In the full list below, links take you to PDFs or unchanging Document Object Identifier (DOI) URLs.  Publishers may charge access fees for some, depending on your / institutional subscriptions.  PubMed links will take you to abstracts and either the published form or the pre-print stored at NIH.  Local links are provided for those not otherwise available.

  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. PDF; PubMed: 2878449.
  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. PDF; DOI; PubMed: 3627277.
  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. PDF; PubMed: 2900091.
  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. PDF
  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. PDF; DOI; PubMed: 3681999.
  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. PDF; DOI; PubMed: 3133767.
  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). Laue Crystallography of Macromolecules and Viruses.  In Daresbury Annal. (Warrington, UK, Daresbury Laboratory) pp. 42-46.
  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. PDF; DOI; PubMed: 2555523.
  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. PDF
  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. DOI; PubMed: 1972986.
  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 New Aspects of Positive Strand RNA Viruses, M.A. Brinton, and F.X. Heinz, eds. (Washington, DC: ASM Press).
  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. PDF; DOI; PubMed: 1847215.
  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. PDF; DOI; PubMed: 2006420.
  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. PDF; DOI; PubMed: 1605933.
  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. PDF; DOI; PubMed: 1335081.
  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. DOI; PubMed: 1318726.
  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. PDF; DOI; PubMed: 1616694.
  18. Chapman, M. S. (1993). Mapping the Surface Properties of Macromolecules. Prot. Sci. 2, 459-469. PDF; PubMed: 8384042.
  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. PDF
  20. Chapman, M. S. & Rossmann, M. G. (1993). Structure, Sequence and Function Correlations among Parvoviruses. Virology 194, 491-508. PDF; DOI; PubMed: 8503170.
  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. PDF; DOI; PubMed: 8337843.
  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. PDF; DOI; PubMed: 8383771.
  23. Chapman, M. S. (1994). Sequence Similarity Scores and the Inference of Structure/Function Relationships. Computer Applications in the Biosciences (CABIOS) 10, 111-119. PDF; PubMed: 8019858.
  24. Chapman, M. S. (1995). Restrained Real-Space Macromolecular Atomic Refinement using a New Resolution-Dependent Electron Density Function. Acta Crystallogr. A51, 69-80. PDF; DOI.
  25. Chapman, M. S. & Rossmann, M. G. (1995). Single-stranded DNA-protein interactions in Canine Parvovirus. Structure 3, 151-62. PDF; DOI; PubMed: 7735832.
  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. PDF; DOI; PubMed: 15299756.
  27. 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, 129-39. PDF; DOI; PubMed: 15299734.
  28. 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. PDF; DOI; PubMed: 15299734.
  29. Xie, Q. & Chapman, M. S. (1996). Canine parvovirus capsid structure, analyzed at 2.9 Å resolution. J. Mol. Biol. 264, 497-520. PDF; DOI; PubMed: 8969301.
  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. PDF; PubMed: 9041648.
  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. DOI
  32. Chapman, M. S. & Blanc, E. (1997). Potential use of Real Space Refinement in Protein Structure Determination. Acta Crystallogr. D53, 203-6. PDF; DOI; PubMed: 15299957.
  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. PDF; PubMed: 9449365.
  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. PDF
  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. PDF
  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. PDF
  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. PDF; DOI; PubMed: 9761907.
  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. PDF; PubMed: 9671698.
  39. Chen, Z., Blanc, E. & Chapman, M. S. (1998). Real Space Molecular Dynamics Refinement. Acta Crystallographica D55: 464-8. PDF; DOI; PubMed: 10089356.
  40. Chen, Z., Blanc, E. & Chapman, M. S. (1999). Improved free R-factors for the cross-validation of structures. Acta Crystallographica D55: 219-224. PDF; DOI; PubMed: 10089412.
  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 PDF; DOI; PubMed: 10089314.
  42. Zhou, G., Ellington, W.R. & Chapman, M.S. (2000). Induced Fit in Arginine Kinase. Biophys J 78: 1541-1550. PDF; PubMed: 10692338.
