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- W2158267005 abstract "Originally, the peroxisomal targeting signal 1 (PTS1) was defined as a tripeptide at the C-terminus of proteins prone to be imported into the peroxisomal matrix. The corresponding receptor PEX5 initiates the translocation of proteins by identifying potential substrates via their C-termini and trapping PTS1s through remodeling of its TPR domain. Thorough studies on the interaction between PEX5 and PTS1 as well as sequence-analytic tools revealed the influence of amino acid residues further upstream of the ultimate tripeptide. Altogether, PTS1s should be defined as dodecamer sequences at the C-terminal ends of proteins. These sequences accommodate physical contacts with both the surface and the binding cavity of PEX5 and ensure accessibility of the extreme C-terminus. Knowledge-based approaches in applied Bioinformatics provide reliable tools to accurately predict the peroxisomal location of proteins not yet determined experimentally." @default.
- W2158267005 created "2016-06-24" @default.
- W2158267005 creator A5019272836 @default.
- W2158267005 creator A5055363713 @default.
- W2158267005 date "2006-12-01" @default.
- W2158267005 modified "2023-10-16" @default.
- W2158267005 title "Peroxisome targeting signal 1: Is it really a simple tripeptide?" @default.
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- W2158267005 doi "https://doi.org/10.1016/j.bbamcr.2006.08.022" @default.
- W2158267005 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17007944" @default.
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