A miniaturized peptidyl-prolyl isomerase enzyme assay
Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The develop...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Vivoli, Mirella [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: |
10 |
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| Übergeordnetes Werk: |
Enthalten in: Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems - Kroon, Frederieke J. ELSEVIER, 2014, methods in the biological sciences, San Diego, Calif |
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| Übergeordnetes Werk: |
volume:536 ; year:2017 ; day:1 ; month:11 ; pages:59-68 ; extent:10 |
| Links: |
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| DOI / URN: |
10.1016/j.ab.2017.08.004 |
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ELV041130685 |
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| 520 | |a Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. | ||
| 520 | |a Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. | ||
| 650 | 7 | |a High throughput |2 Elsevier | |
| 650 | 7 | |a Cyclophilin |2 Elsevier | |
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| 650 | 7 | |a Assay development |2 Elsevier | |
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| 700 | 1 | |a Renou, Julien |4 oth | |
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| 700 | 1 | |a Diaz, Suraya |4 oth | |
| 700 | 1 | |a Juli, Christina |4 oth | |
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| 700 | 1 | |a Renard, Pierre-Yves |4 oth | |
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10.1016/j.ab.2017.08.004 doi GBV00000000000262A.pica (DE-627)ELV041130685 (ELSEVIER)S0003-2697(17)30336-6 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Vivoli, Mirella verfasserin aut A miniaturized peptidyl-prolyl isomerase enzyme assay 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. High throughput Elsevier Cyclophilin Elsevier FKBP12 Elsevier Fluorescence Elsevier Assay development Elsevier Inhibitor Elsevier Peptide Elsevier Renou, Julien oth Chevalier, Arnaud oth Norville, Isobel H. oth Diaz, Suraya oth Juli, Christina oth Atkins, Helen oth Holzgrabe, Ulrike oth Renard, Pierre-Yves oth Sarkar-Tyson, Mitali oth Harmer, Nicholas J. oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:536 year:2017 day:1 month:11 pages:59-68 extent:10 https://doi.org/10.1016/j.ab.2017.08.004 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 536 2017 1 1101 59-68 10 045F 570 |
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10.1016/j.ab.2017.08.004 doi GBV00000000000262A.pica (DE-627)ELV041130685 (ELSEVIER)S0003-2697(17)30336-6 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Vivoli, Mirella verfasserin aut A miniaturized peptidyl-prolyl isomerase enzyme assay 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. High throughput Elsevier Cyclophilin Elsevier FKBP12 Elsevier Fluorescence Elsevier Assay development Elsevier Inhibitor Elsevier Peptide Elsevier Renou, Julien oth Chevalier, Arnaud oth Norville, Isobel H. oth Diaz, Suraya oth Juli, Christina oth Atkins, Helen oth Holzgrabe, Ulrike oth Renard, Pierre-Yves oth Sarkar-Tyson, Mitali oth Harmer, Nicholas J. oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:536 year:2017 day:1 month:11 pages:59-68 extent:10 https://doi.org/10.1016/j.ab.2017.08.004 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 536 2017 1 1101 59-68 10 045F 570 |
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10.1016/j.ab.2017.08.004 doi GBV00000000000262A.pica (DE-627)ELV041130685 (ELSEVIER)S0003-2697(17)30336-6 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Vivoli, Mirella verfasserin aut A miniaturized peptidyl-prolyl isomerase enzyme assay 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. High throughput Elsevier Cyclophilin Elsevier FKBP12 Elsevier Fluorescence Elsevier Assay development Elsevier Inhibitor Elsevier Peptide Elsevier Renou, Julien oth Chevalier, Arnaud oth Norville, Isobel H. oth Diaz, Suraya oth Juli, Christina oth Atkins, Helen oth Holzgrabe, Ulrike oth Renard, Pierre-Yves oth Sarkar-Tyson, Mitali oth Harmer, Nicholas J. oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:536 year:2017 day:1 month:11 pages:59-68 extent:10 https://doi.org/10.1016/j.ab.2017.08.004 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 536 2017 1 1101 59-68 10 045F 570 |
