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Volumn 17, Issue 2, 2013, Pages 111-120

Prolyl 4 hydroxylase: A critical target in the pathophysiology of diseases

Author keywords

Hypoxia inducible factor; Inflammation; Ischemia; Prolyl hydroxylase

Indexed keywords

HYPOXIA INDUCIBLE FACTOR; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE;

EID: 84877986992     PISSN: 12264512     EISSN: 20933827     Source Type: Journal    
DOI: 10.4196/kjpp.2013.17.2.111     Document Type: Review
Times cited : (17)

References (116)
  • 2
    • 0035068434 scopus 로고    scopus 로고
    • Collagens and collagen-related diseases
    • Myllyharju J, Kivirikko KI. Collagens and collagen-related diseases. Ann Med. 2001;33:7-21. (Pubitemid 32238752)
    • (2001) Annals of Medicine , vol.33 , Issue.1 , pp. 7-21
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 3
    • 0033621541 scopus 로고    scopus 로고
    • Cuticle collagen genesexpression in Caenorhabditis elegans
    • DOI 10.1016/S0168-9525(99)01857-0, PII S0168952599018570
    • Johnstone IL. Cuticle collagen genes. Expression in Caenorhabditis elegans. Trends Genet. 2000;16:21-27. (Pubitemid 30062234)
    • (2000) Trends in Genetics , vol.16 , Issue.1 , pp. 21-27
    • Johnstone, I.L.1
  • 4
    • 0037047409 scopus 로고    scopus 로고
    • The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits
    • Myllyharju J, Kukkola L, Winter AD, Page AP. The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits. J Biol Chem. 2002;277:29187-29196.
    • (2002) J Biol Chem , vol.277 , pp. 29187-29196
    • Myllyharju, J.1    Kukkola, L.2    Winter, A.D.3    Page, A.P.4
  • 5
    • 0033525689 scopus 로고    scopus 로고
    • Cloning of the alpha subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties
    • DOI 10.1074/jbc.274.10.6790
    • Annunen P, Koivunen P, Kivirikko KI. Cloning of the alpha subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties. J Biol Chem. 1999;274:6790-6796. (Pubitemid 29111103)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.10 , pp. 6790-6796
    • Annunen, P.1    Koivunen, P.2    Kivirikko, K.I.3
  • 6
    • 0034894096 scopus 로고    scopus 로고
    • Characterization and expression of enzymatically active recombinant filarial prolyl 4-hydroxylase
    • DOI 10.1016/S0166-6851(01)00317-6, PII S0166685101003176
    • Merriweather A, Guenzler V, Brenner M, Unnasch TR. Characterization and expression of enzymatically active recombinant filarial prolyl 4-hydroxylase. Mol Biochem Parasitol. 2001;116:185-197. (Pubitemid 32777827)
    • (2001) Molecular and Biochemical Parasitology , vol.116 , Issue.2 , pp. 185-197
    • Merriweather, A.1    Guenzler, V.2    Brenner, M.3    Unnasch, T.R.4
  • 7
    • 0037462716 scopus 로고    scopus 로고
    • A hypodermally expressed prolyl 4-hydroxylase from the filarial nematode Brugia malayi is soluble and active in the absence of protein disulfide isomerase
    • DOI 10.1074/jbc.M210381200
    • Winter AD, Myllyharju J, Page AP. A hypodermally expressed prolyl 4-hydroxylase from the filarial nematode Brugia malayi is soluble and active in the absence of protein disulfide isomerase. J Biol Chem. 2003;278:2554-2562. (Pubitemid 36801333)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.4 , pp. 2554-2562
    • Winter, A.D.1    Myllyharju, J.2    Page, A.P.3
  • 8
    • 0024289220 scopus 로고
    • Prolyl 4-hydroxylase from Volvox carteri. A low-Mr enzyme antigenically related to the alpha subunit of the vertebrate enzyme
    • Kaska DD, Myllylä R, Günzler V, Gibor A, Kivirikko KI. Prolyl 4-hydroxylase from Volvox carteri. A low-Mr enzyme antigenically related to the alpha subunit of the vertebrate enzyme. Biochem J. 1988;256:257-263.
    • (1988) Biochem J , vol.256 , pp. 257-263
    • Kaska, D.D.1    Myllylä, R.2    Günzler, V.3    Gibor, A.4    Kivirikko, K.I.5
  • 9
    • 0032990359 scopus 로고    scopus 로고
    • Ultrastructural localisation and further biochemical characterisation of prolyl 4-hydroxylase from Phaseolus vulgaris: Comparative analysis
    • DOI 10.1016/S1357-2725(98)00126-5, PII S1357272598001265
    • Wojtaszek P, Smith CG, Bolwell GP. Ultrastructural localisation and further biochemical characterisation of prolyl 4-hydroxylase from Phaseolus vulgaris: comparative analysis. Int J Biochem Cell Biol. 1999;31:463-477. (Pubitemid 29112907)
    • (1999) International Journal of Biochemistry and Cell Biology , vol.31 , Issue.3-4 , pp. 463-477
    • Wojtaszek, P.1    Smith, C.G.2    Bolwell, G.P.3
  • 10
    • 0002079883 scopus 로고
    • Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins
    • Harding JJ, Crabbe JC, eds. Boca Raton, FL: CRC Press
    • Kivirikko, KI, Myllyla R, Pihlajaniemi T. Hydroxylation of proline and lysine residues in collagens and other animal and plant proteins. In: Harding JJ, Crabbe JC, eds. Post-Translational Modifications of Proteins. Boca Raton, FL: CRC Press; 1992. p.1-51.
