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

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Alexander Wlodawer

Macromolecular Crystallography Laboratory

NCI, Frederick

MD 21702

USA

[email]@ncifcrf.gov

Name/email consistency: high

 
 
 
 
 
 
 

Affiliations

  • Macromolecular Crystallography Laboratory, NCI, Frederick, MD 21702, USA. 2008
  • Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Maryland 21702, USA. 2001 - 2004
  • Macromolecular Structure Laboratory, NCI-Frederick Cancer Research and Development Center, ABL-Basic Research Program 21702, USA. 1997 - 2000

References

  1. Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures. Wlodawer, A., Minor, W., Dauter, Z., Jaskolski, M. FEBS J. (2008) [Pubmed]
  2. Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate. Wlodawer, A., Li, M., Gustchina, A., Oyama, H., Oda, K., Beyer, B.B., Clemente, J., Dunn, B.M. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  3. Crystallographic and biochemical investigations of kumamolisin-As, a serine-carboxyl peptidase with collagenase activity. Wlodawer, A., Li, M., Gustchina, A., Tsuruoka, N., Ashida, M., Minakata, H., Oyama, H., Oda, K., Nishino, T., Nakayama, T. J. Biol. Chem. (2004) [Pubmed]
  4. Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases. Wlodawer, A., Li, M., Gustchina, A., Oyama, H., Dunn, B.M., Oda, K. Acta Biochim. Pol. (2003) [Pubmed]
  5. A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases. Wlodawer, A., Durell, S.R., Li, M., Oyama, H., Oda, K., Dunn, B.M. BMC Struct. Biol. (2003) [Pubmed]
  6. Rational approach to AIDS drug design through structural biology. Wlodawer, A. Annu. Rev. Med. (2002) [Pubmed]
  7. Structure-based design of AIDS drugs and the development of resistance. Wlodawer, A. Vox Sang. (2002) [Pubmed]
  8. Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes. Wlodawer, A., Li, M., Dauter, Z., Gustchina, A., Uchida, K., Oyama, H., Dunn, B.M., Oda, K. Nat. Struct. Biol. (2001) [Pubmed]
  9. Inhibitor complexes of the Pseudomonas serine-carboxyl proteinase. Wlodawer, A., Li, M., Gustchina, A., Dauter, Z., Uchida, K., Oyama, H., Goldfarb, N.E., Dunn, B.M., Oda, K. Biochemistry (2001) [Pubmed]
  10. Structural and biochemical studies of retroviral proteases. Wlodawer, A., Gustchina, A. Biochim. Biophys. Acta (2000) [Pubmed]
  11. Inhibitors of HIV-1 protease: a major success of structure-assisted drug design. Wlodawer, A., Vondrasek, J. Annu. Rev. Biophys. Biomol. Struct (1998) [Pubmed]
  12. Deposition of macromolecular coordinates resulting from crystallographic and NMR studies. Wlodawer, A. Nat. Struct. Biol. (1997) [Pubmed]
 
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