Letter to the Editor: No folding upon binding of intrinsically disordered proteins: Still interesting but not unique and novel. A commentary on “A novel mode of interaction between intrinsically disordered proteins. by Hibino, E. and Hoshino, M., Biophysics and Physicobiology 17, 86–93 (2020). DOI: 10.2142/biophysico.BSJ-2020012”
Author:
Affiliation:
1. SignaBlok
Publisher
Biophysical Society of Japan
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/biophysico/17/0/17_BSJ-2020025/_pdf
Reference22 articles.
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2. [2] Sigalov, A., Aivazian, D. & Stern, L. Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. Biochemistry 43, 2049–2061 (2004). DOI: 10.1021/bi035900h
3. [3] Pometun, M. S., Chekmenev, E. Y. & Wittebort, R. J. Quantitative observation of backbone disorder in native elastin. J. Biol. Chem. 279, 7982–7987 (2004). DOI: 10.1074/jbc.M310948200
4. [4] Sigalov, A. B., Kim, W. M., Saline, M. & Stern, L. J. The intrinsically disordered cytoplasmic domain of the T cell receptor zeta chain binds to the nef protein of simian immunodeficiency virus without a disorder-to-order transition. Biochemistry 47, 12942–12944 (2008). DOI: 10.1021/bi801602p
5. [5] Tompa, P. & Fuxreiter, M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 33, 2–8 (2008). DOI: 10.1016/j.tibs.2007.10.003
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1. 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”;Biophysics and Physicobiology;2020
2. Editorial;Biophysics and Physicobiology;2020
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