Reprint
The Amazing World of IDPs in Human Diseases
Edited by
June 2021
196 pages
- ISBN978-3-0365-1028-6 (Hardback)
- ISBN978-3-0365-1029-3 (PDF)
This book is a reprint of the Special Issue The Amazing World of IDPs in Human Diseases that was published in
Biology & Life Sciences
Medicine & Pharmacology
Summary
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.
Format
- Hardback
License
© 2022 by the authors; CC BY-NC-ND license
Keywords
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; intrinsically disordered proteins; EPR spectroscopy; isothermal titration calorimetry; protein-ligand interaction; site-directed spin labeling; protein structural dynamics; WASp interacting protein; protein–protein interactions; intrinsically disordered proteins; actin; cytoskeleton remodeling; SH3 domain; proline-rich motif; intrinsically disordered proteins; single nucleotide variants; protein–protein interactions; interface core and rim; human disease; intrinsically disordered regions; linear motifs; gene duplications; de novo; evolutionary origin; circular dichroism; flexibility; fluorescence; importin; intrinsically disordered protein; 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; isothermal titration calorimetry (ITC); proteostasis; ubiquitin independent degradation; intrinsically disordered proteins; NADH-26S proteasome; n/a