Publications

2019

  1. Chandar N. . B., Efremenko I., Silman I., Martin J. . M. & Sussman J. . L. (2019). Molecular dynamics simulations of the interaction of Mouse and Torpedo acetylcholinesterase with covalent inhibitors explain their differential reactivity: Implications for drug design.  Chemico-Biological Interactions. 310.  Abstract
  2. Oukoloff K., Coquelle N., Bartolini M., Naldi M., Le Guevel R., Bach S., Josselin B., Ruchaud S., Catto M., Pisani L., Denora N., Lacobazzi R. M., Silman I., Sussman J. L., Buron F., Colletier J., Jean L., Routier S. & Renard P. (2019). Design, biological evaluation and X-ray crystallography of nanomolar multifunctional ligands targeting simultaneously acetylcholinesterase and glycogen synthase kinase-3.  European Journal of Medicinal Chemistry. 168:58-77.  Abstract
  3. Dighe S. N., De La Mora E., Chan S., Kantham S., Mccoll G., Miles J. A., Veliyath S. K., Sreenivas B. Y., Nassar Z. D., Silman I., Sussman J. L., Weik M., Mcgeary R. P., Parat M., Brazzolotto X. & Ross B. P. (2019). Rivastigmine and metabolite analogues with putative Alzheimer's disease-modifying properties in a Caenorhabditis elegans model.  Communications chemistry. 2.  Abstract
  4. Lalut J., Santoni G., Karila D., Lecoutey C., Davis A., Nachon F., Silman I., Sussman J., Weik M., Maurice T., Dallemagne P. & Rochais C. (2019). Novel multitarget-directed ligands targeting acetylcholinesterase and sigma(1) receptors as lead compounds for treatment of Alzheimer's disease: Synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase.  European Journal of Medicinal Chemistry. 162:234-248.  Abstract

2018

  1. Leung M. R., Van Bezouwen L. S., Schopfer L. M., Sussman J. L., Silman I., Lockridge O. & Zeev-Ben-Mordehai T. (2018). Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly.  Proceedings Of The National Academy Of Sciences Of The United States Of America-Physical Sciences. 115:(52)13270-13275.  Abstract
  2. Santoni G., De Sousa J., De La Mora E., Dias J., Jean L., Sussman J. L., Silman I., Renard P., Brown R. C. D., Weik M., Baati R. & Nachon F. (2018). Structure-Based Optimization of Nonquaternary Reactivators of Acetylcholinesterase Inhibited by Organophosphorus Nerve Agents.  Journal of Medicinal Chemistry. 61:(17)7630-7639.  Abstract
  3. Zorbaz T., Braiki A., Marakovic N., Renou J., De La Mora E., Hrvat N. M., Katalinic M., Silman I., Sussman J. L., Mercey G., Gomez C., Mougeot R., Perez B., Baati R., Nachon F., Weik M., Jean L., Kovarik Z. & Renard P. (2018). Potent 3-Hydroxy-2-Pyridine Aldoxime Reactivators of Organophosphate-Inhibited Cholinesterases with Predicted Blood-Brain Barrier Penetration.  Chemistry-A European Journal. 24:(38)9675-9691.  Abstract
  4. Faraggi E., Dunker A. K., Sussman J. L. & Kloczkowski A. (2018). Comparing NMR and X-ray protein structure: Lindemann-like parameters and NMR disorder.  Journal of biomolecular structure & dynamics. 36:(9)2331-2341.  Abstract

2017

  1. Silman I. & Sussman J. (2017). Recent developments in structural studies on acetylcholinesterase.  Journal of Neurochemistry. 142:19-25.  Abstract
  2. Xu Y., Cheng S., Sussman J., Silman I. & Jiang H. (2017). Computational Studies on Acetylcholinesterases.  Molecules. 22:(8)  Abstract
  3. Goldsmith M., Aggarwal N., Ashani Y., Jubran H., Greisen P. J., Ovchinnikov S., Leader H., Baker D., Sussman J., Goldenzweig A., Fleishman S. J. & Tawfik D. (2017). Overcoming an optimization plateau in the directed evolution of highly efficient nerve agent bioscavengers.  PROTEIN ENGINEERING DESIGN & SELECTION. 30:(4)333-345.  Abstract

2016

  1. Ashani Y., Leader H., Aggarwal N., Silman I., Worek F., Sussman J. L. & Goldsmith M. (2016). In vitro evaluation of the catalytic activity of paraoxonases and phosphotriesterases predicts the enzyme circulatory levels required for in vivo protection against organophosphate intoxications.  Chemico-Biological Interactions. 259:252-256.  Abstract
  2. Goldsmith M., Eckstein S., Ashani Y., Greisen P. J., Leader H., Sussman J., Aggarwal N., Ovchinnikov S., Tawfik D., Baker D., Thiermann H. & Worek F. (2016). Catalytic efficiencies of directly evolved phosphotriesterase variants with structurally different organophosphorus compounds in vitro.  Archiv fur Toxikologie. 90:(11)2711-2724.  Abstract
  3. Wille T., Neumaier K., Koller M., Ehinger C., Aggarwal N., Ashani Y., Goldsmith M., Sussman J., Tawfik D., Thiermann H. & Worek F. (2016). Single treatment of VX poisoned guinea pigs with the phosphotriesterase mutant C23AL: Intraosseous versus intravenous injection.  Toxicology Letters. 258:198-206.  Abstract
  4. Goldenzweig A., Goldsmith M., Hill S. E., Gertman O., Laurino P., Ashani Y., Dym O., Unger T., Albeck S., Prilusky J., Lieberman R. L., Aharoni A., Silman I., Sussman J., Tawfik D. & Fleishman S. J. (2016). Automated Structure- and Sequence-Based Design of Proteins for High Bacterial Expression and Stability.  Molecular Cell. 63:(2)337-346.  Abstract
  5. Dym O., Song W., Felder C., Roth E., Shnyrov V., Ashani Y., Xu Y., Joosten R. P., Weiner L., Sussman J. & Silman I. (2016). The impact of crystallization conditions on structure-based drug design: A case study on the methylene blue/acetylcholinesterase complex.  Protein Science. 25:(6)1096-1114.  Abstract

2015

  1. Ben David D. M., Sussman J., Maxwel C. L., Szeler K., Kamerlin S. C. L. & Tawfik D. (2015). Catalytic Stimulation by Restrained Active-Site Floppiness-The Case of High Density Lipoprotein-Bound Serum Paraoxonase-1.  Journal of Molecular Biology. 427:(6)1359-1374.  Abstract

2014

  1. Worek F., Seeger T., Reiter G., Goldsmith M., Ashani Y., Leader H., Sussman J., Aggarwal N., Thiermann H. & Tawfik D. (2014). Post-exposure treatment of VX poisoned guinea pigs with the engineered phosphotriesterase mutant C23: A proof-of-concept study.  Toxicology Letters. 231:(1)45-54.  Abstract
  2. Varadi M., Kosol S., Lebrun P., Valentini E., Blackledge M., Dunker A. K., Felli I. C., Forman-Kay J. D., Kriwacki R. W., Pierattelli R., Sussman J., Svergun D. I., Uversky V. N., Vendruscolo M., Wishart D., Wright P. E. & Tompa P. (2014). pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins.  Nucleic Acids Research. 42:(D1)D326-D335.  Abstract

2013

  1. Prilusky J. & Sussman J. (2013). Databases and Bioinformatics Tools.  Israel Journal of Chemistry. 53:(4-Mar)143-143.
  2. Hanson R. M., Prilusky J., Renjian Z., Nakane T. & Sussman J. (2013). JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia.  Israel Journal of Chemistry. 53:(4-Mar)207-216.  Abstract
  3. Silman I., Roth E., Paz A., Triquigneaux M. M., Ehrenshaft M., Xu Y., Shnyrov V. L., Sussman J., Deterding L. J., Ashani Y., Mason R. P. & Weiner L. (2013). The specific interaction of the photosensitizer methylene blue with acetylcholinesterase provides a model system for studying the molecular consequences of photodynamic therapy.  Chemico-Biological Interactions. 203:(1)63-66.  Abstract
  4. Ben David D. M., Wieczorek G., Elias M., Silman I., Sussman J. & Tawfik D. (2013). Catalytic Metal Ion Rearrangements Underline Promiscuity and Evolvability of a Metalloenzyme.  Journal of Molecular Biology. 425:(6)1028-1038.  Abstract

2012

  1. Paz A., Roth E., Ashani Y., Xu Y., Shnyrov V. L., Sussman J., Silman I. & Weiner L. (2012). Structural and functional characterization of the interaction of the photosensitizing probe methylene blue with Torpedo californica acetylcholinesterase.  Protein Science. 21:(8)1138-1152.  Abstract
  2. Ben David D. M., Elias M., Filippi J., Dunach E., Silman I., Sussman J. & Tawfik D. (2012). Catalytic Versatility and Backups in Enzyme Active Sites: The Case of Serum Paraoxonase 1.  Journal of Molecular Biology. 418:(4-Mar)181-196.  Abstract
  3. Goldsmith M., Ashani Y., Simo Y., Ben David D. M., Leader H., Silman I., Sussman J. & Tawfik D. (2012). Evolved Stereoselective Hydrolases for Broad-Spectrum G-Type Nerve Agent Detoxification.  Chemistry & Biology. 19:(4)456-466.  Abstract
  4. Wood K., Paz A., Dijkstra K., Scheek R. M., Otten R., Silman I., Sussman J. & Mulder F. A. A. (2012). Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.  Biomolecular NMR Assignments. 6:(1)15-18.  Abstract
  5. Acheampong M. G., Dueno D. E., Glover B. K., Henry A. A., Mata R., Vanbrakle M. L., Westblade L. F., Sussman J. & Granberry A. L. (2012). Acetylcholinesterase: Substrate traffic and inhibition.  Biochemistry and Molecular Biology Education. 40:(2)144-144.
  6. Greenblatt H. M., Otto T. C., Kirkpatrick M. G., Kovaleva E., Brown S., Buchman G., Cerasoli D. M. & Sussman J. (2012). Structure Of Recombinant Human Carboxylesterase 1 Isolated From Whole Cabbage Looper Larvae.  Acta Crystallographica Section F-Structural Biology And Crystallization Communications. 68:269-272.  Abstract
  7. Khare S. D., Kipnis Y., Greisen P. J., Takeuchi R., Ashani Y., Goldsmith M., Song Y., Gallaher J. L., Silman I., Leader H., Sussman J., Stoddard B. L., Tawfik D. & Baker D. (2012). Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis.  Nature Chemical Biology. 8:(3)294-300.  Abstract
  8. Xu Y., Li M., Greenblatt H., Chen W., Paz A., Dym O., Peleg Y., Chen T., Shen X., He J., Jiang H., Silman I. & Sussman J. (2012). Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations.  Acta Crystallographica Section D-Biological Crystallography. 68:13-25.  Abstract

