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Volumn 6, Issue 4, 2011, Pages

The function of Hypoxia-inducible factor (HIF) is independent of the endoplasmic reticulum protein OS-9

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; HYPOXIA INDUCIBLE FACTOR; HYPOXIA INDUCIBLE FACTOR 1ALPHA; OSTEOSARCOMA 9 PROTEIN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; UNCLASSIFIED DRUG; LECTIN; MONOCLONAL ANTIBODY; OS9 PROTEIN, HUMAN; OXYGEN; TUMOR PROTEIN;

EID: 79955731360     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019151     Document Type: Article
Times cited : (10)

References (56)
  • 1
    • 13944276440 scopus 로고    scopus 로고
    • OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha
    • Baek JH, Mahon PC, Oh J, Kelly B, Krishnamachary B, et al. (2005) OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha. Mol Cell 17 (4): 503-512.
    • (2005) Mol Cell , vol.17 , Issue.4 , pp. 503-512
    • Baek, J.H.1    Mahon, P.C.2    Oh, J.3    Kelly, B.4    Krishnamachary, B.5
  • 2
    • 50449107542 scopus 로고    scopus 로고
    • SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
    • Mueller B, Klemm EJ, Spooner E, Claessen JH, Ploegh HL, (2008) SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc Natl Acad Sci U S A 105 (34): 12325-12330.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.34 , pp. 12325-12330
    • Mueller, B.1    Klemm, E.J.2    Spooner, E.3    Claessen, J.H.4    Ploegh, H.L.5
  • 3
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson JC, Shaler TA, Tyler RE, Kopito RR, (2008) OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 10 (3): 272-282.
    • (2008) Nat Cell Biol , vol.10 , Issue.3 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 4
    • 70449527373 scopus 로고    scopus 로고
    • Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing
    • Webb JD, Coleman ML, Pugh CW, (2009) Hypoxia, hypoxia-inducible factors (HIF), HIF hydroxylases and oxygen sensing. Cell Mol Life Sci 66 (22): 3539-3554.
    • (2009) Cell Mol Life Sci , vol.66 , Issue.22 , pp. 3539-3554
    • Webb, J.D.1    Coleman, M.L.2    Pugh, C.W.3
  • 5
    • 31444444162 scopus 로고    scopus 로고
    • Integration of oxygen signaling at the consensus HRE
    • Wenger RH, Stiehl DP, Camenisch G, (2005) Integration of oxygen signaling at the consensus HRE. Sci STKE 2005 (306): re12.
    • (2005) Sci STKE , vol.2005 , Issue.306 , pp. 12
    • Wenger, R.H.1    Stiehl, D.P.2    Camenisch, G.3
  • 6
    • 19944433653 scopus 로고    scopus 로고
    • Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase
    • Selak MA, Armour SM, MacKenzie ED, Boulahbel H, Watson DG, et al. (2005) Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase. Cancer Cell 7 (1): 77-85.
    • (2005) Cancer Cell , vol.7 , Issue.1 , pp. 77-85
    • Selak, M.A.1    Armour, S.M.2    MacKenzie, E.D.3    Boulahbel, H.4    Watson, D.G.5
  • 7
    • 23644448721 scopus 로고    scopus 로고
    • HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: Novel role of fumarate in regulation of HIF stability
    • Isaacs JS, Jung YJ, Mole DR, Lee S, Torres-Cabala C, et al. (2005) HIF overexpression correlates with biallelic loss of fumarate hydratase in renal cancer: Novel role of fumarate in regulation of HIF stability. Cancer Cell 8 (2): 143-153.
    • (2005) Cancer Cell , vol.8 , Issue.2 , pp. 143-153
    • Isaacs, J.S.1    Jung, Y.J.2    Mole, D.R.3    Lee, S.4    Torres-Cabala, C.5
  • 8
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases
    • Metzen E, Zhou J, Jelkmann W, Fandrey J, Brune B, (2003) Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases. Mol Biol Cell 14 (8): 3470-3481.
