Pub. Date : 2014
PMID : 24563687
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Proline-hydroxylated hypoxia-inducible factor 1alpha (HIF-1alpha) upregulation in human tumours. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 2 | Proline-hydroxylated hypoxia-inducible factor 1alpha (HIF-1alpha) upregulation in human tumours. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 3 | To this end we optimised antibodies against the proline-hydroxylated forms of HIF-1alpha for use in formalin fixed paraffin embedded (FFPE) immunohistochemistry to assess effects in tumour cells in vivo. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 4 | We found that HIF-1alpha proline-hydroxylated at both VHL binding sites (Pro402 and Pro564), was present in hypoxic regions of a wide range of tumours, tumour xenografts and in moderately hypoxic cells in vitro. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 5 | Our conclusions are that the degradation of proline-hydroxylated HIF-1alpha may be rate-limited in tumours and therefore provides new insights into mechanisms of HIF upregulation. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 6 | Persistence of proline-hydroxylated HIF-1alpha in perinecrotic areas suggests there is adequate oxygen to support prolyl hydroxylase domain (PHD) activity and proline-hydroxylated HIF-1alpha may be the predominant form associated with the poorer prognosis that higher levels of HIF-1alpha confer. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 7 | Persistence of proline-hydroxylated HIF-1alpha in perinecrotic areas suggests there is adequate oxygen to support prolyl hydroxylase domain (PHD) activity and proline-hydroxylated HIF-1alpha may be the predominant form associated with the poorer prognosis that higher levels of HIF-1alpha confer. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |
| 8 | Persistence of proline-hydroxylated HIF-1alpha in perinecrotic areas suggests there is adequate oxygen to support prolyl hydroxylase domain (PHD) activity and proline-hydroxylated HIF-1alpha may be the predominant form associated with the poorer prognosis that higher levels of HIF-1alpha confer. | Proline | hypoxia inducible factor 1 subunit alpha | Homo sapiens |