Protein arginine phosphorylation in organisms
Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. R...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Huang, Biling [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2021transfer abstract |
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| Umfang: |
9 |
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| Übergeordnetes Werk: |
Enthalten in: Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor - Penchovsky, Robert ELSEVIER, 2019, structure, function and interactions, New York, NY [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:171 ; year:2021 ; day:28 ; month:02 ; pages:414-422 ; extent:9 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.ijbiomac.2021.01.015 |
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| 520 | |a Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. | ||
| 520 | |a Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. | ||
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10.1016/j.ijbiomac.2021.01.015 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001290.pica (DE-627)ELV05301863X (ELSEVIER)S0141-8130(21)00040-4 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Huang, Biling verfasserin aut Protein arginine phosphorylation in organisms 2021transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Zhao, Zhixing oth Zhao, Yufen oth Huang, Shaohua oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:171 year:2021 day:28 month:02 pages:414-422 extent:9 https://doi.org/10.1016/j.ijbiomac.2021.01.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 171 2021 28 0228 414-422 9 |
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10.1016/j.ijbiomac.2021.01.015 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001290.pica (DE-627)ELV05301863X (ELSEVIER)S0141-8130(21)00040-4 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Huang, Biling verfasserin aut Protein arginine phosphorylation in organisms 2021transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Zhao, Zhixing oth Zhao, Yufen oth Huang, Shaohua oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:171 year:2021 day:28 month:02 pages:414-422 extent:9 https://doi.org/10.1016/j.ijbiomac.2021.01.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 171 2021 28 0228 414-422 9 |
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10.1016/j.ijbiomac.2021.01.015 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001290.pica (DE-627)ELV05301863X (ELSEVIER)S0141-8130(21)00040-4 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Huang, Biling verfasserin aut Protein arginine phosphorylation in organisms 2021transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Zhao, Zhixing oth Zhao, Yufen oth Huang, Shaohua oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:171 year:2021 day:28 month:02 pages:414-422 extent:9 https://doi.org/10.1016/j.ijbiomac.2021.01.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 171 2021 28 0228 414-422 9 |
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10.1016/j.ijbiomac.2021.01.015 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001290.pica (DE-627)ELV05301863X (ELSEVIER)S0141-8130(21)00040-4 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Huang, Biling verfasserin aut Protein arginine phosphorylation in organisms 2021transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Zhao, Zhixing oth Zhao, Yufen oth Huang, Shaohua oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:171 year:2021 day:28 month:02 pages:414-422 extent:9 https://doi.org/10.1016/j.ijbiomac.2021.01.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 171 2021 28 0228 414-422 9 |
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10.1016/j.ijbiomac.2021.01.015 doi /cbs_pica/cbs_olc/import_discovery/elsevier/einzuspielen/GBV00000000001290.pica (DE-627)ELV05301863X (ELSEVIER)S0141-8130(21)00040-4 DE-627 ger DE-627 rakwb eng 570 610 VZ 58.30 bkl 50.22 bkl 44.09 bkl Huang, Biling verfasserin aut Protein arginine phosphorylation in organisms 2021transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. Zhao, Zhixing oth Zhao, Yufen oth Huang, Shaohua oth Enthalten in Elsevier Penchovsky, Robert ELSEVIER Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor 2019 structure, function and interactions New York, NY [u.a.] (DE-627)ELV002200198 volume:171 year:2021 day:28 month:02 pages:414-422 extent:9 https://doi.org/10.1016/j.ijbiomac.2021.01.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA 58.30 Biotechnologie VZ 50.22 Sensorik VZ 44.09 Medizintechnik VZ AR 171 2021 28 0228 414-422 9 |
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Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor |
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Protein arginine phosphorylation in organisms |
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Protein arginine phosphorylation in organisms |
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Huang, Biling |
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Automated DNA hybridization transfer with movable super-paramagnetic microbeads in a microflow reactor |
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10.1016/j.ijbiomac.2021.01.015 |
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protein arginine phosphorylation in organisms |
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Protein arginine phosphorylation in organisms |
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Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. |
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Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. |
| abstract_unstemmed |
Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of “high-energy” phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways. |
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Protein arginine phosphorylation in organisms |
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Zhao, Zhixing Zhao, Yufen Huang, Shaohua |
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