    • (2003) Mol Biol Cell , vol.14 , Issue.8 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brune, B.5
  • 9
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia
    • Berra E, Benizri E, Ginouves A, Volmat V, Roux D, et al. (2003) HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. EMBO J 22 (16): 4082-4090.
    • (2003) EMBO J , vol.22 , Issue.16 , pp. 4082-4090
    • Berra, E.1    Benizri, E.2    Ginouves, A.3    Volmat, V.4    Roux, D.5
  • 10
    • 33750976389 scopus 로고    scopus 로고
    • Placental but not heart defects are associated with elevated hypoxia-inducible factor alpha levels in mice lacking prolyl hydroxylase domain protein 2
    • Takeda K, Ho VC, Takeda H, Duan LJ, Nagy A, et al. (2006) Placental but not heart defects are associated with elevated hypoxia-inducible factor alpha levels in mice lacking prolyl hydroxylase domain protein 2. Mol Cell Biol 26 (22): 8336-8346.
    • (2006) Mol Cell Biol , vol.26 , Issue.22 , pp. 8336-8346
    • Takeda, K.1    Ho, V.C.2    Takeda, H.3    Duan, L.J.4    Nagy, A.5
  • 11
    • 40949090791 scopus 로고    scopus 로고
    • Regulation of adult erythropoiesis by prolyl hydroxylase domain proteins
    • Takeda K, Aguila HL, Parikh NS, Li X, Lamothe K, et al. (2008) Regulation of adult erythropoiesis by prolyl hydroxylase domain proteins. Blood 111 (6): 3229-3235.
    • (2008) Blood , vol.111 , Issue.6 , pp. 3229-3235
    • Takeda, K.1    Aguila, H.L.2    Parikh, N.S.3    Li, X.4    Lamothe, K.5
  • 12
    • 34547905406 scopus 로고    scopus 로고
    • Essential role for prolyl hydroxylase domain protein 2 in oxygen homeostasis of the adult vascular system
    • Takeda K, Cowan A, Fong GH, (2007) Essential role for prolyl hydroxylase domain protein 2 in oxygen homeostasis of the adult vascular system. Circulation 116 (7): 774-781.
    • (2007) Circulation , vol.116 , Issue.7 , pp. 774-781
    • Takeda, K.1    Cowan, A.2    Fong, G.H.3
  • 13
    • 77954222576 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor-targeting prolyl hydroxylase domain-containing protein 2 (PHD2) enhances matrix synthesis by human chondrocytes
    • Thoms BL, Murphy CL, (2010) Inhibition of hypoxia-inducible factor-targeting prolyl hydroxylase domain-containing protein 2 (PHD2) enhances matrix synthesis by human chondrocytes. J Biol Chem 285 (27): 20472-20480.
    • (2010) J Biol Chem , vol.285 , Issue.27 , pp. 20472-20480
    • Thoms, B.L.1    Murphy, C.L.2
  • 14
    • 65649138377 scopus 로고    scopus 로고
    • Tumor vasculature is regulated by PHD2-mediated angiogenesis and bone marrow-derived cell recruitment
    • Chan DA, Kawahara TL, Sutphin PD, Chang HY, Chi JT, et al. (2009) Tumor vasculature is regulated by PHD2-mediated angiogenesis and bone marrow-derived cell recruitment. Cancer Cell 15 (6): 527-538.
    • (2009) Cancer Cell , vol.15 , Issue.6 , pp. 527-538
    • Chan, D.A.1    Kawahara, T.L.2    Sutphin, P.D.3    Chang, H.Y.4    Chi, J.T.5
  • 15
    • 59649117924 scopus 로고    scopus 로고
    • Heterozygous deficiency of PHD2 restores tumor oxygenation and inhibits metastasis via endothelial normalization
    • Mazzone M, Dettori D, Leite de Oliveira R, Loges S, Schmidt T, et al. (2009) Heterozygous deficiency of PHD2 restores tumor oxygenation and inhibits metastasis via endothelial normalization. Cell 136 (5): 839-851.
