J
Jonathan M. Gleadle
Researcher at Flinders Medical Centre
Publications - 99
Citations - 12879
Jonathan M. Gleadle is an academic researcher from Flinders Medical Centre. The author has contributed to research in topics: Hypoxia-inducible factors & Regulation of gene expression. The author has an hindex of 34, co-authored 96 publications receiving 11917 citations. Previous affiliations of Jonathan M. Gleadle include John Radcliffe Hospital & University of Oxford.
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Journal ArticleDOI
C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation.
Andrew C. R Epstein,Jonathan M. Gleadle,Luke A. McNeill,Kirsty S. Hewitson,J F O'Rourke,David R. Mole,Mridul Mukherji,Eric Metzen,Michael A Wilson,Anu Dhanda,Ya-Min Tian,Norma Masson,Donald L. Hamilton,Panu Jaakkola,Robert Barstead,Jonathan Hodgkin,Patrick H. Maxwell,Christopher W. Pugh,Christopher J. Schofield,Peter J. Ratcliffe +19 more
TL;DR: Direct modulation of recombinant enzyme activity by graded hypoxia, iron chelation, and cobaltous ions mirrors the characteristics of HIF induction in vivo, fulfilling requirements for these enzymes being oxygen sensors that regulate HIF.
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Hypoxia-inducible factor-1 modulates gene expression in solid tumors and influences both angiogenesis and tumor growth.
Patrick H. Maxwell,Gabi U. Dachs,Jonathan M. Gleadle,Lynn G. Nicholls,Adrian L. Harris,Ian J. Stratford,Oliver Hankinson,Christopher W. Pugh,Peter J. Ratcliffe +8 more
TL;DR: Findings show that HIF-1 activation occurs in hypoxic regions of tumors and demonstrate a major influence on gene expression, tumor angiogenesis, and growth.
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Differential Function of the Prolyl Hydroxylases PHD1, PHD2, and PHD3 in the Regulation of Hypoxia-inducible Factor *
Rebecca J. Appelhoff,Ya-Min Tian,Raju R. Raval,Helen Turley,Adrian L. Harris,Christopher W. Pugh,Peter J. Ratcliffe,Jonathan M. Gleadle +7 more
TL;DR: It is shown using suppression by small interference RNA that each of the three PHD isoforms contributes in a non-redundant manner to the regulation of both Hif-1α and HIF-2α subunits and that the contribution of each PHD under particular culture conditions is strongly dependent on the abundance of the enzyme.
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Hypoxic enhancement of exosome release by breast cancer cells
TL;DR: Evidence is provided that hypoxia promotes the release of exosomes by breast cancer cells, and that this hypoxic response may be mediated by HIF-1 α, and this has significant implications for understanding the hypoxic tumour phenotype.
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Hypoxia-inducible Factor (HIF) Asparagine Hydroxylase Is Identical to Factor Inhibiting HIF (FIH) and Is Related to the Cupin Structural Family
Kirsty S. Hewitson,Luke A McNeill,Madeline V. Riordan,Ya-Min Tian,Alex N. Bullock,Richard W.D. Welford,Jonathan M. Elkins,Neil J. Oldham,Shoumo Bhattacharya,Jonathan M. Gleadle,Peter J. Ratcliffe,Christopher W. Pugh,Christopher J. Schofield +12 more
TL;DR: Assays using recombinant FIH and HIF-α fragments revealed that FIH is the enzyme that hydroxylates the CAD asparagine residue, that the activity is directly inhibited by cobalt(II) and limited by hypoxia, and that the oxygen in the alcohol of the hydroxyasparagine residues is directly derived from dioxygen.