Sussman/Silman Group Publications

Sussman/Silman Group Publications

2013 2012 2011 2010 2009 2008 2007 2006 2005 2004 2003 2002 2001 2000 & Earlier

    2013

  1. Silman, I., Roth, E., Paz, A., Triquigneaux, M. M., Ehrenshaft, M., Xu, Y., Shnyrov, V. L., Sussman, J. L., Deterding, L. J., Ashani, Y., Mason, R. P. & Weiner, L.
    The specific interaction of the photosensitizer methylene blue with acetylcholinesterase provides a model system for studying the molecular consequences of photodynamic therapy
    Chem Biol Interact [ePub] (2013). [Abstract] [PDF]

  2. Ben-David, M., Wieczorek, G., Elias, M., Silman, I., Sussman, J. L. & Tawfik, D. S.
    Catalytic Metal Ion Rearrangements Underline Promiscuity and Evolvability of a Metalloenzyme
    JMB 425 1028-1038 (2013). [Abstract] [PDF]

    2012

  3. Paz, A., Roth, E., Ashani, Y., Xu, Y., Shnyrov, V.L., Sussman, J.L., Silman, I. & Weiner, L.
    Structural and functional characterization of the interaction of the photosensitizing probe methylene blue with Torpedo californica acetylcholinesterase
    Prot Sci 21 1138-1152 (2012). [Abstract] [PDF]

  4. Ben-David, M., Elias, M., Filippi, J.-J., Duņach, E., Silman, I., Sussman, J. L. & Tawfik, D. S.
    Catalytic versatility and backups in enzyme active sites: The case of serum paraoxonase 1
    J Mol Biol 40 181-196 (2012). [Abstract] [PDF] [Supplementary Material]

  5. Greenblatt, H.M., Otto, T.C., Cerasoli, D.M. & Sussman, J.L.
    Structure of Recombinant Human Carboxylesterase 1 Isolated from Whole Cabbage Looper Larvae
    Acta Cryst F Struct Biol Cryst Comm F68 269-272 (2012). [Abstract] [PDF]

  6. Goldsmith, M, Ashani, Y., Simo, Y., Ben-David, M., Leader, H., Silman, I., Sussman, J.L. & Tawfik, D.S.
    Evolved stereoselective hydrolases for broad-spectrum G-type nerve agent detoxification
    Chem & Biol 40 144 (2012). [Abstract] [PDF] [Supplementary Material]

  7. Acheampong, M. G., Dueno, D. E., Glover, B. K., Henry, A A., Mata, R., VanBrakle, M. L., Westblade, L. F., Sussman, J.L. & Granberry, A. L.
    Acetylcholinesterase: Substrate Traffic and Inhibition
    Biochem Mol Biol Educ 40 144 (2012). [Abstract] [PDF]

  8. Khare SD, Kipnis Y, Greisen PJ, Takeuchi R, Ashani Y, Goldsmith M, Song Y, Gallaher JL, Silman I, Leader H, Sussman JL, Stoddard BL, Tawfik DS, Baker D.
    Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis
    Nat Chem Biol 8 294-300 (2012). [Abstract] [PDF]

  9. Prilusky, J, Hodis, E. & Sussman J.L.
    Proteopedia: Exciting advances in the 3d encyclopedia of Biomolecular structure
    In Macromolecular Crystallography: Deciphering the Structure, Function and Dynamics of Biological Molecules (eds.Carrondo MA and Spadon P) 149-161 (Springer, Dordrecht, 2012). [Book] [PDF]

  10. Xu, Y., Li, M., Greenblatt, H.M., Chen, W., Paz, A., Dym, O., Peleg, Y., Chen, T., Shen, X., He, J., Jiang, H., Silman, I. & Sussman, J.L.
    Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations
    Acta Cryst D68 13-25 (2012). [Abstract] [PDF]

  11. Wood, K., Paz, A., Dijkstra, K., Scheek, R.M., Otten, R., Silman, I., Sussman, J.L. & Mulder, F.A.
    Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3
    Biomol NMR Assign 6, 15-18. (2012). [Abstract] [PDF]

    2011

  12. Ashani, Y., Goldsmith, M., Leader, H., Silman, I., Sussman, J.L. & Tawfik, D.S.
    In vitro detoxification of cyclosarin in human blood pre-incubated ex vivo with recombinant serum paraoxonases
    Toxicol Lett 206 24-28 (2011). [Abstract] [PDF]

  13. Offman, M.N., Krol, M., Rost, B., Silman, I., Sussman, J.L. & Futerman, A.H.
    Comparison of a molecular dynamics model with the X-ray structure of the N370S acid-β-glucosidase mutant that causes Gaucher disease
    PEDS 24, 773-775 (2011). [Abstract] [PDF]

  14. Suskiewicz, M.J., Sussman, J.L., Silman, I. & Shaul, Y.
    Context-dependent resistance to proteolysis of intrinsically disordered proteins
    Protein Sci 20, 1285-1297 (2011). [Abstract] [PDF]

  15. Sanson, B., Colletier, J.P., Xu, Y., Therese Lang, P., Jiang, H., Silman, I., Sussman, J.L. & Weik, M.
    Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and MD simulations
    Protein Sci 20, 1114-1118 (2011). [Abstract] [PDF]

  16. Perrakis, A., Daenke, S., Stuart, D.I. & Sussman, J.L.
    From SPINE to SPINE-2 complexes and beyond
    J Struct Biol 175, 105 (2011). [Abstract] [PDF]

  17. Prilusky, J., Hodis, E., Canner, D., Decatur, W.A., Oberholser, K., Martz, E., Berchanski, A., Harel, M., Sussman, J.L.
    Proteopedia: A status report on the collaborative, 3D web-encyclopedia of proteins and other biomolecules
    J Struct Biol 175, 244-252 (2011). [Abstract] [PDF]

  18. 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., Bussow, K., Adamson, R., Blagova, E., Walton, J., Cartwright, J.L., Bird, L.E., Owens, R.J., Berrow, N.S., Wilson, K.S., Sussman, J.L., Perrakis, A. & Celie, P.H.N.
    Expression of protein complexes using multiple Escherichia coli protein co-expression systems: A benchmarking study
    J Struct Biol 175, 159-170 (2011). [Abstract] [PDF]

  19. Brumshtein, B., Aguilar-Moncayo, M., Benito, J.M., Garcia Fernandez, J.M., Silman, I., Shaaltiel, Y., Aviezer, D., Sussman, J.L., Futerman, A.H. & Ortiz Mellet, C.
    Cyclodextrin-mediated crystallization of acid beta-glucosidase in complex with amphiphilic bicyclic nojirimycin analogues
    Org Biomol Chem 9, 4160-4167 (2011). [Abstract] [PDF]

  20. Li, M.-J., Greenblatt, H.M., Dym, O., Albeck, S., Pais, A., Gunanathan, C., Milstein, D., Degani, H. & Sussman, J.L.
    Structure of estradiol metal chelate and estrogen receptor complex: The basis for designing a new class of selective estrogen receptor modulators
    J Med Chem 54, 3575-3580 (2011). [Abstract] [PDF]

  21. Gupta, R.D., Goldsmith, M., Ashani, Y., Simo, Y., Mullokandov, G., Bar, H., Ben-David, M., Leader, H., Margalit, R., Silman, I., Sussman, J.L. Tawfik D.S.
    Directed evolution of hydrolases for prevention of G-type nerve agent intoxication
    Nat. Chem. Biol. 7, 120-125 (2011). [Abstract] [PDF]

    2010

  22. Xu, Y., Colletier, J.-P., Weik, M., Qin, G., Jiang, H., Silman, I. & Sussman, J.L.
    Long Route or Shortcut? A Molecular Dynamics Study of Traffic of Thiocholine within the Active-Site Gorge of Acetylcholinesterase
    Biophys J. 99, 4003-4011 (2010). [Abstract] [PDF]

  23. Albeck, S., Nordlund, P. & Sussman, J.L.
    New trends in protein expression
    J Struct Biol 172, 1-2 (2010). [Abstract] [PDF]

  24. Offman, M.N., Krol, M., Silman, I., Sussman, J.L. & Futerman, A.H.
    Molecular basis of reduced glucosylceramidase activity in the most common gaucher disease mutant N370S
    J. Biol. Chem. 285, 42105-42114 (2010). [Abstract] [PDF]

  25. Hodis, E., Prilusky, J. & Sussman, J.L.
    Proteopedia: A collaborative, virtual 3D web-resource for protein and biomolecule structure and function
    Biochem. Mol. Biol. Educ. 38, 341-342 (2010). [Abstract] [PDF]

  26. Albeck, S., Nordlund, P. & Sussman, J.L.
    New trends in protein expression
    J Struct Biol 172, 1-2 (2010). [Abstract] [PDF]

  27. Dvir, H., Silman, I., Harel, M., Rosenberry, T. L. & Sussman, J. L.
    Acetylcholinesterase: From 3D structure to function Chemico-Biological Interactions
    Chem Biol Interact 187, 10-22 (2010). [Abstract] [PDF]

  28. Ashani, Y., Gupta, R. D., Goldsmith, M., Silman, I., Sussman, J. L., Tawfik, D. S. & Leader, H.
    Stereo-specific synthesis of analogs of nerve agents and their utilization for selection and characterization of Paraoxonase (PON1) catalytic scavengers
    Chem Biol Interact 187, 362-369 (2010). [Abstract] [PDF]

  29. Brumshtein, B., Salinas, P., Peterson, B., Chan, V., Silman, I., Sussman, J.L., Savickas, P.J., Robinson, G.S. & Futerman, A.H.
    Characterization of Gene-activated Human Acid-β-Glucosidase: Crystal Structure, Glycan Composition and Internalization into Macrophages
    Glycobiology 20, 24-32 (2010). [Abstract] [PDF]

    2009

  30. Zeev-Ben-Mordehai, T., Mylonas, E., Paz, A., Peleg, Y., Toker, L., Silman, I., Svergun, D.I., Sussman, J.L.
    The quaternary structure of amalgam, a Drosophila neuronal adhesion protein, explains its dual adhesion properties
    Biophys J 97, 2316-2326 (2009). [Abstract] [PDF]

  31. Ben-David, M., Noivirt-Brik, O., Paz, A., Prilusky, J., Sussman, J.L. & Levy, Y.
    Assessment of CASP8 structure predictions for template free targets
    Proteins 77, 50-65 (2009). [Abstract] [PDF]

  32. Noivirt-Brik, O., Prilusky, J. & Sussman, J.L.
    Assessment of disorder predictions in CASP8
    Proteins 77, 210-216 (2009). [Abstract] [PDF]

  33. Sanson, B., Nachon, F., Colletier, J.-P., Froment, M.-T., Toker, L., Greenblatt, H., Sussman, J.L., Ashani, Y., Masson, P., Silman, I. & Weik, M.
    Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with Pralidoxime
    J Med Chem 52, 7593-7603 (2009). [Abstract] [PDF]

  34. Sharabi, O., Peleg, Y., Mashiach, E., Vardy, E., Ashani, Y., Silman, I., Sussman, J.L. & Shifman, J.M.
    Design, expression, and characterization of fasciculin mutants optimized for interactions with its target, acetylcholinesterase
    PEDS ePub (2009). [Abstract] [PDF]

  35. Khersonsky, O., Rosenblat, M., Toker, L., Yakobson, S., Hugenmatter, A., Silman, I., Sussman, J.L., Aviram, M. & Tawfik, D.S.
    Directed evolution of serum paraoxonase PON3 by family shuffling and ancestor/consensus mutagenesis, and its biochemical characterization
    Biochemistry 48, 6644-54 (2009). [Abstract] [PDF]

  36. Brumshtein, B., Aguilar-Moncayo, M., Garcia-Moreno, M.I., Ortiz Mellet, C., Garcia Fernandez, J.M., Silman, I., Shaaltiel, Y., Aviezer, D., Sussman, J.L. & Futerman, A.H.
    6-Amino-6-deoxy-5,6-di-N-(N'-octyliminomethylidene)nojirimycin: Synthesis, Biological Evaluation, and Crystal Structure in Complex with Acid β-Glucosidase
    ChemBioChem 10, 1480-5 (2009). [Abstract] [PDF]

