Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity
Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological sele...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Carl, Philip L. [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2020transfer abstract |
|---|
| Schlagwörter: |
|---|
| Übergeordnetes Werk: |
Enthalten in: Influence of the wind farm integration on load flow and voltage in electrical power system - imen, Labed ELSEVIER, 2016, London |
|---|---|
| Übergeordnetes Werk: |
volume:111 ; year:2020 ; pages:0 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.jaut.2020.102471 |
|---|
| Katalog-ID: |
ELV050420933 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | ELV050420933 | ||
| 003 | DE-627 | ||
| 005 | 20230626030504.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 200625s2020 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1016/j.jaut.2020.102471 |2 doi | |
| 028 | 5 | 2 | |a /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001139.pica |
| 035 | |a (DE-627)ELV050420933 | ||
| 035 | |a (ELSEVIER)S0896-8411(20)30087-1 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 082 | 0 | 4 | |a 660 |q VZ |
| 082 | 0 | 4 | |a 620 |q VZ |
| 082 | 0 | 4 | |a 610 |q VZ |
| 084 | |a 44.94 |2 bkl | ||
| 100 | 1 | |a Carl, Philip L. |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity |
| 264 | 1 | |c 2020transfer abstract | |
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. | ||
| 520 | |a Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. | ||
| 650 | 7 | |a Membraneless organelles |2 Elsevier | |
| 650 | 7 | |a RNA-binding proteins |2 Elsevier | |
| 650 | 7 | |a Protein Disorder |2 Elsevier | |
| 650 | 7 | |a Biomolecular condensates |2 Elsevier | |
| 650 | 7 | |a Autoantigen, Prions |2 Elsevier | |
| 650 | 7 | |a Phase transition |2 Elsevier | |
| 700 | 1 | |a Fried, Howard M. |4 oth | |
| 700 | 1 | |a Cohen, Philip L. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Academic Press |a imen, Labed ELSEVIER |t Influence of the wind farm integration on load flow and voltage in electrical power system |d 2016 |g London |w (DE-627)ELV014127067 |
| 773 | 1 | 8 | |g volume:111 |g year:2020 |g pages:0 |
| 856 | 4 | 0 | |u https://doi.org/10.1016/j.jaut.2020.102471 |3 Volltext |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a GBV_ELV | ||
| 912 | |a SYSFLAG_U | ||
| 912 | |a SSG-OLC-PHA | ||
| 936 | b | k | |a 44.94 |j Hals-Nasen-Ohrenheilkunde |q VZ |
| 951 | |a AR | ||
| 952 | |d 111 |j 2020 |h 0 | ||
| author_variant |
p l c pl plc |
|---|---|
| matchkey_str |
carlphiliplfriedhowardmcohenphilipl:2020----:rtisnsebaefrebpaeeaainosspoetetapooehitasomtotata |
| hierarchy_sort_str |
2020transfer abstract |
| bklnumber |
44.94 |
| publishDate |
2020 |
| allfields |
10.1016/j.jaut.2020.102471 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001139.pica (DE-627)ELV050420933 (ELSEVIER)S0896-8411(20)30087-1 DE-627 ger DE-627 rakwb eng 660 VZ 620 VZ 610 VZ 44.94 bkl Carl, Philip L. verfasserin aut Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition Elsevier Fried, Howard M. oth Cohen, Philip L. oth Enthalten in Academic Press imen, Labed ELSEVIER Influence of the wind farm integration on load flow and voltage in electrical power system 2016 London (DE-627)ELV014127067 volume:111 year:2020 pages:0 https://doi.org/10.1016/j.jaut.2020.102471 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 111 2020 0 |
| spelling |
10.1016/j.jaut.2020.102471 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001139.pica (DE-627)ELV050420933 (ELSEVIER)S0896-8411(20)30087-1 DE-627 ger DE-627 rakwb eng 660 VZ 620 VZ 610 VZ 44.94 bkl Carl, Philip L. verfasserin aut Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition Elsevier Fried, Howard M. oth Cohen, Philip L. oth Enthalten in Academic Press imen, Labed ELSEVIER Influence of the wind farm integration on load flow and voltage in electrical power system 2016 London (DE-627)ELV014127067 volume:111 year:2020 pages:0 https://doi.org/10.1016/j.jaut.2020.102471 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 111 2020 0 |
| allfields_unstemmed |
10.1016/j.jaut.2020.102471 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001139.pica (DE-627)ELV050420933 (ELSEVIER)S0896-8411(20)30087-1 DE-627 ger DE-627 rakwb eng 660 VZ 620 VZ 610 VZ 44.94 bkl Carl, Philip L. verfasserin aut Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition Elsevier Fried, Howard M. oth Cohen, Philip L. oth Enthalten in Academic Press imen, Labed ELSEVIER Influence of the wind farm integration on load flow and voltage in electrical power system 2016 London (DE-627)ELV014127067 volume:111 year:2020 pages:0 https://doi.org/10.1016/j.jaut.2020.102471 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 111 2020 0 |
| allfieldsGer |
10.1016/j.jaut.2020.102471 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001139.pica (DE-627)ELV050420933 (ELSEVIER)S0896-8411(20)30087-1 DE-627 ger DE-627 rakwb eng 660 VZ 620 VZ 610 VZ 44.94 bkl Carl, Philip L. verfasserin aut Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition Elsevier Fried, Howard M. oth Cohen, Philip L. oth Enthalten in Academic Press imen, Labed ELSEVIER Influence of the wind farm integration on load flow and voltage in electrical power system 2016 London (DE-627)ELV014127067 volume:111 year:2020 pages:0 https://doi.org/10.1016/j.jaut.2020.102471 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 111 2020 0 |
| allfieldsSound |
10.1016/j.jaut.2020.102471 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001139.pica (DE-627)ELV050420933 (ELSEVIER)S0896-8411(20)30087-1 DE-627 ger DE-627 rakwb eng 660 VZ 620 VZ 610 VZ 44.94 bkl Carl, Philip L. verfasserin aut Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity 2020transfer abstract nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition Elsevier Fried, Howard M. oth Cohen, Philip L. oth Enthalten in Academic Press imen, Labed ELSEVIER Influence of the wind farm integration on load flow and voltage in electrical power system 2016 London (DE-627)ELV014127067 volume:111 year:2020 pages:0 https://doi.org/10.1016/j.jaut.2020.102471 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 111 2020 0 |