    • (2009) Cell , vol.136 , Issue.5 , pp. 839-851
    • Mazzone, M.1    Dettori, D.2    de Leite Oliveira, R.3    Loges, S.4    Schmidt, T.5
  • 16
    • 0037108807 scopus 로고    scopus 로고
    • Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor
    • Ivan M, Haberberger T, Gervasi DC, Michelson KS, Gunzler V, et al. (2002) Biochemical purification and pharmacological inhibition of a mammalian prolyl hydroxylase acting on hypoxia-inducible factor. Proc Natl Acad Sci U S A 99 (21): 13459-13464.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.21 , pp. 13459-13464
    • Ivan, M.1    Haberberger, T.2    Gervasi, D.C.3    Michelson, K.S.4    Gunzler, V.5
  • 17
    • 33745614894 scopus 로고    scopus 로고
    • Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)
    • McDonough MA, Li V, Flashman E, Chowdhury R, Mohr C, et al. (2006) Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2). Proc Natl Acad Sci U S A 103 (26): 9814-9819.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.26 , pp. 9814-9819
    • McDonough, M.A.1    Li, V.2    Flashman, E.3    Chowdhury, R.4    Mohr, C.5
  • 18
    • 36348936212 scopus 로고    scopus 로고
    • Oxygen-dependent ATF-4 stability is mediated by the PHD3 oxygen sensor
    • Koditz J, Nesper J, Wottawa M, Stiehl DP, Camenisch G, et al. (2007) Oxygen-dependent ATF-4 stability is mediated by the PHD3 oxygen sensor. Blood 110 (10): 3610-3617.
    • (2007) Blood , vol.110 , Issue.10 , pp. 3610-3617
    • Koditz, J.1    Nesper, J.2    Wottawa, M.3    Stiehl, D.P.4    Camenisch, G.5
  • 19
    • 42149089909 scopus 로고    scopus 로고
    • The von hippel-lindau tumor suppressor protein and egl-9-type proline hydroxylases regulate the large subunit of RNA polymerase II in response to oxidative stress
    • Mikhaylova O, Ignacak ML, Barankiewicz TJ, Harbaugh SV, Yi Y, et al. (2008) The von hippel-lindau tumor suppressor protein and egl-9-type proline hydroxylases regulate the large subunit of RNA polymerase II in response to oxidative stress. Mol Cell Biol 28 (8): 2701-2717.
    • (2008) Mol Cell Biol , vol.28 , Issue.8 , pp. 2701-2717
    • Mikhaylova, O.1    Ignacak, M.L.2    Barankiewicz, T.J.3    Harbaugh, S.V.4    Yi, Y.5
  • 20
    • 33845321931 scopus 로고    scopus 로고
    • Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity
    • Cummins EP, Berra E, Comerford KM, Ginouves A, Fitzgerald KT, et al. (2006) Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity. Proc Natl Acad Sci U S A 103 (48): 18154-18159.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.48 , pp. 18154-18159
    • Cummins, E.P.1    Berra, E.2    Comerford, K.M.3    Ginouves, A.4    Fitzgerald, K.T.5
  • 21
    • 19644376763 scopus 로고    scopus 로고
    • The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF)
    • Ozer A, Wu LC, Bruick RK, (2005) The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF). Proc Natl Acad Sci U S A 102 (21): 7481-7486.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.21 , pp. 7481-7486
    • Ozer, A.1    Wu, L.C.2    Bruick, R.K.3
  • 22
    • 15844379850 scopus 로고    scopus 로고
    • Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas
    • Su YA, Hutter CM, Trent JM, Meltzer PS, (1996) Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas. Mol Carcinog 15 (4): 270-275.