  37. Sussman, J.L. & Silman I.
    Structural studies on acetylcholinesterase and paraoxonase directed towards development of therapeutic biomolecules for the treatment of degenerative diseases and protection against chemical threat agents
    In From Molecules to Medicines, Structure of Biological Macromolecules and Its Relevance in Combating New Diseases and Bioterrorism (eds. Sussman, J.L & Spadon, P.) 183-199 (Springer, Dordrecht, 2009). [Book] [PDF]

  38. Hodis, E., Prilusky, J. & Sussman, J.L.
    Tools to make 3D structural data more comprehensible: eMovie & Proteopedia
    In From Molecules to Medicines, Structure of Biological Macromolecules and Its Relevance in Combating New Diseases and Bioterrorism (eds. Sussman, J.L & Spadon, P.) 169-182 (Springer, Dordrecht, 2009). [Book] [PDF]

  39. Sussman, J.L & Spadon, P.
    Preface
    In From Molecules to Medicines, Structure of Biological Macromolecules and Its Relevance in Combating New Diseases and Bioterrorism (eds. Sussman, J.L & Spadon, P.) vii (Springer, Dordrecht, 2009). [Book] [PDF]

  40. Sussman, J.L & Spadon, P. (eds)
    From Molecules to Medicines, Structure of Biological Macromolecules and Its Relevance in Combating New Diseases and Bioterrorism (eds. Sussman, J.L & Spadon, P.) (Springer, Dordrecht, 2009). [Book] [Cover]

  41. Paz, A., Xie, Q., Greenblatt, H.M., Fu, W., Tang, Y., Silman, I., Qiu, Z. & Sussman, J.L.
    The Crystal Structure of a Complex of Acetylcholinesterase with a Bis-(-)-nor-meptazinol Derivative Reveals Disruption of the Catalytic Triad
    J Med Chem 52, 2543-9 (2009). [Abstract] [PDF]

  42. Hodis, E. & Sussman, J.L.
    An encyclopedic effort to make 3D structures easier to understand
    TIBS 34, 100-1 (2009). [Abstract] [PDF]

  43. Zeev-Ben-Mordehai, T., Paz, A., Peleg, Y., Toker, L., Wolf, S.G., Rydberg, E.H., Sussman, J.L. & Silman, I.
    Amalgam, an axon guidance Drosophila adhesion protein belonging to the immunoglobulin superfamily: over-expression, purification and biophysical characterization
    Protein Expr Purif 63, 147-57 (2009). [Abstract] [PDF]

    2008

  44. Dunker, A.K., Silman, I., Uversky, V.N. & Sussman, J.L.
    Function and structure of inherently disordered proteins
    Curr Opin Struct Biol 18, 756-764 (2008). [Abstract] [PDF]

  45. Hodis, E., Prilusky, J., Martz, E., Silman, I., Moult, J. & Sussman, J. L.
    Proteopedia - a scientific 'wiki' bridging the rift between 3D structure and function of biomacromolecules
    Genome Biology 9, R121 (2008). [Abstract] [PDF]

  46. Kacher, Y., Brumshtein, B., Boldin-Adamsky, S., Toker, L., Shainskaya, A., Silman, I., Sussman, J.L. & Futerman, A.H.
    Acid beta-glucosidase: insights from structural analysis and relevance to Gaucher disease therapy
    Biol. Chem. 389, 1361-9 (2008). [Abstract] [PDF]

  47. Brumshtein, B., Greenblatt, H.M., Futerman, A.H., Silman, I. & Sussman, J.L.
    Control of the rate of evaporation in protein crystallization by the 'microbatch under oil' method
    J Appl Cryst 41, 969-71 (2008). [Abstract] [PDF]

  48. Colletier, J.-P., Bourgeois, D., Sanson, B., Fournier, D., Sussman, J. L., Silman, I. & Weik, M.
    Shoot-and-Trap: Use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography
    Proc. Natl. Acad. Sci. USA 105, 11742-7 (2008). [Abstract] [PDF]

  49. Banci, L., Baumeister, W., Heinemann, U., Schneider, G., Silman, I. & Sussman, J.L.
    Structural Genomics and Structural Proteomics: A Global Perspective
    In Structural Proteomics and its impact on the Life Science (ed. Sussman, J.L. & Silman, I.), 505-537 (World Scientific Press Co., London, 2008). [Book] [PDF]

  50. Sussman, J.L. & Silman, I.
    Preface
    In Structural Proteomics and its impact on the Life Science (ed. Sussman, J.L. & Silman, I.), v-vii (World Scientific Press Co., London, 2008). [Book] [PDF]

  51. Sussman, J.L. & Silman, I.
    Structural Proteomics and its impact on the Life Sciences (ed. Sussman, J.L. & Silman, I.) (World Scientific Press Co., London, 2008). [Book] [Cover]

  52. Xu, Y., Colletier, J.P., Weik, M., Jiang, H., Moult, J., Silman, I., Sussman, J.L.
    Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray vs MD
    Biophys J. 95, 2500-11 (2008). [Abstract] [PDF] [Cover]

  53. Silman, I. & Sussman, J. L.
    Acetylcholinesterase: How is structure related to function?
    Chem Biol Interact 175, 3-10 (2008). [Abstract] [PDF]

  54. Harel, M., Sonoda, L.K., Silman, I., Sussman, J.L. & Rosenberry, T.L.
    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
    J. Am. Chem. Soc. 130, 7856-61 (2008). [Abstract] [PDF]

  55. 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.L. & Silman, I.
    Biophysical Characterization of the Unstructured Cytoplasmic Domain of the Human Neuronal Adhesion Protein Neuroligin 3
    Biophys J 95, 1928-44 (2008). [Abstract] [PDF]

  56. Meged, R., Dym, O. & Sussman, J.L.
    High-Throughput pH optimization of protein crystallization
    Methods Mol Biol 426, 411-8 (2008). [Abstract] [PDF]

  57. Manicka, S., Peleg, Y., Unger, T., Albeck, S., Dym, O., Greenblatt, H.M., Bourenkov, G., Lamzin, V., Krishnaswamy, S. & Sussman, J.L.
    Crystal structure of YagE, a putative DHDPS-like protein from Escherichia coli K12
    Proteins 71, 2102-8 (2008). [Abstract] [PDF]

  58. Xu, Y., Colletier, J.P., Jiang, H., Silman, I., Sussman, J.L. & Weik, M.
    Induced-fit or pre-existing equilibrium dynamics? Lessons from protein crystallography and MD simulations on acetylcholinesterase
    Protein Sci 17, 601-5 (2008). [Abstract] [PDF]

  59. Tompa, P., Prilusky, J., Silman, I. & Sussman, J.L.
    Structural disorder serves as a weak signal for intracellular protein degradation
    Proteins 71, 903-9 (2008). [Abstract] [PDF]

  60. Tsvetkov, P., Asher, G., Paz, A., Reuven, N., Sussman, J.L., Silman, I. & Shaul, Y.
    Operational definition of intrinsically unstructured protein sequences based on susceptibility to the 20S proteasome Proteins
    Proteins 70, 1357-66 (2008). [Abstract] [PDF]

  61. Gräslun, S., Nordlund, P., Weigelt, J., Bray, J., Gileadi, O., Knapp, S., Oppermann, U., Arrowsmith, C., Hui, R., Ming, J., dhe-Paganon, S., Park, H.W., Savchenko, A., Yee, A., Edwards, A., Vincentelli, R., Cambillau, C., Kim, R., Kim, S.H., Rao, Z., Shi, Y., Terwilliger, T.C., Kim, C.Y., Hung, L.W., Waldo, G.S., Peleg, Y., Albeck, S., Unger, T., Dym, O., Prilusky, J., Sussman, J.L., Stevens, R.C., Lesley, S.A., Wilson, I.A., Joachimiak, A., Collart, F., Dementieva, I., Donnelly, M.I., Eschenfeldt, W.H., Kim, Y., Stols, L., Wu, R., Zhou, M., Burley, S., Emtage, J.S., Sauder, J.M., Thompson, D., Bain, K., Luz, J., Gheyi, T., Zhang, F., Atwell, S., Almo, S.C., Bonanno, J.B., Fiser, A., Swaminathan, S., Studier, F.W., Chance, M.R., Sali, A., Acton, T.B., Xiao, R., Zhao, L., Ma, L.C., Hunt, J.F., Tong, L., Cunningham, K., Inouye, M., Anderson, S., Janjua, H., Shastry, R., Ho, C.K., Wang, D., Wang, H., Jiang, M., Montelione, G.T., Stuart, D.I., Owens, R.J., Daenke, S., Schütz, A., Heinemann, U., Yokoyama, S., Büssow, K. & Gunsalus, K.C.
    Protein production and purification
    Nat Methods 5, 135-146 (2008). [Abstract] [PDF]

    2007

  62. Read, R.J. & Sussman, J.L.
    Preface
    In Evolving Methods for Macromolecular Crystallography; The Structural Path to the Understanding of the Mechanism of Action of CBRN agents (eds. Read, R.J. & Sussman, J.L.) vii-viii (Springer, Dordrecht, 2007). [Book] [PDF]

  63. Read, R.J. & Sussman, J.L. (eds)
    Evolving Methods for Macromolecular Crystallography; The Structural Path to the Understanding of the Mechanism of Action of CBRN agents (eds. Read, R.J. & Sussman, J.L.) (Springer, Dordrecht, 2007). [Book] [Cover]

  64. Man, O., Sussman, J.L. & Pilpel, Y.
    Examination of the tRNA Adaptation Index as a Predictor of Protein Expression Levels
    In Systems Biology and Regulatory Genomics: Joint Annual RECOMB 2005 Satellite Workshops on Systems Biology and on Regulatory Genomics (eds. Eskin, E., Ideker, T., Raphael, B. & Workman, D.) 107-118 (San Diego, CA, USA, 2007). [Book] [PDF]

  65. Banci, L., Baumeister, W., Heinemann, U., Schneider, G., Silman, I., Stuart, D.I., and Sussman, J.L.
    An idea whose time has come
    Genome Biology 8, 408 (2007). [Abstract] [PDF]

  66. Colletier, J.P., Royant, A., Specht, A., Sanson, B., Nachon, F., Masson, P., Zaccai, G., Sussman, J.L., Goeldner, M., Silman, I., Bourgeois, D. & Weik, M.
    Use of 'Caged' analog to study traffic of choline within acetylcholinesterase by kinetic crystallography
    Acta Cryst D63, 1115-1128 (2007). [Abstract] [PDF] [Cover]

  67. Harel, M., Brumshtein, B., Meged, R., Dvir, H., Ravelli, R.B.G., McCarthy, A., Toker, L., Silman, I. & Sussman, J.L.
    3-D Structure of serum paraoxonase 1 sheds light on its activity, stability, solubility and crystallizability
    J Arch. Ind. Hyg. Toxicol. 58, 347-353 (2007). [Abstract] [PDF]

  68. Brumshtein, B., Greenblatt, H. M., Butters, T. D., Shaaltiel, Y., Aviezer, D., Silman, I., Futerman, A. H. & Sussman, J. L.
    Crystal structures of complexes of N-butyl- and N-nonyl-deoxynojirimycin bound to acid-β-glucosidase: Insights into the mechanism of chemical chaperone action in gaucher disease
    J. Biol. Chem. 282, 29052-29058 (2007). [Abstract] [PDF]

  69. Felder, C.E., Prilusky, J., Silman, I. & Sussman, J.L.
    A server and database for dipole moments of proteins
    Nucl. Acids Res 35, (Web Server issue) W512-521 (2007). [Abstract] [PDF]

  70. Shaaltiel, Y., Bartfeld, D., Hashmueli, S., Baum, G., Brill-Almon, E., Galili, G., Dym, O., Boldin-Adamsky, S. A., Silman, I., Sussman, J. L., Futerman A. H. & Aviezer, D.
    Production of glucocerebrosidase with terminal mannose glycans for enzyme replacement therapy of Gaucher's disease using a plant cell system
    Plant Biotechnol J. 5, 579-90 (2007). [Abstract] [PDF]

  71. Hodis, E., Schreiber, G., Rother, K. & Sussman, J.L.
    eMovie: a storyboard-based tool for making molecular movies
    Trends Biochem Sci. 32, 199-204 (2007). [Abstract] [PDF]

  72. Haviv, H., Wong, D.M., Silman, I. & Sussman, J.L.
    Bivalent Ligands Derived from Huperzine A as Acetylcholinesterase Inhibitors
    Curr. Top. Med. Chem. 7, 375-387 (2007). [Abstract ] [PDF]

