J. Schrag

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Binding symmetry and surface flexibility mediate antibody self-association

E. Purisima, T. Sulea, Hervé Hogues, 2019, mAbs.

Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum

J. Schrag, M. Cygler, Yunge Li, 1991, Nature.

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins

J. Sussman, I. Silman, M. Harel, 1993, Protein science : a publication of the Protein Society.

Stability-Diversity Tradeoffs Impose Fundamental Constraints on Selection of Synthetic Human VH/VL Single-Domain Antibodies from In Vitro Display Libraries

Kevin A. Henry, C. MacKenzie, J. Tanha, 2017, Front. Immunol..

Antibody light chain variable domains and their biophysically improved versions for human immunotherapy

J. Tanha, J. Schrag, J. Kelly, 2013, mAbs.

The open conformation of a Pseudomonas lipase.

Y Li, D Schomburg, D. Schomburg, 1997, Structure.

A Structural Basis for the Chiral Preferences of Lipases

J. Schrag, M. Cygler, R. Kazlauskas, 1994 .

Polymorphism in the lipase genes of Geotrichum candidum strains.

T. Vernet, D. Y. Thomas, J. Schrag, 1994, European journal of biochemistry.

Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase.

J. Schrag, M. Cygler, R. Kazlauskas, 1995, Biochemistry.

Characterization of a SARS-CoV-2 spike protein reference material

B. B. Stocks, J. Schrag, J. Melanson, 2022, Analytical and Bioanalytical Chemistry.

Structure-based engineering of pH-dependent antibody binding for selective targeting of solid-tumor microenvironment

Christopher R. Corbeil, E. Purisima, M. Jaramillo, 2019, mAbs.

Asymmetric Fc Engineering for Bispecific Antibodies with Reduced Effector Function

J. Schrag, J. Baardsnes, Y. Durocher, 2017, Antibodies.

Quaternary Structure of Tetrameric Acetylcholinesterase

W. Chiu, G. Phillips, J. Sussman, 1998 .

The effect of freezing rate on the cooperativity of antifreeze glycopeptides

J. Schrag, A. Devries, 1983 .

Relationship of amino acid composition and molecular weight of antifreeze glycopeptides to non-colligative freezing point depression.

J. Schrag, A. Devries, S. O’Grady, 1982, Biochimica et biophysica acta.

Characterization of a SARS-CoV-2 spike protein reference material

B. B. Stocks, J. Schrag, J. Melanson, 2022, Analytical and Bioanalytical Chemistry.

Crystal Structure of N-Succinylarginine Dihydrolase AstB, Bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli*

A. Tocilj, A. Matte, J. Schrag, 2005, Journal of Biological Chemistry.

Sequence Alignment of Esterases and Lipases Based on 3-D Structures of Two Members of This Family

J. Sussman, I. Silman, M. Harel, 1992 .

CRYSTAL STRUCTURE OF METHANOBACTERIUM THERMAOAUTOTROPHICUM PHOSPHORIBOSYL-AMP

T. Sulea, J. Schrag, V. Davisson, 2005 .

Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase HisI.

T. Sulea, J. Schrag, M. Cygler, 2005, Biochemistry.

Comparison of antifreeze glycopeptides from arctic and antarctic fishes

J. Schrag, J. Raymond, A. Devries, 1982 .

A Structural Basis for the Chiral Preferences of Lipases

Miroslaw Cygler, Joseph D. Schrag, Romas J. Kazlauskas, 1995 .

Purification and characterization of aPenicillium sp. lipase which discriminates against diglycerides

J. Schrag, M. Cygler, E. Ziomek, 1996, Lipids.

Multiple crystal forms of lipases from Geotrichum candidum.

J. Schrag, Y. Li, M. Cygler, 1991, Journal of molecular biology.

Different Active‐Site Loop Orientation in Serine Hydrolases versus Acyltransferases

J. Schrag, R. Kazlauskas, K. Morley, 2011, Chembiochem : a European journal of chemical biology.

Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.

A. Matte, Y. Li, J. Schrag, 2001, Biochemistry.

Mutational analysis of the gephyrin-related molybdenum cofactor biosynthetic gene cnxE from the lower eukaryote Aspergillus nidulans.

J. Schrag, S. Unkles, J. R. Kinghorn, 2002, Genetics.

Mechanism of action and NAD+-binding mode revealed by the crystal structure of l-histidinol dehydrogenase

A. Matte, J. Schrag, M. Cygler, 2002, Proceedings of the National Academy of Sciences of the United States of America.

The Structure of calnexin, an ER chaperone involved in quality control of protein folding.

