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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".

作者信息

Sigalov Alexander B

机构信息

SignaBlok, Massachusetts 01545, USA.

出版信息

Biophys Physicobiol. 2020 Dec 18;17:156-158. doi: 10.2142/biophysico.BSJ-2020025. eCollection 2020.

DOI:10.2142/biophysico.BSJ-2020025
PMID:33447498
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7781792/
Abstract
摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dc03/7781792/1e1d0d5bf6ed/17_156-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dc03/7781792/1e1d0d5bf6ed/17_156-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/dc03/7781792/1e1d0d5bf6ed/17_156-g001.jpg

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引用本文的文献

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".致编辑的信：内在无序蛋白质相互作用中一个仍未解决的谜团：它们如何识别多种靶蛋白？对“A. B. Sigalov所著《内在无序蛋白质结合时无折叠：仍然有趣但并非独特新颖》，发表于《生物物理学与物理生物学》第17卷，第156 - 158页（2020年）。DOI: 10.2142/biophysico.BSJ - 2020025”的评论 。
Biophys Physicobiol. 2020 Dec 18;17:159-160. doi: 10.2142/biophysico.BSJ-2020028. eCollection 2020.
2
Editorial.社论。
Biophys Physicobiol. 2020 Dec 18;17:155. doi: 10.2142/biophysico.BSJ-2020030. eCollection 2020.

本文引用的文献

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A novel mode of interaction between intrinsically disordered proteins.内在无序蛋白质之间一种新型的相互作用模式。
Biophys Physicobiol. 2020 Jul 3;17:86-93. doi: 10.2142/biophysico.BSJ-2020012. eCollection 2020.
2
Binding without folding - the biomolecular function of disordered polyelectrolyte complexes.无折叠结合 - 无序聚电解质复合物的生物分子功能。
Curr Opin Struct Biol. 2020 Feb;60:66-76. doi: 10.1016/j.sbi.2019.12.006. Epub 2019 Dec 23.
3
Extreme disorder in an ultrahigh-affinity protein complex.超高亲和力蛋白质复合物中的极端无序。
Nature. 2018 Mar 1;555(7694):61-66. doi: 10.1038/nature25762. Epub 2018 Feb 21.
4
Identification of heteromolecular binding sites in transcription factors Sp1 and TAF4 using high-resolution nuclear magnetic resonance spectroscopy.利用高分辨率核磁共振光谱法鉴定转录因子Sp1和TAF4中的异分子结合位点。
Protein Sci. 2017 Nov;26(11):2280-2290. doi: 10.1002/pro.3287. Epub 2017 Sep 27.
5
The Dynamic Multisite Interactions between Two Intrinsically Disordered Proteins.两种固有无序蛋白质之间的动态多点相互作用。
Angew Chem Int Ed Engl. 2017 Jun 19;56(26):7515-7519. doi: 10.1002/anie.201701883. Epub 2017 May 24.
6
Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4.转录因子Sp1和TAF4中内在无序区域之间的相互作用。
Protein Sci. 2016 Nov;25(11):2006-2017. doi: 10.1002/pro.3013. Epub 2016 Aug 24.
7
Fuzzy complexes: Specific binding without complete folding.模糊复合体：无需完全折叠即可实现特异性结合。
FEBS Lett. 2015 Sep 14;589(19 Pt A):2533-42. doi: 10.1016/j.febslet.2015.07.022. Epub 2015 Jul 27.
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