doi.bio/joel_l_sussman

Professor Joel L. Sussman

Overview

Prof. Joel L. Sussman is an Israeli crystallographer best known for his studies on acetylcholinesterase, a key protein involved in the transmission of nerve signals. He is currently the Morton and Gladys Pickman Professor of Structural Biology at the Weizmann Institute of Science in Rehovot, where he also serves as the director of the Israel Structural Proteomics Center.

Early Life and Education

Sussman was born in Philadelphia, Pennsylvania and received his B.A. in Math and Physics from Cornell University in 1965. He then obtained his PhD in Biophysics from MIT in 1972 and conducted postdoctoral research at the Hebrew University of Jerusalem and Duke University.

Academic Appointments and Positions Held

Sussman has been a Professor at the Weizmann Institute of Science since 1976. He has held various leadership positions, including:

1984-1985: Head, Department of Structural Chemistry
1988-1989: Head, Kimmelman Center for Biomolecular Structure and Assembly
2002-2014: Incumbent of the Morton and Gladys Pickman Chair of Structural Biology
2016-present: Professor Emeritus

From 1994 to 1999, he also served as the director of the Protein Data Bank (PDB) at the Brookhaven National Laboratory.

Scientific Contributions and Research Interests

Sussman is a pioneer in the field of macromolecular refinement, developing CORELS and applying it to yeast tRNAphe. He subsequently determined the structures of 'bulge'-containing DNA fragments, which serve as models for insertion mutations.

His current research focuses on nervous system proteins, particularly acetylcholinesterase (AChE), whose 3D structure was first determined in his lab. This structure revealed important insights into the function and potential therapeutic applications of AChE:

AChE is a prototype of the α/β hydrolase fold
π-cation interactions play a key role in the binding of acetylcholine (ACh) and ligands to AChE
The ACh-binding site has implications for the structure-based design of novel anti-Alzheimer's drugs
Cholinesterase-like adhesion molecules (CLAMs) exhibit a highly asymmetric charge distribution and their cytoplasmic domains are intrinsically disordered, impacting neural development and plasticity
The specific chemical and structural damage to proteins produced by synchrotron radiation was investigated

Sussman has also made significant contributions to the understanding of halophilicity and halotolerance, shedding light on how proteins function over extreme ranges of salt concentration, with implications for kidney diseases. Additionally, he has studied Glucocerebrosidase, which is defective in Gaucher disease, and paraoxonase, which is relevant to the treatment of atherosclerosis.

Awards and Recognition

2014: Ilanit-Katzir Prize for exceptional achievements in the field of Life Sciences (shared with Israel Silman)
2006: Teva Founders' Award for breakthroughs in molecular medicine (shared with Hermona Soreq and Israel Silman)
2005: Honorary Professor, Chinese Academy of Sciences
2005: Samuel and Paula Elkeles Prize for Outstanding Scientist in the field of medicine in Israel (shared with Israel Silman)
1994: Elected member, European Molecular Biology Organization (EMBO)

Selected Publications

Google Scholar Profile

Joel L Sussman)

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Joel Sussman Weizmann Institute of Science http://www.weizmann.ac.il/StructuralBiology/Sussman Atomic Structure of Acetyicholinesterase from JL Sussman, M Harel, F Frolow, C Oefner, A Goldman, L Toker, I Silman Science 253 (5022), 872-879, 1991 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:u5HHmVDuO8C Cited by: 3434

The α/β hydrolase fold DL Ollis, E Cheah, M Cygler, B Dijkstra, F Frolow, SM Franken, M Harel, … Protein Engineering, Design and Selection 5 (3), 197-211, 1992 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:u-x6o8ySG0sC Cited by: 2800

FoldIndex©: a simple tool to predict whether a given protein sequence is intrinsically unfolded J Prilusky, CE Felder, T Zeev-Ben-Mordehai, EH Rydberg, O Man, … Bioinformatics 21 (16), 3435-3438, 2005 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:IjCSPb-OGe4C Cited by: 1169

Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. M Harel, I Schalk, L Ehret-Sabatier, F Bouet, M Goeldner, C Hirth, … Proceedings of the National Academy of Sciences 90 (19), 9031-9035, 1993 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:9yKSN-GCB0IC Cited by: 1162

Three-dimensional tertiary structure of yeast phenylalanine transfer RNA SH Kim, FL Suddath, GJ Quigley, A McPherson, JL Sussman, AHJ Wang, … Science 185 (4149), 435-440, 1974 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:d1gkVwhDpl0C Cited by: 1138