| language |
English |
| source |
Enthalten in Influence of the wind farm integration on load flow and voltage in electrical power system London volume:111 year:2020 pages:0 |
| sourceStr |
Enthalten in Influence of the wind farm integration on load flow and voltage in electrical power system London volume:111 year:2020 pages:0 |
| format_phy_str_mv |
Article |
| bklname |
Hals-Nasen-Ohrenheilkunde |
| institution |
findex.gbv.de |
| topic_facet |
Membraneless organelles RNA-binding proteins Protein Disorder Biomolecular condensates Autoantigen, Prions Phase transition |
| dewey-raw |
660 |
| isfreeaccess_bool |
false |
| container_title |
Influence of the wind farm integration on load flow and voltage in electrical power system |
| authorswithroles_txt_mv |
Carl, Philip L. @@aut@@ Fried, Howard M. @@oth@@ Cohen, Philip L. @@oth@@ |
| publishDateDaySort_date |
2020-01-01T00:00:00Z |
| hierarchy_top_id |
ELV014127067 |
| dewey-sort |
3660 |
| id |
ELV050420933 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV050420933</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626030504.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">200625s2020 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.jaut.2020.102471</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001139.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV050420933</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0896-8411(20)30087-1</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">660</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">620</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">44.94</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Carl, Philip L.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020transfer abstract</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Membraneless organelles</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">RNA-binding proteins</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Protein Disorder</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Biomolecular condensates</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Autoantigen, Prions</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Phase transition</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Fried, Howard M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cohen, Philip L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Academic Press</subfield><subfield code="a">imen, Labed ELSEVIER</subfield><subfield code="t">Influence of the wind farm integration on load flow and voltage in electrical power system</subfield><subfield code="d">2016</subfield><subfield code="g">London</subfield><subfield code="w">(DE-627)ELV014127067</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:111</subfield><subfield code="g">year:2020</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.jaut.2020.102471</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">44.94</subfield><subfield code="j">Hals-Nasen-Ohrenheilkunde</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">111</subfield><subfield code="j">2020</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| author |
Carl, Philip L. |
| spellingShingle |
Carl, Philip L. ddc 660 ddc 620 ddc 610 bkl 44.94 Elsevier Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity |
| authorStr |
Carl, Philip L. |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)ELV014127067 |
| format |
electronic Article |
| dewey-ones |
660 - Chemical engineering 620 - Engineering & allied operations 610 - Medicine & health |
| delete_txt_mv |
keep |
| author_role |
aut |
| collection |
elsevier |
| remote_str |
true |
| illustrated |
Not Illustrated |
| topic_title |
660 VZ 620 VZ 610 VZ 44.94 bkl Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition Elsevier |
| topic |
ddc 660 ddc 620 ddc 610 bkl 44.94 Elsevier Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition |
| topic_unstemmed |
ddc 660 ddc 620 ddc 610 bkl 44.94 Elsevier Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition |
| topic_browse |
ddc 660 ddc 620 ddc 610 bkl 44.94 Elsevier Membraneless organelles Elsevier RNA-binding proteins Elsevier Protein Disorder Elsevier Biomolecular condensates Elsevier Autoantigen, Prions Elsevier Phase transition |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
h m f hm hmf p l c pl plc |
| hierarchy_parent_title |
Influence of the wind farm integration on load flow and voltage in electrical power system |
| hierarchy_parent_id |
ELV014127067 |
| dewey-tens |
660 - Chemical engineering 620 - Engineering 610 - Medicine & health |
| hierarchy_top_title |
Influence of the wind farm integration on load flow and voltage in electrical power system |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)ELV014127067 |
| title |
Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity |
| ctrlnum |
(DE-627)ELV050420933 (ELSEVIER)S0896-8411(20)30087-1 |
| title_full |
Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity |
| author_sort |
Carl, Philip L. |
| journal |
Influence of the wind farm integration on load flow and voltage in electrical power system |
| journalStr |
Influence of the wind farm integration on load flow and voltage in electrical power system |
| lang_code |
eng |
| isOA_bool |
false |
| dewey-hundreds |
600 - Technology |
| recordtype |
marc |
| publishDateSort |
2020 |
| contenttype_str_mv |
zzz |
| container_start_page |
0 |
| author_browse |
Carl, Philip L. |
| container_volume |
111 |
| class |
660 VZ 620 VZ 610 VZ 44.94 bkl |