2011

  1. Offman M. N., Krol M., Rost B., Silman I., Sussman J. & Futerman A. H. (2011). Comparison of a molecular dynamics model with the X-ray structure of the N370S acid--glucosidase mutant that causes Gaucher disease.  PROTEIN ENGINEERING DESIGN & SELECTION. 24:(10)773-775.  Abstract
  2. Ashani Y., Goldsmith M., Leader H., Silman I., Sussman J. & Tawfik D. (2011). In vitro detoxification of cyclosarin in human blood pre-incubated ex vivo with recombinant serum paraoxonases.  Toxicology Letters. 206:(1)24-28.  Abstract
  3. Busso D., Peleg Y., Heidebrecht T., Romier C., Jacobovitch Y., Dantes A., Salim L., Troesch E., Schuetz A., Heinemann U., Folkers G. E., Geerlof A., Wilmanns M., Polewacz A., Quedenau C., Buessow K., Adamson R., Blagova E., Walton J., Cartwright J. L., Bird L. E., Owens R. J., Berrow N. S., Wilson K. S., Sussman J., Perrakis A. & Celie P. H. N. (2011). Expression Of Protein Complexes Using Multiple Escherichia Coli Protein Co-Expression Systems: A Benchmarking Study.  Journal of Structural Biology. 175:(2)159-170.  Abstract
  4. Suskiewicz M. J., Sussman J., Silman I. & Shaul Y. (2011). Context-dependent resistance to proteolysis of intrinsically disordered proteins.  Protein Science. 20:(8)1285-1297.  Abstract
  5. Perrakis A., Daenke S., Stuart D. I. & Sussman J. (2011). From SPINE to SPINE-2 complexes and beyond.  Journal of Structural Biology. 175:(2)105-105.
  6. Prilusky J., Hodis E., Canner D., Decatur W. A., Oberholser K., Martz E., Berchanski A., Harel M. & Sussman J. (2011). Proteopedia: A Status Report On The Collaborative, 3D Web-Encyclopedia Of Proteins And Other Biomolecules.  Journal of Structural Biology. 175:(2)244-252.  Abstract
  7. Sanson B., Colletier J., Xu Y., Lang P. T., Jiang H., Silman I., Sussman J. & Weik M. (2011). Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations.  Protein Science. 20:(7)1114-1118.  Abstract
  8. Li M., Greenblatt H. M., Dym O., Albeck S., Pais A., Gunanathan C., Milstein D., Degani H. & Sussman J. (2011). Structure of Estradiol Metal Chelate and Estrogen Receptor Complex: The Basis for Designing a New Class of Selective Estrogen Receptor Modulators.  Journal of Medicinal Chemistry. 54:(10)3575-3580.  Abstract
  9. Gupta R. D., Goldsmith M., Ashani Y., Simo Y., Mullokandov G., Bar H., Ben David D. M., Leader H., Margalit R., Silman I., Sussman J. & Tawfik D. (2011). Directed evolution of hydrolases for prevention of G-type nerve agent intoxication.  Nature Chemical Biology. 7:(2)120-125.  Abstract
  10. Brumshtein B., Aguilar-Moncayo M., Benito J. M., Garcia Fernandez F. J. M., Silman I., Shaaltiel Y., Aviezer D., Sussman J., Futerman A. H. & Ortiz Mellet M. C. (2011). Cyclodextrin-mediated crystallization of acid beta-glucosidase in complex with amphiphilic bicyclic nojirimycin analogues.  Organic & Biomolecular Chemistry. 9:(11)4160-4167.  Abstract

2010

  1. Offman M. N., Krol M., Silman I., Sussman J. & Futerman A. H. (2010). Molecular Basis of Reduced Glucosylceramidase Activity in the Most Common Gaucher Disease Mutant, N370S.  Journal of Biological Chemistry. 285:(53)42105-42114.  Abstract
  2. Xu Y., Colletier J., Weik M., Qin G., Jiang H., Silman I. & Sussman J. (2010). Long Route or Shortcut? A Molecular Dynamics Study of Traffic of Thiocholine within the Active-Site Gorge of Acetylcholinesterase.  Biophysical Journal. 99:(12)4003-4011.  Abstract
  3. Dvir H., Silman I., Harel M., Rosenberry T. L. & Sussman J. (2010). Acetylcholinesterase: From 3D structure to function.  Chemico-Biological Interactions. 187:(3-Jan)10-22.  Abstract
  4. Ashani Y., Gupta R. D., Goldsmith M., Silman I., Sussman J., Tawfik D. & Leader H. (2010). Stereo-Specific Synthesis Of Analogs Of Nerve Agents And Their Utilization For Selection And Characterization Of Paraoxonase (Pon1) Catalytic Scavengers.  Chemico-Biological Interactions. 187:(1-3)362-369.  Abstract
  5. Hodis E., Prilusky J. & Sussman J. (2010). Proteopedia: A Collaborative, Virtual 3D Web-resource for Protein and Biomolecule Structure and Function.  Biochemistry and Molecular Biology Education. 38:(5)341-342.
  6. Brumshtein B., Salinas P., Peterson B., Chan V., Silman I., Sussman J., Savickas P. J., Robinson G. S. & Futerman A. H. (2010). Characterization of gene-activated human acid-beta-glucosidase: Crystal structure, glycan composition, and internalization into macrophages.  Glycobiology. 20:(1)24-32.  Abstract

2009

  1. Sanson B., Nachon F., Colletier J., Froment M., Toker L., Greenblatt H. M., Sussman J., Ashani Y., Masson P., Silman I. & Weik M. (2009). Crystallographic Snapshots of Nonaged and Aged Conjugates of Soman with Acetylcholinesterase, and of a Ternary Complex of the Aged Conjugate with Pralidoxime.  Journal of Medicinal Chemistry. 52:(23)7593-7603.  Abstract
  2. Sharabi O., Peleg Y., Mashiach E., Vardy E., Ashani Y., Silman I., Sussman J. & Shifman J. M. (2009). Design, expression and characterization of mutants of fasciculin optimized for interaction with its target, acetylcholinesterase.  PROTEIN ENGINEERING DESIGN & SELECTION. 22:(10)641-648.  Abstract
  3. Zeev-Ben-Mordehai T., Mylonas E., Paz A., Peleg Y., Toker L., Silman I., Svergun D. I. & Sussman J. (2009). The Quaternary Structure Of Amalgam, A Drosophila Neuronal Adhesion Protein, Explains Its Dual Adhesion Properties.  Biophysical Journal. 97:(8)2316-2326.  Abstract
  4. Khersonsky O., Rosenblat M., Toker L., Yacobson S., Hugenmatter A., Silman I., Sussman J., Aviram M. & Tawfik D. (2009). Directed Evolution of Serum Paraoxonase PON3 by Family Shuffling and Ancestor/Consensus Mutagenesis, and Its Biochemical Characterization.  Biochemistry. 48:(28)6644-6654.  Abstract
  5. Brumshtein B., Aguilar-Moncayo M., Isabel Garcia-Moreno G. M., Ortiz Mellet M. C., Garcia Fernandez F. J. M., Silman I., Shaaltiel Y., Aviezer D., Sussman J. & Futerman A. H. (2009). 6-Amino-6-deoxy-5,6-di-N-(N '-octyliminomethylidene)nojirimycin: Synthesis, Biological Evaluation, and Crystal Structure in Complex with Acid beta-Glucosidase.  ChemBioChem. 10:(9)1480-1485.
  6. Paz A., Xie Q., Greenblat H. M., Fu W., Tang Y., Silman I., Qiu Z. & Sussman J. (2009). The Crystal Structure of a Complex of Acetylcholinesterase with a Bis-(-)-nor-meptazinol Derivative Reveals Disruption of the Catalytic Triad.  Journal of Medicinal Chemistry. 52:(8)2543-2549.  Abstract
  7. Hodis E. & Sussman J. (2009). An encyclopedic effort to make 3D structures easier to understand.  Trends in Biochemical Sciences. 34:(3)100-101.
  8. Zeev-Ben-Mordehai T., Paz A., Peleg Y., Toker L., Wolf S. G., Rydberg E. H., Sussman J. & Silman I. (2009). Amalgam, an axon guidance Drosophila adhesion protein belonging to the immunoglobulin superfamily: Over-expression, purification and biophysical characterization.  Protein Expression and Purification. 63:(2)147-157.  Abstract
  9. Noivirt-Brik O., Prilusky J. & Sussman J. (2009). Assessment of disorder predictions in CASP8.  Proteins-Structure Function And Bioinformatics. 77:210-216.  Abstract
  10. Sussman J. & Silman I. (2009). STRUCTURAL STUDIES ON ACETYLCHOLINESTERASE AND PARAOXONASE DIRECTED TOWARDS DEVELOPMENT OF THERAPEUTIC BIOMOLECULES FOR THE TREATMENT OF DEGENERATIVE DISEASES AND PROTECTION AGAINST CHEMICAL THREAT AGENTS.  From Molecules To Medicines: Structure Of Biological Macromolecules And Its Relevance In Combating New Diseases And Bioterrorism. 183-199.  Abstract
  11. Hodis E., Prilusky J. & Sussman J. (2009). TOOLS TO MAKE 3D STRUCTURAL DATA MORE COMPREHENSIBLE: EMOVIE & PROTEOPEDIA.  From Molecules To Medicines: Structure Of Biological Macromolecules And Its Relevance In Combating New Diseases And Bioterrorism. 169-182.  Abstract
  12. Ben David D. M., Noivirt-Brik O., Paz A., Prilusky J., Sussman J. & Levy Y. (2009). Assessment of CASP8 structure predictions for template free targets.  Proteins-Structure Function And Bioinformatics. 77:50-65.  Abstract

