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

Amina S. Woods

Structural Biology Unit

Cellular Neurobiology Branch


NIH, Baltimore



Name/email consistency: high



  • Structural Biology Unit, Cellular Neurobiology Branch, NIDA IRP, NIH, Baltimore, USA. 2010
  • National Institute on Drug Abuse, IRP, NIH, DHHS, Baltimore, MD 21224, USA. 2001 - 2008
  • NIDA IRP, NIH, Baltimore, MD 21224, USA. 2003 - 2008
  • NIDA IRP, NIH, 5500 Nathan Shock Drive, Baltimore, USA. 2007
  • The National Institute on Drug Abuse, Intramural Research Program, National Institutes of Health, 5500 Nathan Shock Drive, USA. 2003 - 2006
  • Chemistry and Drug Metabolism, NIDA Intramural Research Program, NIDA, NIH, Baltimore, Maryland 21224, USA. 2001 - 2002


  1. The dopamine D(4) receptor, the ultimate disordered protein. Woods, A.S. J. Recept. Signal Transduct. Res. (2010) [Pubmed]
  2. How calmodulin interacts with the adenosine A(2A) and the dopamine D(2) receptors. Woods, A.S., Marcellino, D., Jackson, S.N., Franco, R., Ferré, S., Agnati, L.F., Fuxe, K. J. Proteome Res. (2008) [Pubmed]
  3. Amazing stability of phosphate-quaternary amine interactions. Woods, A.S., Moyer, S.C., Jackson, S.N. J. Proteome Res. (2008) [Pubmed]
  4. Sulfation, the up-and-coming post-translational modification: its role and mechanism in protein-protein interaction. Woods, A.S., Wang, H.Y., Jackson, S.N. J. Proteome Res. (2007) [Pubmed]
  5. A snapshot of tissue glycerolipids. Woods, A.S., Wang, H.Y., Jackson, S.N. Curr. Pharm. Des. (2007) [Pubmed]
  6. Decoy peptides that bind dynorphin noncovalently prevent NMDA receptor-mediated neurotoxicity. Woods, A.S., Kaminski, R., Oz, M., Wang, Y., Hauser, K., Goody, R., Wang, H.Y., Jackson, S.N., Zeitz, P., Zeitz, K.P., Zolkowska, D., Schepers, R., Nold, M., Danielson, J., Gräslund, A., Vukojevic, V., Bakalkin, G., Basbaum, A., Shippenberg, T. J. Proteome Res. (2006) [Pubmed]
  7. IR-MALDI-LDI combined with ion mobility orthogonal time-of-flight mass spectrometry. Woods, A.S., Ugarov, M., Jackson, S.N., Egan, T., Wang, H.Y., Murray, K.K., Schultz, J.A. J. Proteome Res. (2006) [Pubmed]
  8. Brain tissue lipidomics: direct probing using matrix-assisted laser desorption/ionization mass spectrometry. Woods, A.S., Jackson, S.N. AAPS. J (2006) [Pubmed]
  9. Role of electrostatic interaction in receptor-receptor heteromerization. Woods, A.S., Ciruela, F., Fuxe, K., Agnati, L.F., Lluis, C., Franco, R., Ferré, S. J. Mol. Neurosci. (2005) [Pubmed]
  10. Amazing stability of the arginine-phosphate electrostatic interaction. Woods, A.S., Ferré, S. J. Proteome Res. (2005) [Pubmed]
  11. Lipid/peptide/nucleotide separation with MALDI-ion mobility-TOF MS. Woods, A.S., Ugarov, M., Egan, T., Koomen, J., Gillig, K.J., Fuhrer, K., Gonin, M., Schultz, J.A. Anal. Chem. (2004) [Pubmed]
  12. The mighty arginine, the stable quaternary amines, the powerful aromatics, and the aggressive phosphate: their role in the noncovalent minuet. Woods, A.S. J. Proteome Res. (2004) [Pubmed]
  13. Interaction of chlorisondamine with the neuronal nicotinic acetylcholine receptor. Woods, A.S., Moyer, S.C., Wang, H.Y., Wise, R.A. J. Proteome Res. (2003) [Pubmed]
  14. Angiotensin II-acetylcholine noncovalent complexes analyzed with MALDI-ion mobility-TOF MS. Woods, A.S., Fuhrer, K., Gonin, M., Egan, T., Ugarov, M., Gillig, K.J., Schultz, J.A. J. Biomol. Tech (2003) [Pubmed]
  15. A study of peptide-peptide interactions using MALDI ion mobility o-TOF and ESI mass spectrometry. Woods, A.S., Koomen, J.M., Ruotolo, B.T., Gillig, K.J., Russel, D.H., Fuhrer, K., Gonin, M., Egan, T.F., Schultz, J.A. J. Am. Soc. Mass Spectrom. (2002) [Pubmed]
  16. A study of peptide--peptide interaction by matrix-assisted laser desorption/ionization. Woods, A.S., Huestis, M.A. J. Am. Soc. Mass Spectrom. (2001) [Pubmed]
  17. A direct chemical interaction between dynorphin and excitatory amino acids. Woods, A., Zangen, A. Neurochem. Res. (2001) [Pubmed]
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