LEADER 04265nam 2200973z- 450 001 9910557334303321 005 20231214133331.0 035 $a(CKB)5400000000042535 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/76426 035 $a(EXLCZ)995400000000042535 100 $a20202201d2021 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aThe Amazing World of IDPs in Human Diseases 210 $aBasel, Switzerland$cMDPI - Multidisciplinary Digital Publishing Institute$d2021 215 $a1 electronic resource (196 p.) 311 $a3-0365-1028-1 311 $a3-0365-1029-X 330 $aIt 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. 606 $aResearch & information: general$2bicssc 606 $aBiology, life sciences$2bicssc 610 $aalpha-synuclein 610 $aNMR 610 $asecondary structure propensity 610 $apre-structured motifs (PreSMos) 610 $aintrinsically disordered protein 610 $aubiquitin-proteasome system 610 $aintrinsically disordered proteins 610 $aprotein misfolding 610 $amolecular recognition features 610 $acancer 610 $aneurodegenerative diseases 610 $aprotein degradation 610 $aEPR spectroscopy 610 $aisothermal titration calorimetry 610 $aprotein-ligand interaction 610 $asite-directed spin labeling 610 $aprotein structural dynamics 610 $aWASp interacting protein 610 $aprotein-protein interactions 610 $aactin 610 $acytoskeleton remodeling 610 $aSH3 domain 610 $aproline-rich motif 610 $asingle nucleotide variants 610 $ainterface core and rim 610 $ahuman disease 610 $aintrinsically disordered regions 610 $alinear motifs 610 $agene duplications 610 $ade novo 610 $aevolutionary origin 610 $acircular dichroism 610 $aflexibility 610 $afluorescence 610 $aimportin 610 $aisothermal titration calorimetry (ITC) 610 $amolecular docking 610 $anuclear magnetic resonance (NMR) 610 $anuclear protein 1 (NPR1) 610 $apeptide 610 $aMethyl-CpG-binding protein 2 (MeCP2) 610 $aRett syndrome 610 $aintrinsically disordered protein (IDP) 610 $aprotein stability 610 $aprotein-DNA interaction 610 $aproteostasis 610 $aubiquitin independent degradation 610 $aNADH-26S proteasome 615 7$aResearch & information: general 615 7$aBiology, life sciences 700 $aMonti$b Simona Maria$4edt$0425007 702 $aDe Simone$b Giuseppina$4edt 702 $aLangella$b Emma$4edt 702 $aMonti$b Simona Maria$4oth 702 $aDe Simone$b Giuseppina$4oth 702 $aLangella$b Emma$4oth 906 $aBOOK 912 $a9910557334303321 996 $aThe Amazing World of IDPs in Human Diseases$93034928 997 $aUNINA