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Proteins --- Intrinsically Disordered Proteins. --- Structure --- Structure. --- Natively Unfolded Proteins --- Unstructured Proteins --- Proteids --- Protein Folding --- Protein Unfolding --- Biomolecules --- Polypeptides --- Proteomics --- Animal Biochemistry --- Intrinsically Disordered Protein --- Natively Unfolded Protein --- Unstructured Protein --- Disordered Protein, Intrinsically --- Protein, Intrinsically Disordered --- Protein, Natively Unfolded --- Protein, Unstructured --- Unfolded Protein, Natively

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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: general --- Biology, life sciences --- 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 --- 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

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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.

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 --- n/a --- protein-protein interactions

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This book is an embodiment of a series of articles that were published as part of a Special Issue of Biomolecules. It is dedicated to exploring the role of intrinsically disordered proteins (IDPs) in various chronic diseases. The main goal of the articles is to describe recent progress in elucidating the mechanisms by which IDPs cause various human diseases, such as cancer, cardiovascular disease, amyloidosis, neurodegenerative diseases, diabetes, and genetic diseases, to name a few. Contributed by leading investigators in the field, this compendium serves as a valuable resource for researchers, clinicians as well as postdoctoral fellows and graduate students

Research & information: general --- IDP --- fuzzy interactions --- protein complementation assays --- split-GFP reassembly --- kinetics --- membraneless organelles --- optical tweezer --- liquid–liquid phase separation --- protein diffusion --- depletion interaction --- entropic force --- low-complexity sequences --- intrinsically disordered proteins --- PAGE4 --- conformational plasticity --- order–disorder transition --- phosphorylation --- intrinsic disordered protein --- extremely fuzzy complex --- protein interaction --- binding mechanism --- tumor protein p53 --- mouse double minute 2 --- mouse double minute 4 --- Kinase-inducible domain interacting domain --- phosphomimetics --- nuclear magnetic resonance --- transient secondary structure --- COR15A --- Late embryogenesis abundant --- Trifluoroethanol --- Nuclear magnetic resonance --- intrinsically disordered regions --- functional segments --- disease-related proteins --- protein-protein interaction --- subcellular location --- glucocorticoid receptor --- intrinsically disordered --- transactivation activity --- gene regulation --- coactivators --- microtubule associated protein --- tau --- intrinsically disordered protein --- dynamic configuration --- free energy landscape --- microtubules --- electrostatics --- diffusion --- protein structure prediction --- molecular modelling --- molecular dynamics --- tau–microtubule association --- conformational ensemble --- replica exchange molecular dynamics --- drug design --- n/a --- liquid-liquid phase separation --- order-disorder transition --- tau-microtubule association

Choose an application

• Reference Manager
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This book is an embodiment of a series of articles that were published as part of a Special Issue of Biomolecules. It is dedicated to exploring the role of intrinsically disordered proteins (IDPs) in various chronic diseases. The main goal of the articles is to describe recent progress in elucidating the mechanisms by which IDPs cause various human diseases, such as cancer, cardiovascular disease, amyloidosis, neurodegenerative diseases, diabetes, and genetic diseases, to name a few. Contributed by leading investigators in the field, this compendium serves as a valuable resource for researchers, clinicians as well as postdoctoral fellows and graduate students

Research & information: general --- IDP --- fuzzy interactions --- protein complementation assays --- split-GFP reassembly --- kinetics --- membraneless organelles --- optical tweezer --- liquid-liquid phase separation --- protein diffusion --- depletion interaction --- entropic force --- low-complexity sequences --- intrinsically disordered proteins --- PAGE4 --- conformational plasticity --- order-disorder transition --- phosphorylation --- intrinsic disordered protein --- extremely fuzzy complex --- protein interaction --- binding mechanism --- tumor protein p53 --- mouse double minute 2 --- mouse double minute 4 --- Kinase-inducible domain interacting domain --- phosphomimetics --- nuclear magnetic resonance --- transient secondary structure --- COR15A --- Late embryogenesis abundant --- Trifluoroethanol --- Nuclear magnetic resonance --- intrinsically disordered regions --- functional segments --- disease-related proteins --- protein-protein interaction --- subcellular location --- glucocorticoid receptor --- intrinsically disordered --- transactivation activity --- gene regulation --- coactivators --- microtubule associated protein --- tau --- intrinsically disordered protein --- dynamic configuration --- free energy landscape --- microtubules --- electrostatics --- diffusion --- protein structure prediction --- molecular modelling --- molecular dynamics --- tau-microtubule association --- conformational ensemble --- replica exchange molecular dynamics --- drug design --- IDP --- fuzzy interactions --- protein complementation assays --- split-GFP reassembly --- kinetics --- membraneless organelles --- optical tweezer --- liquid-liquid phase separation --- protein diffusion --- depletion interaction --- entropic force --- low-complexity sequences --- intrinsically disordered proteins --- PAGE4 --- conformational plasticity --- order-disorder transition --- phosphorylation --- intrinsic disordered protein --- extremely fuzzy complex --- protein interaction --- binding mechanism --- tumor protein p53 --- mouse double minute 2 --- mouse double minute 4 --- Kinase-inducible domain interacting domain --- phosphomimetics --- nuclear magnetic resonance --- transient secondary structure --- COR15A --- Late embryogenesis abundant --- Trifluoroethanol --- Nuclear magnetic resonance --- intrinsically disordered regions --- functional segments --- disease-related proteins --- protein-protein interaction --- subcellular location --- glucocorticoid receptor --- intrinsically disordered --- transactivation activity --- gene regulation --- coactivators --- microtubule associated protein --- tau --- intrinsically disordered protein --- dynamic configuration --- free energy landscape --- microtubules --- electrostatics --- diffusion --- protein structure prediction --- molecular modelling --- molecular dynamics --- tau-microtubule association --- conformational ensemble --- replica exchange molecular dynamics --- drug design