  73. Yokoyama, S., Terwilliger, T.C., Kuramitsu, S., Moras, D. & Sussman, J.L.
    RIKEN aids international structural genomics efforts
    Nature 445, 21 (2007). [Abstract] [PDF]

  74. Banci, L., Baumeister, W., Enfedaque, J., Heinemann, U., Schneider, G., Silman, I. & Sussman, J.L.
    Structural proteomics: from the molecule to the system
    Nat. Struct. Mol. Biol. 14, 3-4 (2007). [Abstract] [PDF]

    2006

  75. Brumshtein, B., Wormald, M.R., Silman, I, Futerman, A.H. & Sussman, J.L.
    Structural comparison of differently glycosylated forms of acid-β-glucosidase, the defective enzyme in Gaucher disease
    Acta Cryst D62, 1458-1465 (2006). [Abstract] [PDF] [Cover]

  76. Premkumar, L., Silman, I., Sussman, J. L. & Futerman, A. H.
    The X-ray structure of human acid-β-glucosidase: implications for second-generation enzyme replacement therapy
    In Gaucher disease (eds. (Futerman, A. H. & Zimran, A.) 85-96 (CRC Press, Boca Raton, 2006). [Book]

  77. Peleg, Y., Albeck, A., Burstein, Y., Dym, O., Jacobovitch, Y., Levy, N., Meged, R., Michael, Y., Prilusky, J., Schreiber, G., Silman, I., Unger, T. & Sussman, J.L.
    Protein expression for structural studies
    Microb. Cell Fact. 5(Suppl 1), 1-2 (2006). [Abstract] [PDF]

  78. Esnouf, R.M., Hamer, R., Sussman, J.L., Silman, I., Trudgian, D., Yang, Z.R. & Prilusky, J.
    Honing the in silico toolkit for detecting protein disorder
    Acta Cryst D62, 1243-1250 (2006). [Abstract] [PDF] [Cover]

  79. Romier, C., Ben Jelloul, M., Albeck, S., Buchwald, G., Busso, D., Celie, P.H., Christodoulou, E., De Marco, V., van Gerwen, S., Knipscheer, P., Lebbink, J.H., Notenboom, V., Poterszman, A., Rochel, N., Cohen, S.X., Unger, T., Sussman, J.L., Moras, D., Sixma, T.K. & Perrakis, A.
    Co-expression of protein complexes in prokaryotic and eukaryotic hosts: experimental procedures, database tracking and case studies
    Acta Cryst D62, 1232-1242 (2006). [Abstract] [PDF] [Cover]

  80. Banci, L., Bertini, I., Cusack, S., de Jong, 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.L., Thierry, J.C. & Moras, D.
    First steps towards effective methods in exploiting high-throughput technologies for the determination of human protein structures of high biomedical value
    Acta Cryst D62, 1208-1217 (2006). [Abstract] [PDF] [Cover]

  81. 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, 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.L., Thierry, J.C., Thompson, J.D., Thornton, J.M., Unger, T., Vaughan, B., Vranken, W., Watson, J.D., Whamond, G. & Henrick, K.
    SPINE bioinformatics and data-management aspects of high-throughput structural biology
    Acta Cryst D62,1184-1195 (2006). [Abstract] [PDF] [Cover]

  82. Berry, I.M., Dym, O., Esnouf, R.M., Harlos, K., Meged, R., Perrakis, A., Sussman, J.L., Walter, T.S., Wilson, J. & Messerschmidt, A.
    SPINE high-throughput crystallization, crystal imaging and recognition techniques: current state, performance analysis, new technologies and future aspects
    Acta Cryst D62, 1137-1149. [Abstract] [PDF] [Cover]

  83. 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.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T. & Jones, E.Y.
    Eukaryotic expression: developments for structural proteomics
    Acta Cryst D62, 1114-1124. [Abstract] [PDF] [Cover]

  84. Rydberg, E. H., Brumshtein, B., Greenblatt, H. M., Wong, D. M., Shaya, D., Williams, L. D., Carlier, P. R., Pang, Y.-P., Silman, I. & Sussman, J. L.
    Complexes of alkylene-linked tacrine dimers with Torpedo californica acetylcholinesterase: Binding of bis(5)-tacrine produces a dramatic rearrangement in the active-site gorge
    J. Med. Chem. 49, 5491-5500 (2006). [Abstract] [PDF]

  85. Colletier, J.P., Fournier, D., Greenblatt, H.M., Stojan, J., Sussman, J.L., Zaccai, G., Silman, I. &, Weik, M.
    Structural insights into substrate traffic and inhibition in acetylcholinesterase
    EMBO J. 25, 2746-2756 (2006). [Abstract] [PDF]

  86. Sussman, J.L. & Silman, I.
    Shedding UV Light on the Phase Problem
    Structure 14, 629-630 (2006). [Abstract] [PDF]

  87. Srividhya, K.V., Rao, G.V., Raghavenderan, L., Mehta, P., Prilusky, J., Sankarna rayanan, M., Sussman, J.L. & Krishnaswamy, S.
    Database and comparative identification of prophages in ICIC 2006 LNCIS 344 (eds. Huang, D.-S., Li, K. & Irwin, G.W.), 863-868 (Spinger-Verlag, Berlin, Heid elberg) (2006). [Abstract] [PDF]

    2005

  88. Niu, C. Y., Xu, Y. C., Xu, Y., Luo, X. M., Duan, W. H., Silman, I., Sussman, J. L., Zhu, W. L., Chen, K. X., Shen, J. H. & Jiang, H. L.
    Dynamic mechanism of E2020 binding to acetylcholinesterase: A steered molecular dynamics simulation
    J. Phys. Chem. B 109, 23730-23738 (2005). [Abstract] [PDF]

  89. Harel, M., Hyatt, J.L., Brumshtein, B., Morton, C.L., Wadkins, R.M., Silman, I., Sussman, J.L. & Potter, P.M.
    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
    Chem. Biol. Interact. 157-158, 153-157 (2005). [Abstract] [PDF]

  90. Hyatt, J.L., Tsurkan, L., Morton, C.L., Yoon, K.J., Harel, M., Brumshtein, B., Silman, I., Sussman, J.L., Wadkins, R.M. & Potter, P.M.
    Inhibition of acetylcholinesterase by the anticancer prodrug CPT-11
    Chem. Biol. Interact. 157-158, 247-252 (2005). [Abstract ] [PDF]

  91. Newman, J., Egan, D., Walter, T.S., Meged, R., Berry, I., Ben Jelloul, M., Sussman, J.L., Stuart, D.I. & Perrakis, A.
    Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: the PACT/JCSG+ strategy
    Acta Cryst D61, 1426-1431 (2005). [Abstract] [PDF]

  92. 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.L.
    3D structure determination of proteins related to human health in their functional context at the Israel Structural Proteomics Center (ISPC)
    Acta Crystal D61, 1364-1372 (2005). [Abstract] [PDF]

  93. Haviv, H., Wong, D.M., Greenblatt, H.M., Carlier, P.R., Pang, Y.P., Silman, I. & Sussman, J.L.
    Crystal packing mediates enantioselective ligand recognition at the peripheral site of acetylcholinesterase
    J. Am. Chem. Soc. 127, 11029-11036 (2005). [Abstract] [PDF]

  94. Hasin, Y., Avidan, N., Bercovich, D., Korczyn, A.D., Silman, I., Beckmann, J.S. & Sussman, J.L.
    Analysis of genetic polymorphisms in acetylcholinesterase as reflected in different populations
    Curr. Alzheimer Res. 2, 207-218 (2005). [Abstract] [PDF]

  95. Prilusky, J., Felder, C.E., Zeev-Ben-Mordehai, T., Rydberg, E., Man, O., Beckmann, J.S., Silman, I. & Sussman, J.L.
    FoldIndex©: a simple tool predicts whether a given protein is intrinsically disordered
    Bioinformatics 21, 3435-3438 (2005). [Abstract] [PDF] [Supplementary Material]

  96. 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.L., Janin, J., van Tilbeurgh, H. & Poupon, A.
    HalX: an open-source LIMS (Laboratory Information Management System) for small- to large-scale laboratories
    Acta Crystal D61, 671-678 (2005). [Abstract] [PDF]

  97. Premkumar, L., Sawkar, A.R., Boldin-Adamsky, S., Toker, L., Silman, I., Kelly, J., Futerman, A.H. & Sussman, J.L.
    X-ray structure of human acid-β-glucosidase covalently-bound to Conduritol-B-epoxide: Implications for Gaucher disease
    J. Biol. Chem. 280, 23815-23819 (2005). [Abstract] [PDF] [Paper of the Week] [Suppl Mat 1] [Suppl Mat 2]

  98. Silman, I. & Sussman, J.L.
    Acetylcholinesterase: 'Classical' and 'Non-Classical' Functions and Pharmacology
    Curr. Opin. Pharmacol. 5, 293-302 (2005). [Abstract] [PDF]

  99. Harel, M., Hyatt, J.L., Brumshtein, B., Morton, C.L., Yoon, K.J., Wadkins, R.M., Silman, I., Sussman, J.L. & Potter, P.M.
    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
    Mol. Pharmaco. 67, 1874-1881 (2005). [Abstract] [PDF]

  100. Premkumar L., Greenblatt H.M., Bagashwar U., Savchenkoa T., Gokhmana I., Sussman J.L. and Zamir A.
    3D structure of a halotolerant algal carbonic anhydrase predicts halotole rance of a mammalian homolog.
    Proc. Natl. Acad. Sci. USA 102, 7493-7498 (2005). [Abstract] [PDF] [Supporting Info]

  101. Jaakola, V.-P., Prilusky, J., Sussman, J.L. & Goldmani, A.
    G protein-coupled receptors show unusual patterns of intrinsic unfolding.
    PEDS 18, 103-110 (2005). [Abstract] [PDF]


    2004

  102. Harel, M., Aharoni, A., Gaidukov, L., Brumshtein, B., Khersonsky , O., Meged, R., Dvir, H., Ravelli, R.B., McCarthy, A., Toker, L., Silman, I., Sussman, J.L. & Tawfik, D.S.
    Corrigendum: Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes.
    Nat. Struct. Mol. Biol. 11, 1253 (2004). [Abstract] [PDF]

  103. Greenblatt, H.M., Guillou, C., Guenard, D., Argaman, A., Botti, S., Badet, B., Thal, C., Silman, I. & Sussman, J.L.
    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
    J. Am. Chem. Soc. 126, 15405-15411 (2004). [Abstract] [PDF]

  104. Dvir, H., Harel, M., Bon, S., Liu, W.-Q., Vidal, M., Garbay, C., Sussman, J.L., Massoulié, J. & Silman, I.
    The synaptic acetylcholinesterase tetramer assembles around a polyproline-II helix
    EMBO J. 23, 4394-4405 (2004). [Abstract] [PDF]

  105. Liu, T., Zhu, W., Gu, J., Shen, J., Luo, X., Chen, G., Puah, C.M., Silman, I., Chen, K., Sussman, J.L. & Jiang, H.
    Additivity of Cation-π interactions: An ab initio computational study on π-cation-π sandwich complexes
    J. Phys. Chem. A 108, 9400-9405 (2004). [Abstract] [PDF]

  106. Hasin, Y., Avidan, N., Bercovich, D., Korczyn, A.D., Silman, I., Beckmann, J.S. & Sussman, J.L.
    A paradigm for single nucleotide polymorphism analysis: The case of the acetylcholinesterase gene.
    Hum. Mutat. 24, 408-416 (2004). [Abstract] [PDF]

  107. Zhang, S., Rich, A., Sussman, J.L. & Fersht, A.R. (2004).
    Carl-Ivar Branden 1934-2004.
    Nat. Struct. Mol. Biol. 11, 490-492 (2004). [PDF]

  108. Harel, M., Aharoni, A., Gaidukov, L., Brumshtein, B., Khersonsky, O., Meged, R., Dvir, H., Ravelli, R.B., McCarthy, A., Toker, L., Silman, I., Sussman, J.L. & Tawfik, D.S.
    Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes.
    Nat. Struct. Mol. Biol. 11, 412-419 (2004). [Abstract] [PDF]