    • (1992) Post-Translational Modifications of Proteins , pp. 1-51
    • Kivirikko, K.I.1    Myllyla, R.2    Pihlajaniemi, T.3
  • 11
    • 0031893340 scopus 로고    scopus 로고
    • Prolyl 4-hydroxylases and their protein disulfide isomerase subunit
    • DOI 10.1016/S0945-053X(98)90009-9
    • Kivirikko KI, Myllyharju J. Prolyl 4-hydroxylases and their protein disulfide isomerase subunit. Matrix Biol. 1998;16:357-368. (Pubitemid 28069862)
    • (1998) Matrix Biology , vol.16 , Issue.7 , pp. 357-368
    • Kivirikko, K.I.1    Myllyharju, J.2
  • 12
    • 0031616949 scopus 로고    scopus 로고
    • Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases
    • Kivirikko KI, Pihlajaniemi T. Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases. Adv Enzymol Relat Areas Mol Biol. 1998;72:325-398.
    • (1998) Adv Enzymol Relat Areas Mol Biol , vol.72 , pp. 325-398
    • Kivirikko, K.I.1    Pihlajaniemi, T.2
  • 13
    • 0037189554 scopus 로고    scopus 로고
    • Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana: Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides
    • DOI 10.1074/jbc.M201865200
    • Hieta R, Myllyharju J. Cloning and characterization of a low molecular weight prolyl 4-hydroxylase from Arabidopsis thaliana. Effective hydroxylation of proline-rich, collagen-like, and hypoxia-inducible transcription factor alpha-like peptides. J Biol Chem. 2002;277:23965-23971. (Pubitemid 34952242)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23965-23971
    • Hieta, R.1    Myllyharju, J.2
  • 15
    • 0033529597 scopus 로고    scopus 로고
    • Evidence for 4-hydroxyproline in viral proteins. Characterization of a viral prolyl 4-hydroxylase and its peptide substrates
    • Eriksson M, Myllyharju J, Tu H, Hellman M, Kivirikko KI. Evidence for 4-hydroxyproline in viral proteins. Characterization of a viral prolyl 4-hydroxylase and its peptide substrates. J Biol Chem. 1999;274:22131-22134.
    • (1999) J Biol Chem , vol.274 , pp. 22131-22134
    • Eriksson, M.1    Myllyharju, J.2    Tu, H.3    Hellman, M.4    Kivirikko, K.I.5
  • 16
    • 0037178812 scopus 로고    scopus 로고
    • Streptococcal Scl1 and Scl2 proteins form collagen-like triple helices
    • DOI 10.1074/jbc.M201163200
    • Xu Y, Keene DR, Bujnicki JM, Höök M, Lukomski S. Streptococcal Scl1 and Scl2 proteins form collagen-like triple helices. J Biol Chem. 2002;277:27312-27318. (Pubitemid 34951750)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 27312-27318
    • Xu, Y.1    Keene, D.R.2    Bujnicki, J.M.3    Hook, M.4    Lukomski, S.5
  • 17
    • 0030807022 scopus 로고    scopus 로고
    • 2 tetramer
    • DOI 10.1074/jbc.272.28.17342
    • Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlaja niemi T, Kivirikko KI. Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. J Biol Chem. 1997;272:17342-17348. (Pubitemid 27311159)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.28 , pp. 17342-17348
    • Annunen, P.1    Helaakoski, T.2    Myllyharju, J.3    Veijola, J.4    Pihlajaniemi, T.5    Kivirikko, K.I.6
  • 21
    • 0032513230 scopus 로고    scopus 로고
    • The novel type II prolyl 4-hydroxylase is the main enzyme form in chondrocytes and capillary endothelial cells, whereas the type I enzyme predominates in most cells
    • DOI 10.1074/jbc.273.11.5989
    • Annunen P, Autio-Harmainen H, Kivirikko KI. The novel type II prolyl 4-hydroxylase is the main enzyme form in chondrocytes and capillary endothelial cells, whereas the type I enzyme predominates in most cells. J Biol Chem. 1998;273:5989-5992. (Pubitemid 28144671)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.11 , pp. 5989-5992
    • Annunen, P.1    Autio-Harmainen, H.2    Kivirikko, K.I.3
  • 23
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension
    • Wang GL, Jiang BH, Rue EA, Semenza GL. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. Proc Natl Acad Sci U S A. 1995;92:5510-5514.
    • (1995) Proc Natl Acad Sci U S a , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.H.2    Rue, E.A.3    Semenza, G.L.4
  • 24
    • 0026625037 scopus 로고
    • Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor
    • Reyes H, Reisz-Porszasz S, Hankinson O. Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. Science. 1992;256:1193-1195.
    • (1992) Science , vol.256 , pp. 1193-1195
    • Reyes, H.1    Reisz-Porszasz, S.2    Hankinson, O.3
  • 25
    • 33751169387 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 (HIF-1)
    • Ke Q, Costa M. Hypoxia-inducible factor-1 (HIF-1). Mol Pharmacol. 2006;70:1469-1480.
    • (2006) Mol Pharmacol , vol.70 , pp. 1469-1480
    • Ke, Q.1    Costa, M.2
  • 26
    • 0032190614 scopus 로고    scopus 로고
    • 2 homeostasis
    • DOI 10.1016/S0959-437X(98)80016-6
    • Semenza GL. Hypoxia-inducible factor 1: master regulator of O2 homeostasis. Curr Opin Genet Dev. 1998;8:588-594. (Pubitemid 28477364)
    • (1998) Current Opinion in Genetics and Development , vol.8 , Issue.5 , pp. 588-594
    • Semenza, G.L.1
  • 27
    • 0032030839 scopus 로고    scopus 로고
    • Control of cell lineage-specific development and transcription by bHLH- PAS proteins
    • Crews ST. Control of cell lineage-specific development and transcription by bHLH-PAS proteins. Genes Dev. 1998;12:607-620. (Pubitemid 28134294)
    • (1998) Genes and Development , vol.12 , Issue.5 , pp. 607-620
    • Crews, S.T.1
  • 28
    • 0033118983 scopus 로고    scopus 로고
    • Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: Their stabilization and redox signal-induced interaction with CBP/p300
    • Ema M, Hirota K, Mimura J, Abe H, Yodoi J, Sogawa K, Poellinger L, Fujii-Kuriyama Y. Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300. EMBO J. 1999;18:1905-1904.
