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

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Peter Tompa

Institute of Enzymology

Biological Research Center

Hungarian Academy of Sciences

Budapest

Hungary

[email]@enzim.hu

Name/email consistency: high

 
 
 
 
 
 
 

Affiliation

  • Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary. 2001 - 2009

References

  1. Close encounters of the third kind: disordered domains and the interactions of proteins. Tompa, P., Fuxreiter, M., Oldfield, C.J., Simon, I., Dunker, A.K., Uversky, V.N. Bioessays (2009) [Pubmed]
  2. Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins. Tompa, P. FEBS J. (2009) [Pubmed]
  3. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Tompa, P., Fuxreiter, M. Trends Biochem. Sci. (2008) [Pubmed]
  4. Prevalent structural disorder in E. coli and S. cerevisiae proteomes. Tompa, P., Dosztanyi, Z., Simon, I. J. Proteome Res. (2006) [Pubmed]
  5. Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects. Tompa, P., Bánki, P., Bokor, M., Kamasa, P., Kovács, D., Lasanda, G., Tompa, K. Biophys. J. (2006) [Pubmed]
  6. The interplay between structure and function in intrinsically unstructured proteins. Tompa, P. FEBS Lett. (2005) [Pubmed]
  7. Structural disorder throws new light on moonlighting. Tompa, P., Szász, C., Buday, L. Trends Biochem. Sci. (2005) [Pubmed]
  8. The role of structural disorder in the function of RNA and protein chaperones. Tompa, P., Csermely, P. FASEB J. (2004) [Pubmed]
  9. Intrinsically unstructured proteins evolve by repeat expansion. Tompa, P. Bioessays (2003) [Pubmed]
  10. Calpastatin subdomains A and C are activators of calpain. Tompa, P., Mucsi, Z., Orosz, G., Friedrich, P. J. Biol. Chem. (2002) [Pubmed]
  11. Intrinsically unstructured proteins. Tompa, P. Trends Biochem. Sci. (2002) [Pubmed]
  12. Domain III of calpain is a ca2+-regulated phospholipid-binding domain. Tompa, P., Emori, Y., Sorimachi, H., Suzuki, K., Friedrich, P. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  13. Frequency decoding of fast calcium oscillations by calpain. Tompa, P., Töth-Boconádi, R., Friedrich, P. Cell. Calcium (2001) [Pubmed]
 
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