Quantitative analysis of protein orientation in membrane environments by kinase activity
AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine mem...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Xiong, Wen [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016transfer abstract |
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| Schlagwörter: |
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| Umfang: |
5 |
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| Übergeordnetes Werk: |
Enthalten in: Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) - Saunders, Richard ELSEVIER, 2017, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:121 ; year:2016 ; number:2 ; pages:242-246 ; extent:5 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.jbiosc.2015.06.002 |
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ELV035078731 |
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| 245 | 1 | 0 | |a Quantitative analysis of protein orientation in membrane environments by kinase activity |
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| 520 | |a AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. | ||
| 520 | |a AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. | ||
| 650 | 7 | |a Kinase activity |2 Elsevier | |
| 650 | 7 | |a Protein orientation |2 Elsevier | |
| 650 | 7 | |a AgrC |2 Elsevier | |
| 650 | 7 | |a Liposome |2 Elsevier | |
| 650 | 7 | |a Thiol-reactive reagent |2 Elsevier | |
| 700 | 1 | |a Quan, Chunshan |4 oth | |
| 700 | 1 | |a Zhang, Xuning |4 oth | |
| 700 | 1 | |a Wang, Lina |4 oth | |
| 700 | 1 | |a Liu, Baoquan |4 oth | |
| 700 | 1 | |a Jin, Liming |4 oth | |
| 700 | 1 | |a Fan, Shengdi |4 oth | |
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2016 |
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10.1016/j.jbiosc.2015.06.002 doi GBVA2016003000028.pica (DE-627)ELV035078731 (ELSEVIER)S1389-1723(15)00232-7 DE-627 ger DE-627 rakwb eng 570 540 660 570 DE-600 540 DE-600 660 DE-600 610 VZ 540 660 VZ 58.34 bkl Xiong, Wen verfasserin aut Quantitative analysis of protein orientation in membrane environments by kinase activity 2016transfer abstract 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. Kinase activity Elsevier Protein orientation Elsevier AgrC Elsevier Liposome Elsevier Thiol-reactive reagent Elsevier Quan, Chunshan oth Zhang, Xuning oth Wang, Lina oth Liu, Baoquan oth Jin, Liming oth Fan, Shengdi oth Enthalten in Elsevier Science Saunders, Richard ELSEVIER Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) 2017 Amsterdam [u.a.] (DE-627)ELV020602480 volume:121 year:2016 number:2 pages:242-246 extent:5 https://doi.org/10.1016/j.jbiosc.2015.06.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.34 Lebensmitteltechnologie VZ AR 121 2016 2 242-246 5 045F 570 |
| spelling |
10.1016/j.jbiosc.2015.06.002 doi GBVA2016003000028.pica (DE-627)ELV035078731 (ELSEVIER)S1389-1723(15)00232-7 DE-627 ger DE-627 rakwb eng 570 540 660 570 DE-600 540 DE-600 660 DE-600 610 VZ 540 660 VZ 58.34 bkl Xiong, Wen verfasserin aut Quantitative analysis of protein orientation in membrane environments by kinase activity 2016transfer abstract 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. Kinase activity Elsevier Protein orientation Elsevier AgrC Elsevier Liposome Elsevier Thiol-reactive reagent Elsevier Quan, Chunshan oth Zhang, Xuning oth Wang, Lina oth Liu, Baoquan oth Jin, Liming oth Fan, Shengdi oth Enthalten in Elsevier Science Saunders, Richard ELSEVIER Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) 2017 Amsterdam [u.a.] (DE-627)ELV020602480 volume:121 year:2016 number:2 pages:242-246 extent:5 https://doi.org/10.1016/j.jbiosc.2015.06.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.34 Lebensmitteltechnologie VZ AR 121 2016 2 242-246 5 045F 570 |
| allfields_unstemmed |
10.1016/j.jbiosc.2015.06.002 doi GBVA2016003000028.pica (DE-627)ELV035078731 (ELSEVIER)S1389-1723(15)00232-7 DE-627 ger DE-627 rakwb eng 570 540 660 570 DE-600 540 DE-600 660 DE-600 610 VZ 540 660 VZ 58.34 bkl Xiong, Wen verfasserin aut Quantitative analysis of protein orientation in membrane environments by kinase activity 2016transfer abstract 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. Kinase activity Elsevier Protein orientation Elsevier AgrC Elsevier Liposome Elsevier Thiol-reactive reagent Elsevier Quan, Chunshan oth Zhang, Xuning oth Wang, Lina oth Liu, Baoquan oth Jin, Liming oth Fan, Shengdi oth Enthalten in Elsevier Science Saunders, Richard ELSEVIER Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) 2017 Amsterdam [u.a.] (DE-627)ELV020602480 volume:121 year:2016 number:2 pages:242-246 extent:5 https://doi.org/10.1016/j.jbiosc.2015.06.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.34 Lebensmitteltechnologie VZ AR 121 2016 2 242-246 5 045F 570 |
