S. Demarest

发表

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

Andrew Leaver-Fay, Brian Kuhlman, Steven M Lewis, 2014, Nature Biotechnology.

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

Wei Xu, H. Jane Dyson, Peter E. Wright, 2002, Nature.

Emerging trends in bispecific antibody and scaffold protein therapeutics

S. Atwell, S. Demarest, P. Verdino, 2018 .

Building blocks for bispecific and trispecific antibodies.

Xiufeng Wu, S. Demarest, 2019, Methods.

Stable IgG-like Bispecific Antibodies Directed toward the Type I Insulin-like Growth Factor Receptor Demonstrate Enhanced Ligand Blockade and Anti-tumor Activity

A. Lugovskoy, Xiufeng Wu, A. Sereno, 2010, The Journal of Biological Chemistry.

Influence of canonical structure determining residues on antibody affinity and stability.

L. A. Clark, H. V. van Vlijmen, J. Eldredge, 2014, Journal of structural biology.

Glycosylation Profiling of α/β T Cell Receptor Constant Domains Expressed in Mammalian Cells.

Xiufeng Wu, S. Demarest, J. Fitchett, 2017, Methods in molecular biology.

Generalizable design parameters for soluble T cell receptor-based T cell engagers

A. Sereno, F. Huang, S. Demarest, 2022, Journal for ImmunoTherapy of Cancer.

Structural understanding of stabilization patterns in engineered bispecific Ig‐like antibody molecules

Guohui Li, A. Lugovskoy, Xiufeng Wu, 2009, Proteins.

Transient and stable CHO expression, purification and characterization of novel hetero‐dimeric bispecific IgG antibodies

Xiufeng Wu, S. Demarest, Yashas Rajendra, 2017, Biotechnology progress.

Computational stabilization of T cell receptors allows pairing with antibodies to form bispecifics

Jack B. Maguire, B. Kuhlman, Xiufeng Wu, 2020, Nature Communications.

An Intermediate pH Unfolding Transition Abrogates the Ability of IgE to Interact with Its High Affinity Receptor FcϵRIα*

S. Demarest, M. Kehry, J. Hopp, 2006, Journal of Biological Chemistry.

Fine details of IGF-1R activation, inhibition, and asymmetry determined by associated hydrogen /deuterium-exchange and peptide mass mapping.

S. Demarest, Damian J. Houde, D. Houde, 2011, Structure.

Neutralization of Clostridium difficile toxin A using antibody combinations

B. E. Kimmel, J. Short, S. Demarest, 2010, mAbs.

BIIB022, a fully human nonglycosylated γ4P antibody targeting IGF-1R for cancer therapy

Christilyn P. Graff, S. Demarest, P. Chu, 2007 .

Metric to distinguish closely related domain families using sequence information.

N. Dokholyan, E. Proctor, P. Kota, 2013, Journal of molecular biology.

Generation of orthogonal Fab-based trispecific antibody formats

Xiufeng Wu, S. Demarest, Richard Yuan, 2018, Protein engineering, design & selection : PEDS.

A comparative study of peptide models of the alpha-domain of alpha-lactalbumin, lysozyme, and alpha-lactalbumin/lysozyme chimeras allows the elucidation of critical factors that contribute to the ability to form stable partially folded states.

D. Raleigh, R. Fairman, J. Robblee, 2001, Biochemistry.

Emerging antibody combinations in oncology

S. Demarest, K. Hariharan, Jianying Dong, 2011, mAbs.

Bispecific antibodies: The next generation of targeted inflammatory bowel disease therapies.

L. Peyrin-Biroulet, S. Demarest, A. Nirula, 2019, Autoimmunity reviews.

Stability engineering of scFvs for the development of bispecific and multivalent antibodies.

L. Croner, A. Lugovskoy, Xiufeng Wu, 2010, Protein engineering, design & selection : PEDS.

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

B. E. Kimmel, Jane Y. Wu, J. Short, 2006, Protein engineering, design & selection : PEDS.

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

Scott M Glaser, S. Demarest, Stephen J Demarest, 2008, Current opinion in drug discovery & development.

Evaluation of Tyro3 expression, Gas6-mediated Akt phosphorylation, and the impact of anti-Tyro3 antibodies in melanoma cell lines.

D. Grueneberg, E. Harlow, F. Huang, 2013, Biochemistry.

A stable IgG-like bispecific antibody targeting the epidermal growth factor receptor and the type I insulin-like growth factor receptor demonstrates superior anti-tumor activity

Christilyn P. Graff, Xiufeng Wu, A. Sereno, 2011, mAbs.

