タイトル(掲載誌)Biophysics and Physicobiology
出版事項(掲載誌)The Biophysical Society of Japan
DOI10.2142/biophysico.bsj-2020028
参照Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form
Homooligomerization of the Cytoplasmic Domain of the T Cell Receptor ζ Chain and of Other Proteins Containing the Immunoreceptor Tyrosine-Based Activation Motif
Interaction between isolated transcriptional activation domains of Sp1 revealed by heteronuclear magnetic resonance
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Identification of heteromolecular binding sites in transcription factors Sp1 and TAF4 using high‐resolution nuclear magnetic resonance spectroscopy
Interaction between intrinsically disordered regions in transcription factors Sp1 and TAF4
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”
A novel mode of interaction between intrinsically disordered proteins
連携機関・データベース国立情報学研究所 : CiNii Research