The Amazing World of IDPs in Human Diseases
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...
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| Format: | Online |
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| Język: | angielski |
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MDPI - Multidisciplinary Digital Publishing Institute
2022
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| Hasła przedmiotowe: | |
| Dostęp online: | ONIX_20220111_9783036510286_162 |
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| _version_ | 1869528050072289280 |
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| collection | Directory of Open Access Books |
| description | 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 | Online |
| id | doab-20.500.12854ir-76426 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2022 |
| publishDateRange | 2022 |
| publishDateSort | 2022 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | ojs |
| spelling | doab-20.500.12854ir-764262024-03-28T03:33:52Z The Amazing World of IDPs in Human Diseases Monti, Simona Maria De Simone, Giuseppina Langella, Emma 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 thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences 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. 2022-01-11T13:31:35Z 2022-01-11T13:31:35Z 2021 book ONIX_20220111_9783036510286_162 9783036510286 9783036510293 https://directory.doabooks.org/handle/20.500.12854/76426 eng image/jpeg Attribution 4.0 International https://mdpi.com/books/pdfview/book/3861 https://mdpi.com/books/pdfview/book/3861 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-0365-1029-3 10.3390/books978-3-0365-1029-3 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783036510286 9783036510293 196 Basel, Switzerland open access |
| spellingShingle | 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 thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences The Amazing World of IDPs in Human Diseases |
| title | The Amazing World of IDPs in Human Diseases |
| title_full | The Amazing World of IDPs in Human Diseases |
| title_fullStr | The Amazing World of IDPs in Human Diseases |
| title_full_unstemmed | The Amazing World of IDPs in Human Diseases |
| title_short | The Amazing World of IDPs in Human Diseases |
| title_sort | amazing world of idps in human diseases |
| topic | 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 thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| topic_facet | 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 thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| url | ONIX_20220111_9783036510286_162 |