  109. Bageshwara, U.K., Premkumar, L., Gokhmana, I., Savchenkoa, T., Sussman, J.L. & Zamir, A.
    Natural protein engineering: a uniquely salt-tolerant, but not halophilic, α-type carbonic anhydrase from algae proliferating in low- to hyper-saline environments.
    PEDS 17, 191-200 (2004). [Abstract] [PDF]

  110. Futerman, A. H., Sussman, J. L., Horowitz, M., Silman, I. & Zimran, A.
    New directions in the treatment of Gaucher disease
    Trends Pharm. Sci. 25, 147-151 (2004). [Abstract] [PDF]

  111. Pe'er, I., Felder, C.E., Man, O., Silman, I., Sussman, J.L. & Beckmann, J.S.
    Proteomic signatures: amino acid and oligopeptide compositions differentiate between phyla
    Proteins 54, 20-40 (2004). [Abstract] [PDF] [Cover] [Supplementary Material]


    2003

  112. Zeev-Ben-Mordehai, T., Rydberg, E.H., Solomon, A., Toker, L., Botti, S., Auld, V.J., Silman, I. & Sussman, J.L.
    The intracellular domain of the drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded
    Proteins 53, 758-767 (2003). [Abstract] [PDF]

  113. Dvir, H., Harel, M., McCarthy, A.H., Toker, L., Silman, I., Futerman, A.H. & Sussman, J.L.
    X-ray structure of human acid β-glucosidase, the defective enzyme in Gaucher disease.
    EMBO Rep. 4, 704-709 (2003). [Abstract] [PDF]

  114. Greenblatt, H.M., Dvir, H., Silman, I. & Sussman, J.L.
    Acetylcholinesterase: a multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease.
    J. Mol. Neurosci. 20, 369-384 (2003). [Abstract] [PDF]

  115. Xu, Y., Shen, J., Luo, X., Silman, I., Sussman, J.L., Chen, K. & Jiang, H.
    How does Huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations.
    J. Am. Chem. Soc. 125, 11340-11349 (2003). [Abstract] [PDF]

  116. Fuchs, S., Kasher, R., Balass, M., Scherf, T., Harel, M., Fridkin, M., Sussman, J.L. & Katchalski-Katzir, E.
    The binding site of acetylcholine receptor: From synthetic peptides to solution and crystal structure.
    Ann. NY Acad. Sci. 998, 93-100 (2003). [Abstract] [PDF]

  117. Premkumar, L., Greenblatt, H.M., Savchenkoa, T., Gokhmana, I., Zamir, A. & Sussman, J.L.
    Identification, cDNA cloning, expression, crystallization and preliminary X-ray analysis of an exceptionally halotolerant carbonic anhydrase from Dunaliella salina.
    Acta Cryst D59, 1084-1086 (2003). [Abstract] [PDF]

  118. Premkumar, L., Bageshwara, U., Gokhmana, I., Zamir, A. & Sussman, J.L.
    An unusual halotolerant a-type carbonic anhydrase from the alga Dunaliella salina functionally expressed in Escherichia coli.
    Protein Expr. Purif. 28, 151-157 (2003). [Abstract] [PDF]

  119. Zeev-Ben-Mordehai, T., Silman, I. & Sussman, J.L.
    Acetylcholinesterase in motion: Visualizing conformational changes in crystal structures by a morphing procedure.
    Biopolymers 68, 395-406 (2003). [Abstract] [PDF]

  120. Wong, D.M., Greenblatt, H.M., Dvir, H., Carlier, P.R., Han, Y.-F., Pang, Y.-P., Silman, I. & Sussman, J.L.
    Acetylcholinesterase complexed with bivalent ligands related to Huperzine A: experimental evidence for species-dependent protein-ligand complementarity.
    J. Am. Chem. Soc. 125, 363-373 (2003). [Abstract] [PDF]

  121. Katchalski-Katzir, E., Kasher, R., Balass, M., Scherf, T., Harel, M.,Fridkin, M., Sussman, J.L. & Fuchs, S.
    Design and synthesis of peptides that bind a-bungarotoxin with high affinity and mimic the three-dimensional structure of the binding-site of acetylcholine receptor.
    Biophys. Chem. 100, 293-305 (2003). [Abstract] [PDF]

  122. Harel, D., Unger, R. & Sussman, J.L.
    Beauty is in the genes of the beholder: A golden tribute to a golden anniversary*
    *With apologies to Watson and Crick.
    In DNA 50, The Secret of Life, (ed. Balaban, M.), 98-103 (Faircount, London, 2003). [PDF]


    2002

  123. Luo, X., Feng, C., Tan, X.-J., Tan, C., Zhu, D., Shen, J., Huang, X., Liu, T., Chen, K., Jiang, H., Zhu, W., Puah, C. M., Dvir, H., Harel, M., Sussman, J. L. & Silman, I.
    Structural feature of AChE inhibitor Huperzine B in nature and in the binding site of AChE: Density functional theory study combined with IR determination
    J. Theor. Comp. Chem. 1, 81-92 (2002). [Abstract] [PDF]

  124. Weik, M., Berges, J., Raves, M. L., Gros, P., McSweeney, S., Silman, I., Sussman, J. L., Houeee-Levin, C. & Ravelli, R. B. G.
    Evidence for the formation of disulfide radicals in protein crystals upon X-ray irradiation.
    J. Synchrotron Rad. 9, 342-346 (2002). [Abstract] [PDF]

  125. Liu, T., Gu, J., Tan, X.-J., Zhu, W.-L., Luo, X.-M., Jiang, H.-L., Ji, R.-Y., Chen, K.-X., Silman, I. & Sussman, J. L.
    The relationship between binding models of TMA with furan and imidazole and the molecular electrostatic potentials: DFT and MP2 computational studies.
    J. Phys. Chem. A 106, 157-164 (2002). [Abstract] [PDF]

  126. Koellner, G., Steiner, T., Millard, C. B., Silman, I. & Sussman, J. L.
    A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica.
    J. Mol. Biol. 320, 721-725 (2002). [Abstract] [PDF]

  127. Bar-On, P., Millard, C. B., Harel, M., Dvir, H., Enz, A., Sussman, J. L. & Silman, I.
    Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine.
    Biochemistry 41, 3555-3564 (2002). [Abstract] [PDF]

  128. Dvir, H., Jiang, H. L., Wong, D. M., Harel, M., Chetrit, M., He, X. C., Tang, X. C., Silman, I., Bai, D. L. & Sussman, J. L.
    X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-Huperzine A and (-)-Huperzine B: Structural evidence for an active site rearrangement.
    Biochemistry 41, 10810-10818 (2002). [Abstract] [PDF]

  129. Felder, C. E., Harel, M., Silman, I. & Sussman, J. L.
    Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.
    Acta Cryst D58, 1765-1771 (2002). [Abstract] [PDF]

  130. Dvir, H., Wong, D. M., Harel, M., Barril, X., Orozco, M., Luque, F. J., Munoz-Torrero, D., Camps, P., Rosenberry, T. L., Silman, I. & Sussman, J. L.
    3D structure of Torpedo californica acetylcholinesterase complexed with Huprine X at 2.1 Å resolution: kinetic and molecular dynamic correlates.
    Biochemistry 41, 2970-2981 (2002). [Abstract] [PDF]


    2001

  131. Weik, M., Kryger, G., Schreurs, A. M., Bouma, B., Silman, I., Sussman, J. L., Gros, P. & Kroon, J.
    Solvent behaviour in flash-cooled protein crystals at cryogenic temperatures.
    Acta Cryst D57, 566-573 (2001). [Abstract] [PDF]

  132. Nicolas, A., Ferron, F., Toker, L., Sussman, J. L. & Silman, I.
    Histochemical method for characterization of enzyme crystals: application to crystals of Torpedo californica acetylcholinesterase.
    Acta Crystal D57, 1348-1350 (2001). [Abstract] [PDF]

  133. Felder, C., Jiang, H.-L., Zhu, W.-L., Chen, K.-X., Silman, I., Botti, S. A. & Sussman, J. L.
    Quantum/classical mechanical comparison of cation-π interactions between tetramethylammonium and benzene.
    J. Phys. Chem. A 105, 1326-1333 (2001). [Abstract] [PDF]

  134. Tan, X. J., Zhu, W. L., Cui, M., Luo, X. M., Gu, J. D., Silman, I., Sussman, J. L., Jiang, H. L., Ji, R. Y. & Chen, K. X.
    Noncovalent interaction or chemical bonding between alkaline earth cations and benzene? A quantum chemistry study with MP2 and density-functional theory methods.
    Chem. Phys. Lett. 349, 113-122 (2001). [Abstract] [PDF]

  135. Botti, S., Silman, I. & Sussman, J. L.
    Structural genomics
    in Conformational Diseases - A Compendium, Based on the First International Workshop on Conformational Diseases (eds. Solomon, B.) 73-81 (The Center for the Study of Emerging Diseases, Jerusalem, 2001).

  136. Liu, T., Gu, J.-D., Tan, X.-J., Zhu, W.-L., Luo, X.-M., Li, Q., Jiang, H.-L., Ji, R.-Y., Chen, K.-X., Silman, I. & Sussman, J. L.
    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.
    J. Phys. Chem. A 105, 5431-5437 (2001). [Abstract] [PDF]

  137. Sussman, J. L., Lin, D., Jiang, J., Manning, N. O., Prilusky, J. & Abola, E. E.
    The Protein Data Bank at Brookhaven
    in International Tables for Crystallography, Volume F. Crystallography of Biological Macromolecules (eds. Rossmann, M. G. & Arnold, E.) 649-656 (Kluwer Academic Publishers, Dordrecht, 2001).

  138. Doucet-Personeni, C., Bentley, P. D., Fletcher, R. J., Kinkaid, A., Kryger, G., Pirard, B., Taylor, A., Taylor, R., Taylor, J., Viner, R., Silman, I., Sussman, J. L., Greenblatt, H. M. & Lewis, T.
    A structure-based design approach to the development of novel, reversible AChE inhibitors.
    J. Med. Chem. 44, 3203-3215 (2001). [Abstract] [PDF]

  139. Harel, M., Kasher, R., Nicolas, A., Guss, J. M., Balass, M., Fridkin, M., Smit, A. B., Brejc, K., Sixma, T. K., Katchalski-Katzir, E., Sussman, J. L. & Fuchs, S.
    The structure of the binding site of the acetylcholine receptor as visualized in the X-ray structure of a complex between a-bungarotoxin and a high affinity mimotope peptide.
    Neuron 32, 265-275 (2001). [Abstract] [PDF]

  140. Weik, M., Ravelli, R., Silman, I., Sussman, J. L., Gros, P. & Kroon, J.
    Specific protein dynamics near the solvent glass transition assayed by radiation-induced structural changes.
    Protein Sci. 10, 1953-1961 (2001). [Abstract] [PDF]


    2000

  141. Harel, M., Kryger, G., Rosenberry, T. L., Mallender, W. D., Lewis, T., Fletcher, R. J., Guss, J. M., Silman, I. & Sussman, J. L.
    Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors.
    Protein Sci. 9, 1063-1072 (2000). [Abstract] [PDF]

  142. Kryger, G., Harel, M., Giles, K., Toker, L., Velan, B., Lazar, A., Kronman, C., Barak, D., Ariel, N., Shafferman, A., Silman, I. & Sussman, J. L.
    Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II.
    Acta Crystal D56, 1385-1394 (2000). [Abstract] [PDF] [Cover]

  143. Zhu, W.-L., Tan, X.-J., Puah, C. M., Gu, J.-D., Jiang, H.-L., Chen, K.-X., Felder, C., Silman, I. & Sussman, J. L.
    How does ammonium interact with aromatic groups? A density functional theory (DFT/B3LYP) investigation.
    J. Phys. Chem. A 104, 9573-9580 (2000). [Abstract] [PDF]

  144. Bar-On, P., Harel, M., Millard, C. B., Enz, A., Sussman, J. L. & Silman, I.
    Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug, ENA-713.
    Neurosci. Lett.  Supp. 55, S6 (2000).

  145. Sussman, J. L., Millard, C. B., Gillilan, R. E., Koellner, G., Kryger, G., Harel, H., Greenblatt, H. M., Ordentlich, A., Barak, D., Shafferman, A. & Silman, I.
    Crystal structures of conjugates of AChE with nerve agents at atomic resolution.
    in 2000 U.S. Army Medical Defense Bioscience Review, 38-55 (U.S. Army Medical Research and Material Command, Baltimore, MD., 2000).

