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Probing the informational and regulatory plasticity of a transcription factor DNA-binding domain

PLoS genetics, 2012-03, Vol.8 (3), p.e1002614-e1002614

2012

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Identification of functional paralog shift mutations: Conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase

Proceedings of the National Academy of Sciences - PNAS, 2007-10, Vol.104 (44), p.17353-17357

2007

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The fitness landscapes of cis-acting binding sites in different promoter and environmental contexts

PLoS genetics, 2010-07, Vol.6 (7), p.e1001042

2010

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The enzymology of cystathionine biosynthesis: strategies for the control of substrate and reaction specificity

Archives of biochemistry and biophysics, 2005, Vol.433 (1), p.166-175

2005

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Substrate Specificity of the Escherichia coli Outer Membrane Protease OmpT

Journal of Bacteriology, 2004-09, Vol.186 (17), p.5919-5925

2004

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How Does an Enzyme Evolved In vitro Compare to Naturally Occurring Homologs Possessing the Targeted Function? Tyrosine Aminotransferase from Aspartate Aminotransferase

Journal of molecular biology, 2003-03, Vol.327 (3), p.593-608

2003

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Defining the Mandate of Proteomics in the Post-Genomics Era: Workshop Report

Molecular & cellular proteomics, 2002-10, Vol.1 (10), p.763-780

2002

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Engineering homooligomeric proteins to detect weak intersite allosteric communication: Aminotransferases, a case study

Protein science, 2011-12, Vol.20 (12), p.1991-2003

2011

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A continuous fluorescence assay for the characterization of Nudix hydrolases

Analytical biochemistry, 2013-06, Vol.437 (2), p.178-184

2013

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The Dual-Specific Active Site of 7,8-Diaminopelargonic Acid Synthase and the Effect of the R391A Mutation

Biochemistry (Easton), 2002-10, Vol.41 (42), p.12582-12589

2002

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Glutamate 47 in 1-Aminocyclopropane-1-carboxylate Synthase Is a Major Specificity Determinant

Biochemistry (Easton), 2001-10, Vol.40 (41), p.12276-12284

2001

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The Partially Folded Homodimeric Intermediate of Escherichia coli Aspartate Aminotransferase Contains a “Molten Interface” Structure

Biochemistry (Easton), 2009-01, Vol.48 (2), p.433-441

2009

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Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: Recurrence of tyrosine aminotransferase activity in the Iα subfamily

Proteins, structure, function, and bioinformatics, 2013-09, Vol.81 (9), p.1593-1609

2013

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Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: Recurrence of tyrosine aminotransferase activity in the I[alpha] subfamily

Proteins, structure, function, and bioinformatics, 2013-09, Vol.81 (9), p.1593

2013

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Computational Redesign of the SHV-1 β-Lactamase/β-Lactamase Inhibitor Protein Interface

Journal of molecular biology, 2008-10, Vol.382 (5), p.1265-1275

2008

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Is Aspartate 52 Essential for Catalysis by Chicken Egg White Lysozyme? The Role of Natural Substrate-Assisted Hydrolysis

Biochemistry (Easton), 1996-02, Vol.35 (6), p.1881-1889

1996

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Cofactor-Directed Reversible Denaturation Pathways: The Cofactor-Stabilized Escherichia coli Aspartate Aminotransferase Homodimer Unfolds through a Pathway That Differs from That of the Apoenzyme

Biochemistry (Easton), 2007-05, Vol.46 (19), p.5819-5829

2007

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Specificity and cooperativity at β-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions

Proteins, structure, function, and bioinformatics, 2011-04, Vol.79 (4), p.1267-1276

2011

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Lysine 258 in aspartate aminotransferase: Enforcer of the Circe effect for amino acid substrates and the general-base catalyst for the 1,3-prototropic shift

Biochemistry (Easton), 1993-02, Vol.32 (6), p.1471-1479

1993

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Free energies of protein–protein association determined by electrospray ionization mass spectrometry correlate accurately with values obtained by solution methods

Protein science, 2006-06, Vol.15 (6), p.1465-1475

2006

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The evolution of function within the Nudix homology clan

PYRIDOXAL PHOSPHATE ENZYMES: Mechanistic, Structural, and Evolutionary Considerations

Autoinhibition of Human Dicer by Its Internal Helicase Domain

Active site prediction using evolutionary and structural information

Substrate specificity characterization for eight putative nudix hydrolases. Evaluation of criteria for substrate identification within the Nudix family

Probing the informational and regulatory plasticity of a transcription factor DNA-binding domain

Identification of functional paralog shift mutations: Conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase

The fitness landscapes of cis-acting binding sites in different promoter and environmental contexts

The enzymology of cystathionine biosynthesis: strategies for the control of substrate and reaction specificity

Substrate Specificity of the Escherichia coli Outer Membrane Protease OmpT

How Does an Enzyme Evolved In vitro Compare to Naturally Occurring Homologs Possessing the Targeted Function? Tyrosine Aminotransferase from Aspartate Aminotransferase

Defining the Mandate of Proteomics in the Post-Genomics Era: Workshop Report

Engineering homooligomeric proteins to detect weak intersite allosteric communication: Aminotransferases, a case study

A continuous fluorescence assay for the characterization of Nudix hydrolases

The Dual-Specific Active Site of 7,8-Diaminopelargonic Acid Synthase and the Effect of the R391A Mutation

Glutamate 47 in 1-Aminocyclopropane-1-carboxylate Synthase Is a Major Specificity Determinant

The Partially Folded Homodimeric Intermediate of Escherichia coli Aspartate Aminotransferase Contains a “Molten Interface” Structure

Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: Recurrence of tyrosine aminotransferase activity in the Iα subfamily

Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: Recurrence of tyrosine aminotransferase activity in the I[alpha] subfamily

Computational Redesign of the SHV-1 β-Lactamase/β-Lactamase Inhibitor Protein Interface

Is Aspartate 52 Essential for Catalysis by Chicken Egg White Lysozyme? The Role of Natural Substrate-Assisted Hydrolysis

Cofactor-Directed Reversible Denaturation Pathways: The Cofactor-Stabilized Escherichia coli Aspartate Aminotransferase Homodimer Unfolds through a Pathway That Differs from That of the Apoenzyme

Specificity and cooperativity at β-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions

Lysine 258 in aspartate aminotransferase: Enforcer of the Circe effect for amino acid substrates and the general-base catalyst for the 1,3-prototropic shift

Free energies of protein–protein association determined by electrospray ionization mass spectrometry correlate accurately with values obtained by solution methods

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