Publications

PubMed Listing (with available abstracts / text)

  1. Chapman, M. S., Smith, W. W., Suh, S. W., Cascio, D., Howard, A., Hamlin, R., Xuong, N. H. & Eisenberg, D. (1986). Structural studies of RuBisCO from tobacco. Phil. Trans. Roy. Soc. Lond. B313, 367-378.
  2. Chapman, M., Suh, S. W., Cascio, D., Smith, W. W. & Eisenberg, D. (1987). Sliding-layer conformational change limited by quaternary structure in plant RuBisCO. Nature 329, 354-356.
  3. Eisenberg, D., Almassy, R. J., Janson, C. A., Chapman, M. S., Suh, S. W., Cascio, D. & Smith, W. W. (1987). Some Evolutionary Relationships of the Primary Biological Catalysts Glutamine Synthetase and RuBisCO. Cold Spr. Har. Symp. Quant. Biol. LII, 483-90.
  4. Eisenberg, D., Chapman, M. S., Suh, S. W., Cascio, D. & Smith, W. W. (1987). The Path of the Polypeptide Backbone of Ribulose-1,-5-bis-phosphate from Nicotiana tabacum. In International Workshop on Ribulose-1,-5-bis-phosphate carboxylase-oxygenase (Bohnert, H. J. & Jensen, R. G., eds.). University of Arizona Press, Tuscon, AZ.
  5. Suh, S. W., Cascio, D., Chapman, M. S. & Eisenberg, D. S. (1987). A Crystal Form of Ribulose-1,-5-bis-phosphate Carboxylase--Oxygenase from Nicotiana tabacum in the Activated state. J. Mol. Biol. 197, 363-365.
  6. Chapman, M. S., Suh, S. W., Curmi, P. M. G., Cascio, D., Smith, W. W. & Eisenberg, D. S. (1988). Tertiary Structure of Plant RuBisCO: Domains and their Contacts. Science 241, 71-74.
  7. Hajdu, J., Clifton, I. J., Hadfield, A., Howell, P. L., Almo, S. C., Petsko, G. A., Greenhough, T. J., Shrive, A. K., Campbell, J. W., Parson, M., Harrison, S. C., Liddington, R. C., Rossmann, M. G. & Chapman, M. (1989). Daresbury Annal.
  8. Kim, S., Smith, T. J., Chapman, M. S., Rossmann, M. G., Pevear, D. C., Dutko, F. J., Felock, P. J., Diana, G. D. & McKinlay, M. A. (1989). Crystal Structure of Human Rhinovirus Serotype 1A (HRV1A). J. Mol. Biol. 210, 91-111.
  9. Chapman, M. S., Giranda, V. L. & Rossmann, M. G. (1990). The Structures of Human Rhinovirus and Mengo Virus: Relevance to Function and Drug Design. Sem. Virol. 1, 413-27.
  10. Giranda, V. L., Chapman, M. S. & Rossmann, M. G. (1990). Modelling of the Human Intercellular Adhesion Molecule-1, the Human Rhinovirus Major Group Receptor. Proteins 7, 227-33.
  11. Giranda, V. L., Chapman, M. S., Rossmann, M. G., Staunton, D. & Springer, T. A. (1990). Modelling of the C1 Intercellular Adhesion Molecule 1 (ICAM-1), the Human Rhinovirus Major Group Receptor. In International Symposium on Positive Strand RNA Viruses, Vienna, Austria.
  12. Chapman, M. S., Minor, I., Rossmann, M. G., Diana, G. D. & Andries, K. (1991). Human rhinovirus 14 complexed with antiviral compound R 61837. J. Mol. Biol. 217, 455-63.
  13. Tsao, J., Chapman, M. S., Agbandje, M., Keller, W., Smith, K., Wu, H., Luo, M., Smith, T. J., Rossmann, M. G., Compans, R. W. & Parrish, C. (1991). The Three-Dimensional Structure of Canine Parvovirus and its Functional Implications. Science 251, 1456-1464.
  14. Chapman, M. S., Tsao, J. & Rossmann, M. G. (1992). Ab initio Phase Determination for Spherical Viruses: Parameter Determination for Spherical Shell Models. Acta Crystallogr. A48, 301-312.
  15. Mallamo, J. P., Diana, G. D., Pevear, D. C., Dutko, F. J., Chapman, M. S., Kim, K. H., Minor, I., Oliveira, M. & Rossmann, M. G. (1992). Conformationally Restricted Analogues of Disoxaril: A comparison of the Activity against Human Rhinovirus Type 14 and 1A. J. Med. Chem. 35, 4690-4695.
  16. Tsao, J., Chapman, M. S. & Rossmann, M. G. (1992). Ab initio Phase Determination for Viruses with High Symmetry: A Feasibility Study. Acta Crystallogr. A48, 293-301.
