04302nam 2200997z- 450 991055733430332120220111(CKB)5400000000042535(oapen)https://directory.doabooks.org/handle/20.500.12854/76426(oapen)doab76426(EXLCZ)99540000000004253520202201d2021 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierThe Amazing World of IDPs in Human DiseasesBasel, SwitzerlandMDPI - Multidisciplinary Digital Publishing Institute20211 online 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.Biology, life sciencesbicsscResearch & information: generalbicsscactinalpha-synucleincancercircular dichroismcytoskeleton remodelingde novoEPR spectroscopyevolutionary originflexibilityfluorescencegene duplicationshuman diseaseimportininterface core and rimintrinsically disordered proteinintrinsically disordered protein (IDP)intrinsically disordered proteinsintrinsically disordered regionsisothermal titration calorimetryisothermal titration calorimetry (ITC)linear motifsMethyl-CpG-binding protein 2 (MeCP2)molecular dockingmolecular recognition featuresn/aNADH-26S proteasomeneurodegenerative diseasesNMRnuclear magnetic resonance (NMR)nuclear protein 1 (NPR1)peptidepre-structured motifs (PreSMos)proline-rich motifprotein degradationprotein misfoldingprotein stabilityprotein structural dynamicsprotein-DNA interactionprotein-ligand interactionprotein-protein interactionsproteostasisRett syndromesecondary structure propensitySH3 domainsingle nucleotide variantssite-directed spin labelingubiquitin independent degradationubiquitin-proteasome systemWASp interacting proteinBiology, life sciencesResearch & information: generalMonti Simona Mariaedt425007De Simone GiuseppinaedtLangella EmmaedtMonti Simona MariaothDe Simone GiuseppinaothLangella EmmaothBOOK9910557334303321The Amazing World of IDPs in Human Diseases3034928UNINA