    • (1999) EMBO J , vol.18 , pp. 1905-11904
    • Ema, M.1    Hirota, K.2    Mimura, J.3    Abe, H.4    Yodoi, J.5    Sogawa, K.6    Poellinger, L.7    Fujii-Kuriyama, Y.8
  • 29
    • 0031020884 scopus 로고    scopus 로고
    • Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells
    • Tian H, McKnight SL, Russell DW. Endothelial PAS domain protein 1 (EPAS1), a transcription factor selectively expressed in endothelial cells. Genes Dev. 1997;11:72-82. (Pubitemid 27043825)
    • (1997) Genes and Development , vol.11 , Issue.1 , pp. 72-82
    • Tian, H.1    McKnight, S.L.2    Russell, D.W.3
  • 30
    • 0032213236 scopus 로고    scopus 로고
    • The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development
    • Tian H, Hammer RE, Matsumoto AM, Russell DW, McKnight SL. The hypoxia-responsive transcription factor EPAS1 is essential for catecholamine homeostasis and protection against heart failure during embryonic development. Genes Dev. 1998;12:3320-3324. (Pubitemid 28520979)
    • (1998) Genes and Development , vol.12 , Issue.21 , pp. 3320-3324
    • Tian, H.1    Hammer, R.E.2    Matsumoto, A.M.3    Russell, D.W.4    McKnight, S.L.5
  • 31
    • 0035969508 scopus 로고    scopus 로고
    • Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression
    • DOI 10.1038/35107085
    • Makino Y, Cao R, Svensson K, Bertilsson G, Asman M, Tanaka H, Cao Y, Berkenstam A, Poellinger L. Inhibitory PAS domain protein is a negative regulator of hypoxia-inducible gene expression. Nature. 2001;414:550-554. (Pubitemid 33131538)
    • (2001) Nature , vol.414 , Issue.6863 , pp. 550-554
    • Makino, Y.1    Cao, R.2    Svensson, K.3    Bertilsson, G.4    Asman, M.5    Tanaka, H.6    Cao, Y.7    Berkenstam, A.8    Poellinger, L.9
  • 32
    • 0037064141 scopus 로고    scopus 로고
    • Functional analysis of hypoxia-inducible factor-1alpha-mediated transactivation: Identification of amino acid residues critical for transcriptional activation and/or interaction with creb-binding protein
    • DOI 10.1074/jbc.M205051200
    • Ruas JL, Poellinger L, Pereira T. Functional analysis of hypoxia-inducible factor-1 alpha-mediated transactivation. Identification of amino acid residues critical for transcriptional activation and/or interaction with CREB-binding protein. J Biol Chem. 2002;277:38723-38730. (Pubitemid 35154734)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.41 , pp. 38723-38730
    • Ruas, J.L.1    Poellinger, L.2    Pereira, T.3
  • 33
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain: A hypoxic switch
    • DOI 10.1126/science.1068592
    • Lando D, Peet DJ, Whelan DA, Gorman JJ, Whitelaw ML. Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch. Science. 2002;295:858-861. (Pubitemid 34118367)
    • (2002) Science , vol.295 , Issue.5556 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 34
    • 0034641615 scopus 로고    scopus 로고
    • 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. Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. Proc Natl Acad Sci U S A. 2000;97:10430-10435.
    • (2000) Proc Natl Acad Sci U S a , vol.97 , pp. 10430-10435
    • Kamura, T.1    Sato, S.2    Iwai, K.3    Czyzyk-Krzeska, M.4    Conaway, R.C.5    Conaway, J.W.6
  • 35
    • 0030937718 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1; Definition of regulatory domains within the alpha subunit
    • DOI 10.1074/jbc.272.17.11205
    • Pugh CW, O'Rourke JF, Nagao M, Gleadle JM, Ratcliffe PJ. Activation of hypoxia-inducible factor-1; definition of regulatory domains within the alpha subunit. J Biol Chem. 1997;272:11205-11214. (Pubitemid 27184117)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.17 , pp. 11205-11214
    • Pugh, C.W.1    O'Rourke, J.F.2    Nagao, M.3    Gleadle, J.M.4    Ratcliffe, P.J.5
  • 36
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • DOI 10.1126/science.1066373
    • Bruick RK, McKnight SL. A conserved family of prolyl-4-hydroxylases that modify HIF. Science. 2001;294:1337-1340. (Pubitemid 33063099)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 39
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • DOI 10.1126/science.1066373
    • Bruick RK, McKnight SL. A conserved family of prolyl 4-hydroxylases that modify HIF. Science. 2001;294:1337-1340. (Pubitemid 33063099)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 43
    • 59349098621 scopus 로고    scopus 로고
    • Inhibition of oxygen sensors as a therapeutic strategy for ischaemic and inflammatory disease
