The hidden side of SERPINB1/Leukocyte Elastase Inhibitor
SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution o...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Torriglia, Alicia [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017transfer abstract |
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| Schlagwörter: |
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| Umfang: |
9 |
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| Übergeordnetes Werk: |
Enthalten in: Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate - Cho, Sung Beom ELSEVIER, 2014transfer abstract, London |
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| Übergeordnetes Werk: |
volume:62 ; year:2017 ; pages:178-186 ; extent:9 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.semcdb.2016.07.010 |
|---|
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| 520 | |a SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. | ||
| 520 | |a SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. | ||
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| 650 | 7 | |a Leukocyte elastase inhibitor |2 Elsevier | |
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| 650 | 7 | |a Apoptosis |2 Elsevier | |
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10.1016/j.semcdb.2016.07.010 doi GBVA2017018000003.pica (DE-627)ELV040564983 (ELSEVIER)S1084-9521(16)30205-1 DE-627 ger DE-627 rakwb eng 570 570 DE-600 540 VZ 500 VZ 33.25 bkl 31.00 bkl Torriglia, Alicia verfasserin aut The hidden side of SERPINB1/Leukocyte Elastase Inhibitor 2017transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. Murine neutrophil elastase inhibitor Elsevier Leukocyte elastase inhibitor Elsevier Inflammation Elsevier L-DNase II Elsevier Cell migration Elsevier Serpin B1 Elsevier Apoptosis Elsevier Martin, Elisabeth oth Jaadane, Imene oth Enthalten in Academic Press Cho, Sung Beom ELSEVIER Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate 2014transfer abstract London (DE-627)ELV017968445 volume:62 year:2017 pages:178-186 extent:9 https://doi.org/10.1016/j.semcdb.2016.07.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT GBV_ILN_70 33.25 Thermodynamik statistische Physik VZ 31.00 Mathematik: Allgemeines VZ AR 62 2017 178-186 9 045F 570 |
| spelling |
10.1016/j.semcdb.2016.07.010 doi GBVA2017018000003.pica (DE-627)ELV040564983 (ELSEVIER)S1084-9521(16)30205-1 DE-627 ger DE-627 rakwb eng 570 570 DE-600 540 VZ 500 VZ 33.25 bkl 31.00 bkl Torriglia, Alicia verfasserin aut The hidden side of SERPINB1/Leukocyte Elastase Inhibitor 2017transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. Murine neutrophil elastase inhibitor Elsevier Leukocyte elastase inhibitor Elsevier Inflammation Elsevier L-DNase II Elsevier Cell migration Elsevier Serpin B1 Elsevier Apoptosis Elsevier Martin, Elisabeth oth Jaadane, Imene oth Enthalten in Academic Press Cho, Sung Beom ELSEVIER Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate 2014transfer abstract London (DE-627)ELV017968445 volume:62 year:2017 pages:178-186 extent:9 https://doi.org/10.1016/j.semcdb.2016.07.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT GBV_ILN_70 33.25 Thermodynamik statistische Physik VZ 31.00 Mathematik: Allgemeines VZ AR 62 2017 178-186 9 045F 570 |
| allfields_unstemmed |
10.1016/j.semcdb.2016.07.010 doi GBVA2017018000003.pica (DE-627)ELV040564983 (ELSEVIER)S1084-9521(16)30205-1 DE-627 ger DE-627 rakwb eng 570 570 DE-600 540 VZ 500 VZ 33.25 bkl 31.00 bkl Torriglia, Alicia verfasserin aut The hidden side of SERPINB1/Leukocyte Elastase Inhibitor 2017transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. Murine neutrophil elastase inhibitor Elsevier Leukocyte elastase inhibitor Elsevier Inflammation Elsevier L-DNase II Elsevier Cell migration Elsevier Serpin B1 Elsevier Apoptosis Elsevier Martin, Elisabeth oth Jaadane, Imene oth Enthalten in Academic Press Cho, Sung Beom ELSEVIER Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate 2014transfer abstract London (DE-627)ELV017968445 volume:62 year:2017 pages:178-186 extent:9 https://doi.org/10.1016/j.semcdb.2016.07.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT GBV_ILN_70 33.25 Thermodynamik statistische Physik VZ 31.00 Mathematik: Allgemeines VZ AR 62 2017 178-186 9 045F 570 |
