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Rodrigo A Toledo, Yuejuan Qin, Subramanya Srikantan, Nicole Paes Morales, Qun Li, Yilun Deng, Sang-Woo Kim, Maria Adelaide A Pereira, Sergio P A Toledo, Xiaoping Su, Ricardo C T Aguiar, and Patricia L M Dahia

-Roqueplo et al . 2001 , Dahia et al . 2005 ). The HIF transcription factors form heterodimers comprised of an inducible, oxygen-labile α-subunit (HIF1α, HIF2α, or HIF3α) and a stable β-subunit (HIF1β/ARNT) that bind to the promoter of multiple genes

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Jenny Welander, Adam Andreasson, Michael Brauckhoff, Martin Bäckdahl, Catharina Larsson, Oliver Gimm, and Peter Söderkvist

that cover the HIF2α hydroxylation sites, as an instance of a gain-of-function mutation in exon 9 has been described ( Lorenzo et al . 2013 ). As one mutation of unknown pathogenicity has been described in exon 2, adjacent to the DNA-binding domain

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Zhengping Zhuang, Chunzhang Yang, Ales Ryska, Yuan Ji, Yingyong Hou, Sky D Graybill, Petra Bullova, Irina A Lubensky, Günter Klöppel, and Karel Pacak

Dear Editor, Somatic hypoxia-inducible factor 2 alpha ( HIF2A ) mutations are responsible for a newly discovered syndrome of multiple paragangliomas (PGL) and duodenal somatostatinomas associated with polycythemia (Pacak–Zhuang syndrome

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Nicole Bechmann, Mats Leif Moskopp, Martin Ullrich, Bruna Calsina, Pål William Wallace, Susan Richter, Markus Friedemann, Katharina Langton, Stephanie M J Fliedner, Henri J L M Timmers, Svenja Nölting, Felix Beuschlein, Martin Fassnacht, Aleksander Prejbisz, Karel Pacak, Hans K Ghayee, Stefan R Bornstein, Peter Dieterich, Jens Pietzsch, Ben Wielockx, Mercedes Robledo, Nan Qin, and Graeme Eisenhofer

( Richter et al. 2013 , Toledo et al. 2013 ). Higher expression of HIF2α is in particular a characteristic feature of cluster-1 compared to cluster-2 PPGLs ( Favier et al. 2002 , Eisenhofer et al. 2004 , López-Jiménez et al. 2010 , Qin et al

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K S Kimbro and J W Simons

mediated by prolyl hydroxylase domain-containing (PHD) proteins. The PHDs require O 2 as a co-factor for activity (Fig. 1 ). Biochemical detection of intracellular O 2 levels is directly mediated by the PHD enzymes, which regulate HIF-1α protein

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B Shan, J Gerez, M Haedo, M Fuertes, M Theodoropoulou, M Buchfelder, M Losa, G K Stalla, E Arzt, and U Renner

possible to perform all HIF-1α and VEGF-A stimulation experiments in all adenomas in parallel. Treatment of cells under hypoxia or CoCl 2 Before hypoxia exposure in a hypoxic chamber or CoCl 2 (Sigma) treatment (=hypoxia-mimicking condition), cell lines or

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Eamonn R Maher

The heterodimeric HIF transcription factors regulate cellular responses to hypoxia. Each heterodimer consists of a specific α-subunit (HIF1α, HIF2α and HIF3α) which, in hypoxic conditions, complexes with the HIFβ (ARNT) subunit ( Kaelin & Ratcliffe

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N Burrows, J Resch, R L Cowen, R von Wasielewski, C Hoang-Vu, C M West, K J Williams, and G Brabant

cancer cell lines to graded hypoxia or stimulation by a biochemical hypoxia mimetic cobalt chloride (CoCl 2 ) and tested the impact of inhibitors on the relevant genetically altered pathways in these cells. We show that HIF-1α is expressed in both

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Rodrigo Almeida Toledo

. 1991 , Hanahan et al. 1996 ). Neo-angiogenesis is currently considered a hallmark of cancers ( Hanahan & Weinberg 2011 ) and is briefly illustrated below. (a) the HIF2α-target VEGFA gene is de novo transcribed in hypoxic (or pseudohypoxic, see

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Emma R Woodward and Eamonn R Maher

factors (HIF-1 and HIF-2), which consist of a degradable alpha subunit and a stable constitutively expressed beta subunit ( Schofield & Ratcliffe 2004 ). Under normoxic conditions, HIF-1α and HIF-2α are rapidly polyubiquitylated and destroyed by the