A disorder-to-order structural transition in the COOH-tail of Fz4 determines misfolding of the L501fsX533-Fz4 mutant-Reference-Cited by-同舟云学术

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A disorder-to-order structural transition in the COOH-tail of Fz4 determines misfolding of the L501fsX533-Fz4 mutant

Published:2013-09-16 Issue:1 Volume:3 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

Lemma Valentina,D'Agostino Massimo,Caporaso Maria Gabriella,Mallardo Massimo,Oliviero Giorgia,Stornaiuolo Mariano,Bonatti Stefano

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/srep02659.pdf

Reference40 articles.

1. Yue, P., Li, Z. & Moult, J. Loss of protein structure stability as a major causative factor in monogenic disease. J. Mol. Biol. 353, 459–473 (2005).

2. Vacic, V. et al. Disease-Associated Mutations Disrupt Functionally Important Regions of Intrinsic Protein Disorder. PLoS Comput. Biol. 8, e1002709 (2012).

3. Vacic, V. & Iakoucheva, L. M. Disease mutations in disordered regions-exception to the rule? Mol. Biosyst. 8, 27–32 (2012).

4. Dinkel, H. et al. ELM–the database of eukaryotic linear motifs. Nucleic Acids Res. 40, D242–251 (2012).

5. Fuxreiter, M., Tompa, P. & Simon, I. Local structural disorder imparts plasticity on linear motifs. Bioinformatics 23, 950–956 (2007).

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