  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. PDF; DOI; PubMed: 11042042.
  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. PDF
  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). PDF;
  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. PDF; DOI; PubMed: 11472093.
  47. Chen, Z., and M.S. Chapman. 2001. Conformational Disorder of Proteins Assessed by Real-Space Molecular Dynamics Refinement. Biophys J 80:1466-1472. PDF;; PubMed: 11222306.
  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. PDF; DOI; PubMed: 11976486.
  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. PDF; DOI; PubMed: 11932258.
  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. PDF; DOI; PubMed: 12021440.
  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. PDF; DOI; PubMed: 12136130.
  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. PDF; DOI; PubMed: 12454458.
  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. PDF; DOI; PubMed: 12493833.
  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. PDF; DOI; PubMed: 12777756.
  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. PDF; DOI; PubMed: 12809609.
  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. PDF; DOI; PubMed: 13677047.
  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. PDF; DOI; PubMed: 12732621.
  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. PDF; DOI; PubMed: 12914845.
  59. Chen, J.Z., Furst, J., Chapman, M.S., and Grigorieff, N. 2003. Low-resolution structure refinement in electron microscopy. J Struct Biol 144: 144-151. PDF; DOI; PubMed: 14643217.
  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. PDF; DOI; PubMed: 14978299.
  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. PDF; DOI; PubMed: 15236576.
  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 PDF; DOI; PubMed: 15488616.
  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. PDF; DOI; PubMed: 19836335.
  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. PDF; DOI; PubMed: 15522352.
  65. Fabiola, F. and Chapman, M.S. (2005) Fitting of High Resolution Structures into Electron Microscopy Reconstruction Images, Structure, 13: 389-400. PDF; DOI; PubMed: 15766540.
  66. 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. PDF; DOI; PubMed: 16034675.
  67. Ruben, E. A., Evanseck, J. D., and Chapman, M. S. (2005) Generalized Anomeric Interpretation of the “High-Energy” N-P Bond in N-Methyl-N’-phosphorylguanidine: Importance of Reinforcing Stereoelectronic Effects in “High-Energy” Phosphoester Bonds, Journal of the American Chemical Society, 127: 17789-17798. PDF; DOI; PubMed: 16351108.
  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), pp109-123. Edward Arnold, Ltd., London. PDF
  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. Edward Arnold, Ltd., London. PDF
  70. Chapman, M. S.  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, pp. 69-94 (2006). PDF
  71. Fabiola, F., Korostelev, A. & Chapman, M. S. Bias in cross-validated free R factors: mitigation of the effects of non-crystallographic symmetry. Acta Crystallogr D Biol Crystallogr, 62: 227-38 (2006). PDF; DOI; PubMed: 16510969.
  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, 179: 190-198.  PDF; DOI; PubMed: 16413215.
  73. Murray, S., Nilsson, C. L., Hare, J. T., Emmett, M. R., Korostelev, A., Ongley, H., Marshall, A. G. & Chapman, M. S. Characterization of the Capsid Protein Glycosylation of Adeno-associated Virus (AAV-2) by High Resolution Mass Spectrometry. Journal of Virology, 80: 6171-6 (2006). PDF; DOI; PubMed: 16731956.
  74. Mitra, K., Schaffitzel, C., Fabiola, F., Chapman, M. S., Ban, N. & Frank, J. Elongation arrest by SecM via a cascade of ribosomal RNA rearrangements. Molecular Cell, 22: 533-43 (2006). PDF; DOI; PubMed: 16713583.
  75. Mitchell, D. A. J., O;Donnel, J., Hare, J. T. & Chapman, M. S. Serotype-Specific Detection During Laboratory Preparation of Adeno-Associated Virus. Journal of Virological Methods, 136: 277-82 (2006). PDF; DOI; PubMed: 16815560.
  76. Asbury, T., Bertram, R., Quine, J. R., Achuthan, S., Chapman, M. S. & Cross, T. A. PIPATH: and Algorithm for Assignment of PISEMA Data. Journal of Magnetic Resonance,183:87-95(2006). PDF; DOI; PubMed: 17292830.
