The Amazing World of IDPs in Human Diseases

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...

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Other Authors: Monti, Simona Maria (Editor), De Simone, Giuseppina (Editor), Langella, Emma (Editor)
Format: Electronic Book Chapter
Language:English
Published: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2021
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245 1 0 |a The Amazing World of IDPs in Human Diseases 
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520 |a 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 due to their plasticity such as the capacity to bind their biological targets with high specificity and low affinity, and the possibility of interaction with numerous partners. A correlation between intrinsic disorder and various human diseases such as cancer, diabetes, amyloidoses and neurodegenerative diseases is now evident, highlighting the great importance of the topic. In this volume, we have collected recent high-quality research about IDPs and human diseases. We have selected nine papers which deal with a wide range of topics, from neurodegenerative disease to cancer, from IDR-mediated interactions to bioinformatics tools, all related to IDP peculiar features. Recent advances in the IDPs/IDRs issue are here presented, contributing to the progress of knowledge of the intrinsic disorder field in human disease. 
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650 7 |a Biology, life sciences  |2 bicssc 
653 |a alpha-synuclein 
653 |a NMR 
653 |a secondary structure propensity 
653 |a pre-structured motifs (PreSMos) 
653 |a intrinsically disordered protein 
653 |a ubiquitin-proteasome system 
653 |a intrinsically disordered proteins 
653 |a protein misfolding 
653 |a molecular recognition features 
653 |a cancer 
653 |a neurodegenerative diseases 
653 |a protein degradation 
653 |a EPR spectroscopy 
653 |a isothermal titration calorimetry 
653 |a protein-ligand interaction 
653 |a site-directed spin labeling 
653 |a protein structural dynamics 
653 |a WASp interacting protein 
653 |a protein-protein interactions 
653 |a actin 
653 |a cytoskeleton remodeling 
653 |a SH3 domain 
653 |a proline-rich motif 
653 |a single nucleotide variants 
653 |a interface core and rim 
653 |a human disease 
653 |a intrinsically disordered regions 
653 |a linear motifs 
653 |a gene duplications 
653 |a de novo 
653 |a evolutionary origin 
653 |a circular dichroism 
653 |a flexibility 
653 |a fluorescence 
653 |a importin 
653 |a isothermal titration calorimetry (ITC) 
653 |a molecular docking 
653 |a nuclear magnetic resonance (NMR) 
653 |a nuclear protein 1 (NPR1) 
653 |a peptide 
653 |a Methyl-CpG-binding protein 2 (MeCP2) 
653 |a Rett syndrome 
653 |a intrinsically disordered protein (IDP) 
653 |a protein stability 
653 |a protein-DNA interaction 
653 |a proteostasis 
653 |a ubiquitin independent degradation 
653 |a NADH-26S proteasome 
653 |a n/a 
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