Oncotarget

VOLUME 2 (2011)

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About The Cover

PKM2 contributes to metabolic reprogramming and cancer progression by serving as a PHD3-dependent coactivator for HIF-1. Prolyl hydroxylation of PKM2 by PHD3 promotes the interaction of PKM2 with HIF-1α, thereby stabilizing HIF-1 binding to the HRE of target genes, recruitment of coactivator p300, histone acetylation, and subsequent transcription of HIF-1 target genes, which encode proteins that are involved in metabolic reprogramming, angiogenesis, and many other critical aspects of cancer progression. See Luo and Semenza.

Table of Contents

Editorial

https://doi.org/10.18632/oncotarget.300

525-526
Abstract  |  PDF  |  Full Text  |  How to cite

Editorial Comments

https://doi.org/10.18632/oncotarget.307

527-528
Abstract  |  PDF  |  Full Text  |  How to cite

Research Papers

https://doi.org/10.18632/oncotarget.298

529-537
Abstract  |  PDF  |  Full Text  |  How to cite

https://doi.org/10.18632/oncotarget.302

538-550
Abstract  |  PDF  |  Full Text  |  How to cite

Research Perspectives

https://doi.org/10.18632/oncotarget.299

551-556
Abstract  |  PDF  |  Full Text  |  How to cite

https://doi.org/10.18632/oncotarget.297

557-561
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https://doi.org/10.18632/oncotarget.301

562-568
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https://doi.org/10.18632/oncotarget.305

569-574
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https://doi.org/10.18632/oncotarget.304

575-586
Abstract  |  PDF  |  Full Text  |  How to cite


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