    • Fraisl P, Aragonés J, Carmeliet P. Inhibition of oxygen sensors as a therapeutic strategy for ischaemic and inflammatory disease. Nat Rev Drug Discov. 2009;8:139-152.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 139-152
    • Fraisl, P.1    Aragonés, J.2    Carmeliet, P.3
  • 44
    • 0033526781 scopus 로고    scopus 로고
    • Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-alpha) proteins
    • DOI 10.1006/bbrc.1999.0878
    • Srinivas V, Zhang LP, Zhu XH, Caro J. Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-alpha) proteins. Biochem Biophys Res Commun. 1999;260:557-561. (Pubitemid 29352100)
    • (1999) Biochemical and Biophysical Research Communications , vol.260 , Issue.2 , pp. 557-561
    • Srinivas, V.1    Zhang, L.-P.2    Zhu, X.-H.3    Caro, J.4
  • 45
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • DOI 10.1093/emboj/20.18.5197
    • Masson N, Willam C, Maxwell PH, Pugh CW, Ratcliffe PJ. Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. EMBO J. 2001;20:5197-5206. (Pubitemid 32910914)
    • (2001) EMBO Journal , vol.20 , Issue.18 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 46
    • 0041885339 scopus 로고    scopus 로고
    • 2 levels
    • DOI 10.1242/jcs.00655
    • Masson N, Ratcliffe PJ. HIF prolyl and asparaginyl hydroxylases in the biological response to intracellular O(2) levels. J Cell Sci. 2003;116:3041-3049. (Pubitemid 37038953)
    • (2003) Journal of Cell Science , vol.116 , Issue.15 , pp. 3041-3049
    • Masson, N.1    Ratcliffe, P.J.2
  • 48
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1alpha-pVHL complex: Hydroxyproline recognition in signaling
    • DOI 10.1126/science.1073440
    • Min JH, Yang H, Ivan M, Gertler F, Kaelin WG Jr, Pavletich NP. Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. Science. 2002;296:1886-1889. (Pubitemid 34596278)
    • (2002) Science , vol.296 , Issue.5574 , pp. 1886-1889
    • Min, J.-H.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin Jr., W.G.5    Pavietich, N.P.6
  • 51
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza GL. Targeting HIF-1 for cancer therapy. Nat Rev Cancer. 2003;3:721-732. (Pubitemid 37328811)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.10 , pp. 721-732
    • Semenza, G.L.1
  • 52
    • 0028786601 scopus 로고
    • A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter
    • Melillo G, Musso T, Sica A, Taylor LS, Cox GW, Varesio L. A hypoxia-responsive element mediates a novel pathway of activation of the inducible nitric oxide synthase promoter. J Exp Med. 1995;182:1683-1693.
    • (1995) J Exp Med , vol.182 , pp. 1683-1693
    • Melillo, G.1    Musso, T.2    Sica, A.3    Taylor, L.S.4    Cox, G.W.5    Varesio, L.6
  • 53
    • 0033566693 scopus 로고    scopus 로고
    • Reciprocal positive regulation of hypoxia-inducible factor 1alpha and insulin-like growth factor 2
    • Feldser D, Agani F, Iyer NV, Pak B, Ferreira G, Semenza GL. Reciprocal positive regulation of hypoxia-inducible factor 1alpha and insulin-like growth factor 2. Cancer Res. 1999;59:3915-3918. (Pubitemid 29393552)
    • (1999) Cancer Research , vol.59 , Issue.16 , pp. 3915-3918
    • Feldser, D.1    Agani, F.2    Iyer, N.V.3    Pak, B.4    Ferreira, G.5    Semenza, G.L.6
  • 55
    • 0028068606 scopus 로고
    • Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1
    • Semenza GL, Roth PH, Fang HM, Wang GL. Transcriptional regulation of genes encoding glycolytic enzymes by hypoxia-inducible factor 1. J Biol Chem. 1994;269:23757-23763. (Pubitemid 24293585)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.38 , pp. 23757-23763
    • Semenza, G.L.1    Roth, P.H.2    Fang, H.-M.3    Wang, G.L.4
  • 57
    • 4644370374 scopus 로고    scopus 로고
    • Signalling via the hypoxia-inducible factor-1alpha requires multiple posttranslational modifications
    • DOI 10.1016/j.cellsig.2004.04.010, PII S0898656804001044
    • Brahimi-Horn C, Mazure N, Pouysségur J. Signalling via the hypoxia-inducible factor-1alpha requires multiple posttranslational modifications. Cell Signal. 2005;17:1-9 (Pubitemid 39286774)
    • (2005) Cellular Signalling , vol.17 , Issue.1 , pp. 1-9
    • Brahimi-Horn, C.1    Mazure, N.2    Pouyssegur, J.3
  • 58
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia
    • DOI 10.1093/emboj/cdg392
    • Berra E, Benizri E, Ginouvès A, Volmat V, Roux D, Pouysségur J. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. EMBO J. 2003;22:4082-4090. (Pubitemid 37021737)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3    Volmat, V.4    Roux, D.5    Pouyssegur, J.6
  • 59
    • 0030900808 scopus 로고    scopus 로고
    • Maternal circulation in the first-trimester human placenta - Myth or reality?