  146. Silman, I. & Sussman, J. L.
    Structural studies on acetylcholinesterase.
    in Cholinesterases and Cholinesterase Inhibitors (ed. Giacobini, E.) 9-25 (Martin Dunitz, London, 2000).

  147. Koellner, G., Kryger, G., Millard, C. B., Silman, I., Sussman, J. L. & Steiner, T.
    Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica..
    J. Mol. Biol. 296, 713-735 (2000). [Abstract] [PDF]

  148. Lin, D., Manning, N. O., Jiang, J., Abola, E. E., Stampf, D., Prilusky, J. & Sussman, J. L.
    AutoDep©: A web based system for deposition and validation of macromolecular structural information.
    Acta Crystal D56, 828-841 (2000). [Abstract] [PDF]

  149. Greenblatt, H. M., Silman, I. & Sussman, J. L.
    Structural studies on vertebrate and invertebrate acetylcholinesterases and their complexes with functional ligands.
    Drug Develop. Res. 50, 573-583 (2000). [Abstract] [PDF]

  150. Abola, E. E., Bairoch, A., Barker, W. C., Beck, S., Benson, D. A., Berman, H., Cantor, C., Doubet, S., Hubbard, T. J. P., Jones, T. A., Kleywegt, G. J., Kolaskar, A. S., Van Kuik, A., Lesk, A. M., Mewes, H.-W., Neuhaus, D., Pfeiffer, F., TenEyck, L. F., Simpson, R. J., Stoesser, G., Sussman, J. L., Tateno, Y., Tsugita, A., Ulrich, E. L. & Vliegenthart, J. F. G.
    Quality control in databanks for molecular biology.
    BioEssays 22, 1024-1034 (2000). [Abstract] [PDF]

  151. Weik, M., Ravelli, R. B. G., Kryger, G., McSweeney, S., Raves, M., Harel, M., Gros, P., Silman, I., Kroon, J. & Sussman, J. L.
    Specific chemical and structural damage to proteins produced by synchrotron radiation.
    Proc. Natl. Acad. Sci. USA 97, 623-628 (2000). [Abstract] [PDF] [Cover]

  152. Lamzin, V., Perrakis, A., Bricogne, G., Jiang, J., Swaminathan, S. & Sussman, J. L.
    Apotheosis, not apocalypse: methods in protein crystallography.
    Acta Cryst D56, 1510-1511 (2000). [Abstract] [PDF]

  153. Kraut, D., Goff, H., Pai, R. K., Hosea, N. A., Silman, I., Sussman, J. L., Taylor, P. & Voet, J. G.
    Inactivation studies of acetylcholinesterase with phenylmethanesulfonyl fluoride.
    Mol. Pharmacol. 57, 1243-1248 (2000). [Abstract] [PDF]


    1999

  154. Jiang, J., Abola, E. & Sussman, J. L.
    Deposition of structure factors at the protein data bank.
    Acta Crystal D55, 4 (1999). [Abstract] [PDF]

  155. Sussman, J. L., Abola, E. E., Lin, D., Jiang, J., Manning, N. O. & Prilusky, J.
    in Structural Biology and Functional Genomics (eds. Bradbury, E. M.), 251-264 (Kluwer Academic Publishers, Dordrecht, Boston, London, 1999).

  156. Millard, C. B., Kryger, G., Ordentlich, A., Harel, M., Raves, M., Greenblatt, H. M., Segall, Y., Barak, D., Shafferman, A., Silman, I. & Sussman, J. L.
    Crystal structure of "aged" phosphylated Torpedo acetylcholinesterase: nerve agent reaction products at the atomic level.
    Biochemistry 38, 7032-7039 (1999). [Abstract] [PDF]

  157. Sussman, J. L., Abola, E. E., Lin, D., Jiang, J., Manning, N. O. & Prilusky, J.
    The protein data bank.
    Genetica 106, 149-158 (1999). [Abstract] [PDF]

  158. Botti, S. A., Felder, C., Lifson, S., Sussman, J. L. & Silman, I.
    A modular treatment of molecular traffic through the active site of cholinesterases.
    Biophys. J. 77, 2430-2450 (1999). [Abstract] [PDF]

  159. Morel, N., Bon, S., Greenblatt, H., Wodak, S., Sussman, J. L., Massoulié, J. & Silman, I.
    Effect of mutations in the peripheral anionic site on the stability of acetylcholinesterase.
    Mol. Pharmacol. 55, 982-992 (1999). [Abstract] [PDF]

  160. Kryger, G., Silman, I. & Sussman, J. L.
    Structure of acetylcholinesterase complexed with E2020 (Aricept): implications for the design of new anti-Alzheimer drugs.
    Structure 7, 297-307 (1999). [Abstract] [PDF]

  161. Silman, I., Millard, C. B., Ordentlich, A., Greenblatt, H. M., Harel, M., Barak, D., Shafferman, A. & Sussman, J. L.
    A preliminary comparison of structural models for catalytic intermediates of acetylcholinesterase.
    Chem. Biol. Interactions 119-120, 43-52 (1999). [Abstract] [PDF]

  162. Millard, C. B., Koellner, G., Ordentlich, A., Shafferman, A., Silman, I. & Sussman, J. L.
    Reaction products of acetylcholinesterase and VX reveal a mobile histidine in the catalytic triad.
    J. Am. Chem. Soc. 121, 9883-9884 (1999). [PDF]

  163. Greenblatt, H. M., Kryger, G., Lewis, T., Silman, I. & Sussman, J. L.
    Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3Å resolution.
    FEBS Lett. 463, 321-326 (1999). [Abstract] [PDF] [Cover]


    1998 & Earlier

  164. Wlodawer, A., Davies, D., Petsko, G., Rossmann, M., Olson, A. & Sussman, J.L.
    Immediate release of crystallographic data: a proposal
    Science 279, 306-307 (1998). [Abstract]

  165. Raves, M., Giles, K., Schrag, J. D., Schmid, M. F., Phillips, G. N., Chiu, W., Howard, A. J., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 351-356 (Plenum, New York, 1998).

  166. Bar-On, P., Harel, M., Millard, C. B., Enz, A., Sussman, J. L. & Silman, I.
    in Xth International Symposium on Cholinergic Mechanisms - From Torpedo Electric Organ to Human Brain: Fundamental and Applied Aspects (ed. Massoulié, J.), 406-407 (Elsevier,Paris, 1998).

  167. Morel, N., Bon, S., Sussman, J. L., Massoulié, J. & Silman, I.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 435 (Plenum, New York, 1998).

  168. Giles, K., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 450 (Plenum, New York, 1998).

  169. Kryger, G., Silman, I. & Sussman, J. L.
    Three-dimensional structure of a complex of E2020 with acetylcholinesterase from Torpedo californica
    J. Physiol. (Paris) 92, 191-194 (1998). [Abstract] [PDF]

  170. Botti, S. A., Felder, C., Lifson, S., Sussman, J. L. & Silman, I.
    in Structure and Function of Cholinesterases and Related Proteins (eds. Doctor, B. P.), 227-228 (Plenum, New York, 1998).

  171. Karlsson, E., Harvey, A. L., Cerve'ansky, C., Kleywegt, G. J., Harel, M., Silman, I. & Sussman, J. L.
    in Enzymes from Snake Venoms (ed. Bailey, G. S.), 633-688 (Alaken, Inc., Fort Collins, 1998).

  172. Nicolas, A., Millard, C. B., Raves, M. L., Ravelli, R. B. G., Kroon, J., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 230-231 (Plenum, New York, 1998).

  173. Kryger, G., Giles, K., Harel, M., Toker, L., Velan, B., Lazar, A., Kronman, C., Barak, D., Ariel, N., Shafferman, A., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 370 (Plenum, New York, 1998).

  174. Bar-On, P., Harel, M., Millard, C. B., Enz, A., Sussman, J. L. & Silman, I.
    Kinetic and structural studies on the interaction of the anti-Alzheimer drug, ENA-713, with acetylcholinesterase.
    Neurosci. Lett. Supp. 51, S4 (1998).

  175. Silman, I., Millard, C., Kryger, G., Ordentlich, A., Harel, M., Raves, M., Greenblatt, H. M., Segall, Y., Barak, D., Shafferman, A. & Sussman, J. L.
    in 1998 U.S. Army Medical Defense Bioscience Review, 1-10 (U.S. Army Medical Research Institute of Chemical Defense, Baltimore, MD., 1998).

  176. Millard, C., Kryger, G., Ordentlich, A., Harel, M., Raves, M., Greenblatt, H. M., Segall, Y., Barak, D., Shafferman, A., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 454-455 (Plenum, New York, 1998).

  177. Millard, C., Kryger, G., Ordentlich, A., Harel, M., Raves, M., Greenblatt, H. M., Segall, Y., Barak, D., Shafferman, A., Silman, I. & Sussman, J. L.
    in 1998 U.S. Army Medical Defense Bioscience Review, 1-8 (U.S. Army Medical Research Institute of Chemical Defense, Baltimore, MD., 1998).

  178. Botti, S. A., Felder, C., Sussman, J. L. & Silman, I.
    Electrostatic homology modelling of a set of ChE-like neural adhesion proteins identifies a shared 'annular' motif with ChEs. Structural implications for a cell-recognition role of ChEs.
    J. Physiol. (Paris) 92, 414-416 (1998).

  179. Millard, C., Kryger, G., Ordentlich, A., Harel, M., Raves, M., Greenblatt, H. M., Segall, Y., Barak, D., Shafferman, A., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (eds. Doctor, B. P.), 425-431 (Plenum, New York, 1998).

  180. Botti, S. A., Felder, C., Sussman, J. L. & Silman, I.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 448-449 (Plenum, New York, 1998).

  181. Giles, K., Ben-Yohanan, R., Velan, B., Shafferman, A., Sussman, J. L. & Silman, I.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 442-443 (Plenum, New York, 1998).

  182. Raves, M. L., Greenblatt, H. M., Kryger, G., Nicolas, A., Ravelli, R. B. G., Harel, M., Kroon, J., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 372 (Plenum, New York, 1998).

  183. Botti, S. A., Felder, C. E., Sussman, J. L. & Silman, I.
    Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs.
    Protein Eng. 11, 415-420 (1998). [Abstract] [PDF] [Cover]

  184. Millard, C. B., Koellner, G., Ordentlich, A., Shafferman, A., Silman, I. & Sussman, J. L.
    Crystal structure of acetylcholinesterase from Torpedo californica inhibited with the nerve agent VX.
    Neurosci. Lett. Supp. 51, S29 (1998).

  185. Kryger, G., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 469-475 (Plenum, New York, 1998).

  186. Sussman, J. L., Bernstein, F. C., Jiang, J., Libeson, M., Lin, D., Manning, N. O., McCarthy, J., Shea, R., Abola, E. E., Felder, C. E., Prilusky, J. & Ritter, O.
    in The Encyclopedia of Computational Chemistry (ed. Schleyer, P.), 2160-2168 (John Wiley & Sons Ltd., Chichester, 1998).

  187. Bar-On, P., Harel, M., Millard, C., Enz, A., Sussman, J. L. & Silman, I.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 373-374 (Plenum, New York, 1998).

  188. Kryger, G., Giles, K., Harel, M., Toker, L., Velan, B., Lazar, A., Kronman, C., Barak, D., Ariel, N., Shafferman, A., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 323-326 (Plenum, New York, 1998).

  189. Greenblatt, H., Kryger, G., Harel, M., Lewis, T., Taylor, J., Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 371 (Plenum, New York, 1998).

  190. Ravelli, R. B. G., Raves, M. L., Ren, Z., Bourgeois, D., Roth, M., Kroon, J., Silman, I. & Sussman, J. L.
    Static Laue diffraction studies on acetylcholinesterase.
    Acta Crystal D54, 1359-1366 (1998). [Abstract]

  191. Sussman, J. L.
    Protein data bank deposits.
    Science 282, 1991 (1998). [Abstract]

  192. Silman, I. & Sussman, J. L.
    in Structure and Function of Cholinesterases and Related Proteins (ed. Doctor, B. P.), 25-33 (Plenum, New York, 1998).

  193. Bar-On, P., Harel, M., Millard, C. B., Enz, A., Sussman, J. L. & Silman, I.
    Kinetic and structural studies on the interaction of the anti-Alzheimer drug, ENA-713, with Torpedo californica acetylcholinesterase.
    J. Physiol. (Paris) 92, 406-407 (1998).

