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Ya-Min Tian
Researcher at University of Oxford
Publications - 25
Citations - 12643
Ya-Min Tian is an academic researcher from University of Oxford. The author has contributed to research in topics: Hydroxylation & Procollagen-proline dioxygenase. The author has an hindex of 22, co-authored 24 publications receiving 11709 citations. Previous affiliations of Ya-Min Tian include Ludwig Institute for Cancer Research & Wellcome Trust Centre for Human Genetics.
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Journal ArticleDOI
Targeting of HIF-alpha to the von Hippel-Lindau Ubiquitylation Complex by O2-Regulated Prolyl Hydroxylation
Panu Jaakkola,David R. Mole,Ya-Min Tian,Michael I. Wilson,Janine Gielbert,Simon J. Gaskell,Alex von Kriegsheim,Holger F. Hebestreit,Mridul Mukherji,Christopher J. Schofield,Patrick H. Maxwell,Christopher W. Pugh,Peter J. Ratcliffe +12 more
TL;DR: It is shown that the interaction between human pVHL and a specific domain of the HIF-1α subunit is regulated through hydroxylation of a proline residue by an enzyme the authors have termed Hif-α prolyl-hydroxylase (HIF-PH).
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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.
Journal ArticleDOI
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.
Journal ArticleDOI
The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases
Rasheduzzaman Chowdhury,Kar Kheng Yeoh,Ya-Min Tian,Lars Hillringhaus,Eleanor A.L. Bagg,Nathan R. Rose,Ivanhoe K. H. Leung,Xuan S Li,Esther C. Y. Woon,Ming Yang,Michael A. McDonough,Oliver N. King,Ian J. Clifton,Robert J. Klose,Timothy D. W. Claridge,Peter J. Ratcliffe,Christopher J. Schofield,Akane Kawamura +17 more
TL;DR: The results indicate that candidate oncogenic pathways in IDH‐associated malignancy should include those that are regulated by other 2OG oxygenases than HIF hydroxylases, in particular those involving the regulation of histone methylation.
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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.