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Determination and comparison of specific activity of the HIF‐prolyl hydroxylases
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| In: | FEBS Letters, 576, 2004, 1-2, S. 145-150 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Tuckerman, Jason R. Zhao, Yuguang Hewitson, Kirsty S. Tian, Ya-Min Pugh, Christopher W. Ratcliffe, Peter J. Mole, David R. Tuckerman, Jason R. Zhao, Yuguang Hewitson, Kirsty S. Tian, Ya-Min Pugh, Christopher W. Ratcliffe, Peter J. Mole, David R. |
|---|---|
| author |
Tuckerman, Jason R. Zhao, Yuguang Hewitson, Kirsty S. Tian, Ya-Min Pugh, Christopher W. Ratcliffe, Peter J. Mole, David R. |
| spellingShingle |
Tuckerman, Jason R. Zhao, Yuguang Hewitson, Kirsty S. Tian, Ya-Min Pugh, Christopher W. Ratcliffe, Peter J. Mole, David R. FEBS Letters Determination and comparison of specific activity of the HIF‐prolyl hydroxylases Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
tuckerman, jason r. |
| spelling |
Tuckerman, Jason R. Zhao, Yuguang Hewitson, Kirsty S. Tian, Ya-Min Pugh, Christopher W. Ratcliffe, Peter J. Mole, David R. 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2004.09.005 <jats:p>Hypoxia‐inducible factor (HIF) is a transcriptional complex that is regulated by oxygen sensitive hydroxylation of its α subunits by the prolyl hydroxylases PHD1, 2 and 3. To better understand the role of these enzymes in directing cellular responses to hypoxia, we derived an assay to determine their specific activity in both native cell extracts and recombinant sources of enzyme. We show that all three are capable of high rates of catalysis, in the order PHD2=PHD3 > PHD1, using substrate peptides derived from the C‐terminal degradation domain of HIF‐α subunits, and that each demonstrates similar and remarkable sensitivity to oxygen, commensurate with a common role in signaling hypoxia.</jats:p> Determination and comparison of specific activity of the HIF‐prolyl hydroxylases FEBS Letters |
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10.1016/j.febslet.2004.09.005 |
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Wiley, 2004 |
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| title |
Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_unstemmed |
Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_full |
Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_fullStr |
Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_full_unstemmed |
Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_short |
Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_sort |
determination and comparison of specific activity of the hif‐prolyl hydroxylases |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/j.febslet.2004.09.005 |
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2004 |
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145-150 |
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<jats:p>Hypoxia‐inducible factor (HIF) is a transcriptional complex that is regulated by oxygen sensitive hydroxylation of its α subunits by the prolyl hydroxylases PHD1, 2 and 3. To better understand the role of these enzymes in directing cellular responses to hypoxia, we derived an assay to determine their specific activity in both native cell extracts and recombinant sources of enzyme. We show that all three are capable of high rates of catalysis, in the order PHD2=PHD3 >
PHD1, using substrate peptides derived from the C‐terminal degradation domain of HIF‐α subunits, and that each demonstrates similar and remarkable sensitivity to oxygen, commensurate with a common role in signaling hypoxia.</jats:p> |
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| author | Tuckerman, Jason R., Zhao, Yuguang, Hewitson, Kirsty S., Tian, Ya-Min, Pugh, Christopher W., Ratcliffe, Peter J., Mole, David R. |
| author_facet | Tuckerman, Jason R., Zhao, Yuguang, Hewitson, Kirsty S., Tian, Ya-Min, Pugh, Christopher W., Ratcliffe, Peter J., Mole, David R., Tuckerman, Jason R., Zhao, Yuguang, Hewitson, Kirsty S., Tian, Ya-Min, Pugh, Christopher W., Ratcliffe, Peter J., Mole, David R. |
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| container_title | FEBS Letters |
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| description | <jats:p>Hypoxia‐inducible factor (HIF) is a transcriptional complex that is regulated by oxygen sensitive hydroxylation of its α subunits by the prolyl hydroxylases PHD1, 2 and 3. To better understand the role of these enzymes in directing cellular responses to hypoxia, we derived an assay to determine their specific activity in both native cell extracts and recombinant sources of enzyme. We show that all three are capable of high rates of catalysis, in the order PHD2=PHD3 > PHD1, using substrate peptides derived from the C‐terminal degradation domain of HIF‐α subunits, and that each demonstrates similar and remarkable sensitivity to oxygen, commensurate with a common role in signaling hypoxia.</jats:p> |
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| imprint | Wiley, 2004 |
| imprint_str_mv | Wiley, 2004 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 145-150 |
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| recordtype | ai |
| series | FEBS Letters |
| source_id | 49 |
| spelling | Tuckerman, Jason R. Zhao, Yuguang Hewitson, Kirsty S. Tian, Ya-Min Pugh, Christopher W. Ratcliffe, Peter J. Mole, David R. 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2004.09.005 <jats:p>Hypoxia‐inducible factor (HIF) is a transcriptional complex that is regulated by oxygen sensitive hydroxylation of its α subunits by the prolyl hydroxylases PHD1, 2 and 3. To better understand the role of these enzymes in directing cellular responses to hypoxia, we derived an assay to determine their specific activity in both native cell extracts and recombinant sources of enzyme. We show that all three are capable of high rates of catalysis, in the order PHD2=PHD3 > PHD1, using substrate peptides derived from the C‐terminal degradation domain of HIF‐α subunits, and that each demonstrates similar and remarkable sensitivity to oxygen, commensurate with a common role in signaling hypoxia.</jats:p> Determination and comparison of specific activity of the HIF‐prolyl hydroxylases FEBS Letters |
| spellingShingle | Tuckerman, Jason R., Zhao, Yuguang, Hewitson, Kirsty S., Tian, Ya-Min, Pugh, Christopher W., Ratcliffe, Peter J., Mole, David R., FEBS Letters, Determination and comparison of specific activity of the HIF‐prolyl hydroxylases, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_full | Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_fullStr | Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_full_unstemmed | Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_short | Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| title_sort | determination and comparison of specific activity of the hif‐prolyl hydroxylases |
| title_unstemmed | Determination and comparison of specific activity of the HIF‐prolyl hydroxylases |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/j.febslet.2004.09.005 |