    • DOI 10.1016/S0002-9378(97)70572-6
    • Jaffe R, Jauniaux E, Hustin J. Maternal circulation in the first-trimester human placenta - myth or reality? Am J Obstet Gynecol. 1997;176:695-705. (Pubitemid 27147186)
    • (1997) American Journal of Obstetrics and Gynecology , vol.176 , Issue.3 , pp. 695-705
    • Jaffe, R.1    Jauniaux, E.2    Hustin, J.3
  • 61
    • 0032100732 scopus 로고    scopus 로고
    • HIF-1alpha is required for solid tumor formation and embryonic vascularization
    • DOI 10.1093/emboj/17.11.3005
    • Ryan HE, Lo J, Johnson RS. HIF-1 alpha is required for solid tumor formation and embryonic vascularization. EMBO J. 1998;17:3005-3015. (Pubitemid 28254373)
    • (1998) EMBO Journal , vol.17 , Issue.11 , pp. 3005-3015
    • Ryan, H.E.1    Lo, J.2    Johnson, R.S.3
  • 62
    • 0033562569 scopus 로고    scopus 로고
    • Defective vascularization of HIF-1alpha-null embryos is not associated with VEGF deficiency but with mesenchymal cell death
    • DOI 10.1006/dbio.1999.9253
    • Kotch LE, Iyer NV, Laughner E, Semenza GL. Defective vascularization of HIF-1alpha-null embryos is not associated with VEGF deficiency but with mesenchymal cell death. Dev Biol. 1999;209:254-267. (Pubitemid 29230878)
    • (1999) Developmental Biology , vol.209 , Issue.2 , pp. 254-267
    • Kotch, L.E.1    Iyer, N.V.2    Laughner, E.3    Semenza, G.L.4
  • 64
    • 0036198010 scopus 로고    scopus 로고
    • Inhibition of PPARgamma2 gene expression by the HIF-1-regulated gene DEC1/Stra13: A mechanism for regulation of adipogenesis by hypoxia
    • DOI 10.1016/S1534-5807(02)00131-4
    • Yun Z, Maecker HL, Johnson RS, Giaccia AJ. Inhibition of PPAR gamma 2 gene expression by the HIF-1-regulated gene DEC1/Stra13: a mechanism for regulation of adipogenesis by hypoxia. Dev Cell. 2002;2:331-341. (Pubitemid 34266118)
    • (2002) Developmental Cell , vol.2 , Issue.3 , pp. 331-341
    • Yun, Z.1    Maecker, H.L.2    Johnson, R.S.3    Giaccia, A.J.4
  • 66
    • 0024259872 scopus 로고
    • Syncatalytic inactivation of prolyl 4-hydroxylase by synthetic peptides containing the unphysiologic amino acid 5-oxaproline
    • Günzler V, Brocks D, Henke S, Myllylä R, Geiger R, Kivirikko KI. Syncatalytic inactivation of prolyl 4-hydroxylase by synthetic peptides containing the unphysiologic amino acid 5-oxaproline. J Biol Chem. 1988;263:19498-19504. (Pubitemid 19016428)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.36 , pp. 19498-19504
    • Gunzler, V.1    Brocks, D.2    Henke, S.3    Myllyla, R.4    Geiger, R.5    Kivirikko, K.I.6
  • 67
    • 0028246263 scopus 로고
    • Inhibition of prolyl 4-hydroxylase by oxalyl amino acid derivatives in vitro, in isolated microsomes and in embryonic chicken tissues
    • Baader E, Tschank G, Baringhaus KH, Burghard H, Günzler V. Inhibition of prolyl 4-hydroxylase by oxalyl amino acid derivatives in vitro, in isolated microsomes and in embryonic chicken tissues. Biochem J. 1994;300:525-530. (Pubitemid 24167913)
    • (1994) Biochemical Journal , vol.300 , Issue.2 , pp. 525-530
    • Baader, E.1    Tschank, G.2    Baringhaus, K.-H.3    Burghard, H.4    Gunzler, V.5
  • 68
    • 0020488069 scopus 로고
    • A stereochemical concept for the catalytic mechanism of prolylhydroxylase: Applicability to classification and design of inhibitors
    • Hanauske-Abel HM, Günzler V. A stereochemical concept for the catalytic mechanism of prolylhydroxylase: applicability to classification and design of inhibitors. J Theor Biol. 1982;94:421-455.
    • (1982) J Theor Biol , vol.94 , pp. 421-455
    • Hanauske-Abel, H.M.1    Günzler, V.2
  • 69
    • 0021765030 scopus 로고
    • The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion
    • Majamaa K, Hanauske-Abel HM, Günzler V, Kivirikko KI. The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion. Eur J Biochem. 1984;138:239-245.
    • (1984) Eur J Biochem , vol.138 , pp. 239-245
    • Majamaa, K.1    Hanauske-Abel, H.M.2    Günzler, V.3    Kivirikko, K.I.4
  • 70
    • 0026724983 scopus 로고
    • Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analogue N-oxaloglycine and its derivatives
    • Cunliffe CJ, Franklin TJ, Hales NJ, Hill GB. Novel inhibitors of prolyl 4-hydroxylase. 3. Inhibition by the substrate analogue N-oxaloglycine and its derivatives. J Med Chem. 1992;35:2652-2658.
    • (1992) J Med Chem , vol.35 , pp. 2652-2658
    • Cunliffe, C.J.1    Franklin, T.J.2    Hales, N.J.3    Hill, G.B.4
  • 71
    • 0023021512 scopus 로고
    • Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase
    • Majamaa K, Günzler V, Hanauske-Abel HM, Myllylä R, Kivirikko KI. Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase. J Biol Chem. 1986;261:7819-7823. (Pubitemid 17208708)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.17 , pp. 7819-7823
    • Majamaa, K.1    Gunzler, V.2    Hanauske-Abel, H.M.3
  • 72
    • 0028842107 scopus 로고
    • Specific inhibition of eIF-5A and collagen hydroxylation by a single agent. Antiproliferative and fibrosuppressive effects on smooth muscle cells from human coronary arteries
    • McCaffrey TA, Pomerantz KB, Sanborn TA, Spokojny AM, Du B, Park MH, Folk JE, Lamberg A, Kivirikko KI, Falcone DJ, et al. Specific inhibition of eIF-5A and collagen hydroxylation by a single agent. Antiproliferative and fibrosuppressive effects on smooth muscle cells from human coronary arteries. J Clin Invest. 1995;95:446-455.
