The Amazing World of IDPs in Human Diseases

• Andere auteurs: Monti, Simona Maria (Redacteur), De Simone, Giuseppina (Redacteur), Langella, Emma (Redacteur)
• Formaat: Elektronisch Hoofdstuk
• Taal: Engels
• Gepubliceerd in: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2021
• Onderwerpen: Research & information: general; Biology, life sciences; alpha-synuclein; NMR; secondary structure propensity; pre-structured motifs (PreSMos); intrinsically disordered protein; ubiquitin-proteasome system; intrinsically disordered proteins; protein misfolding; molecular recognition features; cancer; neurodegenerative diseases; protein degradation; EPR spectroscopy; isothermal titration calorimetry; protein-ligand interaction; site-directed spin labeling; protein structural dynamics; WASp interacting protein; protein-protein interactions; actin; cytoskeleton remodeling; SH3 domain; proline-rich motif; single nucleotide variants; interface core and rim; human disease; intrinsically disordered regions; linear motifs; gene duplications; de novo; evolutionary origin; circular dichroism; flexibility; fluorescence; importin; isothermal titration calorimetry (ITC); molecular docking; nuclear magnetic resonance (NMR); nuclear protein 1 (NPR1); peptide; Methyl-CpG-binding protein 2 (MeCP2); Rett syndrome; intrinsically disordered protein (IDP); protein stability; protein-DNA interaction; proteostasis; ubiquitin independent degradation; NADH-26S proteasome; n/a
• Online toegang: DOAB: download the publication; DOAB: description of the publication

It is now clearly established that some proteins or protein regions are devoid of any stable secondary and/or tertiary structure under physiological conditions, but still possess fundamental biological functions. These intrinsically disordered proteins (IDPs) or regions (IDRs) have peculiar features...