| format_se |
Elektronische Aufsätze |
| author-letter |
Carl, Philip L. |
| doi_str_mv |
10.1016/j.jaut.2020.102471 |
| dewey-full |
660 620 610 |
| title_sort |
proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: implications for autoimmunity |
| title_auth |
Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity |
| abstract |
Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. |
| abstractGer |
Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. |
| abstract_unstemmed |
Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens. |
| collection_details |
GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA |
| title_short |
Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity |
| url |
https://doi.org/10.1016/j.jaut.2020.102471 |
| remote_bool |
true |
| author2 |
Fried, Howard M. Cohen, Philip L. |
| author2Str |
Fried, Howard M. Cohen, Philip L. |
| ppnlink |
ELV014127067 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth |
| doi_str |
10.1016/j.jaut.2020.102471 |
| up_date |
2024-07-06T17:29:26.200Z |
| _version_ |
1803851625874325504 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">ELV050420933</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230626030504.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">200625s2020 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1016/j.jaut.2020.102471</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">/cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001139.pica</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)ELV050420933</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(ELSEVIER)S0896-8411(20)30087-1</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">660</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">620</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="082" ind1="0" ind2="4"><subfield code="a">610</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">44.94</subfield><subfield code="2">bkl</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Carl, Philip L.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Proteins in assemblages formed by phase separation possess properties that promote their transformation to autoantigens: Implications for autoimmunity</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2020transfer abstract</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Autoantibodies in systemic autoimmunity are directed against only ~5% of the proteome. The purpose of this study was to assess whether the properties of assemblages (also known as Membraneless Organelles and Biological Condensates) and their protein constituents partly explain the immunological selectivity of autoimmunity. Assemblages arise from phase separation of their protein components, akin to partitioning of oil droplets in water. We obtained from a prediction algorithm (Vernon et al., elife 7, 2018) the propensity scores (PScores), i.e., likelihood, for phase separation of autoantigens and non-autoantigens. We then compared autoantigens with the highest PScores to identify shared structural properties. The mean PScores for autoantigens (n = 1050) and the entire human proteome of non-autoantigens (n = 17,532) were 1.46 and 1.09 (p = 1.2E-08). To varying extents, the 25 autoantigens with the highest phase separation propensities shared additional features such as compositional bias, repeated domains, coiled coil regions, nucleic acid binding, and disorder. Most of these properties were present with greater frequencies than their frequencies in the non-autoantigens. We conclude that, on average, autoantigens have a higher predisposition to undergo phase separation, thus, they are more likely to exist in assemblages compared with the average non-autoantigen. We suggest that assemblage formation and the greater than average presence of certain structural features are key factors in selection of a portion of the autoimmune repertoire. Other properties of assemblage proteins, such as high concentration and tendency to form novel complexes with other proteins, may partially explain why assemblages are potent sources of autoantigens.</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Membraneless organelles</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">RNA-binding proteins</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Protein Disorder</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Biomolecular condensates</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Autoantigen, Prions</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="650" ind1=" " ind2="7"><subfield code="a">Phase transition</subfield><subfield code="2">Elsevier</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Fried, Howard M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Cohen, Philip L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Academic Press</subfield><subfield code="a">imen, Labed ELSEVIER</subfield><subfield code="t">Influence of the wind farm integration on load flow and voltage in electrical power system</subfield><subfield code="d">2016</subfield><subfield code="g">London</subfield><subfield code="w">(DE-627)ELV014127067</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:111</subfield><subfield code="g">year:2020</subfield><subfield code="g">pages:0</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.jaut.2020.102471</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ELV</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SSG-OLC-PHA</subfield></datafield><datafield tag="936" ind1="b" ind2="k"><subfield code="a">44.94</subfield><subfield code="j">Hals-Nasen-Ohrenheilkunde</subfield><subfield code="q">VZ</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">111</subfield><subfield code="j">2020</subfield><subfield code="h">0</subfield></datafield></record></collection>
|
| score |
7.4027834 |