The chromatin nuclear protein NUPR1L is intrinsically disordered and binds to the same proteins as its paralogue

NUPR1 is a protumoral multifunctional intrinsically disordered protein (IDP), which is activated during the acute phases of pancreatitis. It interacts with other IDPs such as prothymosin α, as well as with folded proteins such as the C-terminal region of RING1-B (C-RING1B) of the Polycomb complex; i...

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Veröffentlicht in:	Biochemical journal 2018-07, Vol.475 (14), p.2271-2291
Hauptverfasser:	Neira, José L, López, María Belén, Sevilla, Paz, Rizzuti, Bruno, Cámara-Artigas, Ana, Vidal, Miguel, Iovanna, Juan L
Format:	Artikel
Sprache:	eng
Schlagworte:	Basic Helix-Loop-Helix Transcription Factors - chemistry Basic Helix-Loop-Helix Transcription Factors - metabolism Humans Intrinsically Disordered Proteins - chemistry Intrinsically Disordered Proteins - metabolism Life Sciences Neoplasm Proteins - chemistry Neoplasm Proteins - metabolism Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Multimerization Protein Structure, Quaternary Protein Structure, Secondary Repressor Proteins - chemistry Repressor Proteins - metabolism
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