2008

  1. Dunker A. K., Silman I., Uversky V. N. & Sussman J. (2008). Function and structure of inherently disordered proteins.  Current Opinion in Structural Biology. 18:(6)756-764.  Abstract
  2. Kacher Y., Brumshtein B., Boldin-Adamsky S., Toker L., Shainskaya A., Silman I., Sussman J. & Futerman A. H. (2008). Acid beta-glucosidase: insights from structural analysis and relevance to Gaucher disease therapy.  Biological Chemistry. 389:(11)1361-1369.  Abstract
  3. Brumshtein B., Greenblatt H. M., Futerman A. H., Silman I. & Sussman J. (2008). Control of the rate of evaporation in protein crystallization by the 'microbatch under oil' method.  Journal of Applied Crystallography. 41:969-971.  Abstract
  4. Silman I. & Sussman J. (2008). Acetylcholinesterase: How is structure related to function?.  Chemico-Biological Interactions. 175:(3-Jan)3-10.  Abstract
  5. Xu Y., Colletier J., Weik M., Jiang H., Moult J., Silman I. & Sussman J. (2008). Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics.  Biophysical Journal. 95:(5)2500-2511.  Abstract
  6. Colletier J., Bourgeois D., Sanson B., Fournier D., Sussman J., Silman I. & Weik M. (2008). Shoot-And-Trap: Use Of Specific X-Ray Damage To Study Structural Protein Dynamics By Temperature-Control Led Cryo-Crystallography.  Proceedings of the National Academy of Sciences of the United States of America. 105:(33)11742-11747.  Abstract
  7. Paz A., Zeev-Ben-Mordehai T., Lundqvist M., Sherman E., Mylonas E., Weiner L., Haran G., Svergun D. I., Mulder F. A. A., Sussman J. & Silman I. (2008). Biophysical Characterization Of The Unstructured Cytoplasmic Domain Of The Human Neuronal Adhesion Protein Neuroligin 3.  Biophysical Journal. 95:(4)1928-1944.  Abstract
  8. Harel M., Sonoda L. K., Silman I., Sussman J. & Rosenberry T. L. (2008). Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site.  Journal of the American Chemical Society. 130:(25)7856-7861.  Abstract
  9. Manicka S., Peleg Y., Unger T., Albeck S., Dym O., Greenblatt H. A., Bourenkov G., Lamzin V., Krishnaswamy S. & Sussman J. (2008). Crystal structure of yagE, a putative DHDPS-like protein from Escherichia coli K12.  Proteins-Structure Function And Bioinformatics. 71:(4)2102-2108.
  10. Tompa P., Prilusky J., Silman I. & Sussman J. (2008). Structural Disorder Serves As A Weak Signal For Intracellular Protein Degradation.  Proteins-Structure Function And Bioinformatics. 71:(2)903-909.  Abstract
  11. Gunanathan C., Pais A., Li M., Milstein D., Sussman J. & Degani H. (2008). Novel selective estrogen receptor modulators for non-invasive molecular imaging.  Proceedings of the American Association for Cancer Research Annual Meeting. 49:753-754.
  12. Xu Y., Colletier J. P., Jiang H., Silman I., Sussman J. & Weik M. (2008). Induced-fit or preexisting equilibrium dynamics? Lessons from protein crystallography and MD simulations on acetylcholinesterase and implications for structure-based drug design.  Protein Science. 17:(4)601-605.  Abstract
  13. Tsvetkov P., Asher G., Paz A., Reuven N., Sussman J., Silman I. & Shaul Y. (2008). Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome.  Proteins-Structure Function And Bioinformatics. 70:(4)1357-1366.  Abstract
  14. , Graslund S., Peleg Y., Albeck S., Unger T., Dym O., Prilusky J. & Sussman J. L. (2008). Protein production and purification.  Nature Methods. 5:(2)135-146.  Abstract
  15. Hodis E., Prilusky J., Martz E., Silman I., Moult J. & Sussman J. (2008). Proteopedia - a scientific 'wiki' bridging the rift between three-dimensional structure and function of biomacromolecules.  GENOME BIOLOGY. 9:(8)  Abstract

2007

  1. Colletier J., Royant A., Specht A., Sanson B., Nachon F., Masson P., Zaccai G., Sussman J., Goeldner M., Silman I., Bourgeois D. & Weik M. (2007). Use Of A 'Caged' Analogue To Study The Traffic Of Choline Within Acetylcholinesterase By Kinetic Crystallography.  Acta Crystallographica Section D-Biological Crystallography. 63:1115-1128.  Abstract
  2. Shaaltiel Y., Bartfeld D., Hashmueli S., Baum G., Brill-Almon E., Galili G., Dym O., Boldin-Adamsky S. A., Silman I., Sussman J., Futerman A. H. & Aviezer D. (2007). Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system.  Plant Biotechnology Journal. 5:(5)579-590.  Abstract
  3. Brumshtein B., Greenblatt H. M., Butters T. D., Shaaltiel Y., Aviezer D., Silman I., Futerman A. H. & Sussman J. (2007). Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid beta-glucosidase - Insights into the mechanism of chemical chaperone action in Gaucher disease.  Journal of Biological Chemistry. 282:(39)29052-29058.  Abstract
  4. Felder C. E., Prilusky J., Silman I. & Sussman J. (2007). A server and database for dipole moments of proteins.  Nucleic Acids Research. 35:W512-W521.  Abstract
  5. Hodis E., Schreiber G., Rother K. & Sussman J. (2007). eMovie: a storyboard-based tool for making molecular movies.  Trends in Biochemical Sciences. 32:(5)199-204.  Abstract
  6. Banci L., Baumeister W., Enfedaque J., Heinemann U., Schneider G., Silman I. & Sussman J. (2007). Structural proteomics: from the molecule to the system.  Nature Structural & Molecular Biology. 14:(1)3-4.  Abstract
  7. Banci L., Baumeister W., Heinemann U., Schneider G., Silman I., Stuart D. I. & Sussman J. (2007). An idea whose time has come.  GENOME BIOLOGY. 8:(11)
  8. Man O., Sussman J. & Pilpel Y. (2007). Examination of the tRNA adaptation index as a predictor of protein expression levels.  Systems Biology And Regulatory Genomics. 4023:107-118.  Abstract
  9. Haviv H., Wong D. M., Silman I. & Sussman J. (2007). Bivalent Ligands Derived From Huperzine A As Acetylcholinesterase Inhibitors.  Current Topics in Medicinal Chemistry. 7:(4)375-387.  Abstract

2006

  1. Brumshtein B., Wormald M. R., Silman I., Futerman A. H. & Sussman J. (2006). Structural Comparison Of Differently Glycosylated Forms Of Acid-Beta-Glucosidase, The Defective Enzyme In Gaucher Disease.  Acta Crystallographica Section D-Biological Crystallography. 62:1458-1465.  Abstract
  2. Banci L., Bertini I., Cusack S., De Jong J. R. N., Heinemann U., Jones E. Y., Kozielski F., Maskos K., Messerschmidt A., Owens R., Perrakis A., Poterszman A., Schneider G., Siebold C., Silman I., Sixma T., Stewart-Jones G., Sussman J., Thierry J. -. & Moras D. (2006). First Steps Towards Effective Methods In Exploiting High-Throughput Technologies For The Determination Of Human Protein Structures Of High Biomedical Value.  Acta Crystallographica Section D-Biological Crystallography. 62:1208-1217.  Abstract
  3. Albeck S., Alzari P., Andreini C., Banci L., Berry I. M., Bertini I., Cambillau C., Canard B., Carter L., Cohen S. X., Diprose J. M., Dym O., Esnouf R. M., Felder C., Ferron F., Guillemot F., Hamer R., Ben Jelloul J. M., Laskowski R. A., Laurent T., Longhi S., Lopez R., Luchinat C., Malet H., Mochel T., Morris R. J., Moulinier L., Oinn T., Pajon A., Peleg Y., Perrakis A., Poch O., Prilusky J., Rachedi A., Ripp R., Rosato A., Silman I., Stuart D. I., Sussman J., Thierry J. -., Thompson J. D., Thornton J. M., Unger T., Vaughan B., Vranken W., Watson J. D., Whamond G. & Henrick K. (2006). Spine Bioinformatics And Data-Management Aspects Of High-Throughput Structural Biology.  ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY. 62:1184-1195.  Abstract
  4. Aricescu A. R., Assenberg R., Bill R. M., Busso D., Chang V. T., Davis S. J., Dubrovsky A., Gustafsson L., Hedfalk K., Heinemann U., Jones I. M., Ksiazek D., Lang C., Maskos K., Messerschmidt A., Macieira S., Peleg Y., Perrakis A., Poterszman A., Schneider G., Sixma T. K., Sussman J., Sutton G., Tarboureich N., Zeev-Ben-Mordehai T. & Jones E. Y. (2006). Eukaryotic Expression: Developments For Structural Proteomics.  Acta Crystallographica Section D-Biological Crystallography. 62:1114-1124.  Abstract
  5. Berry I. M., Dym O., Esnouf R. M., Harlos K., Meged R., Perrakis A., Sussman J., Walter T. S., Wilson J. & Messerschmidt A. (2006). Spine High-Throughput Crystallization, Crystal Imaging And Recognition Techniques: Current State, Performance Analysis, New Technologies And Future Aspects.  Acta Crystallographica Section D-Biological Crystallography. 62:1137-1149.  Abstract
  6. Romier C., Ben Jelloul J. M., Albeck S., Buchwald G., Busso D., Celie P. H. N., Christodoulou E., De Marco M. V., Van Gerwen G. S., Knipscheer P., Lebbink J. H., Notenboom V., Poterszman A., Rochel N., Cohen S. X., Unger T., Sussman J., Moras D., Sixma T. K. & Perrakis A. (2006). Co-Expression Of Protein Complexes In Prokaryotic And Eukaryotic Hosts: Experimental Procedures, Database Tracking And Case Studies.  Acta Crystallographica Section D-Biological Crystallography. 62:1232-1242.  Abstract
  7. Esnouf R. M., Hamer R., Sussman J., Silman I., Trudgian D., Yang Z. -. & Prilusky J. (2006). Honing The In Silico Toolkit For Detecting Protein Disorder.  Acta Crystallographica Section D-Biological Crystallography. 62:1260-1266.  Abstract
  8. Sussman J., Aharoni A., Harel M., Gaidukov L., Brumshtein B., Khersonsky O., Yagur S., Toker L., Silman I. & Tawfik D. (2006). 3D structure of mammalian paraoxonase at 2.2A resolution.  Toxicology Letters. 164:S9-S9.  Abstract
  9. Rydberg E. H., Brumshtein B., Greenblatt H. M., Wong D. M., Shaya D., Williams L. D., Carlier P. R., Pang Y., Silman I. & Sussman J. (2006). Complexes of alkylene-linked tacrine dimers with Torpedo californica acetylcholinesterase: Binding of bis(5)-tacrine produces a dramatic rearrangement in the active-site gorge.  Journal of Medicinal Chemistry. 49:(18)5491-5500.  Abstract
  10. Colletier J., Fournier D., Greenblatt H. M., Stojan J., Sussman J., Zaccai G., Silman I. & Weik M. (2006). Structural insights into substrate traffic and inhibition in acetylcholinesterase.  EMBO Journal. 25:(12)2746-2756.  Abstract
  11. Sussman J. & Silman I. (2006). Shedding UV light on the phase problem.  Structure. 14:(4)629-630.  Abstract
  12. Srividhya K. V., Rao G. V., Raghavenderan L., Mehta P., Prilusky J., Manicka S., Sussman J. & Krishnaswamy S. (2006). Database and comparative identification of prophages.  Intelligent Control And Automation. 344:863-868.  Abstract