    • (1996) Mol Carcinog , vol.15 , Issue.4 , pp. 270-275
    • Su, Y.A.1    Hutter, C.M.2    Trent, J.M.3    Meltzer, P.S.4
  • 23
    • 0031474116 scopus 로고    scopus 로고
    • Genomic organization of the OS-9 gene amplified in human sarcomas
    • Kimura Y, Nakazawa M, Tsuchiya N, Asakawa S, Shimizu N, et al. (1997) Genomic organization of the OS-9 gene amplified in human sarcomas. J Biochem 122 (6): 1190-1195.
    • (1997) J Biochem , vol.122 , Issue.6 , pp. 1190-1195
    • Kimura, Y.1    Nakazawa, M.2    Tsuchiya, N.3    Asakawa, S.4    Shimizu, N.5
  • 24
    • 0037144427 scopus 로고    scopus 로고
    • YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-golgi transport of GPI-anchored proteins
    • Friedmann E, Salzberg Y, Weinberger A, Shaltiel S, Gerst JE, (2002) YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-golgi transport of GPI-anchored proteins. J Biol Chem 277 (38): 35274-35281.
    • (2002) J Biol Chem , vol.277 , Issue.38 , pp. 35274-35281
    • Friedmann, E.1    Salzberg, Y.2    Weinberger, A.3    Shaltiel, S.4    Gerst, J.E.5
  • 25
    • 0037072881 scopus 로고    scopus 로고
    • A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
    • Litovchick L, Friedmann E, Shaltiel S, (2002) A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta. J Biol Chem 277 (37): 34413-34423.
    • (2002) J Biol Chem , vol.277 , Issue.37 , pp. 34413-34423
    • Litovchick, L.1    Friedmann, E.2    Shaltiel, S.3
  • 26
    • 42949147649 scopus 로고    scopus 로고
    • A23187, ionomycin and thapsigargin upregulate mRNA of HIF-1alpha via endoplasmic reticulum stress rather than a rise in intracellular calcium
    • Werno C, Zhou J, Brune B, (2008) A23187, ionomycin and thapsigargin upregulate mRNA of HIF-1alpha via endoplasmic reticulum stress rather than a rise in intracellular calcium. J Cell Physiol 215 (3): 708-714.
    • (2008) J Cell Physiol , vol.215 , Issue.3 , pp. 708-714
    • Werno, C.1    Zhou, J.2    Brune, B.3
  • 27
    • 7244242390 scopus 로고    scopus 로고
    • Chelation of cellular calcium modulates hypoxia-inducible gene expression through activation of hypoxia-inducible factor-1alpha
    • Berchner-Pfannschmidt U, Petrat F, Doege K, Trinidad B, Freitag P, et al. (2004) Chelation of cellular calcium modulates hypoxia-inducible gene expression through activation of hypoxia-inducible factor-1alpha. J Biol Chem 279 (43): 44976-44986.
    • (2004) J Biol Chem , vol.279 , Issue.43 , pp. 44976-44986
    • Berchner-Pfannschmidt, U.1    Petrat, F.2    Doege, K.3    Trinidad, B.4    Freitag, P.5
  • 28
    • 10244236478 scopus 로고    scopus 로고
    • Induction of plasminogen activator inhibitor I gene expression by intracellular calcium via hypoxia-inducible factor-1
    • Liu Q, Moller U, Flugel D, Kietzmann T, (2004) Induction of plasminogen activator inhibitor I gene expression by intracellular calcium via hypoxia-inducible factor-1. Blood 104 (13): 3993-4001.
    • (2004) Blood , vol.104 , Issue.13 , pp. 3993-4001
    • Liu, Q.1    Moller, U.2    Flugel, D.3    Kietzmann, T.4
  • 29
    • 0037386143 scopus 로고    scopus 로고
    • Intracellular localisation of human HIF-1 alpha hydroxylases: Implications for oxygen sensing
    • Metzen E, Berchner-Pfannschmidt U, Stengel P, Marxsen JH, Stolze I, et al. (2003) Intracellular localisation of human HIF-1 alpha hydroxylases: Implications for oxygen sensing. J Cell Sci 116 (Pt 7): 1319-1326.
