Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant
Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell deat...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Song, Xiufeng [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2013transfer abstract |
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| Umfang: |
12 |
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| Übergeordnetes Werk: |
Enthalten in: Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells - Zhao, Hailei ELSEVIER, 2013transfer abstract, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:25 ; year:2013 ; number:12 ; pages:2613-2624 ; extent:12 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.cellsig.2013.08.022 |
|---|
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ELV021983631 |
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| 245 | 1 | 0 | |a Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant |
| 264 | 1 | |c 2013transfer abstract | |
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| 520 | |a Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. | ||
| 520 | |a Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. | ||
| 700 | 1 | |a Seo, Jungwon |4 oth | |
| 700 | 1 | |a Baameur, Faiza |4 oth | |
| 700 | 1 | |a Vishnivetskiy, Sergey A. |4 oth | |
| 700 | 1 | |a Chen, Qiuyan |4 oth | |
| 700 | 1 | |a Kook, Seunghyi |4 oth | |
| 700 | 1 | |a Kim, Miyeon |4 oth | |
| 700 | 1 | |a Brooks, Evan K. |4 oth | |
| 700 | 1 | |a Altenbach, Christian |4 oth | |
| 700 | 1 | |a Hong, Yuan |4 oth | |
| 700 | 1 | |a Hanson, Susan M. |4 oth | |
| 700 | 1 | |a Palazzo, Maria C. |4 oth | |
| 700 | 1 | |a Chen, Jeannie |4 oth | |
| 700 | 1 | |a Hubbell, Wayne L. |4 oth | |
| 700 | 1 | |a Gurevich, Eugenia V. |4 oth | |
| 700 | 1 | |a Gurevich, Vsevolod V. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier Science |a Zhao, Hailei ELSEVIER |t Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells |d 2013transfer abstract |g Amsterdam [u.a.] |w (DE-627)ELV011558806 |
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10.1016/j.cellsig.2013.08.022 doi GBVA2013013000016.pica (DE-627)ELV021983631 (ELSEVIER)S0898-6568(13)00257-X DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 620 VZ 610 VZ 44.94 bkl Song, Xiufeng verfasserin aut Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant 2013transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Seo, Jungwon oth Baameur, Faiza oth Vishnivetskiy, Sergey A. oth Chen, Qiuyan oth Kook, Seunghyi oth Kim, Miyeon oth Brooks, Evan K. oth Altenbach, Christian oth Hong, Yuan oth Hanson, Susan M. oth Palazzo, Maria C. oth Chen, Jeannie oth Hubbell, Wayne L. oth Gurevich, Eugenia V. oth Gurevich, Vsevolod V. oth Enthalten in Elsevier Science Zhao, Hailei ELSEVIER Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells 2013transfer abstract Amsterdam [u.a.] (DE-627)ELV011558806 volume:25 year:2013 number:12 pages:2613-2624 extent:12 https://doi.org/10.1016/j.cellsig.2013.08.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_40 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 25 2013 12 2613-2624 12 045F 540 |
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10.1016/j.cellsig.2013.08.022 doi GBVA2013013000016.pica (DE-627)ELV021983631 (ELSEVIER)S0898-6568(13)00257-X DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 620 VZ 610 VZ 44.94 bkl Song, Xiufeng verfasserin aut Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant 2013transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Seo, Jungwon oth Baameur, Faiza oth Vishnivetskiy, Sergey A. oth Chen, Qiuyan oth Kook, Seunghyi oth Kim, Miyeon oth Brooks, Evan K. oth Altenbach, Christian oth Hong, Yuan oth Hanson, Susan M. oth Palazzo, Maria C. oth Chen, Jeannie oth Hubbell, Wayne L. oth Gurevich, Eugenia V. oth Gurevich, Vsevolod V. oth Enthalten in Elsevier Science Zhao, Hailei ELSEVIER Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells 2013transfer abstract Amsterdam [u.a.] (DE-627)ELV011558806 volume:25 year:2013 number:12 pages:2613-2624 extent:12 https://doi.org/10.1016/j.cellsig.2013.08.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_40 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 25 2013 12 2613-2624 12 045F 540 |
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10.1016/j.cellsig.2013.08.022 doi GBVA2013013000016.pica (DE-627)ELV021983631 (ELSEVIER)S0898-6568(13)00257-X DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 620 VZ 610 VZ 44.94 bkl Song, Xiufeng verfasserin aut Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant 2013transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Seo, Jungwon oth Baameur, Faiza oth Vishnivetskiy, Sergey A. oth Chen, Qiuyan oth Kook, Seunghyi oth Kim, Miyeon oth Brooks, Evan K. oth Altenbach, Christian oth Hong, Yuan oth Hanson, Susan M. oth Palazzo, Maria C. oth Chen, Jeannie oth Hubbell, Wayne L. oth Gurevich, Eugenia V. oth Gurevich, Vsevolod V. oth Enthalten in Elsevier Science Zhao, Hailei ELSEVIER Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells 2013transfer abstract Amsterdam [u.a.] (DE-627)ELV011558806 volume:25 year:2013 number:12 pages:2613-2624 extent:12 https://doi.org/10.1016/j.cellsig.2013.08.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_40 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 25 2013 12 2613-2624 12 045F 540 |
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10.1016/j.cellsig.2013.08.022 doi GBVA2013013000016.pica (DE-627)ELV021983631 (ELSEVIER)S0898-6568(13)00257-X DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 620 VZ 610 VZ 44.94 bkl Song, Xiufeng verfasserin aut Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant 2013transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Seo, Jungwon oth Baameur, Faiza oth Vishnivetskiy, Sergey A. oth Chen, Qiuyan oth Kook, Seunghyi oth Kim, Miyeon oth Brooks, Evan K. oth Altenbach, Christian oth Hong, Yuan oth Hanson, Susan M. oth Palazzo, Maria C. oth Chen, Jeannie oth Hubbell, Wayne L. oth Gurevich, Eugenia V. oth Gurevich, Vsevolod V. oth Enthalten in Elsevier Science Zhao, Hailei ELSEVIER Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells 2013transfer abstract Amsterdam [u.a.] (DE-627)ELV011558806 volume:25 year:2013 number:12 pages:2613-2624 extent:12 https://doi.org/10.1016/j.cellsig.2013.08.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_40 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 25 2013 12 2613-2624 12 045F 540 |