  77. Chapman, M.S.  Normalizing Normal Mode Analysis; Structure, 15: 135-6 (2007). PDF; DOI; PubMed: 17292830.
  78. Ruben, E.A., Chapman, M.S. & Evanseck, J.D.  Hydrogen Bonding Mediated by Key Orbital Interactions Determines Hydration Enthalpy Differences of Phosphate Water Clusters; Journal of Physical Chemistry A, 111: 10804-14 (2007). PDF; DOI; PubMed: 17915844.
  79. Ruben, E.A., M.S. Chapman, and J.D. Evanseck, Anomeric effect in “high energy” phosphate bonds – selective destabilization of the scissile bond and modulation of the exothermicity of hydrolysis; Journal of the American Chemical Society, 130: 3349-58 (2008). PDF; DOI; PubMed: 18302368.
  80. Xie, Q., Ongley, H. M., Hare, J., and Chapman, M. S. (2008). Crystallization and preliminary X-ray structural studies of adeno-associated virus serotype 6. Acta Crystallogr Sect F Struct Biol Cryst Commun 64: 1074-8. PDF; DOI; PubMed: 18997346.
  81. O’Donnell, J., Taylor, K. A., and Chapman, M. S. (2009). Adeno-Associated Virus and its Primary Cellular Receptor – Cryo-EM structure of a Heparin Complex. Virology 385: 434-433. PDF; DOI; PubMed: 19144372.
  82. Lerch, T.F., Q. Xie, H.M. Ongley, J. Hare, and M.S. Chapman, Twinned crystals of adeno-associated virus serotype 3b prove suitable for structural studies. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2009. 65: 177-83. PDF; DOI; PubMed: 19194015.
  83. Boudko, S. P., T. Sasaki, J. Engel, T. F. Lerch, J. Nix, M. S. Chapman, and H. P. Bachinger. 2009. Crystal structure of human collagen XVIII trimerization domain: A novel collagen trimerization Fold. J Mol Biol 392:787-802. PDF; DOI; PubMed: 19631658.
  84. Davulcu, O., P. F. Flynn, M. S. Chapman, and J. J. Skalicky. 2009. Intrinsic domain and loop dynamics commensurate with catalytic turnover in an induced-fit enzyme. Structure 17:1356-67. PDF; DOI; PubMed: 19836335.
  85. Lerch, T. F., Q. Xie, and M. S. Chapman. 2010. The structure of adeno-associated virus serotype 3B (AAV-3B): Insights into receptor binding and immune evasion. Virology, 403: 25-36. PDF; DOI; PubMed: 20444480.
  86. Chapman, M. S., and T. Somasundaram. 2010. De-icing: recovery of Diffraction Intensities in the presence of Ice Rings. Acta Cryst. D., Biol. Cryst. 66: 741-4. PDF; DOI; PubMed: 20516627.
  87. Mitchell, D.A.J., Lerch, T.A., Hare, J.T. & Chapman, M.S. 2010. A pseudo-Plaque method for Infectious Particle Assay and Clonal Isolation of Adeno-associated Virus. J. Virol. Meth., 170: 9-15. PDF; DOI; PubMed:20708035
  88. Niu, X., Brüschweiler-Li, L., Davulcu, O., Skalicky, J.J. Brüschweiler, R. and Chapman, M.S. 2011. Arginine Kinase. Joint Crystallographic & NMR RDC Analyses link Substrate-Associated Motions to Intrinsic Flexibility.  J. Mol. Biol. 405: 479-496. PDF; DOI; PubMed: 21075117.
  89. Whittaker, M., Lerch, T., Kirillova, O., Chapman, M. & Whittaker, J. 2011. Subunit dissociation and metal binding by E. coli apo-manganese superoxide dismutase. Arch Bioch. Biophys 505: 213-225; PDF; DOI; PubMed: 21044611
  90. Wirz, J., Boudko, S., T. Lerch, M. Chapman & H. Bachinger. 2011. Crystal structure of the human collagen XV trimerization domain: A potent trimerizing unit common to multiplexin collagens. Matrix Biol. 30: 9-15. PDF;  DOI;  PubMed: 20932905.