    • (1995) J Clin Invest , vol.95 , pp. 446-455
    • McCaffrey, T.A.1    Pomerantz, K.B.2    Sanborn, T.A.3    Spokojny, A.M.4    Du, B.5    Park, M.H.6    Folk, J.E.7    Lamberg, A.8    Kivirikko, K.I.9    Falcone, D.J.10
  • 73
    • 0023096345 scopus 로고
    • Time-dependent inactivation of chick-embryo prolyl 4-hydroxylase by coumalic acid. Evidence for a syncatalytic mechanism
    • Günzler V, Hanauske-Abel HM, Myllylä R, Mohr J, Kivirikko KI. Time-dependent inactivation of chick-embryo prolyl 4-hydroxylase by coumalic acid. Evidence for a syncatalytic mechanism. Biochem J. 1987;242:163-169. (Pubitemid 17015458)
    • (1987) Biochemical Journal , vol.242 , Issue.1 , pp. 163-169
    • Gunzler, V.1    Hanauske-Abel, H.M.2    Myllyla, R.3
  • 76
    • 3342955379 scopus 로고    scopus 로고
    • Novel mechanism of action for hydralazine: Induction of hypoxia-inducible factor-1 alpha, vascular endothelial growth factor, and angiogenesis by inhibition of prolyl hydroxylases
    • DOI 10.1161/01.RES.0000134924.89412.70
    • Knowles HJ, Tian YM, Mole DR, Harris AL. Novel mechanism of action for hydralazine: induction of hypoxia-inducible factor-1alpha, vascular endothelial growth factor, and angiogenesis by inhibition of prolyl hydroxylases. Circ Res. 2004;95:162-169. (Pubitemid 38988682)
    • (2004) Circulation Research , vol.95 , Issue.2 , pp. 162-169
    • Knowles, H.J.1    Tian, Y.-M.2    Mole, D.R.3    Harris, A.L.4
  • 77
    • 34548022880 scopus 로고    scopus 로고
    • Alpha-ketoglutarate stimulates procollagen production in cultured human dermal fibroblasts, and decreases UVB-induced wrinkle formation following topical application on the dorsal skin of hairless mice
    • DOI 10.1248/bpb.30.1395
    • Son ED, Choi GH, Kim H, Lee B, Chang IS, Hwang JS. Alpha-ketoglutarate stimulates procollagen production in cultured human dermal fibroblasts, and decreases UVB-induced wrinkle formation following topical application on the dorsal skin of hairless mice. Biol Pharm Bull. 2007;30:1395-1399. (Pubitemid 47282183)
    • (2007) Biological and Pharmaceutical Bulletin , vol.30 , Issue.8 , pp. 1395-1399
    • Son, E.D.1    Choi, G.H.2    Kim, H.3    Lee, B.4    Chang, I.S.5    Hwang, J.S.6
  • 78
    • 0038165466 scopus 로고    scopus 로고
    • Activation of the prolyl hydroxylase oxygen-sensor results in induction of GLUT1, heme oxygenase-1, and nitric-oxide synthase proteins and confers protection from metabolic inhibition to cardiomyocytes
    • DOI 10.1074/jbc.M301391200
    • Wright G, Higgin JJ, Raines RT, Steenbergen C, Murphy E. Activation of the prolyl hydroxylase oxygen-sensor results in induction of GLUT1, heme oxygenase-1, and nitric-oxide synthase proteins and confers protection from metabolic inhibition to cardiomyocytes. J Biol Chem. 2003;278:20235-20239. (Pubitemid 36799221)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 20235-20239
    • Wright, G.1    Higgin, J.J.2    Raines, R.T.3    Steenbergen, C.4    Murphy, E.5
  • 81
    • 77951552411 scopus 로고    scopus 로고
    • Hearts of hypoxia-inducible factor prolyl 4-hydroxylase-2 hypomorphic mice show protection against acute ischemia-reperfusion injury
    • Hyvärinen J, Hassinen IE, Sormunen R, Mäki JM, Kivirikko KI, Koivunen P, Myllyharju J. Hearts of hypoxia-inducible factor prolyl 4-hydroxylase-2 hypomorphic mice show protection against acute ischemia-reperfusion injury. J Biol Chem. 2010;285:13646-13657.
    • (2010) J Biol Chem , vol.285 , pp. 13646-13657
    • Hyvärinen, J.1    Hassinen, I.E.2    Sormunen, R.3    Mäki, J.M.4    Kivirikko, K.I.5    Koivunen, P.6    Myllyharju, J.7
  • 82
    • 84856568640 scopus 로고    scopus 로고
    • Effect of conjugated linoleic acid on inhibition of prolyl hydroxylase 1 in hearts of mice
    • Zhang J, Li D. Effect of conjugated linoleic acid on inhibition of prolyl hydroxylase 1 in hearts of mice. Lipids Health Dis. 2012;11:22.
    • (2012) Lipids Health Dis , vol.11 , pp. 22
    • Zhang, J.1    Li, D.2
  • 83
    • 0027156412 scopus 로고
    • Neurohumoral activation in preclinical heart failure: Remodeling and the potential for intervention
    • Francis GS, McDonald KM, Cohn JN. Neurohumoral activation in preclinical heart failure. Remodeling and the potential for intervention. Circulation. 1993;87(5 Suppl):IV90-96. (Pubitemid 23135655)
    • (1993) Circulation , vol.87 , Issue.5 SUPPL. IV
    • Francis, G.S.1    McDonald, K.M.2    Cohn, J.N.3
  • 84
    • 0035975982 scopus 로고    scopus 로고
    • Inhibition of collagen synthesis with prolyl 4-hydroxylase inhibitor improves left ventricular function and alters the pattern of left ventricular dilatation after myocardial infarction
    • Nwogu JI, Geenen D, Bean M, Brenner MC, Huang X, Buttrick PM. Inhibition of collagen synthesis with prolyl 4-hydroxylase inhibitor improves left ventricular function and alters the pattern of left ventricular dilatation after myocardial infarction. Circulation. 2001;104:2216-2221. (Pubitemid 33043303)
    • (2001) Circulation , vol.104 , Issue.18 , pp. 2216-2221
    • Nwogu, J.I.1    Geenen, D.2    Bean, M.3    Brenner, M.C.4    Huang, X.5    Buttrick, P.M.6
  • 86
    • 42449163874 scopus 로고    scopus 로고
    • Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure
    • Minamishima YA, Moslehi J, Bardeesy N, Cullen D, Bronson RT, Kaelin WG Jr. Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure. Blood. 2008;111:3236-3244.