  17. Tsao, J., Chapman, M. S., Wu, H., Agbandje, M., Keller, W. & Rossmann, M. G. (1992). Structure Determination of Monoclinic Canine Parvovirus. Acta Crystallogr. B48, 75-88.
  18. Chapman, M. S. (1993). Mapping the Surface Properties of Macromolecules. Prot. Sci. 2, 459-469.
  19. Chapman, M. S., Kim, K. H. & Rossmann, M. G. (1993). Structural Comparisons of Several Antiviral Agents Complexed with Human Rhinoviruses of Different Serotypes. Antiviral News 1, 53-53.
  20. Chapman, M. S. & Rossmann, M. G. (1993). Structure, Sequence and Function Correlations among Parvoviruses. Virology 194, 491-508.
  21. Chapman, M. S. & Rossmann, M. G. (1993). Comparison of Surface Properties of Picornaviruses: Strategies for hiding the Receptor Site form Immune Surveillance. Virology 195, 745-765.
  22. Kim, K. H., Willingmann, P., Gong, Z. X., Kremer, M. J., Chapman, M. S., Minor, I., Oliviera, M. A., Rossmann, M. G., Andries, K., Diana, G. D., Dutko, F. J., McKinlay, M. A. & Pevear, D. C. (1993). A comparison of the anti-rhinoviral drug binding pocket in HRV14 and HRV1A. J. Mol. Biol. 230, 206-227.
  23. Chapman, M. S. (1994). Sequence Similarity Scores and the Inference of Structure/Function Relationships. Computer Applications in the Biosciences (CABIOS) 10, 111-119.
  24. Chapman, M. S. (1995). Restrained Real-Space Macromolecular Atomic Refinement using a New Resolution-Dependent Electron Density Function. Acta Crystallogr. A51, 69-80.
  25. Chapman, M. S. & Rossmann, M. G. (1995). Single-stranded DNA-protein interactions in Canine Parvovirus. Structure 3, 151-62.
  26. Hadfield, A., Hajdu, J., Chapman, M. S. & Rossmann, M. G. (1995). Laue Diffraction Studies of Human Rhinovirus 14 and Canine Parvovirus. Acta Crystallogr. D51, 859-70.
  27. Chapman, M. S. (1996). Cross-validation R-factors and their use in comparing the qualities of refined models for the DNA-containing and empty capsids of canine parvovirus. Acta Crystallogr. D52, 140-2.
  28. Chapman, M. S. & Rossmann, M. G. (1996). Structural Refinement of the DNA-containing Capsid of Canine Parvovirus using RSRef, a Resolution-Dependent Stereochemically Restrained Real-Space Refinement Method. Acta Crystallogr. D52, 129-42.
  29. Xie, Q. & Chapman, M. S. (1996). Canine parvovirus capsid structure, analyzed at 2.9 Å resolution. J. Mol. Biol. 264, 497-520.
  30. Zhou, G., Parthasarathy, G., Somasunduram, T., Ables, A., Roy, L., Strong, S. J., Ellington, W. R. & Chapman, M. S. (1997). Expression, Purification from Inclusion Bodies, and Crystal Characterization of Transition State Analog Complex of Arginine Kinase: a Model for Studying Phosphagen Kinases. Prot. Sci. 6, 444-9.
  31. Blanc, E. & Chapman, M. S. (1997). RSRef: Interactive real-space refinement with stereochemical restraints for use during model-building. J. Appl. Cryst. 30: 566-7.
  32. Chapman, M. S. & Blanc, E. (1997). Potential use of Real Space Refinement in Protein Structure Determination. Acta Crystallogr. D53, 203-6.
  33. Chapman, M. S. (1998). Watching "One's" Ps and Qs: Promiscuity, Plasticity and Quasi-Equivalence in a T=1 virus. Biophys. J. 74: 639-44.
  34. Chapman, M. S. (1998). Introduction to the use of non-crystallographic symmetry in phasing. In Direct Methods for Solving Macromolecular Structures (Fortier, S., ed.), pp. 99-108. Kluwer, Dortrecht, Netherlands.
  35. Chapman, M. S., Blanc, E., Johnson, J. E., McKenna, R., Munshi, S., Rossmann, M. G. & Tsao, J. (1998). Use of non-crystallographic symmetry for ab initio phasing of virus structures. In Direct Methods for Solving Macromolecular Structures (Fortier, S., ed.), pp. 433-442. Kluwer, Dortrecht, Netherlands.
  36. Blanc, E., Chen, Z. & Chapman, M. S. (1998). Real-Space Refinement Using RSRef. In Direct Methods for Solving Macromolecular Structures (Fortier, S., ed.), pp. 513-9. Kluwer, Dortrecht, Netherlands.