  91. Bush, D. J., Kirillova, O., Clark, S. A., Davulcu, O., Fabiola, F., Xie, Q., Somasundaram, T., Ellington, W. R. & Chapman, M. S. (2011). The structure of lombricine kinase: implications for phosphagen kinase conformational changes. J. Biol. Chem. 286: 9338-9350; PDF; DOI; PubMed: 21212263.
  92. Davulcu, O., Skalicky, J. J. & Chapman, M. S. (2011). Rate-Limiting Domain and Loop Motions in Arginine Kinase. Biochemistry 50: 4011-4018; PDF; DOI; PubMed: 21425868.
  93. Xie, Q., T.F. Lerch, N.L. Meyer & M.S. Chapman (2011). Structure-function analysis of receptor-binding in adeno-associated virus serotype 6 (AAV-6). Virology 420: 10-19; PDF; DOI;  PubMed: 21917284.
  94. Lerch, T.F. & M.S. Chapman (2012). Identification of the heparin binding site on adeno-associated virus serotype 3B (AAV-3B). Virology 423: 6-13; PDF; DOI; PubMed: 22169623.
  95. McCraw, D., J. O’Donnell, K.A. Taylor, S.M. Stagg & M.S. Chapman (2012). Structure of adeno-associated virus-2 in complex with neutralizing monoclonal antibody A20. Virology 431: 40-49. PDF; DOI; PubMed: 22682774.
  96. Lerch, T.F., J. O’Donnell, N.L. Meyer, Q. Xie, K.A. Taylor, S.M. Stagg, and M.S. Chapman (2012), Structure of AAV-DJ, a Retargeted Gene Therapy Vector: Cryo-Electron Microscopy at 4.5Å resolution. Structure 20: 1-11; PDF; DOI;  PubMed: 22727812.
  97. Clark, S. A., Davulcu, O. & Chapman, M. S. (2012). Crystal structures of arginine kinase in complex with ADP, nitrate, and various phosphagen analogs. Bioch. Biophys. Res Comm. 427, 212-217; PDF; DOI; PubMed: 22995310; .
  98. Summerton, J.C., Evanseck, J.D. & Chapman, M.S. (2012). Hyperconjugation-mediated solvent effects in phosphoanhydride bonds. J. Phys. Chem. A, 116: 10209-17; PDF; DOI; PubMed: 23009395;
  99. Boudko, S.P., Y. Ishikawa, T.F. Lerch, J. Nix, M.S. Chapman, and H. Bächinger (2012). Crystal structures of wild-type and mutated cyclophilin B that causes hyperelastosis cutis in the American quarter horse. BMC Research Notes, 2012. 5: 1-6. PDF; DOI; PubMed: 23137129.
  100. Chapman, M.S., A. Trzynka, and B.K. Chapman (2013). Atomic Modeling of cryo-Electron Microscopy Reconstructions – Joint refinement of Model and Imaging Parameters. Journal of Structural Biology, 182: 10-21. PDF; DOI; PubMed: 23376441.
  101. Davulcu, O., Niu, X., Bruschweiler-Li, L., Bruschweiler, R., Skalicky, J. J., and Chapman, M. S. (2013) Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form, Biomol NMR Assign, in press. DOI; PubMed: 23893440.
  102. Zhang, F., Aguilera, J., Beaudet, J., Xie, Q., Lerch, T., Davulcu, O., Colon, W., Chapman, M., Linhardt, R. (2013) Characterization of Interactions between Heparin/Glycosaminoglycan and Adeno-associated Virus. Biochemistry 52: 6275-85.  PDF; DOI; PubMed: 23952613.
  103. Xie, Q., Spilman, M., Meyer, N.L., Lerch, T.F., Stagg, S.M. and Chapman, M.S. (2013) Electron Microscopy Analysis of a Disaccharide Analog complex Reveals Receptor Interactions of Adeno-Associated Virus, J. Struct. Biol. In press. DOI; PubMed: 24036405.