D. Y. Thomas, Y. Li, J. Schrag, 2001, Molecular cell.

Ocular Freezing Avoidance in Antarctic Fish

J. Schrag, A. Devries, J. Turner, 1985 .

Rapid, high-yield production of full-length SARS-CoV-2 spike ectodomain by transient gene expression in CHO cells

J. Schrag, Y. Durocher, D. L'abbe, 2020, bioRxiv.

Mirror-image packing in enantiomer discrimination molecular basis for the enantioselectivity of B.cepacia lipase toward 2-methyl-3-phenyl-1-propanol.

J. Schrag, R. Kazlauskas, C. Cheong, 2005, Chemistry & biology.

Selectivity of lipases : Conformational analysis of suggested intermediates in ester hydrolysis of chiral primary and secondary alcohols

J. Schrag, M. Cygler, J. Zuegg, 1997 .

Lipases and alpha/beta hydrolase fold.

J. Schrag, M. Cygler, Miroslaw Cygler, 1997, Methods in enzymology.

Advances in structural understanding of lipases.

J. Schrag, M. Cygler, F. Ergan, 1992, Biotechnology & Genetic Engineering Reviews.

Biological Crystallography Structure of an Aryl Esterase from Pseudomonas Fluorescens

A. Tocilj, J. Schrag, R. Kazlauskas, 2022 .

Structure as basis for understanding interfacial properties of lipases.

J. Schrag, M. Cygler, 1997, Methods in enzymology.

Substrate Binding Site and the Role of the FLAP Loop in Candida rugosa Lipase, A Close Relative of Acetylcholinesterase

J. Schrag, M. Cygler, P. Grochulski, 1995 .

Structural determinants defining common stereoselectivity of lipases toward secondary alcohols.

J. Schrag, M. Cygler, P. Grochulski, 1995, Canadian journal of microbiology.

Two conformational states of Candida rugosa lipase

J. Schrag, M. Cygler, P. Grochulski, 1994, Protein science : a publication of the Protein Society.

Structure and conformational flexibility of Candida rugosa lipase.

J. Schrag, M. Cygler, 1999, Biochimica et biophysica acta.

Insights into interfacial activation from an open structure of Candida rugosa lipase.

B Rubin, Y. Li, J. Schrag, 1994, The Journal of biological chemistry.

The alpha/beta hydrolase fold.

S J Remington, I Silman, D. Ollis, 1992, Protein engineering.

Expression and Characterization of Geotrichum candidum Lipase I Gene

David Y. Thomas, T. Vernet, J. Schrag, 1995 .

Structural and enzymatic characterization of NanS (YjhS), a 9‐O‐Acetyl N‐acetylneuraminic acid esterase from Escherichia coli O157:H7

J. Schrag, M. Cygler, M. Gilbert, 2011, Protein science : a publication of the Protein Society.

Interaction of a G-protein β-subunit with a conserved sequence in Ste20/PAK family protein kinases

Joseph D. Schrag, David Y. Thomas, M. Whiteway, 1998, Nature.

Insights into function of PSI domains from structure of the Met receptor PSI domain.

G. Kozlov, K. Gehring, J. Schrag, 2004, Biochemical and biophysical research communications.

Identification and crystallization of a protease-resistant core of calnexin that retains biological activity.

D. Tessier, D. Y. Thomas, J. Schrag, 1998, Journal of structural biology.

15. Structure Information

Miroslaw Cygler, Allan Matte and, Joseph D. Schrag, 2008 .

Freezing avoidance and the distribution of antifreeze glycopeptides in body fluids and tissues of Antarctic fish.

J. Schrag, A. Devries, C. C. Cheng, 1988, The Journal of experimental biology.

Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP

Allan Matte, Miroslaw Cygler, Joseph D. Schrag, 2002, Nature Structural Biology.

Three-dimensional structure of the HSV1 nucleocapsid

Wah Chiu, Joseph D. Schrag, Frazer J. Rixon, 1989, Cell.

1.8 A refined structure of the lipase from Geotrichum candidum.

J. Schrag, M. Cygler, J D Schrag, 1993, Journal of molecular biology.

Primary and secondary structure of antifreeze peptides from arctic and antarctic zoarcid fishes.

H. Morris, J. Schrag, M. Panico, 1987, Biochimica et biophysica acta.

Cloning and expression of Geotrichum candidum lipase II gene in yeast. Probing of the enzyme active site by site-directed mutagenesis.