2005

  1. Niu C., Xu Y., Xu Y., Luo X., Duan W., Silman I., Sussman J., Zhu W., Chen K., Shen J. & Jiang H. (2005). Dynamic mechanism of E2020 binding to acetylcholinesterase: A steered molecular dynamics simulation.  Journal of Physical Chemistry B. 109:(49)23730-23738.  Abstract
  2. Hyatt J., Tsurkan L., Morton C., Yoon K., Harel M., Brumshtein B., Silman I., Sussman J., Wadkins R. & Potter P. (2005). Inhibition of acetylcholinesterase by the anticancer prodrug CPT-11.  Chemico-Biological Interactions. 157:247-252.  Abstract
  3. Harel M., Hyatt J., Brumshtein B., Morton C., Wadkins R., Silman I., Sussman J. & Potter P. (2005). The 3D structure of the anticancer prodrug CPT-11 with Torpedo californica acetylcholinesterase rationalizes its inhibitory action on AChE and its hydrolysis by butyrylcholinesterase and carboxylesterase.  Chemico-Biological Interactions. 157:153-157.  Abstract
  4. Albeck S., Burstein Y., Dym O., Jacobovitch Y., Levi N., Meged R., Michael Y., Peleg Y., Prilusky J., Schreiber G., Silman I., Unger T. & Sussman J. (2005). Three-dimensional structure determination of proteins related to human health in their functional context at The Israel Structural Proteomics Center (ISPC).  Acta Crystallographica Section D-Biological Crystallography. 61:1364-1372.  Abstract
  5. Newman J., Egan D., Walter T., Meged R., Berry I., Ben Jelloul J. M., Sussman J., Stuart D. & Perrakis A. (2005). Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: the PACT/JCSG plus strategy.  Acta Crystallographica Section D-Biological Crystallography. 61:1426-1431.  Abstract
  6. Prilusky J., Felder C., Zeev-Ben-Mordehai T., Rydberg E., Man O., Beckmann J., Silman I. & Sussman J. (2005). FoldIndex((c)): a simple tool to predict whether a given protein sequence is intrinsically unfolded.  Bioinformatics. 21:(16)3435-3438.  Abstract
  7. Haviv H., Wong D., Greenblatt H., Carlier P., Pang Y., Silman I. & Sussman J. (2005). Crystal packing mediates enantioselective ligand recognition at the peripheral site of acetylcholinesterase.  Journal of the American Chemical Society. 127:(31)11029-11036.  Abstract
  8. Premkumar L., Sawkar A., Boldin-Adamsky S., Toker L., Silman I., Kelly J., Futerman A. H. & Sussman J. (2005). X-ray structure of human acid-beta-glucosidase covalently bound to conduritol-B-epoxide - Implications for Gaucher disease.  Journal of Biological Chemistry. 280:(25)23815-23819.  Abstract
  9. Silman I. & Sussman J. (2005). Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology.  Current Opinion in Pharmacology. 5:(3)293-302.  Abstract
  10. Prilusky J., Oueillet E., Ulryck N., Pajon A., Bernauer J., Krimm I., Quevillon-Cheruel S., Leulliot N., Graille M., Liger D., Tresaugues L., Sussman J., Janin J., Van Tilbeurgh T. H. & Poupon A. (2005). Halx: An Open-Source Lims (Laboratory Information Management System) For Small- To Large-Scale Laboratories.  Acta Crystallographica Section D-Biological Crystallography. 61:671-678.  Abstract
  11. Harel M., Hyatt J., Brumshtein B., Morton C., Yoon K., Wadkins R., Silman I., Sussman J. & Potter P. (2005). The crystal structure of the complex of the anticancer prodrug 7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin (CPT-11) with Torpedo californica acetylcholinesterase provides a molecular explanation for its cholinergic action.  Molecular Pharmacology. 67:(6)1874-1881.  Abstract
  12. Premikumar L., Greenblatt H., Bageshwar U., Savchenko T., Gokhman I., Sussman J. & Zamir A. (2005). Three-Dimensional Structure Of A Halotolerant Algal Carbonic Anhydrase Predicts Halotolerance Of A Mammalian Homolog.  Proceedings of the National Academy of Sciences of the United States of America. 102:(21)7493-7498.  Abstract
  13. Jaakola V., Prilusky J., Sussman J. & Goldman A. (2005). G protein-coupled receptors show unusual patterns of intrinsic unfolding.  PROTEIN ENGINEERING DESIGN & SELECTION. 18:(2)103-110.  Abstract
  14. Premkumar L., Volkovitsky M., Gokhman I., Sussman J. & Zamir A. (2005). Molecular determinants of protein halotolerance: Structural and functional studies of the extremely salt tolerant carbonic anhydrases from Dunaliella salina.  Adaptation To Life At High Salt Concentrations In Archaea, Bacteria, And Eukarya. 9:503-515.  Abstract

2004

  1. Greenblatt H., Guillou C., Guenard D., Argaman A., Botti S., Badet B., Thal C., Silman I. & Sussman J. (2004). The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: Implications for structure-based drug design.  Journal of the American Chemical Society. 126:(47)15405-15411.  Abstract
  2. Dvir H., Harel M., Bon S., Liu W., Vidal M., Garbay C., Sussman J., Massoulie J. & Silman I. (2004). The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix.  EMBO Journal. 23:(22)4394-4405.  Abstract
  3. Liu T., Zhu W., Gu J., Shen J., Luo X., Chen G., Puah C., Silman I., Chen K., Sussman J. & Jiang H. (2004). Additivity of cation-pi interactions: An ab initio computational study on pi-cation-pi sandwich complexes.  Journal of Physical Chemistry A. 108:(43)9400-9405.  Abstract
  4. Zhang S., Rich A., Sussman J. & Fersht A. (2004). Carl-Ivar Branden - 1934-2004 - Obituary.  Nature Structural & Molecular Biology. 11:(6)490-492.
  5. Harel M., Aharoni A., Gaidukov L., Brumshtein B., Khersonsky O., Meged R., Dvir H., Ravelli R. B. G., Mccarthy A., Toker L., Silman I., Sussman J. & Tawfik D. (2004). Structure And Evolution Of The Serum Paraoxonase Family Of Detoxifying And Anti-Atherosclerotic Enzymes.  Nature Structural & Molecular Biology. 11:(5)412-419.  Abstract
  6. Futerman A. H., Sussman J., Horowitz M., Silman I. & Zimran A. (2004). New directions in the treatment of Gaucher disease.  Trends in Pharmacological Sciences. 25:(3)147-151.  Abstract
  7. Bageshwar U., Premkumar L., Gokhman I., Savchenko T., Sussman J. & Zamir A. (2004). Natural protein engineering: a uniquely salt-tolerant, but not halophilic, alpha-type carbonic anhydrase from algae proliferating in low- to hyper-saline environments.  PROTEIN ENGINEERING DESIGN & SELECTION. 17:(2)191-200.  Abstract
  8. Pe'Er I., Felder C., Man O., Silman I., Sussman J. & Beckmann J. (2004). Proteomic signatures: Amino acid and oligopeptide compositions differentiate among phyla.  Proteins-Structure Function And Genetics. 54:(1)20-40.  Abstract
  9. Hasin Y., Avidan N., Bercovich D., Korczyn A., Silman I., Beckmann J. & Sussman J. (2004). A paradigm for single nucleotide polymorphism analysis: The case of the acetylcholinesterase gene.  Human Mutation. 24:(5)408-416.  Abstract

2003

  1. Zeev-Ben-Mordehai T., Rydberg E., Solomon A., Toker L., Auld V., Silman I., Botti S. & Sussman J. (2003). The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded.  Proteins-Structure Function And Genetics. 53:(3)758-767.  Abstract
  2. Xu Y., Shen J., Luo X., Silman I., Sussman J., Chen K. & Jiang H. (2003). How does Huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations.  Journal of the American Chemical Society. 125:(37)11340-11349.  Abstract
  3. Dvir H., Harel M., Mccarthy A., Toker L., Silman I., Futerman A. H. & Sussman J. (2003). X-ray structure of human acid-beta-glucosidase, the defective enzyme in Gaucher disease.  EMBO Reports. 4:(7)704-709.  Abstract
  4. Premkumar L., Greenblatt H., Bageshwar U., Savchenko T., Gokhman I., Zamir A. & Sussman J. (2003). Identification, Cdna Cloning, Expression, Crystallization And Preliminary X-Ray Analysis Of An Exceptionally Halotolerant Carbonic Anhydrase From Dunaliella Salina.  Acta Crystallographica Section D-Biological Crystallography. 59:1084-1086.  Abstract
  5. Zeev-Ben-Mordehai T., Silman I. & Sussman J. (2003). Acetylcholinesterase In Motion: Visualizing Conformational Changes In Crystal Structures By A Morphing Procedure.  Biopolymers. 68:(3)395-406.  Abstract
  6. Premkumar L., Bageshwar U., Gokhman I., Zamir A. & Sussman J. (2003). An unusual halotolerant alpha-type carbonic anhydrase from the alga Dunaliella salina functionally expressed in Escherichia coli.  Protein Expression and Purification. 28:(1)151-157.  Abstract
  7. Wong D., Greenblatt H., Dvir H., Carlier P., Han Y., Pang Y., Silman I. & Sussman J. (2003). Acetylcholinesterase complexed with bivalent ligands related to huperzine A: Experimental evidence for species-dependent protein-ligand complementarity.  Journal of the American Chemical Society. 125:(2)363-373.  Abstract
  8. Greenblatt H., Dvir H., Silman I. & Sussman J. (2003). Acetylcholinesterase - A multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease.  Journal of Molecular Neuroscience. 20:(3)369-383.  Abstract
  9. Katchalski-Katzir E., Kasher R., Balass M., Scherf T., Harel M., Fridkin M., Sussman J. & Fuchs S. (2003). Design and synthesis of peptides that bind alpha-bungarotoxin with high affinity and mimic the three-dimensional structure of the binding-site of acetylcholine receptor.  Biophysical Chemistry. 100:(3-Jan)293-305.  Abstract