  104. Boudko, S. P., Ishikawa, Y., Nix, J., Chapman, M. S., and Bächinger, H. P. (2014) Structure of human peptidyl-prolyl cis-trans isomerase FKBP22 containing two EF-hand motifs, Protein Science, 23: 67-75.  DOI; PubMed: 24272907.
  105. Stagg, S.M., A.J. Noble, M. Spilman and M.S. Chapman (2014). ResLog plots as an empirical metric of the quality of cryo-EM reconstructions. J. Struct. Biol. 185: 418-26.  DOI; PubMed: 24384117.
  106. Summerton, J.C., Martin, G.M., Evanseck, J.D. and Chapman, M.S. (2014).  Common Hydrogen Bond Interactions in Diverse Phosphoryl Transfer Active Sites. PLoS-One, 9: e108310. DOI; Pubmed: 25238155.
  107. Chapman, B.K., Davulcu, O., Skalicky, J.J., Brűschweiler, R.P. and Chapman, M.S. (2015).  Parsimony in Protein Conformational Change, Structure, 23: 1190-1198. DOI; Pubmed: 26095029
  108. Spear, J.M., Noble, A.J., Xie, Q., Sousa, D.R., Chapman, M.S., and Stagg, S.M. (2015). The influence of frame alignment with dose compensation on the quality of single particle reconstructions. J Struct Biol 192, 196-203. DOI; Pubmed: 26391007
  109. Pillay, S¹., Meyer, N.L.¹, Puschnik, A.S., Davulcu, O., Diep, J., Ishikawa, Y., Jae, L.T., Wosen, J.E., Nagamine, C.M., Chapman, M.S.², and Carette, J.E.² (2016). An essential receptor for adeno-associated virus infection. Nature 530, 108-112. ¹Co-1st / ²corresopnding authors. doi:10.1038/nature16465. DOI;
  110. Godsey, M.H., Davulcu, O., Nix, J., Skalicky, J.J., Brüschweiler, R.P. and Chapman, M.S. (2016). The Sampling of Conformational Dynamics in Ambient-Temperature Crystal Structure of Arginine Kinase, Structure 24: 1658-67.  DOI; doi:10.1016/j/str.2016.07.013
  111. Earley, L.F., Powers, J.M., Adachi, K., Baumgart, J.T., Meyer, N.L., Xie, Q., Chapman, M.S., Nakai, H. (2017). Adeno-Associated Virus Assembly-Activating Protein Is Not an Essential Requirement for Capsid Assembly of AAV Serotypes 4, 5 and 11. J. Virol. 91 (3), in press. DOI; doi:10.1128/JVI.01980-16.
  112. Xie, Q., Noble, A.J., Sousa, D.R., Meyer, N.L., Davulcu, O., Zhang, F., Linhardt, R.J., Stagg, S.M., Chapman, M.S. (2017). The 2.8 Å Electron Microscopy Structure of Adeno-Associated Virus-DJ Bound by a Heparanoid Pentasaccharide. Mol. Ther. Methods Clin. Dev. 5, in press. DOI; doi:10.1016/j.omtm.2017.02.004
  113. Peng,Y.,  Hansen, A.L., Bruschweiler-Li, L.,  Davulcu, O.,  Skalicky, J.J.,  Chapman, M.S. and Brüschweiler, R.P. (2017). The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency that Matches the Catalytic Rate. J. Am. Chem. Soc., 139: 4846-4853; DOI; doi:10.1021/jacs.7b00236.
  114. Davulcu O., Peng Y., Brüschweiler R., Skalicky J.J., Chapman M.S. Elevated μs-ms timescale backbone dynamics in the transition state analog form of arginine kinase. (2017) J. Struct. Biol., 200: 256-66. DOI; doi:10.1016/j.jsb.2017.05.002.