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10.1016/j.cellsig.2013.08.022 doi GBVA2013013000016.pica (DE-627)ELV021983631 (ELSEVIER)S0898-6568(13)00257-X DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 660 VZ 620 VZ 610 VZ 44.94 bkl Song, Xiufeng verfasserin aut Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant 2013transfer abstract 12 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. Seo, Jungwon oth Baameur, Faiza oth Vishnivetskiy, Sergey A. oth Chen, Qiuyan oth Kook, Seunghyi oth Kim, Miyeon oth Brooks, Evan K. oth Altenbach, Christian oth Hong, Yuan oth Hanson, Susan M. oth Palazzo, Maria C. oth Chen, Jeannie oth Hubbell, Wayne L. oth Gurevich, Eugenia V. oth Gurevich, Vsevolod V. oth Enthalten in Elsevier Science Zhao, Hailei ELSEVIER Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells 2013transfer abstract Amsterdam [u.a.] (DE-627)ELV011558806 volume:25 year:2013 number:12 pages:2613-2624 extent:12 https://doi.org/10.1016/j.cellsig.2013.08.022 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_20 GBV_ILN_40 44.94 Hals-Nasen-Ohrenheilkunde VZ AR 25 2013 12 2613-2624 12 045F 540 |
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Enthalten in Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells Amsterdam [u.a.] volume:25 year:2013 number:12 pages:2613-2624 extent:12 |
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Enthalten in Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells Amsterdam [u.a.] volume:25 year:2013 number:12 pages:2613-2624 extent:12 |
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Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells |
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Song, Xiufeng @@aut@@ Seo, Jungwon @@oth@@ Baameur, Faiza @@oth@@ Vishnivetskiy, Sergey A. @@oth@@ Chen, Qiuyan @@oth@@ Kook, Seunghyi @@oth@@ Kim, Miyeon @@oth@@ Brooks, Evan K. @@oth@@ Altenbach, Christian @@oth@@ Hong, Yuan @@oth@@ Hanson, Susan M. @@oth@@ Palazzo, Maria C. @@oth@@ Chen, Jeannie @@oth@@ Hubbell, Wayne L. @@oth@@ Gurevich, Eugenia V. @@oth@@ Gurevich, Vsevolod V. @@oth@@ |
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rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant |
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Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant |
| abstract |
Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. |
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Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. |
| abstract_unstemmed |
Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization. |
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Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Arrestin-1 binds light-activated phosphorhodopsin and ensures timely signal shutoff. We show that high transgenic expression of an arrestin-1 mutant with enhanced rhodopsin binding and impaired oligomerization causes apoptotic rod death in mice. Dark rearing does not prevent mutant-induced cell death, ruling out the role of arrestin complexes with light-activated rhodopsin. Similar expression of WT arrestin-1 that robustly oligomerizes, which leads to only modest increase in the monomer concentration, does not affect rod survival. Moreover, WT arrestin-1 co-expressed with the mutant delays retinal degeneration. Thus, arrestin-1 mutant directly affects cell survival via binding partner(s) other than light-activated rhodopsin. Due to impaired self-association of the mutant its high expression dramatically increases the concentration of the monomer. The data suggest that monomeric arrestin-1 is cytotoxic and WT arrestin-1 protects rods by forming mixed oligomers with the mutant and/or competing with it for the binding to non-receptor partners. Thus, arrestin-1 self-association likely serves to keep low concentration of the toxic monomer. The reduction of the concentration of harmful monomer is an earlier unappreciated biological function of protein oligomerization.</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Seo, Jungwon</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Baameur, Faiza</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Vishnivetskiy, Sergey A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chen, Qiuyan</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kook, Seunghyi</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kim, Miyeon</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Brooks, Evan K.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Altenbach, Christian</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hong, Yuan</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hanson, Susan M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Palazzo, Maria C.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Chen, Jeannie</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hubbell, Wayne L.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gurevich, Eugenia V.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gurevich, Vsevolod V.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="n">Elsevier Science</subfield><subfield code="a">Zhao, Hailei ELSEVIER</subfield><subfield code="t">Electrochemical performance of Pr1−x Y x BaCo2O5+δ layered perovskites as cathode materials for intermediate-temperature solid oxide fuel cells</subfield><subfield code="d">2013transfer abstract</subfield><subfield code="g">Amsterdam [u.a.]</subfield><subfield code="w">(DE-627)ELV011558806</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:25</subfield><subfield code="g">year:2013</subfield><subfield code="g">number:12</subfield><subfield code="g">pages:2613-2624</subfield><subfield code="g">extent:12</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://doi.org/10.1016/j.cellsig.2013.08.022</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="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_20</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_40</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">25</subfield><subfield code="j">2013</subfield><subfield code="e">12</subfield><subfield code="h">2613-2624</subfield><subfield code="g">12</subfield></datafield><datafield tag="953" ind1=" " ind2=" "><subfield code="2">045F</subfield><subfield code="a">540</subfield></datafield></record></collection>
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