2002

  1. Weik M., Berges J., Raves M., Gros P., Mcsweeney S., Silman I., Sussman J., Houee-Levin C. & Ravelli R. (2002). Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation.  Journal of Synchrotron Radiation. 9:342-346.  Abstract
  2. Felder C., Harel M., Silman I. & Sussman J. (2002). Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.  Acta Crystallographica Section D-Biological Crystallography. 58:1765-1771.  Abstract
  3. Dvir H., Jiang H., Wong D., Harel M., Chetrit M., He X., Jin G., Yu G., Tang X., Silman I., Bai D. & Sussman J. (2002). X-Ray Structures Of Torpedo Californica Acetylcholinesterase Complexed With (+)-Huperzine A And (-)-Huperzine B: Structural Evidence For An Active Site Rearrangement.  Biochemistry. 41:(35)10810-10818.  Abstract
  4. Koellner G., Steiner T., Millard C., Silman I. & Sussman J. (2002). A neutral molecule in a cation-binding site: Specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica.  Journal of Molecular Biology. 320:(4)721-725.  Abstract
  5. Bar-On P., Millard C., Harel M., Dvir H., Enz A., Sussman J. & Silman I. (2002). Kinetic And Structural Studies On The Interaction Of Cholinesterases With The Anti-Alzheimer Drug Rivastigmine.  Biochemistry. 41:(11)3555-3564.  Abstract
  6. Dvir H., Wong D., Harel M., Barril X., Orozco M., Luque F., Munoz-Torrero D., Camps P., Rosenberry T., Silman I. & Sussman J. (2002). 3D Structure Of Torpedo Californica Acetylcholinesterase Complexed With Huprine X At 2.1 Angstrom Resolution: Kinetic And Molecular Dynamic Correlates.  Biochemistry. 41:(9)2970-2981.  Abstract
  7. Liu T., Gu J., Tan X., Zhu W., Luo X., Jiang H., Ji R., Chen K., Silman I. & Sussman J. (2002). The relationship between binding models of TMA with furan and imidazole and the molecular electrostatic potentials: DFT and MP2 computational studies.  Journal of Physical Chemistry A. 106:(1)157-164.  Abstract

2001

  1. Tan X., Zhu W., Cui M., Luo X., Gu J., Silman I., Sussman J., Jiang H., Ji R. & Chen K. (2001). Noncovalent interaction or chemical bonding between alkaline earth cations and benzene? A quantum chemistry study using MP2 and density-functional theory methods.  Chemical Physics Letters. 349:(2-Jan)113-122.  Abstract
  2. Weik M., Ravelli R., Silman I., Sussman J., Gros P. & Kroon J. (2001). Specific Protein Dynamics Near The Solvent Glass Transition Assayed By Radiation-Induced Structural Changes.  Protein Science. 10:(10)1953-1961.  Abstract
  3. Harel M., Kasher R., Nicolas A., Guss J., Balass M., Fridkin M., Smit A., Brejc K., Sixma T., Katchalski-Katzir E., Sussman J. & Fuchs S. (2001). The Binding Site Of Acetylcholine Receptor As Visualized In The X-Ray Structure Of A Complex Between Alpha-Bungarotoxin And A Mimotope Peptide.  Neuron. 32:(2)265-275.  Abstract
  4. Doucet-Personeni C., Bentley P., Fletcher R., Kinkaid A., Kryger G., Pirard B., Taylor A., Taylor R., Taylor J., Viner R., Silman I., Sussman J., Greenblatt H. & Lewis T. (2001). A Structure-Based Design Approach To The Development Of Novel, Reversible Ache Inhibitors.  Journal of Medicinal Chemistry. 44:(20)3203-3215.  Abstract
  5. Nicolas A., Ferron F., Toker L., Sussman J. & Silman I. (2001). Histochemical Method For Characterization Of Enzyme Crystals: Application To Crystals Of Torpedo Californica Acetylcholinesterase.  Acta Crystallographica Section D-Biological Crystallography. 57:1348-1350.  Abstract
  6. Liu T., Gu J., Tan X., Zhu W., Luo X., Jiang H., Ji R., Chen K., Silman I. & Sussman J. (2001). Theoretical insight into the interactions of TMA-benzene and TMA-pyrrole with B3LYP density-functional theory (DFT) and ab initio second order Moller-Plesset perturbation theory (MP2) calculations.  Journal of Physical Chemistry A. 105:(22)5431-5437.  Abstract
  7. Weik M., Kryger G., Schreurs A., Bouma B., Silman I., Sussman J., Gros P. & Kroon J. (2001). Solvent Behaviour In Flash-Cooled Protein Crystals At Cryogenic Temperatures.  Acta Crystallographica Section D-Biological Crystallography. 57:566-573.  Abstract
  8. Felder C., Jiang H., Zhu W., Chen K., Silman I., Botti S. & Sussman J. (2001). Quantum/classical mechanical comparison of cation-pi interactions between tetramethylammonium and benzene.  Journal of Physical Chemistry A. 105:(8)1326-1333.  Abstract
  9. Sussman, J. L., Lin, D., Jiang, J., Manning, N. O., Prilusky, J. & Abola, E. E. (2001). The Protein Data Bank at Brookhaven .  International Tables for Crystallography. Vol. F:649-656.

2000

  1. Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A., Kronman C., Barak D., Ariel N., Shafferman A., Silman I. & Sussman J. (2000). Structures Of Recombinant Native And E202Q Mutant Human Acetylcholinesterase Complexed With The Snake-Venom Toxin Fasciculin-Ii.  Acta Crystallographica Section D-Biological Crystallography. 56:1385-1394.  Abstract
  2. Zhu W., Tan X., Puah C., Gu J., Jiang H., Chen K., Felder C., Silman I. & Sussman J. (2000). How does ammonium interact with aromatic groups? A density functional theory (DFT/B3LYP) investigation.  Journal of Physical Chemistry A. 104:(42)9573-9580.  Abstract
  3. Lin D., Manning N., Jiang J., Abola E., Stampf D., Prilusky J. & Sussman J. (2000). Autodep: A Web-Based System For Deposition And Validation Of Macromolecular Structural Information.  Acta Crystallographica Section D-Biological Crystallography. 56:828-841.  Abstract
  4. Greenblatt H., Silman I. & Sussman J. (2000). Structural studies on vertebrate and invertebrate acetylcholinesterases and their complexes with functional ligands.  Drug Development Research. 50:(4-Mar)573-583.  Abstract
  5. Kraut D., Goff H., Pai R., Hosea N., Silman I., Sussman J., Taylor P. & Voet J. (2000). Inactivation studies of acetylcholinesterase with phenylmethylsulfonyl fluoride.  Molecular Pharmacology. 57:(6)1243-1248.  Abstract
  6. Harel M., Kryger G., Rosenberry T., Mallender W., Lewis T., Fletcher R., Guss J., Silman I. & Sussman J. (2000). Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors.  Protein Science. 9:(6)1063-1072.  Abstract
  7. Koellner G., Kryger G., Millard C., Silman I., Sussman J. & Steiner T. (2000). Active-Site Gorge And Buried Water Molecules In Crystal Structures Of Acetylcholinesterase From Torpedo Californica.  Journal of Molecular Biology. 296:(2)713-735.  Abstract
  8. Weik M., Ravelli R., Kryger G., Mcsweeney S., Raves M., Harel M., Gros P., Silman I., Kroon J. & Sussman J. (2000). Specific Chemical And Structural Damage To Proteins Produced By Synchrotron Radiation.  Proceedings of the National Academy of Sciences of the United States of America. 97:(2)623-628.  Abstract

1999

  1. Greenblatt H., Kryger G., Lewis T., Silman I. & Sussman J. (1999). Structure Of Acetylcholinesterase Complexed With (-)-Galanthamine At 2.3 Angstrom Resolution.  FEBS Letters. 463:(3)321-326.  Abstract
  2. Botti S., Felder C., Lifson S., Sussman J. & Silman I. (1999). A Modular Treatment Of Molecular Traffic Through The Active Site Of Cholinesterase.  Biophysical Journal. 77:(5)2430-2450.  Abstract
  3. Millard C., Koellner G., Ordentlich A., Shafferman A., Silman I. & Sussman J. (1999). Reaction products of acetylcholinesterase and VX reveal a mobile histidine in the catalytic triad.  Journal of the American Chemical Society. 121:(42)9883-9884.
  4. Sussman J., Abola E., Lin D., Jiang J. H., Manning N. & Prilusky J. (1999). The Protein Data Bank - Bridging The Gap Between The Sequence And 3D Structure World.  Genetica. 106:(1-2)149-158.  Abstract
  5. Millard C., Kryger G., Ordentlich A., Greenblatt H., Harel M., Raves M., Segall Y., Barak D., Shafferman A., Silman I. & Sussman J. (1999). Crystal Structures Of Aged Phosphonylated Acetylcholinesterase: Nerve Agent Reaction Products At The Atomic Level.  Biochemistry. 38:(22)7032-7039.  Abstract
  6. Morel N., Bon S., Greenblatt H., Van Belle B. D., Wodak S., Sussman J., Massoulie J. & Silman I. (1999). Effect of mutations within the peripheral anionic site on the stability of acetylcholinesterase.  Molecular Pharmacology. 55:(6)982-992.  Abstract
  7. Silman I., Millard C., Ordentlich A., Greenblatt H., Harel M., Barak D., Shafferman A. & Sussman J. (1999). A Preliminary Comparison Of Structural Models For Catalytic Intermediates Of Acetylcholinesterase.  Chemico-Biological Interactions. 119:43-52.  Abstract
  8. Kryger G., Silman I. & Sussman J. (1999). Structure Of Acetylcholinesterase Complexed With E2020 (Aricept (R)): Implications For The Design Of New Anti-Alzheimer Drugs.  Structure with Folding & design. 7:(3)297-307.  Abstract
  9. Jiang J., Abola E. & Sussman J. (1999). Deposition Of Structure Factors At The Protein Data Bank.  Acta Crystallographica Section D-Biological Crystallography. 55:4-4.