  194. Sussman, J. L., Lin, D., Jiang, J., Manning, N. O., Prilusky, J., Ritter, O. & Abola, E. E.
    Protein data bank (PDB): a database of 3D structural information of biological macromolecules.
    Acta Crystal D54, 1078-1084 (1998). [Abstract] [PDF]

  195. Bar-On, P., Millard, C. B., Enz, A., Sussman, J. L. & Silman, I.
    Evidence that the anti-Alzheimer drug, ENA-713, inhibits acetylcholinesterase by more than one mechanism.
    Neurosci. Lett.  Supp. 48, S6-S7 (1997).

  196. Giles, K., Sussman, J. L. & Silman, I.
    Human acetylcholinesterase II: in vivo expression and tissue distribution via EST analysis.
    Neurosci. Lett.  Supp. 48, S19-S29 (1997).

  197. Sussman, J. L., Ritter, O. & Abola, E. E.
    in Transactions ACA 1997 (ed. Berman, H. M.), 7-11 (American Crsytallographic Assoication, Buffalo, NY, 1997).

  198. Abola, E. E., Sussman, J. L., Prilusky, J. & Manning, N. O.
    in Methods in Enzymology (ed. Carter, C. W.), 556-571 (Academic Press, New York, 1997).

  199. Felder, C. E., Botti, S. A., Lifson, S., Silman, I. & Sussman, J. L.
    External and internal electrostatic potentials of cholinesterase models.
    J. Molec. Graphics & Modelling 15, 318-327 (1997). [Abstract] [PDF] [html]

  200. Giles, K., Sussman, J. L. & Silman, I.
    Human acetylcholinesterase I: in vitro assembly of subunits.
    Neurosci. Lett.  Supp. 48, S19 (1997).

  201. Botti, S. A., Felder, C., Lifson, S., Silman, I. & Sussman, J. L.
    An integrated model for the molecular traffic through the active site of cholinesterases.
    Neurosci. Lett.  Supp. 48, S11 (1997).

  202. Botti, S. A., Felder, C., Sussman, J. L. & Silman, I.
    The conjunction of a conserved electrostatic motif and a common cholinesterase fold defines a class of adhesion proteins.
    Neurosci. Lett.  Supp. 48, S11 (1997).

  203. Silman, I., Harel, M., Raves, M. & Sussman, J. L.
    in Progress in Alzheimers and Parkinsons Diseases (ed. Fisher, A.), 523-530 (Plenum Press, New York, 1997).

  204. Giles, K., Raves, M. L., Silman, I. & Sussman, J. L.
    in Theoretical and Computational Methods in Genome Research (ed. Suhai, S.), 303-315 (Plenum Press, New York, 1997).

  205. Sussman, J. L.
    Bridging the gap.
    Nat. Struct. Biol. 4, 517 (1997).

  206. Raves, M. L., Harel, M., Pang, Y.-P., Silman, I., Kozikowski, A. P. & Sussman, J. L.
    3D structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.
    Nat. Struct. Biol. 4, 57-63 (1997). [Abstract] [PDF]

  207. Frolow, F., Harel, M., Mevarech, M., Sussman, J. L. & Shoham, M.
    Protein adaptation to a saturated salt environment: Insights from the crystal structure of a halophilic 2Fe-2S ferredoxin.
    Nat. Struct. Biol. 3, 451-457 (1996). [Abstract]

  208. Faerman, C., Ripoll, D., Bon, S., Le Feuvre, Y., Morel, N., Massoulié , J., Sussman, J. L. & Silman, I.
    Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function.
    FEBS Lett. 386, 65-71 (1996). [Abstract]

  209. Baker, E.N., Blundell, T.L., Vijayan, M., Dodson, E., Dodson, G., Gilliland, G.I. & Sussman, J.L.
    Crystallographic data deposition.
    Nature 379, 202 (1996). [Abstract]

  210. Baker, E.N., Blundell, T.L., Vijayan, M., Dodson, E., Gilliland, G.I. & Sussman, J.L.
    Deposition of macromolecular data.
    Acta Crystal D52, 609 (1996). [Abstract]

  211. Baker, E.N., Blundell, T.L., Vijayan, M., Dodson, E., Dodson, G., Gilliland, G.I. & Sussman, J.L.
    Archival journal requirements for data deposition.
    Biophys. J. 70, 2994 (1996). [Abstract]

  212. Wlodek, S. T., Antosiewicz, J., McCammon, J. A., Straatsma, T. P., Gilson, M. K., Briggs, J. M., Humblet, C. & Sussman, J. L.
    Binding of tacrine and 6-chlorotacrine by acetylcholinesterase.
    Biopolymers 38, 109-117 (1996). [Abstract]

  213. Peng, L., Silman, I., Sussman, J. L. & Goeldner, M.
    Biochemical evaluation of photolabile precursors of choline and carbamoylcholine for potential time-resolved crystallographic studies on cholinesterases.
    Biochemistry 35, 10854-10861 (1996). [Abstract]

  214. Marchot, P., Ravelli, R. B. G., Raves, M. L., Bourne, Y., Vellom, D. C., Kanter, J., Camp, S., Sussman, J. L. & Taylor, P.
    Soluble monomeric acetylcholinesterase from mouse: expression, purification, and crystallization in complex with fasciculin.
    Protein Sci. 5, 672-679 (1996). [Abstract]

  215. Harel, M., Quinn, D. M., Nair, H. K., Silman, I. & Sussman, J. L.
    The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase.
    J. Am. Chem. Soc. 118, 2340-2346 (1996).

  216. Abola, E. E., Manning, N. O., Prilusky, J., Stampf, D. R. & Sussman, J. L.
    The protein data bank: current status and future challenges.
    J. Res. Natl. Inst. Stand. Technol. 101, 231-241 (1996).

  217. Sussman, J. L., Abola, E. E., Manning, N. O. & Prilusky, J.
    The protein data bank: current status and future challenges.
    in Crystallographic Computing (ed. Bourne, P. & Watenpaugh, K.), 9-34 (Oxford Univ. Press, New York, 1996). [PDF]

  218. Sussman, J. L., Harel, M., Raves, M. L., Giles, K., Ravelli, R. B. G., Peng, L., Goeldner, M., Kleywegt, G. J., Quinn, D. M., Nair, H. K. & Silman, I.
    in 1996 U.S. Army Medical Defense Bioscience Review, 13-22 (U.S. Army Medical Research Institute of Chemical Defense, Baltimore, MD., 1996).

  219. Porschke, D., Crminon, C., Cousin, X., Bon, C., Sussman, J. L. & Silman, I.
    Electrooptical measurements demonstrate a large permanent dipole moment associated with acetylcholinesterase.
    Biophys. J. 70, 1603-1608 (1996). [Abstract]

  220. Dym, O., Mevarech, M. & Sussman, J. L.
    Structural features that stabilize Halophilic malate dehydrogenase from an Archaebacterium.
    Science 267, 1344-1346 (1995). [Abstract] [PDF]

  221. Sussman, J. L., Harel, M., Raves, M., Quinn, D. M., Nair, H. K. & Silman, I.
    in Enzymes of the Cholinesterase Family (ed. Balasubramanian, A. L.), 59-65 (Plenum Press, New York, 1995).

  222. Alon, R. N., Mirny, L., Sussman, J. L. & Gutnick, D. L.
    Detection of a/b-hydrolase gold in the cell surface esterases of Acinetobacter species using an analysis of 3D profiles.
    FEBS Lett. 371, 231-235 (1995). [Abstract]

  223. Sussman, J. L., Harel, M., Raves, M., Quinn, D. & Silman, I.
    in Modelling of Biomolecular Structures and Mechanisms (ed. Pullman, A.), 455-560 (Kluwer Academic Publishers, Dordrecht, Holland, 1995).

  224. Ripoll, D. R., Faerman, C. H., Gillilan, R., Silman, I. & Sussman, J. L.
    in Enzymes of the Cholinesterase Family (ed. Balasubramanian, A. L.), 67-70 (Plenum Press, New York, 1995).

  225. Silman, I., Kreimer, D. I., Shin, I., Dolginova, E. A., Roth, E., Goldfarb, D., Szosenfogel, R., Raves, M., Sussman, J. L., Borochov, N. & Weiner, L.
    in Enzymes of the Cholinesterase Family (ed. Balasubramanian, A. L.), 77-82 (Plenum Press, New York, 1995).

  226. Peitsch, M. C., Stampf, D. R., Wells, T. N. C. & Sussman, J. L.
    The Swiss 3D-Image collection and Brookhaven protein data bank browser on the World-Wide Web.
    TIBS 20, 82-84 (1995). [Abstract] [PDF]

  227. Stampf, D. R., Felder, C. E. & Sussman, J. L.
    PDBBrowse - a graphics interface to the Brookhaven protein data bank
    Nature 374, 572-574 (1995). [Abstract] [PDF]

  228. Harel, M., Kleywegt, G. J., Ravelli, R. B. G., Silman, I. & Sussman, J. L.
    Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.
    Structure 3, 1355-1366 (1995). [Abstract] [PDF]

  229. Silman, I., Harel, M., Eichler, J., Sussman, J. L., Anselmet, A. & Massoulié, J.
    in Alzheimer Disease: Therapeutic Strategies (ed. Giacobini, E.), 88-92 (Birkhîuser, Boston, 1994).

  230. Eichler, J., Anselmet, A., Sussman, J. L., Massoulié, J. & Silman, I.
    Differential effects of "peripheral" site ligands on Torpedo and chicken acetylcholinesterase.
    Mol. Pharmacol. 45, 335-340 (1994). [Abstract]

  231. Axelsen, P. H., Harel, M., Silman, I. & Sussman, J. L.
    Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography.
    Protein Sci. 3, 188-197 (1994). [Abstract] [PDF]

  232. Silman, I., Harel, M., Axelsen, P., Raves, M. & Sussman, J. L.
    Three-dimensional structures of acetylcholinesterase and of its complexes with anticholinesterase agents.
    Biochemical Soc. Trans. 22, 745-749 (1994). [Abstract]

  233. Gilson, M. K., Straatsma, T. P., McCammon, J. A., Ripoll, D. R., Faerman, C. H., Axelsen, P., Silman, I. & Sussman, J. L.
    Open "back door" in a molecular dynamics simulation of acetylcholinesterase.
    Science 263, 1276-1278 (1994). [Abstract] [Cover] [PDF]

  234. Kreimer, D. I., Dolginova, E. A., Raves, M., Sussman, J. L., Silman, I. & Weiner, L.
    A metastable state of Torpedo acetylcholinesterase generated by modification with organomercurials.
    Biochemistry 33, 14407-14418 (1994). [Abstract]

  235. Joshua-Tor, L. & Sussman, J. L.
    The coming of age of DNA crystallography.
    Curr. Opin. Struct. Biol. 3, 323-335 (1993).

  236. Silman, I., Harel, M., Eichler, J., Krejci, E., Anselmet, A., Chanal, P., Bon, S., Sussman, J. L. & Massoulié, J.
    in 1993 U.S. Army Medical Defense Bioscience Review, 1149-1157 (U.S. Army Medical Research Institute of Chemical Defense, Baltimore, MD., 1993).

  237. Gentry, M. K., Doctor, B. P., Cygler, M., Schrag, J. D., Sussman, J. L., Harel, M. & Silman, I.
    in 1993 U.S. Army Medical Defense Bioscience Review, 1127-1137 (U.S. Army Medical Research Institute of Chemical Defense, Baltimore, MD., 1993).

  238. Sussman, J. L., Harel, M. & Silman, I.
    in 1993 U.S. Army Medical Defense Bioscience Review, 1139-1148 (U.S. Army Medical Research Institute of Chemical Defense, Baltimore, MD., 1993).