Function and structure of inherently disordered proteins AK Dunker, I Silman, VN Uversky, JL Sussman Current opinion in structural biology 18 (6), 756-764, 2008 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:MXK_kJrjxJIC Cited by: 1120

Protein production and purification Architecture et Fonction des Macromolécules Biologiques Vincentelli Renaud 4 … Nature methods 5 (2), 135-146, 2008 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:27LrP4qxOz0C Cited by: 992

Structure of acetylcholinesterase complexed with E2020 (Aricept®): implications for the design of new anti-Alzheimer drugs G Kryger, I Silman, JL Sussman Structure 7 (3), 297-307, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:YsMSGLbcyi4C Cited by: 913

Three-dimensional structures of avidin and the avidin-biotin complex. O Livnah, EA Bayer, M Wilchek, JL Sussman Proceedings of the National Academy of Sciences 90 (11), 5076-5080, 1993 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:UeHWp8X0CEIC Cited by: 909

Acetylcholinesterase: from 3D structure to function H Dvir, I Silman, M Harel, TL Rosenberry, JL Sussman Chemico-biological interactions 187 (1-3), 10-22, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:SdhP9T11ey4C Cited by: 893

Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes M Harel, A Aharoni, L Gaidukov, B Brumshtein, O Khersonsky, R Meged, … Nature structural & molecular biology 11 (5), 412-419, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:Tyk-4Ss8FVUC Cited by: 873

Protein Data Bank (PDB): database of three-dimensional structural information of biological macromolecules JL Sussman, D Lin, J Jiang, NO Manning, J Prilusky, O Ritter, EE Abola Acta Crystallographica Section D: Biological Crystallography 54 (6), 1078-1084, 1998 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:W7OEmFMy1HYC Cited by: 818

The pitch of chromatin DNA is reflected in its nucleotide sequence. EN Trifonov, JL Sussman Proceedings of the National Academy of Sciences 77 (7), 3816-3820, 1980 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:2osOgNQ5qMEC Cited by: 756

Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins M Cygler, JD Schrag, JL Sussman, M Harel, I Silman, MK Gentry, … Protein Science 2 (3), 366-382, 1993 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:qjMakFHDy7sC Cited by: 733

Acetylcholinesterase:‘classical’and ‘non-classical’functions and pharmacology I Silman, JL Sussman Current opinion in pharmacology 5 (3), 293-302, 2005 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:ULOm3_A8WrAC Cited by: 656

Specific chemical and structural damage to proteins produced by synchrotron radiation M Weik, RBG Ravelli, G Kryger, S McSweeney, ML Raves, M Harel, … Proceedings of the National Academy of Sciences 97 (2), 623-628, 2000 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:Y0pCki6q_DkC Cited by: 615

Structure of acetylcholinesterase complexed with the nootropic alkaloid,(–)-huperzine A ML Raves, M Harel, YP Pang, I Silman, AP Kozikowski, JL Sussman Nature structural biology 4 (1), 57-63, 1997 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:zYLM7Y9cAGgC Cited by: 550

Automated structure-and sequence-based design of proteins for high bacterial expression and stability A Goldenzweig, M Goldsmith, SE Hill, O Gertman, P Laurino, Y Ashani, … Molecular cell 63 (2), 337-346, 2016 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:U0iAMwwPxtsC Cited by: 486

Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system Y Shaaltiel, D Bartfeld, S Hashmueli, G Baum, E Brill‐Almon, G Galili, … Plant biotechnology journal 5 (5), 579-590, 2007 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:mB3voiENLucC Cited by: 481

The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase M Harel, DM Quinn, HK Nair, I Silman, JL Sussman Journal of the American Chemical Society 118 (10), 2340-2346, 1996 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:_FxGoFyzp5QC Cited by: 444