1998

  1. Sussman J. (1998). Protein data bank deposits.  Science. 282:(5396)1993-1993.
  2. Ravelli R., Raves M., Ren Z., Bourgeois D., Roth M., Kroon J., Silman I. & Sussman J. (1998). Static Laue Diffraction Studies On Acetylcholinesterase.  Acta Crystallographica Section D-Biological Crystallography. 54:1359-1366.  Abstract
  3. Sussman J., Lin D., Jiang J., Manning N., Prilusky J., Ritter O. & Abola E. (1998). Protein Data Bank (Pdb): Database Of Three-Dimensional Structural Information Of Biological Macromolecules.  Acta Crystallographica Section D-Biological Crystallography. 54:1078-1084.  Abstract
  4. Kryger G., Silman I. & Sussman J. (1998). Three-Dimensional Structure Of A Complex Of E2020 With Acetylcholinesterase From Torpedo Californica.  Journal Of Physiology-Paris. 92:(3-4)191-194.  Abstract
  5. Botti S., Felder C., Sussman J. & Silman I. (1998). Electrotactins: A Class Of Adhesion Proteins With Conserved Electrostatic And Structural Motifs.  Protein Engineering, Design and Selection. 11:(6)415-420.  Abstract
  6. Sussman J. & Barton G. (1998). Re: Letter To The Editor Regarding Deposition Of 3D Structural Studies Of Biological Macromolecules.  Biochemical and Biophysical Research Communications. 245:(3)946-946.
  7. Wlodawer A., Davies D., Petsko G., Rossmann M., Olson A. & Sussman J. (1998). Immediate release of crystallographic data: A proposal.  Science. 279:(5349)306-307.
  8. Raves M., Giles K., Schrag J., Schmid M., Phillips G., Chiu W., Howard N., Silman I. & Sussman J. (1998). Quaternary structure of tetrameric acetylcholinesterase.  Structure And Function Of Cholinesterases And Related Proteins. 351-+.  Abstract
  9. Kryger G., Giles K., Harel M., Toker L., Velan B., Lazar A., Kronman C., Barak D., Ariel N., Shafferman A., Silman I. & Sussman J. (1998). 3D structure at 2.7A resolution of native and E202Q mutant human acetylcholinesterase complexed with fasciculin-II.  Structure And Function Of Cholinesterases And Related Proteins. 323-326.  Abstract
  10. Silman I., Harel M., Raves M. & Sussman J. (1998). Crystallographic studies on complexes of acetylcholinesterase with the natural cholinesterase inhibitors fasciculin and huperzine A.  Progress In Alzheimer'S And Parkinson'S Diseases. 49:523-530.  Abstract

1997

  1. Felder C., Botti S., Lifson S., Silman I. & Sussman J. (1997). External And Internal Electrostatic Potentials Of Cholinesterase Models.  JOURNAL OF MOLECULAR GRAPHICS & MODELLING. 15:(5)318-+.  Abstract
  2. Sussman J. (1997). Bridging The Gap.  Nature Structural and Molecular Biology. 4:(7)517-517.
  3. Raves M., Harel M., Pang Y., Silman I., Kozikowski A. & Sussman J. (1997). Structure Of Acetylcholinesterase Complexed With The Nootropic Alkaloid, (-)-Huperzine A.  Nature Structural and Molecular Biology. 4:(1)57-63.  Abstract
  4. Giles K., Raves M., Silman I. & Sussman J. (1997). How three-fingered snake toxins recognise their targets - Acetylcholinesterase-fasciculin complex, a case study.  Theoretical And Computational Methods In Genome Research. 303-315.  Abstract
  5. Abola E., Sussman J., Prilusky J. & Manning N. (1997). Protein Data Bank Archives Of Three-Dimensional Macromolecular Structures.  MACROMOLECULAR CRYSTALLOGRAPHY, PT B. 277:556-571.

1996

  1. Peng L., Silman I., Sussman J. & Goeldner M. (1996). Biochemical evaluation of photolabile precursors of choline and of carbamylcholine for potential time-resolved crystallographic studies on cholinesterases.  Biochemistry. 35:(33)10854-10861.  Abstract
  2. Baker E., Blundell T., Vijayan M., Dodson E., Dodson G., Gilliland G. & Sussman J. (1996). Archival journal requirements for data deposition.  Biophysical Journal. 70:(6)2994-2994.
  3. Abola E., Manning N., Prilusky J., Stampf D. & Sussman J. (1996). The Protein Data Bank: Current Status And Future Challenges.  Journal of Research of the National Institute of Standards and Technology. 101:(3)231-241.  Abstract
  4. Baker E., Blundell T., Vijayan M., Dodson E., Dodson G., Gilliland G. & Sussman J. (1996). Deposition Of Macromolecular Data.  Acta Crystallographica Section D-Biological Crystallography. 52:609-609.
  5. Faerman C., Ripoll D., Bon S., Lefeuvre Y., Morel N., Massoulie J., Sussman J. & Silman I. (1996). Site-Directed Mutants Designed To Test Back-Door Hypotheses Of Acetylcholinesterase Function.  FEBS Letters. 386:(1)65-71.  Abstract
  6. Frolow F., Harel M., Sussman J., Mevarech M. & Shoham M. (1996). Insights Into Protein Adaptation To A Saturated Salt Environment From The Crystal Structure Of A Halophilic 2Fe-2S Ferredoxin.  Nature Structural and Molecular Biology. 3:(5)452-458.  Abstract
  7. Marchot P., Ravelli R., Raves M., Bourne Y., Vellom D., Kanter J., Camp S., Sussman J. & Taylor P. (1996). Soluble monomeric acetylcholinesterase from mouse: Expression, purification, and crystallization in complex with fasciculin.  Protein Science. 5:(4)672-679.  Abstract
  8. Porschke D., Creminon C., Cousin X., Bon C., Sussman J. & Silman I. (1996). Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase.  Biophysical Journal. 70:(4)1603-1608.  Abstract
  9. Baker E., Blundell T., Vijayan M., Dodson E., Dodson G., Gilliland G. & Sussman J. (1996). Untitled letter to the editor.  Biopolymers. 38:(4)437-438.
  10. Harel M., Quinn D., Nair H., Silman I. & Sussman J. (1996). The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase.  Journal of the American Chemical Society. 118:(10)2340-2346.  Abstract
  11. Baker E., Bluntell T., Vijayan M., Dodson E., Dodson G., Gilliland G. & Sussman J. (1996). Publication of macromolecular crystal structures.  FEBS Letters. 380:(3)302-302.
  12. Baker E., Blundell T., Dodson E., Dodson G., Gilliland G., Sussman J. & Vijayan M. (1996). Diffraction Data Deposition.  Structure with Folding & design. 4:(2)217-217.
  13. Baker E., Blundell T., Vijayan M., Dodson E., Dodson G., Gilliland G. & Sussman J. (1996). Untitled.  Biochemical and Biophysical Research Communications. 219:(3)976-977.
  14. Wlodek S., Antosiewicz J., Mccammon J., Straatsma T., Gilson M., Briggs J., Humblet C. & Sussman J. (1996). Binding Of Tacrine And 6-Chlorotacrine By Acetylcholinesterase.  Biopolymers. 38:(1)109-117.  Abstract
  15. Baker E., Blundell T., Vijayan M., Dodson E., Dodson G., Gilliland G. & Sussman J. (1996). Crystallographic Data Deposition.  Nature. 379:(6562)202-202.

1995

  1. Sussman J. & Berman H. (1995). New Guidelines For Deposition Of Nucleic Acid Structures.  Structure with Folding & design. 3:(12)1426-1426.
  2. Harel M., Kleywegt G., Ravelli R., Silman I. & Sussman J. (1995). Crystal Structure Of An Acetylcholinesterase-Fasciculin Complex: Interaction Of A Three-Fingered Toxin From Snake Venom With Its Target.  Structure with Folding & design. 3:(12)1355-1366.  Abstract
  3. Alon R., Mirny L., Sussman J. & Gutnick D. (1995). Detection Of Alpha/Beta-Hydrolase Fold In The Cell-Surface Esterases Of Acinetobacter Species Using An Analysis Of 3D Profiles.  FEBS Letters. 371:(3)231-235.  Abstract
  4. Stampf D., Felder C. & Sussman J. (1995). PDBBROWSE - A GRAPHICS INTERFACE TO THE BROOKHAVEN PROTEIN DATA-BANK.  Nature. 374:(6522)572-574.
  5. Dym O., Mevarech M. & Sussman J. (1995). Structural Features That Stabilize Halophilic Malate-Dehydrogenase From An Archaebacterium.  Science. 267:(5202)1344-1346.  Abstract
  6. Peitsch M., Wells T., Stampf D. & Sussman J. (1995). The Swiss-3Dimage Collection And Pdb-Browser On The Worldwide Web.  Trends in Biochemical Sciences. 20:(2)82-84.
  7. Sussman J., Harel M., Raves M., Quinn D. & Silman I. (1995). 3-D structure of acetylcholinesterase and its complexes with anticholinesterase agents.  Modelling Of Biomolecular Structures And Mechanisms. 27:455-460.  Abstract
  8. Sussman J., Harel M., Raves M., Quinn D., Nair H. & Silman I. (1995). Structures of complexes of acetylcholinesterase with covalently and non-covalently bound inhibitors.  Enzymes Of The Cholinesterase Family. 59-65.  Abstract
  9. Silman I., Kreimer D., Shin I., Dolginova E., Roth E., Goldfarb D., Szosenfogel R., Raves M., Sussman J., Borochov N. & Weiner L. (1995). Studies on partially unfolded states of Torpedo californica acetylcholinesterase.  Enzymes Of The Cholinesterase Family. 77-82.  Abstract

1994

  1. Kreimer D., Dolginova E., Raves M., Sussman J., Silman I. & Weiner L. (1994). A Metastable State Of Torpedo-Californica Acetylcholinesterase Generated By Modification With Organomercurials.  Biochemistry. 33:(48)14407-14418.  Abstract
  2. Silman I., Harel M., Axelsen P., Raves M. & Sussman J. (1994). 3-DIMENSIONAL STRUCTURES OF ACETYLCHOLINESTERASE AND OF ITS COMPLEXES WITH ANTICHOLINESTERASE AGENTS.  Biochemical Society Transactions. 22:(3)745-749.  Abstract
  3. Gilson M., Straatsma T., Mccammon J., Ripoll D., Faerman C., Axelsen P., Silman I. & Sussman J. (1994). Open Back Door In A Molecular-Dynamics Simulation Of Acetylcholinesterase.  Science. 263:(5151)1276-1278.  Abstract
  4. Axelsen P., Harel M., Silman I. & Sussman J. (1994). STRUCTURE AND DYNAMICS OF THE ACTIVE-SITE GORGE OF ACETYLCHOLINESTERASE - SYNERGISTIC USE OF MOLECULAR-DYNAMICS SIMULATION AND X-RAY CRYSTALLOGRAPHY.  Protein Science. 3:(2)188-197.  Abstract
  5. Eichler J., Anselmet A., Sussman J., Massoulie J. & Silman I. (1994). DIFFERENTIAL-EFFECTS OF PERIPHERAL SITE LIGANDS ON TORPEDO AND CHICKEN ACETYLCHOLINESTERASE.  Molecular Pharmacology. 45:(2)335-340.  Abstract
  6. Elber R. & Sussman J. (1994). STRUCTURE AND DYNAMICS OF PROTEINS - FOREWORD.  Israel Journal of Chemistry. 34:(2)149-149.