  239. Massoulié, J., Sussman, J. L., Bon, S. & Silman, I.
    Structure and functions of acetylcholinesterase and butyrylcholinesterase.
    Prog. Brain Res. 98, 139-146 (1993). [Abstract]

  240. Tan, R. C., Truong, T. N., McCammon, J. A. & Sussman, J. L.
    Acetylcholinesterase: electrostatic steering increases the rate of ligand binding.
    Biochemistry 32, 401-403 (1993). [Abstract]

  241. Sussman, J. L., Harel, M. & Silman, I.
    Three-dimensional structure of acetylcholinesterase and of its complexes with anticholinesterase drugs.
    Chem. Biol. Interactions 87, 187-197 (1993). [Abstract]

  242. Livnah, O., Bayer, E. A., Wilchek, M. & Sussman, J. L.
    The structure of the complex between avidin and the dye, 2-(4'-hydroxyazobenzene) benzoic acid (HABA).
    FEBS Lett. 328, 165-168 (1993). [Abstract] [PDF]

  243. Cygler, M., Schrag, J. D., Sussman, J. L., Harel, M., Silman, I., Gentry, M. K. & Doctor, B. P.
    Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins.
    Protein Sci. 2, 366-382 (1993). [Abstract] [PDF]

  244. Reich, Z., Friedman, P., Scolnik, Y., Sussman, J. L. & Minsky, A.
    On the metastability of left-handed DNA motifs.
    Biochemistry 32, 2116-2119 (1993). [Abstract]

  245. Wagner, U. G., Pattridge, K. A., Ludwig, M. L., Stallings, W. C., Werber, M. M., Oefner, C., Frolow, F. & Sussman, J. L.
    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 Sci. 2, 814-825 (1993). [Abstract] [PDF]

  246. Livnah, O., Bayer, E. A., Wilchek, M. & Sussman, J. L.
    The three-dimensional structure of avidin and the avidin-biotin Complex.
    Proc. Natl. Acad. Sci. USA 90, 5076-5080 (1993). [Abstract] [PDF]

  247. Ripoll, D. R., Faerman, C. H., Axelsen, P., Silman, I. & Sussman, J. L.
    An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase.
    Proc. Natl. Acad. Sci. USA 90, 5128-5132 (1993). [Abstract] [PDF]

  248. Harel, M., Schalk, I., Ehret-Sabatier, L., Bouet, F., Goeldner, M., Hirth, C., Axelsen, P., Silman, I. & Sussman, J. L.
    Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase.
    Proc. Natl. Acad. Sci. USA 90, 9031-9035 (1993). [Abstract] [PDF]

  249. Unger, R. & Sussman, J. L.
    The importance of short structural motifs in protein structure analysis.
    J. Comput. Aided Mol. Des. 7, 457-472 (1993). [Abstract] [PDF]

  250. Sadoff, J. C., Shafferman, A., Soreq, H., Sussman, J. L. & Silman, I.
    in Emerging Technologies: Life Science (Borg Biomedical Services, The Woodlands, Texas, 1992).

  251. Sussman, J. L. & Silman, I.
    Acetylcholinesterase: structure and use as a model for specific cation-protein interactions.
    Curr. Opin. Struct. Biol. 2, 721-729 (1992). [Abstract] [PDF]

  252. Duval, N., Bon, S., Silman, I., Sussman, J. L. & Massoulié, J.
    Site-directed mutagenesis of active-site-related residues in Torpedo acetylcholinesterase. Presence of a glutamic acid in the catalytic triad.
    FEBS Lett. 309, 421-423 (1992).

  253. Berman, H. M., Sussman, J. L., Joshua-Tor, L., Revich, G. G. & Ripley, L. S.
    A structural model for sequence-specific proflavin-DNA interactions during In vitro frameshift mutagenesis.
    J. Biomol. Struct. Dyn. 10, 317-331 (1992). [Abstract]

  254. Joshua-Tor, L., Frolow, F., Appella, E., Hope, H., Rabinovich, D. & Sussman, J. L.
    Three-dimensional structures of bulge-containing DNA fragments.
    J. Mol. Biol. 225, 397-431 (1992). [Abstract]

  255. Sussman, J. L., Harel, M. & Silman, I.
    in Membrane Proteins: Structures, Interactions and Models (ed. Pullman, A.), 161-175 (Kluwer Academic Publishers, Dordrecht, Holland, 1992).

  256. Silman, I., Harel, M., Krejci, E., Bon, S., Chanal, P., Sussman, J. L. & Massoulié, J.
    in Membrane Proteins: Structures, Interactions and Models (ed. Pullman, A.), 177-184 (Kluwer Academic Publishers, Dordrecht, Holland, 1992).

  257. Harel, M., Sussman, J. L., Krejci, E., Bon, S., Chanal, P., Massoulié, J. & Silman, I.
    Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis.
    Proc. Natl. Acad. Sci. USA 89, 10827-10831 (1992). [Abstract] [PDF]

  258. J., Sussman, J. L., Doctor, B. P., Soreq, H., Velan, B., Cygler, M., Rotundo, R., Shafferman, A., Silman, I. & Taylor, P.
    in Multidisciplinary Approaches to Cholinesterase Functions (ed. Shafferman, A.), 285-288 (Plenum Press, New York, 1992).

  259. Sussman, J. L., Harel, M. & Silman, I.
    in Multidisciplinary Approaches to Cholinesterase Functions (ed. Shafferman, A.), 95-107 (Plenum Press, New York, 1992).

  260. Harel, M., Silman, I. & Sussman, J. L.
    in Multidisciplinary Approaches to Cholinesterase Functions (ed. Shafferman, A.), 189-194 (Plenum Press, New York, 1992).

  261. Silman, I., Krejci, E., Duval, N., Bon, S., Chanal, P., Harel, M., Sussman, J. L. & Massoulié, J.
    in Multidisciplinary Approaches to Cholinesterase Functions (ed. Shafferman, A.), 177-183 (Plenum Press, New York, 1992).

  262. 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. L. & Velan, B.
    Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding.
    J. Biol. Chem. 267, 17640-17648 (1992). [Abstract]

  263. Cygler, M., Schrag, J. D., Sussman, J. L., Harel, M., Silman, I., Gentry, M. K. & Doctor, B. P.
    in Multidisciplinary Approaches to Cholinesterase Functions (ed. Shafferman, A.), 109-116 (Plenum Press, New York, 1992).

  264. Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., Sussman, J. L., Verschueren, K. H. G. & Goldman, A.
    The α/β hydrolase fold
    Protein Eng. 5, 197-211 (1992). [Abstract] [PDF]

  265. Sussman, J. L.
    in Crystallographic Computing (ed. Moras, D.), 382-391 (Oxford Univ. Press, New York, 1991).

  266. Sussman, J. L., Harel, M., Frolow, F., Goldman, A., Oefner, C., Toker, L. & Silman, I.
    in 1991 U.S. Army Medical Defense Bioscience Review, 441-448 (U.S. Army Medical Research Institute of Chemical Defense, Aberdeen Proving Ground, MD, 1991).

  267. Baldwin, E. T., Sussman, J. L., St. Charles, R. & Wlodawer, A.
    in Techniques in Protein Chemistry II (ed. Villafranka, J.), 347-356 (Academic Press, New York, 1991).

  268. Harel, M., Su, C.-T., Frolow, F., Silman, I. & Sussman, J. L.
    γ-chymotrypsin is a complex of α-chymotrypsin with its own autolysis products
    Biochemistry 30, 5217-5225 (1991). [Abstract] [PDF]

  269. Harel, M., Su, C. T., Frolow, F., Ashani, Y., Silman, I. & Sussman, J. L.
    Refined crystal structures of "aged" and "non-aged" organophosphoryl conjugates of γ-chymotrypsin.
    J. Mol. Biol. 221, 909-918 (1991). [Abstract] [PDF]

  270. Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Toker, L. & Silman, I.
    in Cholinesterases: Structure, Function, Mechanism, Genetics and Cell Biology (ed. Massoulié, J.), 7-11 (American Chemical Society, Washington, DC, 1991).

  271. Sussman, J. L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L. & Silman, I.
    Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
    Science 253, 872-879 (1991). [Abstract] ] [PDF]

  272. Unger, R., Harel, D., Wherland, S. & Sussman, J. L.
    Analysis of the dihedral angles distribution - the doublets distribution determines polypeptides conformations.
    Biopolymers 30, 499-508 (1990).

  273. Livnah, O. & Sussman, J. L.
    in Avidin-Biotin Technology (ed. Wilchek, M.), 90-93 (Academic Press, New York, 1990).

  274. Sussman, J. L., Harel, M., Frolow, F. & Silman, I.
    in 1989 U.S. Army Medical Defense Bioscience Review, 309-316 (U.S. Army Medical Research Institute of Chemical Defense, Columbia, MD, 1989).

  275. Unger, R., Harel, D., Wherland, S. & Sussman, J. L.
    A 3D building blocks approach to analyzing and predicting structure of proteins.
    Proteins 5, 355-373 (1989). [Abstract]

  276. Hope, H., Frolow, F. & Sussman, J. L.
    Macromolecular X-ray data collection on a rotating anode diffractometer.
    The Rigaku Journal (Japanese) 20, 20-27 (1989).

  277. Sussman, J. L., Shoham, M. & Harel, M.
    in Computer-Assisted Modeling of Receptor-Ligand Interactions. Theoretical Aspects and Applications to Drug Design (ed. Rein,R.), 171-187 (A.R. Liss, New York, 1989).

  278. Wagner, U. G., Werber, M. M., Beck, Y., Hartman, J. R., Frolow, F. & Sussman, J. L.
    Characterization of crystals of genetically engineered human manganese superoxide dismutase.
    J. Mol. Biol. 206, 787-788 (1989). [Abstract][PDF]

  279. Hirshberg, M., Sharon, R. & Sussman, J. L.
    A kinked model for the solution structure of DNA tridecamers with inserted adenosines: energy minimization and molecular dynamics.
    J. Biomol. Struct. Dyn. 5, 965-979 (1988). [Abstract]

  280. Joshua-Tor, L., Rabinovich, D., Hope, H., Frolow, F., Appella, E. & Sussman, J. L.
    The three-dimensional structure of a DNA duplex containing looped out bases.
    Nature 334, 82-84 (1988). [Abstract] [PDF]

  281. Sussman, J. L., Harel, M., Frolow, F., Varon, L., Toker, L., Futerman, A. H. & Silman, I.
    Purification and crystallization of a dimeric form of acetylcholinesterase from Torpedo californica subsequent to solubilization with phosphatidylinositol-specific phospholipase C.
    J. Mol. Biol. 203, 821-823 (1988). [Abstract] [PDF]

  282. Harel, M., Shoham, M., Frolow, F., Eisenberg, H., Mevarech, M., Yonath, A. & Sussman, J. L.
    Crystallization of halophilic malate dehydrogenase from Halobacterium marismortuI.
    J. Mol. Biol. 200, 609-610 (1988). [Abstract]

  283. Miller, M., Harrison, R. W., Wlodawer, A., Appella, E. & Sussman, J. L.
    Crystal structure of 15-mer DNA duplex containing unpaired bases.
    Nature 334, 85-86 (1988). [Abstract]

  284. Miller, M., Kirchoff, W., Schwarz, F., Appella, E., Chiu, Y. H., Cohen, J. S. & Sussman, J. L.
    Conformational transitions of synthetic DNA sequences with inserted bases, related to the dodecamer d(CGCGAATTCGCG).
    Nucl. Acids Res. 15, 3877-3890 (1987). [Abstract]

  285. Sussman, J. L., Joshua-Tor, L., Hirschberg, M., Saper, M. A., Frolow, F., Hope, H. & Appella, E.
    in Molecular Structure: Chemical Reactivity and Biological Activity (ed. Stezowski, J. J.),195-200 (Oxford University Press, Oxford, 1987). [PDF]

  286. Miller, M., Wlodawer, A., Appella, E. & Sussman, J. L.
    Crystallization of a DNA duplex 15-mer containing unpaired bases: d(CGCGAAATTTACGCG).
    J. Mol. Biol. 195, 967-968 (1987). [Abstract]

  287. Holland, D., Zilberstein, A., Zamir, A. & Sussman, J. L.
    A quantitative approach to sequence comparisons of nitrogenase MoFe protein a- and b-subunits including the newly sequenced nifK Gene from Klebsiella pneumoniae.
    Biochem. J. 247, 277-285 (1987). [Abstract]

  288. Hope, H., Frolow, F. & Sussman, J. L.
    Macromolecular X-ray data collection on a rotating anode diffractometer.
    The Rigaku Journal 4, 3-10 (1987). [PDF]

  289. Abad-Zapatero, C., Griffith, J. P., Sussman, J. L. & Rossmann, M. G.
    Refined crystal structure of Dogfish M4 apo-lactate dehydrogenase.
    J. Mol. Biol. 198, 445-467 (1987). [Abstract]

  290. Unger, R., Harel, D. & Sussman, J. L.
    DNAMAT - An efficient graphic matrix sequence homology algorithm and its application to structural analysis.
    Computer Applications in the Biosciences 2, 283-289 (1986). [Abstract]

  291. Yagil, G. & Sussman, J. L.
    Structural models for non-helical DNA.
    The EMBO Journal 5, 1719-1725 (1986). [Abstract]

  292. Harel, D., Unger, R. & Sussman, J. L.
    Beauty is in the genes of the beholder.
    TIBS 11, 155-156 (1986). [Abstract] [PDF]

  293. Sussman, J. L., Brown, J. H. & Shoham, M.
    in Iron-Sulfur protein research (ed. Matsubara, H.), 69-82 (Japan Scientific Societies Press, Tokyo, 1986).