Co-authors

Dan S Tawfik fy8CjqwAAAAJ

Felix Frolow r-Ps_WQAAAAJ

Hay Dvir, Ph.D. wGaqoQsAAAAJ

martin weik qIz45ZwAAAAJ

Raimond Ravelli AnU6rWsAAAAJ

moshe goldsmith pOPaOTUAAAAJ

Tzviya Zeev 7UNWMWMAAAAJ

Jacques-Philippe Colletier CWiop4kAAAAJ

Nadrian C. Seeman OLf4b6QAAAAJ

Dawei Lin kUBWyDwAAAAJ

Paul H. Axelsen bvfGgXYAAAAJ

Miroslaw Cygler MMCyOO4AAAAJ

Amir Aharoni 6z30BoIAAAAJ

Aviv Paz ZmUqSxcAAAAJ

moshe ben-David o9utvyMAAAAJ

Piet Gros fYwKExoAAAAJ

Menachem Shoham ziuLUMkAAAAJ

George Church SfDzdgEAAAAJ

Oded Livnah tBaEUDEAAAAJ

David Ollis jo5raLcAAAAJ

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Co-authors

Dan S Tawfik googlescholarauthor_id:fy8CjqwAAAAJ

Felix Frolow googlescholarauthorid:r-PsWQAAAAJ

Hay Dvir, Ph.D. googlescholarauthor_id:wGaqoQsAAAAJ

martin weik googlescholarauthor_id:qIz45ZwAAAAJ

Raimond Ravelli googlescholarauthor_id:AnU6rWsAAAAJ

moshe goldsmith googlescholarauthor_id:pOPaOTUAAAAJ

Tzviya Zeev googlescholarauthor_id:7UNWMWMAAAAJ

Jacques-Philippe Colletier googlescholarauthor_id:CWiop4kAAAAJ

Nadrian C. Seeman googlescholarauthor_id:OLf4b6QAAAAJ

Dawei Lin googlescholarauthor_id:kUBWyDwAAAAJ

Paul H. Axelsen googlescholarauthor_id:bvfGgXYAAAAJ

Miroslaw Cygler googlescholarauthor_id:MMCyOO4AAAAJ

Amir Aharoni googlescholarauthor_id:6z30BoIAAAAJ

Aviv Paz googlescholarauthor_id:ZmUqSxcAAAAJ

moshe ben-David googlescholarauthor_id:o9utvyMAAAAJ

Piet Gros googlescholarauthor_id:fYwKExoAAAAJ

Menachem Shoham googlescholarauthor_id:ziuLUMkAAAAJ

George Church googlescholarauthor_id:SfDzdgEAAAAJ

Oded Livnah googlescholarauthor_id:tBaEUDEAAAAJ

David Ollis googlescholarauthor_id:jo5raLcAAAAJ

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Co-authors

Dan S Tawfik googlescholarauthorid dans_tawfik.md:fy8CjqwAAAAJ

Felix Frolow googlescholarauthorid felixfrolow.md:r-Ps_WQAAAAJ

Hay Dvir, Ph.D. googlescholarauthorid haydvir,_ph.d..md:wGaqoQsAAAAJ

martin weik googlescholarauthorid martinweik.md:qIz45ZwAAAAJ

Raimond Ravelli googlescholarauthorid raimondravelli.md:AnU6rWsAAAAJ

moshe goldsmith googlescholarauthorid moshegoldsmith.md:pOPaOTUAAAAJ

Tzviya Zeev googlescholarauthorid tzviyazeev.md:7UNWMWMAAAAJ

Jacques-Philippe Colletier googlescholarauthorid jacques-philippecolletier.md:CWiop4kAAAAJ

Nadrian C. Seeman googlescholarauthorid nadrianc._seeman.md:OLf4b6QAAAAJ

Dawei Lin googlescholarauthorid daweilin.md:kUBWyDwAAAAJ

Paul H. Axelsen googlescholarauthorid paulh._axelsen.md:bvfGgXYAAAAJ

Miroslaw Cygler googlescholarauthorid miroslawcygler.md:MMCyOO4AAAAJ

Amir Aharoni googlescholarauthorid amiraharoni.md:6z30BoIAAAAJ

Aviv Paz googlescholarauthorid avivpaz.md:ZmUqSxcAAAAJ

moshe ben-David googlescholarauthorid mosheben-david.md:o9utvyMAAAAJ

Piet Gros googlescholarauthorid pietgros.md:fYwKExoAAAAJ

Menachem Shoham googlescholarauthorid menachemshoham.md:ziuLUMkAAAAJ

George Church googlescholarauthorid georgechurch.md:SfDzdgEAAAAJ

Oded Livnah googlescholarauthorid odedlivnah.md:tBaEUDEAAAAJ

David Ollis googlescholarauthorid davidollis.md:jo5raLcAAAAJ

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Joel Sussman

Weizmann Institute of Science

http://www.weizmann.ac.il/Structural_Biology/Sussman

Atomic Structure of Acetyicholinesterase from JL Sussman, M Harel, F Frolow, C Oefner, A Goldman, L Toker, I Silman Science 253 (5022), 872-879, 1991 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=KbxB0JgAAAAJ&citationforview=KbxB0JgAAAAJ:u5HHmVD_uO8C