| allfieldsGer |
10.1016/j.jbiosc.2015.06.002 doi GBVA2016003000028.pica (DE-627)ELV035078731 (ELSEVIER)S1389-1723(15)00232-7 DE-627 ger DE-627 rakwb eng 570 540 660 570 DE-600 540 DE-600 660 DE-600 610 VZ 540 660 VZ 58.34 bkl Xiong, Wen verfasserin aut Quantitative analysis of protein orientation in membrane environments by kinase activity 2016transfer abstract 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. Kinase activity Elsevier Protein orientation Elsevier AgrC Elsevier Liposome Elsevier Thiol-reactive reagent Elsevier Quan, Chunshan oth Zhang, Xuning oth Wang, Lina oth Liu, Baoquan oth Jin, Liming oth Fan, Shengdi oth Enthalten in Elsevier Science Saunders, Richard ELSEVIER Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) 2017 Amsterdam [u.a.] (DE-627)ELV020602480 volume:121 year:2016 number:2 pages:242-246 extent:5 https://doi.org/10.1016/j.jbiosc.2015.06.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.34 Lebensmitteltechnologie VZ AR 121 2016 2 242-246 5 045F 570 |
| allfieldsSound |
10.1016/j.jbiosc.2015.06.002 doi GBVA2016003000028.pica (DE-627)ELV035078731 (ELSEVIER)S1389-1723(15)00232-7 DE-627 ger DE-627 rakwb eng 570 540 660 570 DE-600 540 DE-600 660 DE-600 610 VZ 540 660 VZ 58.34 bkl Xiong, Wen verfasserin aut Quantitative analysis of protein orientation in membrane environments by kinase activity 2016transfer abstract 5 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. Kinase activity Elsevier Protein orientation Elsevier AgrC Elsevier Liposome Elsevier Thiol-reactive reagent Elsevier Quan, Chunshan oth Zhang, Xuning oth Wang, Lina oth Liu, Baoquan oth Jin, Liming oth Fan, Shengdi oth Enthalten in Elsevier Science Saunders, Richard ELSEVIER Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) 2017 Amsterdam [u.a.] (DE-627)ELV020602480 volume:121 year:2016 number:2 pages:242-246 extent:5 https://doi.org/10.1016/j.jbiosc.2015.06.002 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.34 Lebensmitteltechnologie VZ AR 121 2016 2 242-246 5 045F 570 |
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Enthalten in Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) Amsterdam [u.a.] volume:121 year:2016 number:2 pages:242-246 extent:5 |
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Enthalten in Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) Amsterdam [u.a.] volume:121 year:2016 number:2 pages:242-246 extent:5 |
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Oral Squamous Cell Carcinoma in Three Related Kowari (Dasyuroides byrnei) |
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Xiong, Wen @@aut@@ Quan, Chunshan @@oth@@ Zhang, Xuning @@oth@@ Wang, Lina @@oth@@ Liu, Baoquan @@oth@@ Jin, Liming @@oth@@ Fan, Shengdi @@oth@@ |
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AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. |
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AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. |
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AgrC is an integral membrane receptor protein with histidine kinase activity in the accessory gene regulator (agr) quorum-sensing system of Staphylococcus aureus. In this study, proteoliposomes were used as a model to investigate AgrC orientation. Many approaches have been described to determine membrane protein orientation, but they are often complicated and time consuming. In this study, AgrC orientation in liposomes was determined by thiol-reactive reagent labeling and a kinase activity assay. Our results suggest use of a kinase activity assay could get an accurate percentage of functional protein orientation and only cost nearly one-sixth of the time compared with the method based on thiol-reactive reagent labeling. We present an effective and rapid method for determining the orientation of membrane protein kinases like AgrC. |
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