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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Dashuang Shi

Center for Genetic Medicine Research and Department of Integrative Systems Biology

Children's National Medical Center

The George Washington University

Washington

DC, United States of America

[email]@cnmcresearch.org

Name/email consistency: high

 
 
 
 
 
 
 

Affiliation

  • Center for Genetic Medicine Research and Department of Integrative Systems Biology, Children's National Medical Center, The George Washington University, Washington, DC, United States of America. 2006 - 2012

References

  1. Crystal structure and biochemical properties of putrescine carbamoyltransferase from Enterococcus faecalis: Assembly, active site, and allosteric regulation. Shi, D., Yu, X., Zhao, G., Ho, J., Lu, S., Allewell, N.M., Tuchman, M. Proteins (2012) [Pubmed]
  2. A Novel N-acetylglutamate synthase architecture revealed by the crystal structure of the bifunctional enzyme from Maricaulis maris. Shi, D., Li, Y., Cabrera-Luque, J., Jin, Z., Yu, X., Zhao, G., Haskins, N., Allewell, N.M., Tuchman, M. PLoS. ONE (2011) [Pubmed]
  3. The crystal structure of N-acetyl-L-glutamate synthase from Neisseria gonorrhoeae provides insights into mechanisms of catalysis and regulation. Shi, D., Sagar, V., Jin, Z., Yu, X., Caldovic, L., Morizono, H., Allewell, N.M., Tuchman, M. J. Biol. Chem. (2008) [Pubmed]
  4. A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase. Shi, D., Yu, X., Cabrera-Luque, J., Chen, T.Y., Roth, L., Morizono, H., Allewell, N.M., Tuchman, M. Protein Sci. (2007) [Pubmed]
  5. Structure of a novel N-acetyl-L-citrulline deacetylase from Xanthomonas campestris. Shi, D., Yu, X., Roth, L., Tuchman, M., Allewell, N.M. Biophys. Chem. (2007) [Pubmed]
  6. Expression, crystallization and preliminary crystallographic studies of a novel bifunctional N-acetylglutamate synthase/kinase from Xanthomonas campestris homologous to vertebrate N-acetylglutamate synthase. Shi, D., Caldovic, L., Jin, Z., Yu, X., Qu, Q., Roth, L., Morizono, H., Hathout, Y., Allewell, N.M., Tuchman, M. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
  7. Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Shi, D., Yu, X., Roth, L., Morizono, H., Tuchman, M., Allewell, N.M. Proteins (2006) [Pubmed]
  8. Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria. Shi, D., Morizono, H., Yu, X., Roth, L., Caldovic, L., Allewell, N.M., Malamy, M.H., Tuchman, M. J. Biol. Chem. (2005) [Pubmed]
  9. Expression, purification, crystallization and preliminary X-ray crystallographic studies of a novel acetylcitrulline deacetylase from Xanthomonas campestris. Shi, D., Yu, X., Roth, L., Morizono, H., Hathout, Y., Allewell, N.M., Tuchman, M. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (2005) [Pubmed]
 
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