1993

  1. Harel M., Schalk I., Ehretsabatier L., Bouet F., Goeldner M., Hirth C., Axelsen P., Silman I. & Sussman J. (1993). Quaternary Ligand-Binding To Aromatic Residues In The Active-Site Gorge Of Acetylcholinesterase.  Proceedings of the National Academy of Sciences of the United States of America. 90:(19)9031-9035.  Abstract
  2. Bayer E., Livnah O., Sussman J. & Wilchek M. (1993). THE CRYPTIC SUGAR RESIDUE OF DEGLYCOSYLATED AVIDIN.  Glycoconjugate Journal. 10:(4)276-277.  Abstract
  3. Livnah O., Bayer E., Wilchek M. & Sussman J. (1993). The Structure Of The Complex Between Avidin And The Dye, 2-(4'-Hydroxyazobenzene) Benzoic-Acid (Haba).  FEBS Letters. 328:(1-2)165-168.  Abstract
  4. Unger R. & Sussman J. (1993). The Importance Of Short Structural Motifs In Protein-Structure Analysis.  Journal of Computer-Aided Molecular Design. 7:(4)457-472.  Abstract
  5. Joshuator L. & Sussman J. (1993). THE COMING OF AGE OF DNA CRYSTALLOGRAPHY.  Current Opinion in Structural Biology. 3:(3)323-335.  Abstract
  6. Livnah O., Bayer E., Wilchek M. & Sussman J. (1993). 3-Dimensional Structures Of Avidin And The Avidin-Biotin Complex.  Proceedings of the National Academy of Sciences of the United States of America. 90:(11)5076-5080.  Abstract
  7. Sussman J., Harel M. & Silman I. (1993). 3-Dimensional Structure Of Acetylcholinesterase And Of Its Complexes With Anticholinesterase Drugs.  Chemico-Biological Interactions. 87:(1-3)187-197.  Abstract
  8. Ripoll D., Faerman C., Axelsen P., Silman I. & Sussman J. (1993). An Electrostatic Mechanism For Substrate Guidance Down The Aromatic Gorge Of Acetylcholinesterase.  Proceedings of the National Academy of Sciences of the United States of America. 90:(11)5128-5132.  Abstract
  9. Wagner U., Pattridge K., Ludwig M., Stallings W., Werber M., Oefner C., Frolow F. & Sussman J. (1993). COMPARISON OF THE CRYSTAL-STRUCTURES OF GENETICALLY ENGINEERED HUMAN MANGANESE SUPEROXIDE-DISMUTASE AND MANGANESE SUPEROXIDE-DISMUTASE FROM THERMUS-THERMOPHILUS - DIFFERENCES IN DIMER DIMER INTERACTION.  Protein Science. 2:(5)814-825.  Abstract
  10. Cygler M., Schrag J., Sussman J., Harel M., Silman I., Gentry M. & Doctor B. (1993). RELATIONSHIP BETWEEN SEQUENCE CONSERVATION AND 3-DIMENSIONAL STRUCTURE IN A LARGE FAMILY OF ESTERASES, LIPASES, AND RELATED PROTEINS.  Protein Science. 2:(3)366-382.  Abstract
  11. Reich Z., Friedman P., Scolnik Y., Sussman J. & Minsky A. (1993). On The Metastability Of Left-Handed Dna Motifs.  Biochemistry. 32:(8)2116-2119.  Abstract
  12. Tan R., Truong T., Mccammon J. & Sussman J. (1993). Acetylcholinesterase - Electrostatic Steering Increases The Rate Of Ligand-Binding.  Biochemistry. 32:(2)401-403.  Abstract
  13. Massoulie J., Sussman J., Bon S. & Silman I. (1993). STRUCTURE AND FUNCTIONS OF ACETYLCHOLINESTERASE AND BUTYRYLCHOLINESTERASE.  Progress in Brain Research. 98:139-146.

1992

  1. Harel M., Sussman J., Krejci E., Bon S., Chanal P., Massoulie J. & Silman I. (1992). Conversion Of Acetylcholinesterase To Butyrylcholinesterase - Modeling And Mutagenesis.  Proceedings of the National Academy of Sciences of the United States of America. 89:(22)10827-10831.  Abstract
  2. Berman H., Sussman J., Joshuator L., Revich G. & Ripley L. (1992). A STRUCTURAL MODEL FOR SEQUENCE-SPECIFIC PROFLAVIN-DNA INTERACTIONS DURING INVITRO FRAMESHIFT MUTAGENESIS.  Journal of biomolecular structure & dynamics. 10:(2)317-331.  Abstract
  3. Shafferman A., Kronman C., Flashner Y., Leitner M., Grosfeld H., Ordentlich A., Gozes Y., Cohen S., Ariel N., Barak D., Harel M., Silman I., Sussman J. & Velan B. (1992). MUTAGENESIS OF HUMAN ACETYLCHOLINESTERASE - IDENTIFICATION OF RESIDUES INVOLVED IN CATALYTIC ACTIVITY AND IN POLYPEPTIDE FOLDING.  Journal of Biological Chemistry. 267:(25)17640-17648.  Abstract
  4. Duval N., Bon S., Silman I., Sussman J. & Massoulie J. (1992). SITE-DIRECTED MUTAGENESIS OF ACTIVE-SITE-RELATED RESIDUES IN TORPEDO ACETYLCHOLINESTERASE - PRESENCE OF A GLUTAMIC-ACID IN THE CATALYTIC TRIAD.  FEBS Letters. 309:(3)421-423.  Abstract
  5. Joshuator L., Frolow F., Appella E., Hope H., Rabinovich D. & Sussman J. (1992). 3-Dimensional Structures Of Bulge-Containing Dna Fragments.  Journal of Molecular Biology. 225:(2)397-431.
  6. Ollis D., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S., Harel M., Remington S., Silman I., Schrag J., Sussman J., Verschueren K. & Goldman A. (1992). THE ALPHA/BETA-HYDROLASE FOLD.  Protein Engineering. 5:(3)197-211.  Abstract

1991

  1. Harel M., Su C., Frolow F., Ashani Y., Silman I. & Sussman J. (1991). Refined Crystal-Structures Of Aged And Non-Aged Organophosphoryl Conjugates Of Gamma-Chymotrypsin.  Journal of Molecular Biology. 221:(3)909-918.
  2. Sussman J., Harel M., Frolow F., Oefner C., Goldman A., Toker L. & Silman I. (1991). Atomic-Structure Of Acetylcholinesterase From Torpedo-Californica - A Prototypic Acetylcholine-Binding Protein.  Science. 253:(5022)872-879.  Abstract
  3. Harel M., Su C., Frolow F., Silman I. & Sussman J. (1991). Gamma-Chymotrypsin Is A Complex Of Alpha-Chymotrypsin With Its Own Autolysis Products.  Biochemistry. 30:(21)5217-5225.  Abstract

1990

  1. Livnah O. & Sussman J. (1990). CRYSTAL FORMS OF AVIDIN.  Methods in Enzymology. 184:90-93.
  2. Unger R., Harel D., Wherland S. & Sussman J. (1990). ANALYSIS OF DIHEDRAL ANGLES DISTRIBUTION - THE DOUBLETS DISTRIBUTION DETERMINES POLYPEPTIDES CONFORMATIONS.  Biopolymers. 30:(6-May)499-508.

1989

  1. Wagner U., Werber M., Beck Y., Hartman J., Frolow F. & Sussman J. (1989). Characterization Of Crystals Of Genetically Engineered Human Manganese Superoxide-Dismutase.  Journal of Molecular Biology. 206:(4)787-788.
  2. Unger R., Harel D., Wherland S. & Sussman J. (1989). A 3D Building-Blocks Approach To Analyzing And Predicting Structure Of Proteins.  Proteins-Structure Function And Bioinformatics. 5:(4)355-373.
  3. Hope, H., Frolow, F., Sussman, J.L. (1989). Macromolecular X-ray data collection on a rotating anode diffractometer.  The RIgaku Journal (Japanese). 20:(1)20-27.

1988

  1. Sussman J., Harel M., Frolow F., Varon L., Toker L., Futerman A. H. & Silman I. (1988). Purification And Crystallization Of A Dimeric Form Of Acetylcholinesterase From Torpedo-Californica Subsequent To Solubilization With Phosphatidylinositol-Specific Phospholipase-C.  Journal of Molecular Biology. 203:(3)821-822.
  2. Joshuator L., Rabinovich D., Hope H., Frolow F., Appella E. & Sussman J. (1988). The 3-Dimensional Structure Of A Dna Duplex Containing Looped-Out Bases.  Nature. 334:(6177)82-84.
  3. Miller M., Harrison R., Wlodawer A., Appella E. & Sussman J. (1988). Crystal-Structure Of 15-Mer Dna Duplex Containing Unpaired Bases.  Nature. 334:(6177)85-86.
  4. Harel M., Shoham M., Frolow F., Eisenberg H., Mevarech M., Yonath A. & Sussman J. (1988). Crystallization Of Halophilic Malate-Dehydrogenase From Halobacterium-Marismortui.  Journal of Molecular Biology. 200:(3)609-610.
  5. Hirshberg M., Sharon R. & Sussman J. (1988). A KINKED MODEL FOR THE SOLUTION STRUCTURE OF DNA TRIDECAMERS WITH INSERTED ADENOSINES - ENERGY MINIMIZATION AND MOLECULAR-DYNAMICS.  Journal of biomolecular structure & dynamics. 5:(5)965-&.
  6. Sussman, J.L., Joshua-Tor, L., Hirschberg, M., Saper, M.A., Frolow, F., Hope, H., Appella, E. (1988). A kinked model of a DNA tridecamer with an unpaired adenosine: energy minimization and X-ray structural studies.  in ''Molecular Structure: Chemical Reactivity and Biological Activity". 195-200.

1987

  1. Abadzapatero C., Griffith J., Sussman J. & Rossmann M. (1987). Refined Crystal-Structure Of Dogfish M4 Apo-Lactate Dehydrogenase.  Journal of Molecular Biology. 198:(3)445-467.
  2. Holland D., Zilberstein A., Zamir A. & Sussman J. (1987). A QUANTITATIVE APPROACH TO SEQUENCE COMPARISONS OF NITROGENASE MOFE PROTEIN ALPHA-SUBUNITS AND BETA-SUBUNITS INCLUDING THE NEWLY SEQUENCED NIFK-GENE FROM KLEBSIELLA-PNEUMONIAE.  Biochemical Journal. 247:(2)277-285.
  3. Miller M., Wlodawer A., Appella E. & Sussman J. (1987). Crystallization Of A Dna Duplex 15-Mer Containing Unpaired Bases - D(Cgcgaaatttacgcg).  Journal of Molecular Biology. 195:(4)967-968.
  4. Miller M., Kirchhoff W., Schwarz F., Appella E., Chiu Y., Cohen J. & Sussman J. (1987). Conformational Transitions Of Synthetic Dna-Sequences With Inserted Bases, Related To The Dodecamer D(Cgcgaattcgcg).  Nucleic Acids Research. 15:(9)3877-3890.
  5. Hope, H, Frolow, F., Sussman, J.L (1987). Macromolecular X-ray data collection on a rotating anode diffractometer.  The Rigaku Journal. 4:(1/2)3-10.

