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Different sequence environments of cysteines and half cystines in proteins. Application to predict disulfide forming residues.
Fiser A, Cserzö M, Tüdös E, Simon I. Fiser A, et al. Among authors: tudos e. FEBS Lett. 1992 May 11;302(2):117-20. doi: 10.1016/0014-5793(92)80419-h. FEBS Lett. 1992. PMID: 1633841 Free article.
A word of caution about biological inference - Revisiting cysteine covalent state predictions.
Tüdős E, Mészáros B, Fiser A, Simon I. Tüdős E, et al. FEBS Open Bio. 2014 Mar 12;4:310-4. doi: 10.1016/j.fob.2014.03.003. eCollection 2014. FEBS Open Bio. 2014. PMID: 24918043 Free PMC article.
Noncovalent cross-links in context with other structural and functional elements of proteins.
Tüdos E, Fiser A, Simon A, Dosztányi Z, Fuxreiter M, Magyar C, Simon I. Tüdos E, et al. J Chem Inf Comput Sci. 2004 Mar-Apr;44(2):347-51. doi: 10.1021/ci030409i. J Chem Inf Comput Sci. 2004. PMID: 15032510 Review.
Functionally and structurally relevant residues of enzymes: are they segregated or overlapping?
Magyar C, Tüdos E, Simon I. Magyar C, et al. Among authors: tudos e. FEBS Lett. 2004 Jun 4;567(2-3):239-42. doi: 10.1016/j.febslet.2004.04.070. FEBS Lett. 2004. PMID: 15178329 Free article.
Different sequence environments of amino acid residues involved and not involved in long-range interactions in proteins.
Tüdös E, Fiser A, Simon I. Tüdös E, et al. Int J Pept Protein Res. 1994 Feb;43(2):205-8. doi: 10.1111/j.1399-3011.1994.tb00524.x. Int J Pept Protein Res. 1994. PMID: 8200741
Predicting isomorphic residue replacements for protein design.
Tüdös E, Cserzö M, Simon I. Tüdös E, et al. Int J Pept Protein Res. 1990 Sep;36(3):236-9. doi: 10.1111/j.1399-3011.1990.tb00973.x. Int J Pept Protein Res. 1990. PMID: 2279846
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