Author

J. L. Sussman

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:drug response / drug discovery· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Organism:bacteria (other)· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Organism:mouse· 1

Frequent Co-Authors

I. Silman· 3 shared D. S. Tawfik· 1 shared I. Efremenko· 1 shared J. M. L. Martin· 1 shared L. M. Schopfer· 1 shared L. S. Bezouwen· 1 shared M. R. Leung· 1 shared N. Aggawal· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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3 shared papersBiophysics

I. Silman

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Author profile →

3 papers

Recent·Most cited

The impact of molecular variants, crystallization conditions and space group on structure-ligand complexes: A case study on Bacterial Phosphotriesterase Variants and complexes

O. Dym, N. Aggawal, Y. Ashani, S. Albeck, T. Unger, S. Hamer Rogotner, I. Silman, D. S. Tawfik, J. L. Sussman

This study examines how molecular variants, crystallization conditions, and space group affect the visualization of ligand-bound protein structures, using bacterial phosphotriesterase as a case study.

bioRxiv · May 31, 2023 · PreprintBiochemistry

Molecular Dynamics Simulations of the Interaction of Mouse and Torpedo Acetylcholinesterase with Covalent Inhibitors Explain Their Differential Reactivity: Implications for Drug Design

N. B. Chandar, I. Efremenko, I. Silman, J. M. L. Martin, J. L. Sussman

This paper uses molecular dynamics simulations to explain why mouse and Torpedo acetylcholinesterase differ in reactivity to covalent inhibitors, highlighting the importance of enzyme flexibility in drug design.

bioRxiv · Jan 28, 2019Biophysics

The physiological butyrylcholinesterase tetramer is a dimer of dimers stabilized by a superhelical assembly

M. R. Leung, L. S. Bezouwen, L. M. Schopfer, J. L. Sussman, I. Silman, O. Lockridge, T. Zeev-Ben-Mordehai

This paper determines the cryo-EM structure of human butyrylcholinesterase tetramer, revealing its superhelical assembly mechanism and implications for therapeutic applications.

bioRxiv · Sep 30, 2018Biophysics