1986

  1. Unger R., Harel D. & Sussman J. (1986). DNAMAT - AN EFFICIENT GRAPHIC MATRIX SEQUENCE HOMOLOGY ALGORITHM AND ITS APPLICATION TO STRUCTURAL-ANALYSIS.  Bioinformatics. 2:(4)283-289.
  2. Roy S., Weinstein S., Borah B., Nickol J., Appella E., Sussman J., Miller M., Shindo H. & Cohen J. (1986). Mechanism Of Oligonucleotide Loop Formation In Solution.  Biochemistry. 25:(23)7417-7423.
  3. Werber M., Sussman J. & Eisenberg H. (1986). MOLECULAR-BASIS FOR THE SPECIAL PROPERTIES OF PROTEINS AND ENZYMES FROM HALOBACTERIUM-MARISMORTUI.  FEMS Microbiology Letters. 39:(2-Jan)129-135.
  4. Yagil G. & Sussman J. (1986). STRUCTURAL MODELS FOR NON-HELICAL DNA.  EMBO Journal. 5:(7)1719-1725.
  5. Harel D., Unger R. & Sussman J. (1986). BEAUTY IS IN THE GENES OF THE BEHOLDER.  Trends in Biochemical Sciences. 11:(4)155-156.
  6. Saper M., Eldar H., Mizuuchi K., Nickol J., Appella E. & Sussman J. (1986). Crystallization Of A Dna Tridecamer D(C-G-C-A-G-A-A-T-T-C-G-C-G).  Journal of Molecular Biology. 188:(1)111-113.

1985

  1. Sussman J. (1985). CONSTRAINED RESTRAINED LEAST-SQUARES (CORELS) REFINEMENT OF PROTEINS AND NUCLEIC-ACIDS.  Methods in Enzymology. 115:271-303.
  2. Murata M., Richardson J. & Sussman J. (1985). Simultaneous Comparison Of 3 Protein Sequences.  Proceedings of the National Academy of Sciences of the United States of America. 82:(10)3073-3077.

1983

  1. Bandel G. & Sussman J. (1983). PLORTEP - A COMPUTER-PROGRAM TO TRANSLATE PLUTO INSTRUCTIONS INTO THOSE OF ORTEP.  Journal of Applied Crystallography. 16:(DEC)650-651.
  2. Herzberg O. & Sussman J. (1983). PROTEIN MODEL-BUILDING BY THE USE OF A CONSTRAINED-RESTRAINED LEAST-SQUARES PROCEDURE.  Journal of Applied Crystallography. 16:(FEB)144-150.
  3. Sussman J. & Podjarny A. (1983). THE USE OF A CONSTRAINED RESTRAINED LEAST-SQUARES PROCEDURE FOR THE LOW-RESOLUTION REFINEMENT OF A MACROMOLECULE, YEAST TRANSFER RNAMET.  Acta Crystallographica Section B-Structural Science. 39:(AUG)495-505.

1982

  1. Olson W. & Sussman J. (1982). HOW FLEXIBLE IS THE FURANOSE RING .1. A COMPARISON OF EXPERIMENTAL AND THEORETICAL-STUDIES.  Journal of the American Chemical Society. 104:(1)270-278.
  2. Traub W. & Sussman J. (1982). Adenine-Guanine Base-Pairing In Ribosomal-Rna.  Nucleic Acids Research. 10:(8)2701-2708.

1981

  1. Holbrook S., Sussman J. & Kim S. (1981). ABSENCE OF CORRELATION BETWEEN BASE-PAIR SEQUENCE AND RNA CONFORMATION.  Science. 212:(4500)1275-1277.
  2. Wainhobson S., Nussinov R., Brown R. & Sussman J. (1981). Preferential Codon Usage In Genes.  Gene. 13:(4)355-364.

1980

  1. Nussinov R., Sussman J. & Trifonov E. (1980). Ms2 Rna Has A Potential To Form An Unusually Large Number Of Stable Hairpins.  Journal of Theoretical Biology. 85:(3)481-486.
  2. Trifonov E. & Sussman J. (1980). The Pitch Of Chromatin Dna Is Reflected In Its Nucleotide-Sequence.  Proceedings Of The National Academy Of Sciences Of The United States Of America-Biological Sciences. 77:(7)3816-3820.

1979

  1. Sussman J., Zipori P., Harel M., Yonath A. & Werber M. (1979). Preliminary-X-Ray Diffraction Studies On 2 Fe-Ferredoxin From Halobacterium Of The Dead Sea.  Journal of Molecular Biology. 134:(2)375-377.
  2. Shoham M., Yonath A., Sussman J., Moult J., Traub W. & Kalbgilboa A. (1979). Crystal-Structure Of Demetallized Concanavalin-A - Metal-Binding Region.  Journal of Molecular Biology. 131:(2)137-155.
  3. Trifonov, E., Sussman, J. L. (1979). Smooth bending of DNA in chromatin.  In M. Balaban (Ed.) Molecular mechanisms of biological recognition (Elsevier/North-Holland: Biomedical Press). 227-232 .

1978

  1. Sussman J. & Trifonov E. N. (1978). Possibility Of Nonkinked Packing Of Dna In Chromatin.  Proceedings of the National Academy of Sciences of the United States of America. 75:(1)103-107.
  2. Shoham M., Sussman J., Yonath A., Moult J., Traub W. & Kalbgilboa A. (1978). Effect Of Binding Of Metal-Ions On 3-Dimensional Structure Of De-Metallized Concanavalin-A.  FEBS Letters. 95:(1)54-56.
  3. Sussman J., Holbrook S., Warrant R., Church G. & Kim S. (1978). Crystal-Structure Of Yeast Phenylalanine Transfer-Rna .1. Crystallographic Refinement.  Journal of Molecular Biology. 123:(4)607-630.
  4. Holbrook S., Sussman J., Warrant R. & Kim S. (1978). Crystal-Structure Of Yeast Phenylalanine Transfer-Rna .2. Structural Features And Functional Implications.  Journal of Molecular Biology. 123:(4)631-660.

1977

  1. Sussman, J. L., Holbrook, S. R., Church, G. M., Kim, S.-H. (1977). A structure-factor least-squares refinement procedure for macromolecular structure using constrained and restrained parameters.  Acta Crystallographica Section A. A33:800-804.
  2. Kim, S. H. & Sussman, J. L. (1977). Transfer RNA: structure-function correlation.  In Quagliariello, (Ed.) Horizons in Biochemistry and Biophysics, (Addison-Wesley Publ. Co., Reading, MA). 159-199.
  3. Holbrook S. R., Sussman J., Warrant R. W., Church G. M. & Kim S. (1977). Rna-Ligand Interactions: (I) magnesium binding sites in yeast tRNA Phe.  Nucleic Acids Research. 4:(8)2811-2820.  Abstract
  4. Church G., Sussman J. & Kim S. (1977). Secondary Structural Complementarity Between Dna And Proteins.  Proceedings of the National Academy of Sciences of the United States of America. 74:(4)1458-1462.

1976

  1. Kim S. & Sussman J. (1976). Pi Turn Is A Conformational Pattern In Rna Loops And Bends.  Nature. 260:(5552)645-646.
  2. Sussman J. & Kim S. (1976). 3-Dimensional Structure Of A Transfer-Rna In 2 Crystal Forms.  Science. 192:(4242)853-858.
  3. Sussman, J. L. & Kim, S. H. (1976). A preliminary refinement of yeast tRNAPhe at 3Å resolution .  In ed. Pullman, B. (Ed.), Environmental Effects on Molecular Structure and Properties (D. Reidel Publishing Co., Dordrecht). 535-545 .
  4. Sussman J. & Kim S. (1976). Idealized Atomic Coordinates Of Yeast Phenylalanine Transfer-Rna.  Biochemical and Biophysical Research Communications. 68:(1)89-96.

1975

  1. Quigley G., Wang A., Seeman N., Suddath F., Rich A., Sussman J. & Kim S. (1975). Hydrogen-Bonding In Yeast Phenylalanine Transfer-Rna.  Proceedings of the National Academy of Sciences of the United States of America. 72:(12)4866-4870.
  2. Kim, S-H., Suddath, F. L., Quigley, G. J., Mcpherson, A., Sussman, J. L., Wang, A. H-J., Seeman, N.C., Rich, A. (1975). The tertiary structure of yeast phenylalanine transfer RNA.  In M. Sundaralingam, & S. T. Rao (Eds.), Structure and conformations of nucleic acids and protein-nucleic acid interactions. Baltimore: University Park Press. 7-23.
  3. Kim, S. H., Sussman, J. L., Church, G. M. (1975). A model for a recognition scheme between double stranded DNA and proteins.  In M. Sundaralingam, & S. T. Rao (Eds.),Structure and Conformation of Nucleic Acids and Protein-Nucleic Acid Interaction. (Baltimore: University Park Press. . 571-575.

1974

  1. Kim S., Sussman J., Suddath F., Quigley G., Mcpherson A., Wang A., Seeman N. & Rich A. (1974). General Structure Of Transfer-Rna Molecules.  Proceedings of the National Academy of Sciences of the United States of America. 71:(12)4970-4974.
  2. Kim S., Suddath F., Quigley G., Sussman J., Wang A., Seeman N. & Rich A. (1974). 3-Dimensional Tertiary Structure Of Yeast Phenylalanine Transfer-Rna.  Science. 185:(4149)435-440.

1973

  1. Sussman J., Barzilay I., Kerenzur M. & Lapidot Y. (1973). Correlation Of Differences In Conformation Between 2'-5' And 3'-5' Dinucleoside Monophosphates With Their Behavior On A Sephadex Lh-20 Column.  Biochimica Et Biophysica Acta. 308:(2)189-197.
  2. Sussman, J.L., Wodak, S.J. (1973). The crystal structure of fulvine: a pyrrolizidine alkaloid.  Acta Crystallographica Section B. B29:2918-2926.
  3. Barzilay I., Sussman J. & Lapidot Y. (1973). Further Studies On Chromatographic Behavior Of Dinucleoside Monophosphates.  Journal of Chromatography. 79:(MAY16)139-146.

1972

  1. Sussman J., Seeman N., Kim S. & Berman H. (1972). Crystal-Structure Of A Naturally Occurring Dinucleoside Phosphate - Uridylyl 3',5' Adenosine Phosphate Model For Rna Chain Folding.  Journal of Molecular Biology. 66:(3)403-+.

1971

  1. Seeman N., Sussman J., Berman H. & Kim S. (1971). Nucleic Acid Conformation - Crystal Structure Of A Naturally Occurring Dinucleoside Phosphate (Upa).  Nature-New Biology. 233:(37)90-+.