    • (2003) J Cell Sci , vol.116 , Issue.Pt 7 , pp. 1319-1326
    • Metzen, E.1    Berchner-Pfannschmidt, U.2    Stengel, P.3    Marxsen, J.H.4    Stolze, I.5
  • 30
    • 69249137859 scopus 로고    scopus 로고
    • Hypoxia-inducible factor prolyl-4-hydroxylase PHD2 protein abundance depends on integral membrane anchoring of FKBP38
    • Barth S, Edlich F, Berchner-Pfannschmidt U, Gneuss S, Jahreis G, et al. (2009) Hypoxia-inducible factor prolyl-4-hydroxylase PHD2 protein abundance depends on integral membrane anchoring of FKBP38. J Biol Chem 284 (34): 23046-23058.
    • (2009) J Biol Chem , vol.284 , Issue.34 , pp. 23046-23058
    • Barth, S.1    Edlich, F.2    Berchner-Pfannschmidt, U.3    Gneuss, S.4    Jahreis, G.5
  • 31
    • 79955726953 scopus 로고    scopus 로고
    • Nanoscopy of the cellular response to hypoxia by means of fluorescence resonance energy transfer (FRET) and new FRET software
    • Wotzlaw C, Gneuss S, Konietzny R, Fandrey J, (2010) Nanoscopy of the cellular response to hypoxia by means of fluorescence resonance energy transfer (FRET) and new FRET software. PMC Biophys 3 (1): 5.
    • (2010) PMC Biophys , vol.3 , Issue.1 , pp. 5
    • Wotzlaw, C.1    Gneuss, S.2    Konietzny, R.3    Fandrey, J.4
  • 32
    • 2942640371 scopus 로고    scopus 로고
    • Photobleaching-corrected FRET efficiency imaging of live cells
    • Zal T, Gascoigne NR, (2004) Photobleaching-corrected FRET efficiency imaging of live cells. Biophys J 86 (6): 3923-3939.
    • (2004) Biophys J , vol.86 , Issue.6 , pp. 3923-3939
    • Zal, T.1    Gascoigne, N.R.2
  • 33
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging fluorescence resonance energy transfer
    • Kenworthy AK, Edidin M, (1998) Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging fluorescence resonance energy transfer. J Cell Biol 142 (1): 69-84.
    • (1998) J Cell Biol , vol.142 , Issue.1 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 34
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias DA, Violin JD, Newton AC, Tsien RY, (2002) Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296 (5569): 913-916.
    • (2002) Science , vol.296 , Issue.5569 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 35
    • 77954408709 scopus 로고    scopus 로고
    • An automated real-time microscopy system for analysis of fluorescence resonance energy transfer
    • Bernardini A, Wotzlaw C, Lipinski H, Fandrey J, (2010) An automated real-time microscopy system for analysis of fluorescence resonance energy transfer. Proc SPIE 7723: 772311.
    • (2010) Proc SPIE , vol.7723 , pp. 772311
    • Bernardini, A.1    Wotzlaw, C.2    Lipinski, H.3    Fandrey, J.4
  • 36
    • 0031970586 scopus 로고    scopus 로고
    • Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines
    • Kimura Y, Nakazawa M, Yamada M, (1998) Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines. J Biochem 123 (5): 876-882.
    • (1998) J Biochem , vol.123 , Issue.5 , pp. 876-882
    • Kimura, Y.1    Nakazawa, M.2    Yamada, M.3
  • 37
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
    • Hara MR, Agrawal N, Kim SF, Cascio MB, Fujimuro M, et al. (2005) S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol 7 (7): 665-674.
    • (2005) Nat Cell Biol , vol.7 , Issue.7 , pp. 665-674
    • Hara, M.R.1    Agrawal, N.2    Kim, S.F.3    Cascio, M.B.4    Fujimuro, M.5
  • 38
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • Berney C, Danuser G, (2003) FRET or no FRET: A quantitative comparison. Biophys J 84 (6): 3992-4010.
