Letter to the Editor: A still unresolved mystery in the interaction between intrinsically disordered proteins: How do they recognize multiple target proteins? A commentary on “No folding upon binding of intrinsically disordered proteins: Still interesting but not unique and novel. by Sigalov, A. B., Biophysics and Physicobiology 17, 156–158 (2020). DOI: 10.2142/biophysico.BSJ-2020025”
Author:
Affiliation:
1. Graduate School of Pharmaceutical Sciences, Kyoto University
Publisher
Biophysical Society of Japan
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/biophysico/17/0/17_BSJ-2020028/_pdf
Reference8 articles.
1. [1] Wright, P. E. & Dyson, H. J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321–331 (1999). DOI: 10.1006/jmbi.1999.3110
2. [2] Sigalov, A., Aivazian, D. & Stern, L. Homooligomerization of the cytoplasmic domain of the T cell receptor ζ chain and of other proteins containing the immunoreceptor yyrosine-based activation motif. Biochemistry 43, 2049–2061 (2004). DOI: 10.1021/bi035900h
3. [3] Sigalov, A. B., Zhuravleva, A. V. & Orekhov, V. Y. Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Biochimie 89, 419–421 (2007). DOI: 10.1016/j.biochi.2006.11.003
4. [4] Sigalov, A. B. No folding upon binding of intrinsically disordered proteins: Still interesting but not unique and novel. Biophys. Physicobiol. 17, 156–158 (2020). DOI: 10.2142/biophysico.BSJ-2020025
5. [5] Hibino, E. & Hoshino, M. A novel mode of interaction between intrinsically disordered proteins. Biophys. Physicobiol. 17, 86–93 (2020). DOI: 10.2142/biophysico.BSJ-2020012
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1. Editorial;Biophysics and Physicobiology;2020
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