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Items: 1 to 20 of 156

1.

TCTP increases stability of hypoxia-inducible factor 1α by interaction with and degradation of the tumour suppressor VHL.

Chen K, Chen S, Huang C, Cheng H, Zhou R.

Biol Cell. 2013 May;105(5):208-18. doi: 10.1111/boc.201200080. Epub 2013 Mar 15.

PMID:
23387829
2.

Phospholipase D2 promotes degradation of hypoxia-inducible factor-1α independent of lipase activity.

Park MH, Bae SS, Choi KY, Min do S.

Exp Mol Med. 2015 Nov 27;47:e196. doi: 10.1038/emm.2015.87.

3.

Estrogen receptor α is a novel target of the Von Hippel-Lindau protein and is responsible for the proliferation of VHL-deficient cells under hypoxic conditions.

Jung YS, Lee SJ, Yoon MH, Ha NC, Park BJ.

Cell Cycle. 2012 Dec 1;11(23):4462-73. doi: 10.4161/cc.22794. Epub 2012 Nov 16.

4.

The LIMD1 protein bridges an association between the prolyl hydroxylases and VHL to repress HIF-1 activity.

Foxler DE, Bridge KS, James V, Webb TM, Mee M, Wong SC, Feng Y, Constantin-Teodosiu D, Petursdottir TE, Bjornsson J, Ingvarsson S, Ratcliffe PJ, Longmore GD, Sharp TV.

Nat Cell Biol. 2012 Jan 29;14(2):201-8. doi: 10.1038/ncb2424.

PMID:
22286099
5.
6.

Phosphorylation of the von Hippel-Lindau protein (VHL) by protein kinase CK2 reduces its protein stability and affects p53 and HIF-1alpha mediated transcription.

Ampofo E, Kietzmann T, Zimmer A, Jakupovic M, Montenarh M, Götz C.

Int J Biochem Cell Biol. 2010 Oct;42(10):1729-35. doi: 10.1016/j.biocel.2010.07.008. Epub 2010 Jul 15.

PMID:
20637892
8.
9.

Regulation of glucose metabolism by p62/SQSTM1 through HIF1α.

Chen K, Zeng J, Xiao H, Huang C, Hu J, Yao W, Yu G, Xiao W, Xu H, Ye Z.

J Cell Sci. 2016 Feb 15;129(4):817-30. doi: 10.1242/jcs.178756. Epub 2016 Jan 7.

10.

Runx2 protein stabilizes hypoxia-inducible factor-1α through competition with von Hippel-Lindau protein (pVHL) and stimulates angiogenesis in growth plate hypertrophic chondrocytes.

Lee SH, Che X, Jeong JH, Choi JY, Lee YJ, Lee YH, Bae SC, Lee YM.

J Biol Chem. 2012 Apr 27;287(18):14760-71. doi: 10.1074/jbc.M112.340232. Epub 2012 Feb 20.

11.

Mechanism of regulation of the hypoxia-inducible factor-1 alpha by the von Hippel-Lindau tumor suppressor protein.

Tanimoto K, Makino Y, Pereira T, Poellinger L.

EMBO J. 2000 Aug 15;19(16):4298-309.

13.

The von Hippel-Lindau tumor suppressor gene product interacts with Sp1 to repress vascular endothelial growth factor promoter activity.

Mukhopadhyay D, Knebelmann B, Cohen HT, Ananth S, Sukhatme VP.

Mol Cell Biol. 1997 Sep;17(9):5629-39.

14.

CUL2-mediated clearance of misfolded TDP-43 is paradoxically affected by VHL in oligodendrocytes in ALS.

Uchida T, Tamaki Y, Ayaki T, Shodai A, Kaji S, Morimura T, Banno Y, Nishitsuji K, Sakashita N, Maki T, Yamashita H, Ito H, Takahashi R, Urushitani M.

Sci Rep. 2016 Jan 11;6:19118. doi: 10.1038/srep19118.

15.

Regulation of STRA13 by the von Hippel-Lindau tumor suppressor protein, hypoxia, and the UBC9/ubiquitin proteasome degradation pathway.

Ivanova AV, Ivanov SV, Danilkovitch-Miagkova A, Lerman MI.

J Biol Chem. 2001 May 4;276(18):15306-15. Epub 2001 Feb 6.

16.

EGLN3 prolyl hydroxylase regulates skeletal muscle differentiation and myogenin protein stability.

Fu J, Menzies K, Freeman RS, Taubman MB.

J Biol Chem. 2007 Apr 27;282(17):12410-8. Epub 2007 Mar 6.

17.

Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex.

Kamura T, Sato S, Iwai K, Czyzyk-Krzeska M, Conaway RC, Conaway JW.

Proc Natl Acad Sci U S A. 2000 Sep 12;97(19):10430-5.

18.

Glycogen synthase kinase 3 phosphorylates hypoxia-inducible factor 1alpha and mediates its destabilization in a VHL-independent manner.

Flügel D, Görlach A, Michiels C, Kietzmann T.

Mol Cell Biol. 2007 May;27(9):3253-65. Epub 2007 Feb 26.

19.

Activation of hypoxia-induced transcription in normoxia.

Hägg M, Wennström S.

Exp Cell Res. 2005 May 15;306(1):180-91. Epub 2005 Mar 19.

PMID:
15878343
20.

SUMO-specific protease 1 is essential for stabilization of HIF1alpha during hypoxia.

Cheng J, Kang X, Zhang S, Yeh ET.

Cell. 2007 Nov 2;131(3):584-95.

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