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  1. Frank Zucker, P. Christoph Champ, and Ethan A. Merritt (2010). "Validation of crystallographic models containing TLS or other descriptions of anisotropy". Acta Cryst., D66:889-900. DOI:10.1107/S0907444910020421
  2. P. Christoph Champ and Carlos J. Camacho (2007). "FastContact: a free energy scoring tool for protein-protein complex structures". Nucleic Acids Research (Web Issue). DOI:10.1093/nar/gkm326 . [HubMed]
  3. P. Christoph Champ, Tim T. Binnewies, Natasja Nielsen, Guy Zinman, Kristoffer Kiil, Hang Wu, Jon Bohlin, and David W. Ussery (2006). "Genome update: purine strand bias in 280 bacterial chromosomes". Microbiology, 152(3):579-583 DOI:10.1099/mic.0.28637-0 . [HubMed]
  4. Carlos J. Camacho, Ma H, and P. Christoph Champ (2006). "Scoring a diverse set of high-quality docked conformations: A metascore based on electrostatic and desolvation interactions". Proteins, 63(4):868-77 DOI:10.1002/prot.20932 . [HubMed]
  5. P. Christoph Champ, Sandor Maurice, Jeffery M. Vargason, Tracy Camp, and P. Shing Ho (2004). "Distributions of Z-DNA and nuclear factor I in human chromosome 22: a model for coupled transcriptional regulation". Nucleic Acids Research, 32(22):6501-6510 DOI:10.1093/nar/gkh988 . [HubMed] (The Online server of ZHunt can be found here)


  • Camacho CJ, Zhang C (2005). "FastContact: rapid estimate of contact and binding free energies". Bioinformatics, 21(10):2534-2536; DOI:10.1093/bioinformatics/bti322 .


Note: The following is an incomplete list.

  1. Edwards SF, Siritoc M, Krahec R, Sinden RR (2009). "A Z-DNA sequence reduces slipped-strand structure formation in the myotonic dystrophy type 2 (CCTG).(CAGG) repeat". PNAS, 106(9):3270-327. DOI:10.1073/pnas.0807699106
  2. Ho PS (2008). "Thermogenomics: Thermodynamic-based approaches to genomic analyses of DNA structure". Methods, [Epub ahead of print]. PMID: 18848994. DOI:10.1016/j.ymeth.2008.09.007
  3. Lee W, Tillo D, Bray N, Morse RH, Davis RW, Hughes TR, Nislow C (2007). "A high-resolution atlas of nucleosome occupancy in yeast". Nature Genetics, 39:1235:1244. DOI:10.1038/ng2117
  4. Kulisha VV, Heng L, Dröge P (2007). "Z-DNA-induced super-transport of energy within genomes". Physica A: Statistical Mechanics and its Applications, 384(2):733-738. DOI:10.1016/j.physa.2007.06.023
  5. Kouzine F, Levens D (2007). "Supercoil-driven DNA structures regulate genetic transactions". Frontiers in Bioscience, 12:4409-4423.
  6. Khuu P, Sandor M, DeYoung J, Ho PS (2007). "Phylogenomic analysis of the emergence of GC-rich transcription elements". PNAS, 104(42):16528-16533. DOI:10.1073/pnas.0707203104
  7. Yoshida N, Amanai M, Fukui T, Kajikawa E, Brahmajosyula M, Iwahori A, Nakano Y, Shoji S, Diebold J, Hessel H, Huss R, Perry ACF (2007). "Broad, ectopic expression of the sperm protein PLCZ1 induces parthenogenesis and ovarian tumours in mice". Development, 134:3941-3952. DOI:10.1242/10.1242/dev.007930
  8. Lorenzen S, Zhang Y (2007). Identification of near-native structures by clustering protein docking conformations. Proteins: Structure, Function, and Bioinformatics, 68(1):187-194; DOI:10.1002/prot.21442 .
  9. Mobley DL, Dumont É, Chodera JD, Dill KA (2007). "Comparison of Charge Models for Fixed-Charge Force Fields: Small-Molecule Hydration Free Energies in Explicit Solvent". J Phys Chem B, 111(9):2242-2254. DOI:10.1021/jp0667442
  10. Panpan Z, Lijuan W, Wenyuan Q (2006). The junction between B-DNA and Z-DNA. Chemistry, 69(11):822-825.
  11. Bala Gupta V, Hegde, ML, Jagnnathan Rao KS (2006). Role of Protein Conformational Dynamics and DNA Integrity in Relevance to Neuronal Cell Death in Neurodegeneration. Current Alzheimer Research, 3(4):297-309(13); DOI:10.2174/156720506778249452 .
  12. Gajecka M, Pavlicek A, Glotzbach CD, Ballif BC, Jarmuz M, Jurka J, Shaffer LG (2006). Identification of sequence motifs at the breakpoint junctions in three t(1;9)(p36.3;q34) and delineation of mechanisms involved in generating balanced translocations. J Human Genetics, 120(4):519-526; DOI:10.1007/s00439-006-0222-1 .
  13. Morohashi N, Yamamoto Y, Kuwana S, Morita W, Shindo H, Mitchell AP, Shimizu M (2006). Effect of Sequence-Directed Nucleosome Disruption on Cell-Type-Specific Repression by α2/Mcm1 in the Yeast Genome. Eukaryotic Cell, 5(11):1925-1933. DOI:10.1128/EC.00105-06
  14. Kastenholz MA, Schwartz TU, Hunenberger PH (2006). The transition between the B and Z conformations of DNA investigated by targeted molecular dynamics simulations with explicit solvation. Biophys J, 91:2976-2990.
  15. Liu H, Mulholland N, Fu H, Zhao K (2006). Cooperative activity of BRG1 and Z-DNA formation in chromatin remodeling. Mol Cell Biol, 26(7):2550-9.
  16. Quyen DV, Kim KK, Kim YG (2006). Sequence-dependent kinetic behavior of protein-induced B- to Z-DNA transition. Bulletin of the Korean Chemical Society, 27(7):1071-1074.
  17. Ha SC, Lowenhaupt K, Rich A, Kim YG, Kim KK (2005). Crystal structure of a junction between B-DNA and Z-DNA reveals two extruded bases. Nature, 437:1183-1186.
  18. Kwon JA, Rich A (2005). Biological function of the vaccinia virus Z-DNA-binding protein E3L: Gene transactivation and antiapoptotic activity in HeLa cells. Proc Natl Acad Sci USA, 102:12759-12764.