  115. Pillay, S., Zou, W., Cheng, F., Puschnik, A.S., Ganaie, S.S., Deng, X., Wosen, J.E., Davulcu, O., Yan, Z., Engelhardt, J.F., Brown, K.E., Chapman, M.S., Qiu, J. and Carette, J.E. (2017) AAV2 and AAV5 interact with separate domains of the multi-serotype AAV receptor, AAVR. J. Virol., 91: e00391-17; doi:10.1128/JVI.00391-17.
  116. Meyer, N. L., Hu, G., Davulcu, O., Xie, Q., Noble, A. J., Yoshioka, C., Gingerich, D. S., Trzynka, A., David, L., Stagg, S. M. & Chapman, M. S. Structure of the gene therapy vector, adeno-associated virus with its cell receptor, AAVR. eLife 8, e44707 (2019). DOI: 7554/eLife.44707
  117. Meyer, N., Davulcu, O., Xie, Q., Silveria, M., Zane, G. M., Large, E. & Chapman, M. S. Expression and Purification of Adeno-associated Virus Virus-like Particles in a Baculovirus System and AAVR Ectodomain Constructs in E. coli. Bio-protocol 10, e3513 (2020). doi:10.21769/BioProtoc.3513.
  118. Xie, Q., Yoshioka, C. K. & Chapman, M. S. Adeno-Associated Virus (AAV-DJ)-Cryo-EM Structure at 1.56 Å Resolution. Viruses 12: 1194 (2020) doi:10.3390/v12101194.
  119. Silveria, M. A., Large, E. E., Zane, G. M., White, T. A. & Chapman, M. S. The Structure of an AAV5-AAVR Complex at 2.5 Å Resolution: Implications for Cellular Entry and Immune Neutralization of AAV Gene Therapy Vectors. Viruses 12:1326 (2020) doi:10.3390/v12111326.
  120. Large, E. E., Silveria, M. A., Zane, G. M., Weerakoon, O. & Chapman, M. S. Adeno-Associated Virus (AAV) Gene Delivery: Dissecting Molecular Interactions upon Cell Entry. Viruses 13 (2021) doi:10.3390/v13071336.
  121. Meyer, N.L & Chapman, M.S. Adeno-Associated Virus (AAV) Cell Entry: Structural Insights. Trends in Microbiology 30: 432-451 (2022) doi:10.1016/j.tim.2021.09.005.
  122. Stagg, S.L., Yoshioka, C., Davulcu, O. & Chapman, M.S. Cryo-Electron Microscopy of Adeno-Associated Virus. In Cryo-EM in Biology and Materials Research, Danino, D. & Subramaniam, S. Eds., Chemical Reviews, in press (2022) doi:10.1021/acs.chemrev.1c00936.
  123. Hu, Q., Silveria, M.A., Chapman, M.S. and Stagg, S.M. Adeno-associated Virus Receptor-binding: Flexible Domains and Alternative Conformations through cryo-Electron Tomography of AAV2 and AAV5 complexes. J. Virol., in press (2022), doi:10.1128/jvi.00106-22. See also bioRxiv, 2022.2001.2010.475736 (2022); https://doi.org/10.1101/2022.01.10.475736.
  124. Zane, G.M. Silveria, M.A., Meyer, N.L., White, T.A., Duan, R, Zou, X and Chapman, M.S. Cryo-EM Structure of Adeno-associated virus-4 at 2.2 Å resolution. Acta Crystallographica D79: 140-153 (2023) doi: 10.1107/S2059798322012190
  125. Large, E. E., Silveria, M. A., Weerakoon, O., White, T. A. & Chapman, M. S. Cross-species permissivity: structure of a goat adeno-associated virus and its complex with the human receptor, AAVR. J. Virol. 96, e01484-22 (2022) doi: 10.1128/jvi.01484-22.
  126. Large, E. & Chapman, M. S. AAV Receptor complexes and implications for AAV immune neutralization. Front. Microbiol. 14 (2023) doi: 10.3389/fmicb.2023.1116896.

(PubMed search that may include publications since last update, 08/09/23.)