2022 - Research.com Chemistry in Israel Leader Award
2012 - Fellow of the American Association for the Advancement of Science (AAAS)
Joel L. Sussman mainly focuses on Stereochemistry, Biochemistry, Active site, Protein structure and Acetylcholinesterase. His Stereochemistry research is multidisciplinary, relying on both Hydrolase, Crystallography, Crystal structure, Catalytic triad and Serine hydrolase. His Catalytic triad research includes themes of Haloalkane dehalogenase, Cholinesterase, Acyl binding, Butyrylcholinesterase and Histidine.
The concepts of his Active site study are interwoven with issues in Lysozyme, Indole test, Synchrotron, Substrate and Binding site. His work in the fields of Protein structure, such as Protein Data Bank, overlaps with other areas such as Dipole. His biological study spans a wide range of topics, including Torpedo, Cholinergic and Acetylcholine, Pharmacology.
Stereochemistry, Acetylcholinesterase, Biochemistry, Torpedo and Crystallography are his primary areas of study. The various areas that Joel L. Sussman examines in his Stereochemistry study include Hydrolase, Catalytic triad, Active site, Protein structure and Binding site. His Active site research is multidisciplinary, incorporating perspectives in Docking, Substrate, Hydrogen bond and Molecular dynamics.
His Acetylcholinesterase study combines topics in areas such as Biophysics, Acetylcholine, Pharmacology and Cholinergic. His work is connected to Enzyme and Peptide sequence, as a part of Biochemistry. Joel L. Sussman has included themes like X-ray crystallography, Duplex, DNA and Transfer RNA in his Crystallography study.
His main research concerns Acetylcholinesterase, Stereochemistry, Enzyme, Torpedo and Biophysics. In general Acetylcholinesterase study, his work on Tabun often relates to the realm of Structure function, Injury control and Substrate, thereby connecting several areas of interest. His studies in Stereochemistry integrate themes in fields like Hydrolase, Cyclosarin and Crystal structure.
His studies deal with areas such as Enzyme catalysis, Active site, Protein evolution, Protein structure and Reversion as well as Hydrolase. To a larger extent, Joel L. Sussman studies Biochemistry with the aim of understanding Enzyme. His work deals with themes such as Agonist, σ1 receptor and Binding site, which intersect with Torpedo.
His primary areas of investigation include Stereochemistry, Enzyme, Hydrolase, Nerve agent and Acetylcholinesterase. His study in Stereochemistry is interdisciplinary in nature, drawing from both Linker, Crystal structure and Cytotoxicity. His Enzyme research is under the purview of Biochemistry.
His work carried out in the field of Hydrolase brings together such families of science as Enzyme catalysis, Active site, Protein structure, Metal ions in aqueous solution and Histidine. His work focuses on many connections between Active site and other disciplines, such as Substrate, that overlap with his field of interest in Nanotechnology. His work on Cyclosarin as part of general Acetylcholinesterase research is frequently linked to GSK-3, bridging the gap between disciplines.
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Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein
Joel L. Sussman;Michal Harel;Felix Frolow;Christian Oefner.
The α/β hydrolase fold
David L. Ollis;Eong Cheah;Miroslaw Cygler;Bauke Dijkstra.
Protein Engineering (1992)
Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.
M Harel;I Schalk;L Ehret-Sabatier;F Bouet.
Proceedings of the National Academy of Sciences of the United States of America (1994)
Three-dimensional tertiary structure of yeast phenylalanine transfer RNA.
S. H. Kim;F. L. Suddath;G. J. Quigley;A. McPherson.
FoldIndex©: a simple tool to predict whether a given protein sequence is intrinsically unfolded
Jaime Prilusky;Clifford E. Felder;Tzviya Zeev-Ben-Mordehai;Edwin H. Rydberg.
Function and structure of inherently disordered proteins
A Keith Dunker;Israel Silman;Vladimir N Uversky;Vladimir N Uversky;Joel L Sussman.
Current Opinion in Structural Biology (2008)
Protein production and purification.
Nature Methods (2008)
Three-dimensional structures of avidin and the avidin-biotin complex
Oded Livnah;Edward A. Bayer;Meir Wilchek;Joel L. Sussman.
Proceedings of the National Academy of Sciences of the United States of America (1993)
Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs.
Gitay Kryger;Israel Silman;Joel L Sussman.
Structure and Evolution of the Serum Paraoxonase Family of Detoxifying and Anti-Atherosclerotic Enzymes
Michal Harel;Amir Aharoni;Leonid Gaidukov;Boris Brumshtein.
Nature Structural & Molecular Biology (2004)
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