    • (2008) Blood , vol.111 , pp. 3236-3244
    • Minamishima, Y.A.1    Moslehi, J.2    Bardeesy, N.3    Cullen, D.4    Bronson, R.T.5    Kaelin Jr., W.G.6
  • 87
    • 4043119692 scopus 로고    scopus 로고
    • The HIF pathway as a therapeutic target
    • DOI 10.1016/S1359-6446(04)03202-7, PII S1359644604032027
    • Hewitson KS, Schofield CJ. The HIF pathway as a therapeutic target. Drug Discov Today. 2004;9:704-711. (Pubitemid 39070283)
    • (2004) Drug Discovery Today , vol.9 , Issue.16 , pp. 704-711
    • Hewitson, K.S.1    Schofield, C.J.2
  • 88
    • 0037490210 scopus 로고    scopus 로고
    • Hypoxia-inducible factor and its biomedical relevance
    • DOI 10.1074/jbc.R200030200
    • Huang LE, Bunn HF. Hypoxia-inducible factor and its biomedical relevance. J Biol Chem. 2003;278:19575-19578. (Pubitemid 36799137)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 19575-19578
    • Huang, L.E.1    Bunn, H.F.2
  • 89
    • 79551629623 scopus 로고    scopus 로고
    • Prolyl-4-hydroxylase PHD2- and hypoxia-inducible factor 2-dependent regulation of amphiregulin contributes to breast tumorigenesis
    • Bordoli MR, Stiehl DP, Borsig L, Kristiansen G, Hausladen S, Schraml P, Wenger RH, Camenisch G. Prolyl-4-hydroxylase PHD2- and hypoxia-inducible factor 2-dependent regulation of amphiregulin contributes to breast tumorigenesis. Oncogene. 2011;30:548-560.
    • (2011) Oncogene , vol.30 , pp. 548-560
    • Bordoli, M.R.1    Stiehl, D.P.2    Borsig, L.3    Kristiansen, G.4    Hausladen, S.5    Schraml, P.6    Wenger, R.H.7    Camenisch, G.8
  • 90
    • 84865339304 scopus 로고    scopus 로고
    • Low expression of prolyl hydroxylase 2 is associated with tumor grade and poor prognosis in patients with colorectal cancer
    • Xie G, Zheng L, Ou J, Huang H, He J, Li J, Pan F, Liang H. Low expression of prolyl hydroxylase 2 is associated with tumor grade and poor prognosis in patients with colorectal cancer. Exp Biol Med (Maywood). 2012;237:860-866.
    • (2012) Exp Biol Med (Maywood) , vol.237 , pp. 860-866
    • Xie, G.1    Zheng, L.2    Ou, J.3    Huang, H.4    He, J.5    Li, J.6    Pan, F.7    Liang, H.8
  • 92
    • 84857466801 scopus 로고    scopus 로고
    • HIF prolyl hydroxylase-2 inhibition diminishes tumor growth through matrix metalloproteinase-induced TGFβ activation
    • Klotzsche-von Ameln A, Muschter A, Heimesaat MM, Breier G, Wielockx B. HIF prolyl hydroxylase-2 inhibition diminishes tumor growth through matrix metalloproteinase-induced TGFβ activation. Cancer Biol Ther. 2012;13:216-223.
    • (2012) Cancer Biol Ther , vol.13 , pp. 216-223
    • Klotzsche-von Ameln, A.1    Muschter, A.2    Heimesaat, M.M.3    Breier, G.4    Wielockx, B.5
  • 94
    • 84874471550 scopus 로고    scopus 로고
    • The expression of hypoxia-inducible factor-1alpha and its hydroxylases in pulmonary arteries of patient with chronic obstructive pulmonary disease
    • Chen YR, Dai AG, Hu RC, Kong CC. The expression of hypoxia-inducible factor-1alpha and its hydroxylases in pulmonary arteries of patient with chronic obstructive pulmonary disease. Zhongguo Ying Yong Sheng Li Xue Za Zhi. 2012;28: 234-238.
    • (2012) Zhongguo Ying Yong Sheng Li Xue Za Zhi , vol.28 , pp. 234-238
    • Chen, Y.R.1    Dai, A.G.2    Hu, R.C.3    Kong, C.C.4
  • 98
    • 84877965333 scopus 로고    scopus 로고
    • Novel neuroprotective agents: A HIF activator and an Akt activator
    • Takizawa S, Nagata E, Luo HR. Novel neuroprotective agents: a HIF activator and an Akt activator. Rinsho Shinkeigaku. 2012;52:911-912.
    • (2012) Rinsho Shinkeigaku , vol.52 , pp. 911-912
    • Takizawa, S.1    Nagata, E.2    Luo, H.R.3
  • 99
    • 75149154666 scopus 로고    scopus 로고
    • HIF prolyl hydroxylase inhibitors prevent neuronal death induced by mitochondrial toxins: Therapeutic implications for Huntington's disease and Alzheimer's disease
    • Niatsetskaya Z, Basso M, Speer RE, McConoughey SJ, Coppola G, Ma TC, Ratan RR. HIF prolyl hydroxylase inhibitors prevent neuronal death induced by mitochondrial toxins: therapeutic implications for Huntington's disease and Alzheimer's disease. Antioxid Redox Signal. 2010;12:435-443.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 435-443
    • Niatsetskaya, Z.1    Basso, M.2    Speer, R.E.3    McConoughey, S.J.4    Coppola, G.5    Ma, T.C.6    Ratan, R.R.7
  • 100
    • 70350365391 scopus 로고    scopus 로고
    • Inhibition of prolyl hydroxylase protects against 1-methyl-4-phenyl-1,2, 3,6-tetrahydropyridine-induced neurotoxicity: Model for the potential involvement of the hypoxia-inducible factor pathway in Parkinson disease
    • Lee DW, Rajagopalan S, Siddiq A, Gwiazda R, Yang L, Beal MF, Ratan RR, Andersen JK. Inhibition of prolyl hydroxylase protects against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced neurotoxicity: model for the potential involvement of the hypoxia-inducible factor pathway in Parkinson disease. J Biol Chem. 2009;284:29065-29076.