  37. Zhou, G., Wang, J., Blanc, E. & Chapman, M. S. (1998). Determination of the Relative Precision of Atoms in a Macromolecular Structure. Acta Crystallographica D54, 391-9.
  38. Zhou, G., Somasundaram, T., Blanc, E., Parthsarathy, G., Ellington, W. R. & Chapman, M. S. (1998). Transition state structure of arginine kinase: Implications for catalysis of bimolecular reactions. Proceedings of the National Academy of Sciences, USA 95, 8449-54.
  39. Chen, Z., Blanc, E. & Chapman, M. S. (1998). Real Space Molecular Dynamics Refinement. Acta Crystallographica D55: 464-8.
  40. Chen, Z., Blanc, E. & Chapman, M. S. (1999). Improved free R-factors for the cross-validation of structures. Acta Crystallographica D55: 219-224.
  41. Zhou, G., Somasundaram, T., Blanc, E. & Chapman, M. S. (1999). Critical Initial Real Space Refinement in the Structure Determination of Arginine Kinase. Acta Crystallographica D55: 835-845
  42. Zhou, G., Ellington, W.R. & Chapman, M.S. (2000). Induced Fit in Arginine Kinase. Biophys J 78: 1541-1550.
  43. Bertram, R., J. R. Quine, M. S. Chapman and T. A. Cross (2000). “Atomic Refinement Using Orientational Restraints from Solid-State NMR.” J. Magnetic Resonance, 147: 9-16.
  44. Blanc, E., G. Zhou, Z. Chen, Q. Xie, J. Tang, J. Wang, and M.S. Chapman. 2001. Electron Density Representation and Real Space Refinement (New tricks from an old dog). In: Watenpaugh, K.D., and P.E. Bourne, editors. Crystallographic Computing 7: Proceedings of the IUCr Macromolecular Computing School, 1996. Corby, UK: Oxford University Press..
  45. Gerstein, M., F. Richards, M.S. Chapman, and M. Connolly. 2001. Protein surfaces and volumes: measurement and use. In: Rossmann, M.G., and E. Arnold, editors. International Tables for Crystallography. Crystallography of Biological Molecules. Dortrecht, Netherlands: Kluwer Academic Publishers. p 531-45 (Cpt. 22.1).
  46. Chen, L.F., E. Blanc, M.S. Chapman, and K.A. Taylor. 2001. Real space refinement of acto-myosin structures from sectioned muscle. J Struct Biol 133:221-32.
  47. Chen, Z., and M.S. Chapman. 2001. Conformational Disorder of Proteins Assessed by Real-Space Molecular Dynamics Refinement. Biophys J 80:1466-1472.
  48. Korostelev, A., Bertram, R., and Chapman, M.S. 2002. Simulated Annealing Real-Space Refinement as a Tool in Model Building. Acta Crystallogr. D58: 761-767.
  49. Bubb, M.R., Govindasamy, L., Yarmola, E.G., Vorobiev, S.M., Almo, S.C., Somasundaram, T., Chapman, M.S., Agbandje-McKenna, M., and McKenna, R. 2002. Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-A resolution. J Biol Chem 277: 20999-21006.
  50. Fabiola, F., Bertram, R., Korostelev, A., and Chapman, M.S. 2002. An improved hydrogen bond potential: impact on medium resolution protein structures. Protein Sci 11: 1415-1423.
  51. Xie, Q., Bu, W., Bhatia, S., Hare, J., Somasundaram, T., Azzi, A., and Chapman, M.S. 2002. The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapy. Proc Natl Acad Sci U S A 99: 10405-10410.
  52. Yousef, M.S., Fabiola, F., Gattis, J., Somasundaram, T., and Chapman, M.S. 2002. Refinement of Arginine Kinase Transition State Analogue Complex at 1.2 Å resolution; mechanistic insights. Acta Crystallogr. D. Biol. Crystallogr. 58: 2009-2017.
  53. Yousef, M.S., Clark, S., Pruett, P.S., Somasundaram, T., Ellington, W.R., and Chapman, M.S. 2003. Induced Fit in Guanidino Kinases - Comparison of Substrate-free and Transition State Analog Structures of Arginine Kinase. Protein Sci.  12: 103-111.
  54. Xie, Q., T. Somasundaram, S. Bhatia, W. Bu, and M.S. Chapman, Structure determination of adeno-associated virus 2: three complete virus particles per asymmetric unit. Acta Crystallogr D Biol Crystallogr, 2003. 59: 959-70.
