The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression
• Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the trans...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Staab, Julia [verfasserIn] |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
2015transfer abstract |
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| Schlagwörter: |
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| Umfang: |
11 |
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| Übergeordnetes Werk: |
Enthalten in: Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls - Gayda, Mathieu ELSEVIER, 2015, Amsterdam [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:67 ; year:2015 ; number:2 ; pages:596-606 ; extent:11 |
| Links: |
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| DOI / URN: |
10.1016/j.molimm.2015.07.015 |
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| 520 | |a • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. | ||
| 520 | |a • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. | ||
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10.1016/j.molimm.2015.07.015 doi GBVA2015003000016.pica (DE-627)ELV023269251 (ELSEVIER)S0161-5890(15)30023-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 610 VZ 630 640 610 VZ Staab, Julia verfasserin aut The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. Interferon signalling Elsevier Cooperative DNA binding Elsevier Tetramerization Elsevier STAT proteins Elsevier Riebeling, Theresa oth Koch, Verena oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier Gayda, Mathieu ELSEVIER Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls 2015 Amsterdam [u.a.] (DE-627)ELV012849286 volume:67 year:2015 number:2 pages:596-606 extent:11 https://doi.org/10.1016/j.molimm.2015.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_40 GBV_ILN_227 GBV_ILN_674 AR 67 2015 2 596-606 11 045F 570 |
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10.1016/j.molimm.2015.07.015 doi GBVA2015003000016.pica (DE-627)ELV023269251 (ELSEVIER)S0161-5890(15)30023-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 610 VZ 630 640 610 VZ Staab, Julia verfasserin aut The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. Interferon signalling Elsevier Cooperative DNA binding Elsevier Tetramerization Elsevier STAT proteins Elsevier Riebeling, Theresa oth Koch, Verena oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier Gayda, Mathieu ELSEVIER Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls 2015 Amsterdam [u.a.] (DE-627)ELV012849286 volume:67 year:2015 number:2 pages:596-606 extent:11 https://doi.org/10.1016/j.molimm.2015.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_40 GBV_ILN_227 GBV_ILN_674 AR 67 2015 2 596-606 11 045F 570 |
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10.1016/j.molimm.2015.07.015 doi GBVA2015003000016.pica (DE-627)ELV023269251 (ELSEVIER)S0161-5890(15)30023-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 610 VZ 630 640 610 VZ Staab, Julia verfasserin aut The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. Interferon signalling Elsevier Cooperative DNA binding Elsevier Tetramerization Elsevier STAT proteins Elsevier Riebeling, Theresa oth Koch, Verena oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier Gayda, Mathieu ELSEVIER Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls 2015 Amsterdam [u.a.] (DE-627)ELV012849286 volume:67 year:2015 number:2 pages:596-606 extent:11 https://doi.org/10.1016/j.molimm.2015.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_40 GBV_ILN_227 GBV_ILN_674 AR 67 2015 2 596-606 11 045F 570 |
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10.1016/j.molimm.2015.07.015 doi GBVA2015003000016.pica (DE-627)ELV023269251 (ELSEVIER)S0161-5890(15)30023-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 610 VZ 630 640 610 VZ Staab, Julia verfasserin aut The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. Interferon signalling Elsevier Cooperative DNA binding Elsevier Tetramerization Elsevier STAT proteins Elsevier Riebeling, Theresa oth Koch, Verena oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier Gayda, Mathieu ELSEVIER Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls 2015 Amsterdam [u.a.] (DE-627)ELV012849286 volume:67 year:2015 number:2 pages:596-606 extent:11 https://doi.org/10.1016/j.molimm.2015.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_40 GBV_ILN_227 GBV_ILN_674 AR 67 2015 2 596-606 11 045F 570 |
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10.1016/j.molimm.2015.07.015 doi GBVA2015003000016.pica (DE-627)ELV023269251 (ELSEVIER)S0161-5890(15)30023-7 DE-627 ger DE-627 rakwb eng 570 610 570 DE-600 610 DE-600 610 VZ 630 640 610 VZ Staab, Julia verfasserin aut The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression 2015transfer abstract 11 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. • Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. Interferon signalling Elsevier Cooperative DNA binding Elsevier Tetramerization Elsevier STAT proteins Elsevier Riebeling, Theresa oth Koch, Verena oth Herrmann-Lingen, Christoph oth Meyer, Thomas oth Enthalten in Elsevier Gayda, Mathieu ELSEVIER Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls 2015 Amsterdam [u.a.] (DE-627)ELV012849286 volume:67 year:2015 number:2 pages:596-606 extent:11 https://doi.org/10.1016/j.molimm.2015.07.015 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OLC-PHA GBV_ILN_40 GBV_ILN_227 GBV_ILN_674 AR 67 2015 2 596-606 11 045F 570 |
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Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls |
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570 - Life sciences; biology 610 - Medicine & health 630 - Agriculture 640 - Home & family management |
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Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls |
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The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression |
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(DE-627)ELV023269251 (ELSEVIER)S0161-5890(15)30023-7 |
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The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression |
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Staab, Julia |
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Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls |
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Letter regarding the article: Changes in BNP and cardiac troponin I after high-intensity interval and endurance exercise in heart failure patients and healthy controls |
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2015 |
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Staab, Julia |
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Staab, Julia |
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10.1016/j.molimm.2015.07.015 |
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570 610 630 640 |
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two interfaces of the stat1 n-terminus exhibit opposite functions in ifnγ-regulated gene expression |
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The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression |
| abstract |
• Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. |
| abstractGer |
• Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. |
| abstract_unstemmed |
• Four surfaced exposed and negatively charged amino acid residues in the N-terminal domain of STAT1 are engaged in the release of tyrosine-phosphorylated tetramers from DNA. • Despite elevated tyrosine-phosphorylation and prolonged nuclear accumulation upon stimulation of cells with IFNγ, the transcriptional consequences of STAT1 N-terminal gain-of-function mutants affect gene expression not globally, but in a promoter-specific manner. • The STAT1 N-domain is involved in the termination of IFNγ-mediated signal transduction by disrupting higher-order oligomers on DNA. • Our findings reveal a new mechanistic insight into how protein-DNA interactions regulate STAT1-mediated target gene recognition. |
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The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression |
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https://doi.org/10.1016/j.molimm.2015.07.015 |
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Riebeling, Theresa Koch, Verena Herrmann-Lingen, Christoph Meyer, Thomas |
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