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10.1016/j.semcdb.2016.07.010 doi GBVA2017018000003.pica (DE-627)ELV040564983 (ELSEVIER)S1084-9521(16)30205-1 DE-627 ger DE-627 rakwb eng 570 570 DE-600 540 VZ 500 VZ 33.25 bkl 31.00 bkl Torriglia, Alicia verfasserin aut The hidden side of SERPINB1/Leukocyte Elastase Inhibitor 2017transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. Murine neutrophil elastase inhibitor Elsevier Leukocyte elastase inhibitor Elsevier Inflammation Elsevier L-DNase II Elsevier Cell migration Elsevier Serpin B1 Elsevier Apoptosis Elsevier Martin, Elisabeth oth Jaadane, Imene oth Enthalten in Academic Press Cho, Sung Beom ELSEVIER Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate 2014transfer abstract London (DE-627)ELV017968445 volume:62 year:2017 pages:178-186 extent:9 https://doi.org/10.1016/j.semcdb.2016.07.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT GBV_ILN_70 33.25 Thermodynamik statistische Physik VZ 31.00 Mathematik: Allgemeines VZ AR 62 2017 178-186 9 045F 570 |
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10.1016/j.semcdb.2016.07.010 doi GBVA2017018000003.pica (DE-627)ELV040564983 (ELSEVIER)S1084-9521(16)30205-1 DE-627 ger DE-627 rakwb eng 570 570 DE-600 540 VZ 500 VZ 33.25 bkl 31.00 bkl Torriglia, Alicia verfasserin aut The hidden side of SERPINB1/Leukocyte Elastase Inhibitor 2017transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. Murine neutrophil elastase inhibitor Elsevier Leukocyte elastase inhibitor Elsevier Inflammation Elsevier L-DNase II Elsevier Cell migration Elsevier Serpin B1 Elsevier Apoptosis Elsevier Martin, Elisabeth oth Jaadane, Imene oth Enthalten in Academic Press Cho, Sung Beom ELSEVIER Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate 2014transfer abstract London (DE-627)ELV017968445 volume:62 year:2017 pages:178-186 extent:9 https://doi.org/10.1016/j.semcdb.2016.07.010 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U SSG-OPC-MAT GBV_ILN_70 33.25 Thermodynamik statistische Physik VZ 31.00 Mathematik: Allgemeines VZ AR 62 2017 178-186 9 045F 570 |
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Enthalten in Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate London volume:62 year:2017 pages:178-186 extent:9 |
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Enthalten in Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate London volume:62 year:2017 pages:178-186 extent:9 |
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Murine neutrophil elastase inhibitor Leukocyte elastase inhibitor Inflammation L-DNase II Cell migration Serpin B1 Apoptosis |
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Spin-polarized bandgap of graphene induced by alternative chemisorption with MgO (111) substrate |
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Torriglia, Alicia @@aut@@ Martin, Elisabeth @@oth@@ Jaadane, Imene @@oth@@ |
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SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. |
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SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. |
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SERPINB1, also called Leukocyte Elastase Inhibitor (LEI) is a member of the clade B of SERPINS. It is an intracellular protein and acts primarily to protect the cell from proteases released into the cytoplasm during stress. Its role in inflammation is clear due to its involvement in the resolution of chronic inflammatory lung and bowel diseases. LEI/SERPINB1 intrinsically possesses two enzymatic activities: an antiprotease activity dependent on its reactive site loop, which is analogous to the other proteins of the family and an endonuclease activity which is unveiled by the cleavage of the reactive site loop. The conformational change induced by this cleavage also unveils a bipartite nuclear localization signal allowing the protein to translocate to the nucleus. Recent data indicate that it has also a role in cell migration suggesting that it could be involved in diverse processes like wound healing and malignant metastases. |
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