  294. Roy, S., Weinstein, S., Borah, B., Nickol, J., Appella, E., Sussman, J. L., Miller, M., Shindo, H. & Cohen, J. S.
    Mechanism of oligonucleotide loop formation in solution.
    Biochemistry 25, 7417-7423 (1986). [Abstract]

  295. Werber, M. M., Sussman, J. L. & Eisenberg, H.
    Molecular basis for the special properties of proteins and enzymes from Halobacterium marismortui.
    FEMS Microbiology Reviews 39, 129-135 (1986).

  296. Saper, M. A., Eldar, H., Mizuuchi, K., Nickol, J., Appella, E. & Sussman, J. L.
    Crystallization of a DNA tridecamer d(C-G-C-A-G-A-A-T-T-C-G-C-G).
    J. Mol. Biol. 188, 111-113 (1986). [Abstract]

  297. Murata, M., Richardson, J. S. & Sussman, J. L.
    Simultaneous comparison of three protein sequences.
    Proc. Natl. Acad. Sci. USA 82, 3073-3077 (1985). [Abstract] [PDF]

  298. Sussman, J. L.
    in Diffraction Methods for Biological Macromolecules (ed. Wyckoff, H. W.), 271-303 (Academic Press, New York, 1985).

  299. Sussman, J. L.
    in Methods and Applications in Crystallographic Computing (ed. Hall, S. R.), 206-237 (Clarendon Press, Oxford, 1984).

  300. Bandel, G. & Sussman, J. L.
    PLORTEP: a computer program to translate PLUTO instructions into those of ORTEP.
    J. Appl. Cryst. 16, 650-651 (1983).

  301. Sussman, J. L. & Podjarny, A. D.
    The use of a constrained-restrained least-squares procedure for the low-resolution refinement of a macromolecule, yeast tRNAfMET.
    Acta Cryst B39, 495-505 (1983).

  302. Herzberg, O. & Sussman, J. L.
    Protein model building by the use of a constrained-restrained least-squares procedure.
    J. Appl. Cryst. 16, 144-150 (1983).

  303. Olson, W. K. & Sussman, J. L.
    How flexible is the furanose ring? 1. a comparison of experimental and theoretical studies.
    J. Am. Chem. Soc. 104, 270-278 (1982).

  304. Traub, W. & Sussman, J. L.
    Adenine-guanine base pairing in ribosomal RNA.
    Nucl. Acids Res. 10, 2701-2708 (1982). [Abstract]

  305. Holbrook, S. R., Sussman, J. L. & Kim, S.-H.
    Absence of correlation between base-pair sequence and RNA conformation.
    Science 212, 1275-1277 (1981) [Abstract]

  306. Wain-Hobson, S., Nussinov, R., Brown, R. J. & Sussman, J. L.
    Preferencial codon usage in genes.
    Gene 13, 355-364 (1981). [Abstract]

  307. Balaban, M., Sussman, J. L., Traub, W. & Yonath, A. (eds.)
    Structural Aspects of Recognition and Assembly in Biological Macromolecules - The Seventh Aharon Katzir-Katchalsky Conference, (Balaban ISS, Rehovot & Philadelphia, 1981).

  308. Sigler, P. B., Schevitz, R. W., Gross, G. M., Kaplansky, R. A., Podjarny, A. D. & Sussman, J. L.
    in Structural Aspects of Recognition and Assembly in Biological Macromolecules - The Seventh Aharon Katzir-Katchalsky Conference (ed. Balaban, M., Sussman, J.L., Traub, W., Yonath, A.), 631-643 (Balaban ISS, Rehovot and Philadelphia, 1981).

  309. Sussman, J. L.
    in Refinement of Protein Structures - Proceedings of the Daresbury Study Weekend (ed. Machin, P. A.), 13-23 (Daresbury Laboratory, Daresbury, 1981).

  310. Sussman, J. L., Podjarny, A. D., Schevitz, R. W. & Sigler, P. B.
    in Structural Aspects of Recognition and Assembly in Biological Macromolecules - The Seventh Aharon Katzir-Katchalsky Conference (ed. Balaban, M., Sussman, J.L., Traub, W., Yonath, A.), 597-614 (Balaban ISS, Rehovot and Philadelphia, 1981).

  311. Trifonov, E. N. & Sussman, J. L.
    The pitch of chromatin DNA is reflected in its nucleotide sequence.
    Proc. Natl. Acad. Sci. USA 77, 3816-3820 (1980). [Abstract] [PDF]

  312. Nussinov, R., Sussman, J. L. & Trifonov, E. N.
    MS2 RNA has a potential to form an unusually large number of stable hairpins.
    J. Theor. Biol. 85, 481-486 (1980). [Abstract]

  313. Shoham, M., Yonath, A., Sussman, J. L., Moult, J., Traub, W. & Kalb, A. J.
    The crystal structure of demetallized concanavalin A: the metal-binding region.
    J. Mol. Biol. 131, 137-155 (1979). [Abstract]

  314. Trifonov, E. & Sussman, J. L.
    in Molecular mechanisms of biological recognition (ed. Balaban, M.), 227-232 (Elsevier/North-Holland: Biomedical Press, 1979).

  315. Schevitz, R. W., Podjarny, A. D., Krishnamachari, N., Hughes, J. J., Sigler, P. B. & Sussman, J. L.
    Crystal structure of eukaryotic initiator tRNA.
    Nature 278, 188-190 (1979). [Abstract] [PDF]

  316. Sussman, J. L., Zipori, P., Harel, M., Yonath, A. & Werber, M. M.
    Preliminary X-ray diffraction studies on 2 Fe-Ferredoxin from Halobacterium of the Dead Sea.
    J. Mol. Biol. 134, 375-377 (1979). [Abstract]

  317. Shoham, M., Sussman, J. L., Yonath, A., Moult, J., Traub, W. & Kalb, A. J.
    The effect of binding of metal ions on the three-dimensional structure of demetallized concanavalin A.
    FEBS Lett. 95, 54-56 (1978). [Abstract]

  318. Holbrook, S. R., Sussman, J. L., Warrant, R. W. & Kim, S.-H.
    Crystal structure of yeast phenylalanine transfer RNA. II Structural features and functional implications.
    J. Mol. Biol. 123, 631-660 (1978).

  319. Sussman, J. L. & Trifonov, E. N.
    Possibility of nonkinked packing of DNA in chromatin.
    Proc. Natl. Acad. Sci. USA 75, 103-107 (1978). [Abstract]

  320. Sussman, J. L., Holbrook, S. R., Warrant, R. W., Church, G. M. & Kim, S.-H.
    Crystal structure of yeast phenylalanine transfer RNA. I. crystallographic refinement.
    J. Mol. Biol. 123, 607-630 (1978). [Abstract] [PDF]

  321. Sussman, J. L., Holbrook, S. R., Church, G. M. & Kim, S. H.
    A structure-factor least squares refinement procedure for macromolecular structures using constrained and restrained parameters.
    Acta Cryst A33, 800-804 (1977) . [Abstract] [PDF]

  322. Holbrook, S. R., Sussman, J. L., Warrant, R. W., Church, G. M. & Kim, S.-H.
    RNA-ligand interactions: (I) magnesium binding sites in yeast tRNAPhe.
    Nucl. Acids Res. 4, 2811-2820 (1977). [Abstract][PDF]

  323. Robillard, G. T., Tarr, C. E., Vosman, F. & Sussman, J. L.
    An NMR approach to tRNA tertiary structure in solution.
    Biophys. Chem 6, 291-298 (1977).

  324. Church, G. M., Sussman, J. L. & Kim, S. H.
    Secondary structural complementary between DNA and proteins.
    Proc. Natl. Acad. Sci. USA 74, 1458-1462 (1977). [Abstract][PDF]

  325. Kim, S. H. & Sussman, J. L.
    in Horizons in Biochemistry and Biophysics (ed. Quagliariello), 159-199 (Addison-Wesley Publ. Co., Reading, MA, 1977).

  326. Sussman, J. L. & Kim., S. H.
    Idealized atomic coordinates of yeast phenylalanine transfer RNA.
    Biochem. Biophys. Res. Commun. 68, 89-96 (1976). [Abstract] [PDF]

  327. Sussman, J. L. & Kim, S. H.
    in Environmental Effects on Molecular Structure and Properties (ed. Pullman, B.), 535-545 (D. Reidel Publishing Co., Dordrecht, 1976).

  328. Kim, S. H. & Sussman, J. L.
    π turn is a conformational pattern in RNA loop and bends
    Nature 260, 645-646 (1976).

  329. Sussman, J. L. & Kim, S.H.
    Three-dimensional structure of a transfer RNA in two crystal forms.
    Science 192, 853-858 (1976).

  330. Kim, S. H., Suddath, F. L., Quigley, G. J., McPherson, A., Sussman, J. L., Wang, A. H. J., Seeman, N. C. & Rich, A.
    in Structure and Conformation of Nucleic Acids and Protein-Nucleic Acid Interaction (ed. Sundaralingam, M.), 7-23 (University Park Press, Baltimore, 1975).

  331. Kim, S. H., Sussman, J. L. & Church, G. M.
    in Structure and Conformation of Nucleic Acids and Protein-Nucleic Acid Interaction (ed. Sundaralingam, M.), 571-575 (University Park Press, Baltimore, 1975).

  332. Quigley, G. J., Wang, A. H. J., Seeman, N. C., Suddath, F. L., Rich, A., Sussman, J. L. & Kim, S. H.
    Hydrogen bonding in yeast phenylalanine transfer RNA.
    Proc. Natl. Acad. Sci. USA 72, 4866-4870 (1975). [Abstract]

  333. Kim, S.-H., Suddath, F. L., Quigley, G. J., McPherson, A., Sussman, J. L., Wang, A. H. J., Seeman, N. C. & Rich, A.
    Three-dimensional tertiary structure of yeast phenylalanine transfer RNA.
    Science 185, 435-439 (1974). [Abstract] [PDF]

  334. Kim, S. H., Sussman, J. L., Suddath, F. L., Quigley, G. J., McPherson, A., Wang, A. H. J., Seeman, N. C. & Rich, A.
    The general structure of transfer RNA molecules.
    Proc. Natl. Acad. Sci. USA 71, 4970-4974 (1974).

  335. Barzilay, I., Sussman, J. L. & Lapidot, Y.
    Further studies on the chromatographic behaviour of dinucleoside monophosphates.
    J. Chromatogr. 79, 130-146 (1973).

  336. Sussman, J. L. & Wodak, S. J.
    The crystal structure of fulvine: a pyrrolizidine alkaloid.
    Acta Cryst B29, 2918-2926 (1973). [Abstract] [ PDF]

  337. Sussman, J. L., Barzilay, I., Keren-Zur, M. & Lapidot, Y. br>Correlation of the differences in conformation between 2'-5' and 3'-5' dinucleoside monophosphates with their behaviour on a Sephadex LH-20 column.
    Biochim. Biophys. Acta 308, 189-197 (1973).

  338. Sussman, J. L., Seeman, N. C., Kim, S. H. & Berman, H. M.
    The crystal structure of a naturally occurring dinucleotide phosphate Uridylyl 3',5'-adenosine phosphate. Models for RNA chain folding.
    J. Mol. Biol. 66, 403-421 (1972). [Abstract] [ PDF]

  339. Seeman, N. C., Sussman, J. L., Berman, H. M. & Kim, S. H.
    Nucleic acid conformation: crystal structure of a naturally occurring dinucleoside phosphate (UpA).
    Nature New Biol. 233, 90-92 (1971) [Abstract] [ PDF]