    • (2009) J Biol Chem , vol.284 , pp. 29065-29076
    • Lee, D.W.1    Rajagopalan, S.2    Siddiq, A.3    Gwiazda, R.4    Yang, L.5    Beal, M.F.6    Ratan, R.R.7    Andersen, J.K.8
  • 101
    • 84862294186 scopus 로고    scopus 로고
    • A possible novel anti-inflammatory mechanism for the pharmacological prolyl hydroxylase inhibitor 3,4-dihydroxybenzoate: Implications for use as a therapeutic for Parkinson's disease
    • Chinta SJ, Rajagopalan S, Ganesan A, Andersen JK. A possible novel anti-inflammatory mechanism for the pharmacological prolyl hydroxylase inhibitor 3,4-dihydroxybenzoate: implications for use as a therapeutic for Parkinson's disease. Parkinsons Dis. 2012;2012:364684.
    • (2012) Parkinsons Dis , vol.2012 , pp. 364684
    • Chinta, S.J.1    Rajagopalan, S.2    Ganesan, A.3    Andersen, J.K.4
  • 102
    • 77956604234 scopus 로고    scopus 로고
    • HIF prolyl hydroxylase inhibition increases cell viability and potentiates dopamine release in dopaminergic cells
    • Johansen JL, Sager TN, Lotharius J, Witten L, Mørk A, Egebjerg J, Thirstrup K. HIF prolyl hydroxylase inhibition increases cell viability and potentiates dopamine release in dopaminergic cells. J Neurochem. 2010;115:209-219.
    • (2010) J Neurochem , vol.115 , pp. 209-219
    • Johansen, J.L.1    Sager, T.N.2    Lotharius, J.3    Witten, L.4    Mørk, A.5    Egebjerg, J.6    Thirstrup, K.7
  • 105
    • 79960683641 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible factor-1α (Hif-1α) delays inflammation resolution by reducing neutrophil apoptosis and reverse migration in a zebrafish inflammation model
    • Elks PM, van Eeden FJ, Dixon G, Wang X, Reyes-Aldasoro CC, Ingham PW, Whyte MK, Walmsley SR, Renshaw SA. Activation of hypoxia-inducible factor-1α (Hif-1α) delays inflammation resolution by reducing neutrophil apoptosis and reverse migration in a zebrafish inflammation model. Blood. 2011;118:712-722.
    • (2011) Blood , vol.118 , pp. 712-722
    • Elks, P.M.1    Van Eeden, F.J.2    Dixon, G.3    Wang, X.4    Reyes-Aldasoro, C.C.5    Ingham, P.W.6    Whyte, M.K.7    Walmsley, S.R.8    Renshaw, S.A.9
  • 108
    • 79953644844 scopus 로고    scopus 로고
    • Prolyl hydroxylase domain protein 2 (PHD2) mediates oxygen-induced retinopathy in neonatal mice
    • Duan LJ, Takeda K, Fong GH. Prolyl hydroxylase domain protein 2 (PHD2) mediates oxygen-induced retinopathy in neonatal mice. Am J Pathol. 2011;178:1881-1890.
    • (2011) Am J Pathol , vol.178 , pp. 1881-1890
    • Duan, L.J.1    Takeda, K.2    Fong, G.H.3
  • 109
  • 112
    • 42149153182 scopus 로고    scopus 로고
    • Remote renal preconditioning-induced cardioprotection: A key role of hypoxia inducible factor-prolyl 4-hydroxylases
    • Kant R, Diwan V, Jaggi AS, Singh N, Singh D. Remote renal preconditioning-induced cardioprotection: a key role of hypoxia inducible factor-prolyl 4-hydroxylases. Mol Cell Biochem. 2008;312:25-31.
    • (2008) Mol Cell Biochem , vol.312 , pp. 25-31
    • Kant, R.1    Diwan, V.2    Jaggi, A.S.3    Singh, N.4    Singh, D.5
  • 113
    • 79953846587 scopus 로고    scopus 로고
    • Brief anoxia preconditioning and HIF prolyl-hydroxylase inhibition enhances neuronal resistance in organotypic hippocampal slices on model of ischemic damage
    • Lushnikova I, Orlovsky M, Dosenko V, Maistrenko A, Skibo G. Brief anoxia preconditioning and HIF prolyl-hydroxylase inhibition enhances neuronal resistance in organotypic hippocampal slices on model of ischemic damage. Brain Res. 2011;1386:175-183.
    • (2011) Brain Res , vol.1386 , pp. 175-183
    • Lushnikova, I.1    Orlovsky, M.2    Dosenko, V.3    Maistrenko, A.4    Skibo, G.5
  • 114
    • 83155175207 scopus 로고    scopus 로고
    • Neuroprotection by hypoxic preconditioning involves upregulation of hypoxia-inducible factor-1 in a prenatal model of acute hypoxia
    • Giusti S, Fiszer de Plazas S. Neuroprotection by hypoxic preconditioning involves upregulation of hypoxia-inducible factor-1 in a prenatal model of acute hypoxia. J Neurosci Res. 2012;90:468-478.
    • (2012) J Neurosci Res , vol.90 , pp. 468-478
    • Giusti, S.1    Fiszer De Plazas, S.2
  • 116
    • 84865660860 scopus 로고    scopus 로고
    • Prolyl hydroxylase domain enzyme 2 is the major player in regulating hypoxic responses in rheumatoid arthritis
    • Muz B, Larsen H, Madden L, Kiriakidis S, Paleolog EM. Prolyl hydroxylase domain enzyme 2 is the major player in regulating hypoxic responses in rheumatoid arthritis. Arthritis Rheum. 2012;64:2856-2867.
    • (2012) Arthritis Rheum , vol.64 , pp. 2856-2867
    • Muz, B.1    Larsen, H.2    Madden, L.3    Kiriakidis, S.4    Paleolog, E.M.5


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