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”

• Material Type: 記事
• Title: 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 Heading: Hoshino Masaru
• Publication Date: 2020
• Publication Date (W3CDTF): 2020
• Periodical title: Biophysics and Physicobiology
• No. or year of volume/issue: 17 0
• Volume: 17
• Issue: 0
• Pages: 159-160
• Publication date of volume/issue (W3CDTF): 2020
• Publication (Periodical Title): The Biophysical Society of Japan
• Text Language Code: en
• Subject Heading: intrinsically disordered proteins; molecular recognition; no folding upon binding; specific binding; interaction with multiple target molecules
• Target Audience: 一般
• DOI: 10.2142/biophysico.bsj-2020028
• Access Restrictions: インターネット公開
• Related Material (URI): https://www.jstage.jst.go.jp/article/biophysico/17/0/17_BSJ-2020028/_pdf; https://search.jamas.or.jp/link/ui/2022006355
• Is Referenced By: Editorial; https://cir.nii.ac.jp/crid/1391975831221091072
• References: Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form; https://cir.nii.ac.jp/crid/1360011142936040576; Homooligomerization of the Cytoplasmic Domain of the T Cell Receptor ζ Chain and of Other Proteins Containing the Immunoreceptor Tyrosine-Based Activation Motif; https://cir.nii.ac.jp/crid/1360011146222240768; Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance; https://cir.nii.ac.jp/crid/1360285705247040896; Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm; https://cir.nii.ac.jp/crid/1360292617909338240; Identification of heteromolecular binding sites in transcription factors Sp1 and TAF4 using high‐resolution nuclear magnetic resonance spectroscopy; https://cir.nii.ac.jp/crid/1360567180224150528; Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4; https://cir.nii.ac.jp/crid/1360848655200751744; 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”; https://cir.nii.ac.jp/crid/1390286981360830080; A novel mode of interaction between intrinsically disordered proteins; https://cir.nii.ac.jp/crid/1390566775160296704
• Data Provider (Database): 国立情報学研究所 : CiNii Research
• Original Data Provider (Database): Japan Link Center; https://japanlinkcenter.org/top; Crossref; https://www.crossref.org; CiNii Articles; 科学研究費助成事業データベース; https://kaken.nii.ac.jp/ja
• NAID: 130007958012