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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). 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.
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 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.
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) 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.
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. Cross-validation with
Over-sampled Structure Factors. 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.
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