04265nam 2200973z- 450 991055733430332120231214133331.0(CKB)5400000000042535(oapen)https://directory.doabooks.org/handle/20.500.12854/76426(EXLCZ)99540000000004253520202201d2021 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierThe Amazing World of IDPs in Human DiseasesBasel, SwitzerlandMDPI - Multidisciplinary Digital Publishing Institute20211 electronic resource (196 p.)3-0365-1028-1 3-0365-1029-X 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.Research & information: generalbicsscBiology, life sciencesbicsscalpha-synucleinNMRsecondary structure propensitypre-structured motifs (PreSMos)intrinsically disordered proteinubiquitin-proteasome systemintrinsically disordered proteinsprotein misfoldingmolecular recognition featurescancerneurodegenerative diseasesprotein degradationEPR spectroscopyisothermal titration calorimetryprotein-ligand interactionsite-directed spin labelingprotein structural dynamicsWASp interacting proteinprotein-protein interactionsactincytoskeleton remodelingSH3 domainproline-rich motifsingle nucleotide variantsinterface core and rimhuman diseaseintrinsically disordered regionslinear motifsgene duplicationsde novoevolutionary origincircular dichroismflexibilityfluorescenceimportinisothermal titration calorimetry (ITC)molecular dockingnuclear magnetic resonance (NMR)nuclear protein 1 (NPR1)peptideMethyl-CpG-binding protein 2 (MeCP2)Rett syndromeintrinsically disordered protein (IDP)protein stabilityprotein-DNA interactionproteostasisubiquitin independent degradationNADH-26S proteasomeResearch & information: generalBiology, life sciencesMonti Simona Mariaedt425007De Simone GiuseppinaedtLangella EmmaedtMonti Simona MariaothDe Simone GiuseppinaothLangella EmmaothBOOK9910557334303321The Amazing World of IDPs in Human Diseases3034928UNINA