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Computational design of a specific heavy chain/κ light chain interface for expressing fully IgG bispecific antibodies

Protein science, 2017-10, Vol.26 (10), p.2021-2038

2017

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Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators

Nature (London), 2002-01, Vol.415 (6871), p.549-553

2002

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A broad range of Fab stabilities within a host of therapeutic IgGs

Biochemical and biophysical research communications, 2007-04, Vol.355 (3), p.751-757

2007

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A Comparative Study of Peptide Models of the α-Domain of α-Lactalbumin, Lysozyme, and α-Lactalbumin/Lysozyme Chimeras Allows the Elucidation of Critical Factors That Contribute to the Ability to Form Stable Partially Folded States

Biochemistry (Easton), 2001-02, Vol.40 (7), p.2138-2147

2001

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Defining the core structure of the alpha-lactalbumin molten globule state

Journal of molecular biology, 1999-11, Vol.294 (1), p.213-221

1999

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Peptide models of local and long-range interactions in the molten globule state of human α-lactalbumin

Journal of molecular biology, 1998, Vol.283 (1), p.279-291

1998

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Computational design of a specific heavy chain/[kappa] light chain interface for expressing fully IgG bispecific antibodies

Protein science, 2017-10, Vol.26 (10), p.2021

2017

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Computational design of a specific heavy chain/κ light chain interface for expressing fully IgG bispecific antibodies: Computational Design of a novel C H 1/Cκ interface

Protein science, 2017-07, Vol.26 (10)

2017

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Local Interactions Drive the Formation of Nonnative Structure in the Denatured State of Human α-Lactalbumin: A High Resolution Structural Characterization of a Peptide Model in Aqueous Solution

Biochemistry (Easton), 1999-06, Vol.38 (22), p.7380-7387

1999

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Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of nonnative structure in the denatured state

Proteins, structure, function, and bioinformatics, 2000-02, Vol.38 (2), p.189-196

2000

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Engineering stability into Escherichia coli secreted Fabs leads to increased functional expression

Protein engineering, design and selection, 2006-07, Vol.19 (7), p.325-336

2006

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Optimization of the Antibody CH3 Domain by Residue Frequency Analysis of IgG Sequences

Journal of molecular biology, 2004-01, Vol.335 (1), p.41-48

2004

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Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB‐binding protein

Protein science, 2004-01, Vol.13 (1), p.203-210

2004

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Optimization of the antibody C(H)3 domain by residue frequency analysis of IgG sequences

Journal of molecular biology, 2004-01, Vol.335 (1), p.41-48

2004

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Antibody therapeutics, antibody engineering, and the merits of protein stability

Current opinion in drug discovery & development, 2008-09, Vol.11 (5), p.675

2008

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Local interactions and the role of the 6-120 disulfide bond in α-lactalbumin: implications for formation of the molten globule state

Biochimica et biophysica acta, 2000-01, Vol.1476 (1), p.9-19

2000

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A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin

Proteins, structure, function, and bioinformatics, 2001-02, Vol.42 (2), p.237-242

2001

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Structural Characterization of the Cell Wall Binding Domains of Clostridium difficile Toxins A and B; Evidence that Ca super(2) super(+) Plays a Role in Toxin A Cell Surface Association

Journal of molecular biology, 2005-03, Vol.346 (5), p.1197-1206

2005

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Structural characterization of the cell wall binding domains of Clostridium difficile toxins A and B; evidence that Ca2+ plays a role in toxin A cell surface association

Journal of molecular biology, 2005-03, Vol.346 (5), p.1197-1206

2005

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pH-dependent stability of the human α-lactalbumin molten globule state: Contrasting roles of the 6-120 disulfide and the β-subdomain at low and neutral pH

Proteins, structure, function, and bioinformatics, 2003-08, Vol.52 (2), p.193-202

2003

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Letter to the Editor: Assignment of a 15 kDa protein complex formed between the p160 coactivator ACTR and CREB binding protein

Journal of biomolecular NMR, 2002-04, Vol.22 (4), p.377

2002

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MMAPPR: mutation mapping analysis pipeline for pooled RNA-seq

Genome research, 2013-04, Vol.23 (4), p.687-697

2013

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Generation of bispecific IgG antibodies by structure-based design of an orthogonal Fab interface

Nature biotechnology, 2014-02, Vol.32 (2), p.191-198

2014

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Transient genomic instability drives tumorigenesis through accelerated clonal evolution

Genes & development, 2021-08, Vol.35 (15-16), p.1093-1108

2021

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Revisiting the effects of molybdenum and tungsten alloying on corrosion behavior of nickel-chromium alloys in aqueous corrosion

Current opinion in solid state & materials science, 2019-06, Vol.23 (3), p.129-141

2019

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Computational design of a specific heavy chain/κ light chain interface for expressing fully IgG bispecific antibodies

Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators

A broad range of Fab stabilities within a host of therapeutic IgGs

A Comparative Study of Peptide Models of the α-Domain of α-Lactalbumin, Lysozyme, and α-Lactalbumin/Lysozyme Chimeras Allows the Elucidation of Critical Factors That Contribute to the Ability to Form Stable Partially Folded States

Defining the core structure of the alpha-lactalbumin molten globule state

Peptide models of local and long-range interactions in the molten globule state of human α-lactalbumin

Computational design of a specific heavy chain/[kappa] light chain interface for expressing fully IgG bispecific antibodies

Computational design of a specific heavy chain/κ light chain interface for expressing fully IgG bispecific antibodies: Computational Design of a novel C H 1/Cκ interface

Local Interactions Drive the Formation of Nonnative Structure in the Denatured State of Human α-Lactalbumin: A High Resolution Structural Characterization of a Peptide Model in Aqueous Solution

Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of nonnative structure in the denatured state

Engineering stability into Escherichia coli secreted Fabs leads to increased functional expression

Optimization of the Antibody CH3 Domain by Residue Frequency Analysis of IgG Sequences

Packing, specificity, and mutability at the binding interface between the p160 coactivator and CREB‐binding protein

Optimization of the antibody C(H)3 domain by residue frequency analysis of IgG sequences

Antibody therapeutics, antibody engineering, and the merits of protein stability

Local interactions and the role of the 6-120 disulfide bond in α-lactalbumin: implications for formation of the molten globule state

A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin

Structural Characterization of the Cell Wall Binding Domains of Clostridium difficile Toxins A and B; Evidence that Ca super(2) super(+) Plays a Role in Toxin A Cell Surface Association

Structural characterization of the cell wall binding domains of Clostridium difficile toxins A and B; evidence that Ca2+ plays a role in toxin A cell surface association

pH-dependent stability of the human α-lactalbumin molten globule state: Contrasting roles of the 6-120 disulfide and the β-subdomain at low and neutral pH

Letter to the Editor: Assignment of a 15 kDa protein complex formed between the p160 coactivator ACTR and CREB binding protein

MMAPPR: mutation mapping analysis pipeline for pooled RNA-seq

Generation of bispecific IgG antibodies by structure-based design of an orthogonal Fab interface

Transient genomic instability drives tumorigenesis through accelerated clonal evolution

Revisiting the effects of molybdenum and tungsten alloying on corrosion behavior of nickel-chromium alloys in aqueous corrosion

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