    • (2003) Biophys J , vol.84 , Issue.6 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 39
    • 11244315697 scopus 로고    scopus 로고
    • Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1
    • Manalo DJ, Rowan A, Lavoie T, Natarajan L, Kelly BD, et al. (2005) Transcriptional regulation of vascular endothelial cell responses to hypoxia by HIF-1. Blood 105 (2): 659-669.
    • (2005) Blood , vol.105 , Issue.2 , pp. 659-669
    • Manalo, D.J.1    Rowan, A.2    Lavoie, T.3    Natarajan, L.4    Kelly, B.D.5
  • 40
    • 33745003285 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-kappaB
    • Frede S, Stockmann C, Freitag P, Fandrey J, (2006) Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-kappaB. Biochem J 396 (3): 517-527.
    • (2006) Biochem J , vol.396 , Issue.3 , pp. 517-527
    • Frede, S.1    Stockmann, C.2    Freitag, P.3    Fandrey, J.4
  • 41
    • 44849100198 scopus 로고    scopus 로고
    • NF-kappaB links innate immunity to the hypoxic response through transcriptional regulation of HIF-1alpha
    • Rius J, Guma M, Schachtrup C, Akassoglou K, Zinkernagel AS, et al. (2008) NF-kappaB links innate immunity to the hypoxic response through transcriptional regulation of HIF-1alpha. Nature 453 (7196): 807-811.
    • (2008) Nature , vol.453 , Issue.7196 , pp. 807-811
    • Rius, J.1    Guma, M.2    Schachtrup, C.3    Akassoglou, K.4    Zinkernagel, A.S.5
  • 42
    • 0033587146 scopus 로고    scopus 로고
    • The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
    • Maxwell PH, Wiesener MS, Chang GW, Clifford SC, Vaux EC, et al. (1999) The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis. Nature 399 (6733): 271-275.
    • (1999) Nature , vol.399 , Issue.6733 , pp. 271-275
    • Maxwell, P.H.1    Wiesener, M.S.2    Chang, G.W.3    Clifford, S.C.4    Vaux, E.C.5
  • 43
    • 29644442625 scopus 로고    scopus 로고
    • Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1
    • Lu H, Dalgard CL, Mohyeldin A, McFate T, Tait AS, et al. (2005) Reversible inactivation of HIF-1 prolyl hydroxylases allows cell metabolism to control basal HIF-1. J Biol Chem 280 (51): 41928-41939.
    • (2005) J Biol Chem , vol.280 , Issue.51 , pp. 41928-41939
    • Lu, H.1    Dalgard, C.L.2    Mohyeldin, A.3    McFate, T.4    Tait, A.S.5
  • 44
    • 27144458505 scopus 로고    scopus 로고
    • ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth
    • Bi M, Naczki C, Koritzinsky M, Fels D, Blais J, et al. (2005) ER stress-regulated translation increases tolerance to extreme hypoxia and promotes tumor growth. EMBO J 24 (19): 3470-3481.
    • (2005) EMBO J , vol.24 , Issue.19 , pp. 3470-3481
    • Bi, M.1    Naczki, C.2    Koritzinsky, M.3    Fels, D.4    Blais, J.5
  • 45
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen B, Braakman I, (2004) Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol 16 (4): 343-349.
    • (2004) Curr Opin Cell Biol , vol.16 , Issue.4 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 46
    • 0036877146 scopus 로고    scopus 로고
    • Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum
    • Michalak M, Robert Parker JM, Opas M, (2002) Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum. Cell Calcium 32 (5-6): 269-278.
    • (2002) Cell Calcium , vol.32 , Issue.5-6 , pp. 269-278
    • Michalak, M.1    Robert Parker, J.M.2    Opas, M.3
  • 47
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • Vembar SS, Brodsky JL, (2008) One step at a time: Endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9 (12): 944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.12 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 48
    • 34447512641 scopus 로고    scopus 로고
    • Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins
    • Olivari S, Molinari M, (2007) Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins. FEBS Lett 581 (19): 3658-3664.
