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引用本文的文献

1
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

1
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".致编辑的信：内在无序蛋白质结合时不折叠：仍然有趣但并非独特新颖。对“Hibino, E. 和 Hoshino, M. 所著《内在无序蛋白质之间的一种新型相互作用模式》的评论，《生物物理学与物理生物学》17卷，86 - 93页（2020年）。DOI: 10.2142/biophysico.BSJ - 2020012”
Biophys Physicobiol. 2020 Dec 18;17:156-158. doi: 10.2142/biophysico.BSJ-2020025. eCollection 2020.
2
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.
3
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.
4
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.
5
Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance.异核磁共振揭示 Sp1 孤立转录激活结构域之间的相互作用。
Protein Sci. 2012 Oct;21(10):1481-8. doi: 10.1002/pro.2137.
6
Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form.内在无序蛋白质的结合不一定伴随着向折叠形式的结构转变。
Biochimie. 2007 Mar;89(3):419-21. doi: 10.1016/j.biochi.2006.11.003. Epub 2006 Nov 22.
7
Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif.T细胞受体ζ链胞质结构域与其他含有基于免疫受体酪氨酸的激活基序的蛋白质的同源寡聚化。
Biochemistry. 2004 Feb 24;43(7):2049-61. doi: 10.1021/bi035900h.
8
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.内在无序蛋白质：重新评估蛋白质结构-功能范式。
J Mol Biol. 1999 Oct 22;293(2):321-31. doi: 10.1006/jmbi.1999.3110.

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".

作者信息

Hoshino Masaru

机构信息

Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan.

出版信息

Biophys Physicobiol. 2020 Dec 18;17:159-160. doi: 10.2142/biophysico.BSJ-2020028. eCollection 2020.

DOI:10.2142/biophysico.BSJ-2020028
PMID:33447499
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7781793/
Abstract
摘要