Structural and Functional Analysis of a Highly Active Designed Phosphotriesterase for the Detoxification of Organophosphate Nerve Agents Reveals an Unpredicted Conformation of the Active Site Loop

Catalytic activity and stereoselectivity of engineered phosphotriesterases towards structurally different nerve agents in vitro

(2021) Anja Köhler et al.   ARCHIVES OF TOXICOLOGY

Highly accurate protein structure prediction with AlphaFold

(2021) John Jumper et al.   NATURE

Post-VX exposure treatment of rats with engineered phosphotriesterases

(2021) Lisa Stigler et al.   ARCHIVES OF TOXICOLOGY

A catalytic bioscavenger with improved stability and reduced susceptibility to oxidation for treatment of acute poisoning with neurotoxic organophosphorus compounds

(2019) Laura Job et al.   TOXICOLOGY LETTERS

Automated Design of Efficient and Functionally Diverse Enzyme Repertoires

(2018) Olga Khersonsky et al.   MOLECULAR CELL

Overcoming an optimization plateau in the directed evolution of highly efficient nerve agent bioscavengers

(2017) Moshe Goldsmith et al.   PROTEIN ENGINEERING DESIGN & SELECTION

Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and Stability

(2016) Adi Goldenzweig et al.   MOLECULAR CELL

Catalytic bioscavengers in nerve agent poisoning: A promising approach?

(2016) Franz Worek et al.   TOXICOLOGY LETTERS

Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro

(2015) Moshe Goldsmith et al.   ARCHIVES OF TOXICOLOGY

Variants of Phosphotriesterase for the Enhanced Detoxification of the Chemical Warfare Agent VR

(2015) Andrew N. Bigley et al.   BIOCHEMISTRY

Efficacy of the rePON1 mutant IIG1 to prevent cyclosarin toxicity in vivo and to detoxify structurally different nerve agents in vitro

(2014) Franz Worek et al.   ARCHIVES OF TOXICOLOGY

ThePDB_REDOserver for macromolecular structure model optimization

(2014) Robbie P. Joosten et al.   IUCrJ

Engineering V-Type Nerve Agents Detoxifying Enzymes Using Computationally Focused Libraries

(2013) Izhack Cherny et al.   ACS Chemical Biology

Enzymatic Neutralization of the Chemical Warfare Agent VX: Evolution of Phosphotriesterase for Phosphorothiolate Hydrolysis

(2013) Andrew N. Bigley et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Enzymes for the Homeland Defense: Optimizing Phosphotriesterase for the Hydrolysis of Organophosphate Nerve Agents

(2012) Ping-Chuan Tsai et al.   BIOCHEMISTRY

Reconstructing a Missing Link in the Evolution of a Recently Diverged Phosphotriesterase by Active-Site Loop Remodeling

(2012) Livnat Afriat-Jurnou et al.   BIOCHEMISTRY

Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin

(2012) Uwe Mueller et al.   JOURNAL OF SYNCHROTRON RADIATION

REFMAC5 for the refinement of macromolecular crystal structures

(2011) Garib N. Murshudov et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Overview of theCCP4 suite and current developments

(2011) Martyn D. Winn et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

De Novo Enzyme Design Using Rosetta3

(2011) Florian Richter et al.   PLoS One

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Ligand docking and binding site analysis with PyMOL and Autodock/Vina

(2010) Daniel Seeliger et al.   JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN

MolProbity: all-atom structure validation for macromolecular crystallography

(2009) Vincent B. Chen et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase

(2009) C. J. Jackson et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structure of Diethyl Phosphate Bound to the Binuclear Metal Center of Phosphotriesterase†‡

(2008) Jungwook Kim et al.   BIOCHEMISTRY

Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7

(2008) Gerrit Langer et al.   Nature Protocols