Pellegrini, M., Renda, M.E. and Vecchio, A. (2012) Ab Initio Detection of Fuzzy Amino Acid Tandem Repeats in Protein Sequences. BMC Bioinformatics, 13, S8.
http://dx.doi.org/10.1186/1471-2105-13-S3-S8

has been cited by the following article:

• TITLE: Hidden Sequence Repeats: Additional Evidence for the Origin of TIM-Barrel Family

  AUTHORS: Xiaofeng Ji, Yuan Zheng, Zhipeng Wang, Jun Sheng

  KEYWORDS: TIM-Barrel, Hidden Symmetry, Primary Sequences, Repeat Pattern, Recurrence Quantification Analysis

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.9 No.6, May 31, 2016

  ABSTRACT: Most proteins adopt an approximate structural symmetry. However, they have no symmetry detectable in their sequences and it is unclear for most of these proteins whether their structural symmetry originates from duplication. As one of the six popular folds (super-folds) possessing an approximate structural symmetry, the triosephosphate isomerase barrel (TIM-barrel) domain has been widely studied. Using modified recurrent quantification analysis of primary sequences, we identified the same 2-, 3-, and 4-fold symmetry pattern as their tertiary structures. This result indicates that the symmetry in tertiary structure is coded by symmetry in the primary sequence and that the TIM-barrel adopts a 2-, 3-, or 4-fold repeat pattern during evolution. This discovery will be useful for understanding the evolutionary mechanisms of this protein family and the symmetry pattern that may be a clue into the ancient origin of duplication of half-barrels or the β a unit.