D. Tessier, T. Vernet, D. Y. Thomas, 1993, The Journal of biological chemistry.

The crystal structure and dimerization interface of GADD45γ

M. Jaramillo, M. O’Connor-McCourt, J. Schrag, 2008, Proceedings of the National Academy of Sciences.

Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72.

Greg L. Hura, David Y. Thomas, G. Kozlov, 2009, Structure.

Crystal structure of the bb' domains of the protein disulfide isomerase ERp57.

David Y. Thomas, G. Kozlov, K. Gehring, 2006, Structure.

An anti-HER2 biparatopic antibody that induces unique HER2 clustering and complement-dependent cytotoxicity

Joshua M. Scurll, L. Presta, M. Gold, 2023, Nature Communications.

Achieving High-Yield Production of Functional AAV5 Gene Delivery Vectors via Fedbatch in an Insect Cell-One Baculovirus System

J. Schrag, A. Kamen, S. Zolotukhin, 2019, Molecular therapy. Methods & clinical development.

Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate.

A. Matte, Y. Li, J. Schrag, 2001, Journal of molecular biology.

Pancreatic lipases: evolutionary intermediates in a positional change of catalytic carboxylates?

F. Winkler, J. Schrag, M. Cygler, 1992, The Journal of biological chemistry.

Lectin control of protein folding and sorting in the secretory pathway.

David Y. Thomas, J. Schrag, M. Cygler, 2003, Trends in biochemical sciences.

Crystallization and preliminary X-ray diffraction analysis of 11 S acetylcholinesterase.

M. Schmid, J. Schrag, G. Phillips, 1988, The Journal of biological chemistry.

A structural genomics pilot project based on gene targets selected from Escherichia coli

T. Gaasterland, A. Matte, J. Schrag, 2001 .

The crystal structure of Escherichia coli MoeA, a protein from the molybdopterin synthesis pathway.

A. Matte, J. Schrag, M. Cygler, 2001, Journal of molecular biology.

Development of a scalable and robust AEX method for enriched rAAV preparations in genome-containing VCs of serotypes 5, 6, 8, and 9

J. Schrag, A. Kamen, P. Chahal, 2021, Molecular therapy. Methods & clinical development.

Crystal Structures of Escherichia coli ATP-Dependent Glucokinase and Its Complex with Glucose

Allan Matte, Miroslaw Cygler, Joseph D. Schrag, 2004, Journal of bacteriology.

Switching catalysis from hydrolysis to perhydrolysis in Pseudomonas fluorescens esterase.

J. Schrag, R. Kazlauskas, K. Morley, 2010, Biochemistry.

The structure of the exopolyphosphatase (PPX) from Escherichia coli O157:H7 suggests a binding mode for long polyphosphate chains.

A. Matte, J. Schrag, M. Cygler, 2006, Journal of molecular biology.

Expression and characterization of Geotrichum candidum lipase I gene. Comparison of specificity profile with lipase II.

T. Vernet, D. Y. Thomas, J. Schrag, 1995, European journal of biochemistry.

A CHO stable pool production platform for rapid clinical development of trimeric SARS‐CoV‐2 spike subunit vaccine antigens

J. Schrag, J. Baardsnes, J. Kelly, 2023, Biotechnology and bioengineering.

Molecular dynamics-solvated interaction energy studies of protein-protein interactions: the MP1-p14 scaffolding complex.

Marwen Naïm, Traian Sulea, Miroslaw Cygler, 2008, Journal of molecular biology.

Redesigning the active site of Geotrichum candidum lipase.

T. Vernet, D. Y. Thomas, J. Schrag, 1995, Protein engineering.

Structure-guided design of a potent Clostridioides difficile toxin A inhibitor

J. Tanha, J. Schrag, K. Ng, 2023, Frontiers in Microbiology.

1.8 ANGSTROMS REFINED STRUCTURE OF THE LIPASE FROM GEOTRICHUM CANDIDUM

J. Schrag, M. Cygler, 1993 .

The α/β hydrolase fold

Joel L. Sussman, Miroslaw Cygler, Israel Silman, 1992 .

AlbuCORE: an albumin-based molecular scaffold for multivalent biologics design

M. Jaramillo, J. Schrag, J. Baardsnes, 2020, mAbs.

Enantioselectivity of Candida Rugosa Lipase Toward Carboxylic Acids: A Predictive Rule from Substrate Mapping and X-Ray Crystallography

J. Schrag, M. Cygler, Sharmin N. Ahmed, 1994 .

Molecular dynamics-solvated interaction energy studies of protein-protein interactions: the MP1-p14 scaffolding complex.

E. Purisima, T. Sulea, J. Schrag, 2008, Journal of molecular biology.