  title={{Distributions of Z-DNA and nuclear factor I in human chromosome 22: a model for coupled transcriptional regulation}},
  author={Champ, P.C. and Maurice, S. and Vargason, J.M. and Camp, T. and Ho, P.S.},
  journal={Nucleic Acids Research},
  publisher={Oxford Univ Press}
  title={{Genome update: purine strand bias in 280 bacterial genomes}},
  author={Champ, P.C. and Binnewies, T.T. and Nielsen, N. and Zinman, G. and Kiil, K. and Wu, H. and Bohlin, J. and Ussery, D.W.},
  publisher={Soc General Microbiol}

  title={{Scoring a Diverse Set of High-Quality Docked Conformations: A Metascore Based on Electrostatic and Desolvation Interactions}},
  author={Camacho, C.J. and Ma, H. and Champ, P.C.},
  journal={PROTEINS: Structure, Function, and Bioinformatics},

@article{P.Christoph Champ05302007,
  author = {Champ, P. Christoph and Camacho, Carlos J.},
  title = {{FastContact: a free energy scoring tool for protein-protein complex structures}},
  journal = {Nucl. Acids Res.},
  volume = {},
  number = {},
  pages = {gkm326},
  doi = {10.1093/nar/gkm326},
  year = {2007},
  abstract = {FastContact' is a server that estimates the direct electrostatic and desolvation interaction free energy between two proteins in units of kcal/mol. Users submit two proteins in PDB format, and the output is emailed back to the user in three files: one output file, and the two processed proteins. Besides the electrostatic and desolvation free energy, the server reports residue contact free energies that rapidly highlight the hotspots of the interaction and evaluates the van der Waals interaction using CHARMm. Response time is[~] 1 min. The server has been successfully tested and validated, scoring refined complex structures and blind sets of docking decoys, as well as proven useful predicting protein interactions.  FastContact' offers unique capabilities from biophysical insights to scoring and identifying important contacts.
  URL = {http://nar.oxfordjournals.org/cgi/content/abstract/gkm326v1},
  eprint = {http://nar.oxfordjournals.org/cgi/reprint/gkm326v1.pdf}