    • (2007) FEBS Lett , vol.581 , Issue.19 , pp. 3658-3664
    • Olivari, S.1    Molinari, M.2
  • 49
    • 59849119398 scopus 로고    scopus 로고
    • Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
    • Clerc S, Hirsch C, Oggier DM, Deprez P, Jakob C, et al. (2009) Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol 184 (1): 159-172.
    • (2009) J Cell Biol , vol.184 , Issue.1 , pp. 159-172
    • Clerc, S.1    Hirsch, C.2    Oggier, D.M.3    Deprez, P.4    Jakob, C.5
  • 50
    • 57749083532 scopus 로고    scopus 로고
    • Defining the glycan destruction signal for endoplasmic reticulum-associated degradation
    • Quan EM, Kamiya Y, Kamiya D, Denic V, Weibezahn J, et al. (2008) Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol Cell 32 (6): 870-877.
    • (2008) Mol Cell , vol.32 , Issue.6 , pp. 870-877
    • Quan, E.M.1    Kamiya, Y.2    Kamiya, D.3    Denic, V.4    Weibezahn, J.5
  • 51
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • Lederkremer GZ, (2009) Glycoprotein folding, quality control and ER-associated degradation. Curr Opin Struct Biol 19 (5): 515-523.
    • (2009) Curr Opin Struct Biol , vol.19 , Issue.5 , pp. 515-523
    • Lederkremer, G.Z.1
  • 52
    • 33846990665 scopus 로고    scopus 로고
    • A domain responsible for HIF-1alpha degradation by YC-1, a novel anticancer agent
    • Kim HL, Yeo EJ, Chun YS, Park JW, (2006) A domain responsible for HIF-1alpha degradation by YC-1, a novel anticancer agent. Int J Oncol 29 (1): 255-260.
    • (2006) Int J Oncol , vol.29 , Issue.1 , pp. 255-260
    • Kim, H.L.1    Yeo, E.J.2    Chun, Y.S.3    Park, J.W.4
  • 53
    • 58149336774 scopus 로고    scopus 로고
    • Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins
    • Alcock F, Swanton E, (2009) Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins. J Mol Biol 385 (4): 1032-1042.
    • (2009) J Mol Biol , vol.385 , Issue.4 , pp. 1032-1042
    • Alcock, F.1    Swanton, E.2
  • 54
    • 33847378142 scopus 로고    scopus 로고
    • Optical analysis of the HIF-1 complex in living cells by FRET and FRAP
    • Wotzlaw C, Otto T, Berchner-Pfannschmidt U, Metzen E, Acker H, et al. (2007) Optical analysis of the HIF-1 complex in living cells by FRET and FRAP. FASEB J 21 (3): 700-707.
    • (2007) FASEB J , vol.21 , Issue.3 , pp. 700-707
    • Wotzlaw, C.1    Otto, T.2    Berchner-Pfannschmidt, U.3    Metzen, E.4    Acker, H.5
  • 55
    • 0030765016 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2+ disturbances, and cell death in renal epithelial cells
    • Liu H, Bowes RC 3rd, van de Water B, Sillence C, Nagelkerke JF, et al. (1997) Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2+ disturbances, and cell death in renal epithelial cells. J Biol Chem 272 (35): 21751-21759.
    • (1997) J Biol Chem , vol.272 , Issue.35 , pp. 21751-21759
    • Liu, H.1    Bowes III., R.C.2    van de Water, B.3    Sillence, C.4    Nagelkerke, J.F.5
  • 56
    • 0034064179 scopus 로고    scopus 로고
    • Resolution of glycoproteins by a lectin gel-shift assay
    • Popov M, Li J, Reithmeier RA, (2000) Resolution of glycoproteins by a lectin gel-shift assay. Anal Biochem 279 (1): 90-95.
    • (2000) Anal Biochem , vol.279 , Issue.1 , pp. 90-95
    • Popov, M.1    Li, J.2    Reithmeier, R.A.3


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