  55. Gao, H., J. Sengupta, M. Valle, A. Korostelev, N. Eswar, S.M. Stagg, P. VanRoey, R.K. Agrawal, S.C. Harvey, A. Sali, M. Chapman, and J. Frank, Study of the Structural Dynamics of the E. coli 70S Ribosome Using Real Space Refinement. Cell, 2003. 113: 789-801.
  56. Chapman, M.S., and Liljas, L. 2003. Structural Folds of Viral Proteins. In Advances in Protein Chemistry. (eds. W. Chiu, and J.E. Johnson), 64: 125-196. Academic Press.
  57. Pruett, P.S., A. Azzi, S.A. Clark, M. Yousef, J.L. Gattis, T. Somasundaram, W.R. Ellington, and M.S. Chapman, The putative catalytic bases have, at most, an accessory role in the mechanism of arginine kinase. J Biol Chem, 2003. 29: 26952-7.
  58. Bertram, R., T. Asbury, F. Fabiola, J. R. Quine, T. A. Cross and M. S. Chapman (2003). "Atomic Refinement with Correlated Solid-State NMR Restraints." Journal of Magnetic Resonance, 2003. 163: 300-9.
  59. Chen, J.Z, Furst, J., Chapman, M.S., Grigorieff, N. 2003.  Low Resolution Refinement in Electron Microscopy.  Journal of Structural Biology, 144: 144-151.
  60. Azzi, A., Clark, S.A., Ellington, W.R., and Chapman, M.S. 2004. The Role of Phosphagen Specificity Loops in Arginine Kinase. Protein Sci. 13: 575-585.
  61. Gattis, J. L., E. Ruben, Fenley, M.O., Ellington, W.R., and Chapman, M.S (2004). "The active site cysteine of arginine kinase - structural and functional analysis of partially active mutants." Biochemistry, 43: 8680-8689.
  62. Xie, Q., Hare, J., Bu, W., Jackson, W., Turnigan, J., and Chapman, M. S. (2004) Large-scale Preparation, Purification and Crystallization of Wild-type Adeno-Associated Virus 2, Journal of Virological Methods, 122: 17-27
  63. Korostelev, A., Fenley, M. O., and Chapman, M. S. (2004) Impact of a Poisson-Boltzmann Electrostatic Restraint on Protein Structures Refined at Medium Resolution, Acta Crystallographica D, Biological Crystallography, 60: 1786-1794.
  64. Quine, J.R., Cross, T.A., Chapman, M.S. and Bertram, R., 2004. Mathematical Aspects of protein structure determination with NMR orientational restraints. Bull. Math. Biol. 66: 1705-1730.
  65. 65. Fabiola, F. and Chapman, M.S. (2005) Fitting of High Resolution Structures into Electron Miscroscopy Reconstruction Images, Structure, 13: 389-400.
  66. 69. Davulcu, O., S. A. Clark, M. S. Chapman and J. J. Skalicky (2005). "Main chain 1H, 13C, and 15N resonance assignments of the 42 kDa enzyme arginine kinase." Journal of Biological NMR, 32: 178.
  67. Ruben, E. A., Evanseck, J. D., and Chapman, M. S. (2006) A theoretical study of N-phosphoryl-guanidinium tautomers - influences of hyperconjugation on N-P bond strength, Journal of the American Chemical Society, 127: 17789-17798.
  68. Chapman, M.S., and Agbandje-McKenna, M. 2006. Atomic structure of viral particles. In Parvoviruses. (eds. M.E. Bloom, S.F. Cotmore, R.M. Linden, C.R. Parrish, and J.R. Kerr), pp107-123. Hodder Arnold, London.
  69. Agbandje-McKenna, M., and Chapman, M.S. 2006. Structure-function relationships. In Parvoviruses. (eds. M.E. Bloom, S.F. Cotmore, R.M. Linden, C.R. Parrish, and J.R. Kerr), pp125-139. Hodder Arnold, London.
  70. Chapman, M. S. (2006) The Structural Enzymology of Arginine Kinase and its Implications for Creatine Kinase, in Creatine kinase biochemistry, physiology, structure and function (Vial, C., Ed.), NovaScience, New York, in press.
  71. Fabiola, F., Korostelev, A. & Chapman, M. S. Cross-validation with Over-sampled Structure Factors. Acta Crystallogr D Biol Crystallogr, accepted (2006).
  72. Quine, J.R., Achuthan, S., Asbury, T., Bertram, R., Chapman, M.S., Hu, J. and Cross, T.A., 2006. Intensity and mosaic spread analysis from PISEMA tensors in solid state NMR. Journal of Magnetic Resonance, accepted.
  73. Blanc, E., Giranda, V., Alexander, R.S., Pevear, D.C., Grorke, J., Gattis, J., and Chapman, M.S. 2004. The 2 Å Structure of Human Rhino Virus 50. Structure in preparation.

Last updated 12/22/05