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10.1016/j.ab.2017.08.004 doi GBV00000000000262A.pica (DE-627)ELV041130685 (ELSEVIER)S0003-2697(17)30336-6 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Vivoli, Mirella verfasserin aut A miniaturized peptidyl-prolyl isomerase enzyme assay 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. High throughput Elsevier Cyclophilin Elsevier FKBP12 Elsevier Fluorescence Elsevier Assay development Elsevier Inhibitor Elsevier Peptide Elsevier Renou, Julien oth Chevalier, Arnaud oth Norville, Isobel H. oth Diaz, Suraya oth Juli, Christina oth Atkins, Helen oth Holzgrabe, Ulrike oth Renard, Pierre-Yves oth Sarkar-Tyson, Mitali oth Harmer, Nicholas J. oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:536 year:2017 day:1 month:11 pages:59-68 extent:10 https://doi.org/10.1016/j.ab.2017.08.004 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 536 2017 1 1101 59-68 10 045F 570 |
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10.1016/j.ab.2017.08.004 doi GBV00000000000262A.pica (DE-627)ELV041130685 (ELSEVIER)S0003-2697(17)30336-6 DE-627 ger DE-627 rakwb eng 570 540 570 DE-600 540 DE-600 550 VZ 333.7 VZ 610 VZ 15,3 ssgn PHARM DE-84 fid 44.40 bkl Vivoli, Mirella verfasserin aut A miniaturized peptidyl-prolyl isomerase enzyme assay 2017transfer abstract 10 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. High throughput Elsevier Cyclophilin Elsevier FKBP12 Elsevier Fluorescence Elsevier Assay development Elsevier Inhibitor Elsevier Peptide Elsevier Renou, Julien oth Chevalier, Arnaud oth Norville, Isobel H. oth Diaz, Suraya oth Juli, Christina oth Atkins, Helen oth Holzgrabe, Ulrike oth Renard, Pierre-Yves oth Sarkar-Tyson, Mitali oth Harmer, Nicholas J. oth Enthalten in Elsevier Kroon, Frederieke J. ELSEVIER Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems 2014 methods in the biological sciences San Diego, Calif (DE-627)ELV018040411 volume:536 year:2017 day:1 month:11 pages:59-68 extent:10 https://doi.org/10.1016/j.ab.2017.08.004 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U FID-PHARM SSG-OLC-PHA SSG-OPC-PHA 44.40 Pharmazie Pharmazeutika VZ AR 536 2017 1 1101 59-68 10 045F 570 |
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Enthalten in Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems San Diego, Calif volume:536 year:2017 day:1 month:11 pages:59-68 extent:10 |
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Enthalten in Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems San Diego, Calif volume:536 year:2017 day:1 month:11 pages:59-68 extent:10 |
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Informing policy to protect coastal coral reefs: Insight from a global review of reducing agricultural pollution to coastal ecosystems |
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Vivoli, Mirella @@aut@@ Renou, Julien @@oth@@ Chevalier, Arnaud @@oth@@ Norville, Isobel H. @@oth@@ Diaz, Suraya @@oth@@ Juli, Christina @@oth@@ Atkins, Helen @@oth@@ Holzgrabe, Ulrike @@oth@@ Renard, Pierre-Yves @@oth@@ Sarkar-Tyson, Mitali @@oth@@ Harmer, Nicholas J. @@oth@@ |
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a miniaturized peptidyl-prolyl isomerase enzyme assay |
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A miniaturized peptidyl-prolyl isomerase enzyme assay |
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Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. |
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Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. |
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Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates and products are challenging to distinguish. A well described continuous assay, coupled with the hydrolysis of a peptide by chymotrypsin is highly effective, but comparatively slow. |
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