Combination of Two Insulin-Like Growth Factor-I Receptor Inhibitory Antibodies Targeting Distinct Epitopes Leads to an Enhanced Antitumor Response

A. Sereno, S. Demarest, E. Langley, 2010, Molecular Cancer Therapeutics.

Fab-based bispecific antibody formats with robust biophysical properties and biological activity

Brian Kuhlman, Steven M Lewis, Xiufeng Wu, 2015, mAbs.

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

P. Wright, R. Evans, S. Demarest, 2004, Protein science : a publication of the Protein Society.

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.

B. E. Kimmel, Jingping Zhong, S. Demarest, 2005, Journal of molecular biology.

Dichotomous impact of affinity on the function of T cell engaging bispecific antibodies

Xiufeng Wu, A. Sereno, F. Huang, 2021, Journal for ImmunoTherapy of Cancer.

Anti-tumor activity of stability-engineered IgG-like bispecific antibodies targeting TRAIL-R2 and LTβR

A. Lugovskoy, G. Farrington, J. Browning, 2009 .

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

S. Demarest, G. Hansen, J. Rogers, 2004, Journal of molecular biology.

Computational stabilization of T cell receptors allows pairing with antibodies to form bispecifics

Jack B. Maguire, B. Kuhlman, Xiufeng Wu, 2020, Nature Communications.

Differential scanning calorimetry in the biopharmaceutical sciences

S. Demarest, V. Frasca, 2020, Biophysical Characterization of Proteins in Developing Biopharmaceuticals.

Secretion from bacterial versus mammalian cells yields a recombinant scFv with variable folding properties.

F. Huang, S. Demarest, A. Capili, 2012, Archives of biochemistry and biophysics.

Protein design of IgG/TCR chimeras for the co-expression of Fab-like moieties within bispecific antibodies

Dongmei He, Xiufeng Wu, A. Sereno, 2015, mAbs.

Comparing domain interactions within antibody Fabs with kappa and lambda light chains

M. Dickey, Xiufeng Wu, F. Huang, 2016, mAbs.

Characterization of Inhibitory Anti-insulin-like Growth Factor Receptor Antibodies with Different Epitope Specificity and Ligand-blocking Properties

Christilyn P. Graff, Xiufeng Wu, A. Sereno, 2009, Journal of Biological Chemistry.

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

S. Demarest, E. Garber, Ellen Garber, 2007, Biochemical and biophysical research communications.

Conserved amino acid networks involved in antibody variable domain interactions

L. Croner, A. Lugovskoy, S. Demarest, 2009, Proteins.

Computationally Designed Bispecific Antibodies using Negative State Repertoires.

B. Kuhlman, A. Leaver-Fay, S. Atwell, 2016, Structure.

Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution.

D. Raleigh, S. Demarest, D P Raleigh, 1999, Biochemistry.

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

D. Raleigh, S. Demarest, J. Horng, 2003, Proteins.

Anti-tumor activity of stability-engineered IgG-like bispecific antibodies targeting TRAIL-R2 and LTbetaR.

A. Lugovskoy, G. Farrington, J. Browning, 2009, mAbs.

Rapid screening platform for stabilization of scFvs in Escherichia coli.

S. Demarest, B. Miller, S. Glaser, 2009, Methods in molecular biology.

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

B. Kuhlman, B. Kuhlman, Xiufeng Wu, 2017, Protein science : a publication of the Protein Society.

Highly Covarying Residues Have a Functional Role in Antibody Constant Domains

N. Dokholyan, E. Proctor, P. Kota, 2022 .

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

D. Raleigh, S. Demarest, J. Horng, 2001, Proteins.

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

D. Raleigh, R. Fairman, J. Boice, 1999, Journal of molecular biology.

Resource Computationally Designed Bispecific Antibodies using Negative State Repertoires Graphical Abstract Highlights

Andrew Leaver-Fay, Brian Kuhlman, Karen J. Froning, 2016 .

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

D. Raleigh, S. Demarest, 2000, Proteins.

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

D. Raleigh, R. Fairman, J. Robblee, 2000, Biochimica et biophysica acta.

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

D. Raleigh, R. Fairman, S. Demarest, 1998, Journal of molecular biology.

Conserved amino acid networks involved in antibody variable domain interactions

L. Croner, A. Lugovskoy, S. Demarest, 2009, Proteins.

Structural understanding of stabilization patterns in engineered bispecific Ig‐like antibody molecules

Guohui Li, A. Lugovskoy, Xiufeng Wu, 2009, Proteins.

Highly covarying residues have a functional role in antibody constant domains

N. Dokholyan, E. Proctor, P. Kota, 2013, Proteins.