Is the small heat shock protein HSPB7 (cvHsp) a genuine actin-binding protein?
It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Muranova, Lydia K. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022transfer abstract |
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| Schlagwörter: |
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| Umfang: |
7 |
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| Übergeordnetes Werk: |
Enthalten in: Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation - Duan, Cong ELSEVIER, 2022, an international journal of biochemistry and molecular biology, Paris [u.a.] |
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| Übergeordnetes Werk: |
volume:202 ; year:2022 ; pages:103-109 ; extent:7 |
| Links: |
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| DOI / URN: |
10.1016/j.biochi.2022.08.007 |
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| 520 | |a It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. | ||
| 520 | |a It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. | ||
| 650 | 7 | |a Actin-binding proteins |2 Elsevier | |
| 650 | 7 | |a Actin |2 Elsevier | |
| 650 | 7 | |a Small heat shock proteins |2 Elsevier | |
| 700 | 1 | |a Shatov, Vladislav M. |4 oth | |
| 700 | 1 | |a Slushchev, Andrei V. |4 oth | |
| 700 | 1 | |a Gusev, Nikolai B. |4 oth | |
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10.1016/j.biochi.2022.08.007 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001967.pica (DE-627)ELV059520728 (ELSEVIER)S0300-9084(22)00211-5 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Muranova, Lydia K. verfasserin aut Is the small heat shock protein HSPB7 (cvHsp) a genuine actin-binding protein? 2022transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. Actin-binding proteins Elsevier Actin Elsevier Small heat shock proteins Elsevier Shatov, Vladislav M. oth Slushchev, Andrei V. oth Gusev, Nikolai B. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:202 year:2022 pages:103-109 extent:7 https://doi.org/10.1016/j.biochi.2022.08.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 202 2022 103-109 7 |
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10.1016/j.biochi.2022.08.007 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001967.pica (DE-627)ELV059520728 (ELSEVIER)S0300-9084(22)00211-5 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Muranova, Lydia K. verfasserin aut Is the small heat shock protein HSPB7 (cvHsp) a genuine actin-binding protein? 2022transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. Actin-binding proteins Elsevier Actin Elsevier Small heat shock proteins Elsevier Shatov, Vladislav M. oth Slushchev, Andrei V. oth Gusev, Nikolai B. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:202 year:2022 pages:103-109 extent:7 https://doi.org/10.1016/j.biochi.2022.08.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 202 2022 103-109 7 |
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10.1016/j.biochi.2022.08.007 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001967.pica (DE-627)ELV059520728 (ELSEVIER)S0300-9084(22)00211-5 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Muranova, Lydia K. verfasserin aut Is the small heat shock protein HSPB7 (cvHsp) a genuine actin-binding protein? 2022transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. Actin-binding proteins Elsevier Actin Elsevier Small heat shock proteins Elsevier Shatov, Vladislav M. oth Slushchev, Andrei V. oth Gusev, Nikolai B. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:202 year:2022 pages:103-109 extent:7 https://doi.org/10.1016/j.biochi.2022.08.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 202 2022 103-109 7 |
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10.1016/j.biochi.2022.08.007 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001967.pica (DE-627)ELV059520728 (ELSEVIER)S0300-9084(22)00211-5 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Muranova, Lydia K. verfasserin aut Is the small heat shock protein HSPB7 (cvHsp) a genuine actin-binding protein? 2022transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. Actin-binding proteins Elsevier Actin Elsevier Small heat shock proteins Elsevier Shatov, Vladislav M. oth Slushchev, Andrei V. oth Gusev, Nikolai B. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:202 year:2022 pages:103-109 extent:7 https://doi.org/10.1016/j.biochi.2022.08.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 202 2022 103-109 7 |
| allfieldsSound |
10.1016/j.biochi.2022.08.007 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001967.pica (DE-627)ELV059520728 (ELSEVIER)S0300-9084(22)00211-5 DE-627 ger DE-627 rakwb eng 600 VZ 50.70 bkl Muranova, Lydia K. verfasserin aut Is the small heat shock protein HSPB7 (cvHsp) a genuine actin-binding protein? 2022transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. Actin-binding proteins Elsevier Actin Elsevier Small heat shock proteins Elsevier Shatov, Vladislav M. oth Slushchev, Andrei V. oth Gusev, Nikolai B. oth Enthalten in Elsevier Duan, Cong ELSEVIER Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation 2022 an international journal of biochemistry and molecular biology Paris [u.a.] (DE-627)ELV008857954 volume:202 year:2022 pages:103-109 extent:7 https://doi.org/10.1016/j.biochi.2022.08.007 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 50.70 Energie: Allgemeines VZ AR 202 2022 103-109 7 |
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Enthalten in Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation Paris [u.a.] volume:202 year:2022 pages:103-109 extent:7 |
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Enthalten in Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation Paris [u.a.] volume:202 year:2022 pages:103-109 extent:7 |
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Energy-saving improvement of heat integration for separating dilute azeotropic components in extractive distillation |
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Muranova, Lydia K. @@aut@@ Shatov, Vladislav M. @@oth@@ Slushchev, Andrei V. @@oth@@ Gusev, Nikolai B. @@oth@@ |
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Is the small heat shock protein HSPB7 (cvHsp) a genuine actin-binding protein? |
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It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. |
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It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. |
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It is postulated that the small heat shock proteins directly interact with actin, affect formation and stabilize actin filaments. To verify this suggestion, we have analyzed interaction of recombinant human small heat shock protein HspB7 with skeletal muscle actin. In blot overlay HspB7 binds both G- and F-actin. The sites of interaction are located in the C-terminal large core domain of actin. In the course of ultracentrifugation F-actin and F-actin/tropomyosin complexes were pelleted and trapped HspB7. However, HspB7 pelleting was nonspecific and saturation was not achieved even at very high HspB7 concentration. HspB7 was unable to retard or prevent heat-induced F-actin aggregation. Native gel electrophoresis and chemical crosslinking failed to detect interaction of G-actin with HspB7, although both these methods clearly demonstrated formation of complexes formed by G-actin with DNAse I and cofilin-2. It is concluded that HspB7 is not a genuine actin-binding protein and its effect on actin filaments seems to be determined by interaction of HspB7 with minor regulatory proteins of actin filaments. |
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