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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Monti, Simona Maria edt The Amazing World of IDPs in Human Diseases Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2021 1 electronic resource (196 p.) text txt rdacontent computer c rdamedia online resource cr rdacarrier 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. English Research & information: general bicssc Biology, life sciences bicssc 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 3-0365-1028-1 3-0365-1029-X De Simone, Giuseppina edt Langella, Emma edt Monti, Simona Maria oth De Simone, Giuseppina oth Langella, Emma oth |
language |
English |
format |
eBook |
author2 |
De Simone, Giuseppina Langella, Emma Monti, Simona Maria De Simone, Giuseppina Langella, Emma |
author_facet |
De Simone, Giuseppina Langella, Emma Monti, Simona Maria De Simone, Giuseppina Langella, Emma |
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s m m sm smm s g d sg sgd e l el |
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HerausgeberIn HerausgeberIn Sonstige Sonstige Sonstige |
title |
The Amazing World of IDPs in Human Diseases |
spellingShingle |
The Amazing World of IDPs in Human Diseases |
title_full |
The Amazing World of IDPs in Human Diseases |
title_fullStr |
The Amazing World of IDPs in Human Diseases |
title_full_unstemmed |
The Amazing World of IDPs in Human Diseases |
title_auth |
The Amazing World of IDPs in Human Diseases |
title_new |
The Amazing World of IDPs in Human Diseases |
title_sort |
the amazing world of idps in human diseases |
publisher |
MDPI - Multidisciplinary Digital Publishing Institute |
publishDate |
2021 |
physical |
1 electronic resource (196 p.) |
isbn |
3-0365-1028-1 3-0365-1029-X |
illustrated |
Not Illustrated |
work_keys_str_mv |
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The Amazing World of IDPs in Human Diseases |
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