메뉴 건너뛰기




Volumn 9, Issue 12, 2007, Pages 2187-2195

Biliverdin reductase: PKC interaction at the cross-talk of MAPK and PI3K signaling pathways

Author keywords

[No Author keywords available]

Indexed keywords

BASIC LEUCINE ZIPPER TRANSCRIPTION FACTOR; BILIRUBIN; BILIVERDIN; BILIVERDIN REDUCTASE; GROWTH FACTOR; INSULIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOTRANSFERASE; PROTEIN KINASE C; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 35848965713     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2007.1805     Document Type: Review
Times cited : (50)

References (73)
  • 1
    • 0037088596 scopus 로고    scopus 로고
    • Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress
    • Ahmad Z, Salim M, and Maines MD. Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress. J Biol Chem 277: 9226-9232, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 9226-9232
    • Ahmad, Z.1    Salim, M.2    Maines, M.D.3
  • 2
    • 0034817067 scopus 로고    scopus 로고
    • CTP:phosphocholine cytidylyltransferase inhibition by ceramide via PKC-alpha, p38 MAPK, cPLA2, and 5-lipoxygenase
    • Awasthi S, Vivekananda J, Awasthi V, Smith D, and King RJ. CTP:phosphocholine cytidylyltransferase inhibition by ceramide via PKC-alpha, p38 MAPK, cPLA2, and 5-lipoxygenase. Am J Physiol Lung Cell Mol Physiol 281: L108-L118, 2001.
    • (2001) Am J Physiol Lung Cell Mol Physiol , vol.281
    • Awasthi, S.1    Vivekananda, J.2    Awasthi, V.3    Smith, D.4    King, R.J.5
  • 4
    • 0021693482 scopus 로고
    • Enzymatic heme oxygenase activity in soluble extracts of the unicellular red alga
    • Beale SI and Cornejo J. Enzymatic heme oxygenase activity in soluble extracts of the unicellular red alga, Cyanidium caldarium. Arch Biochem Biophys 235: 371-384, 1984.
    • (1984) Cyanidium caldarium. Arch Biochem Biophys , vol.235 , pp. 371-384
    • Beale, S.I.1    Cornejo, J.2
  • 5
    • 0023927014 scopus 로고
    • Kinetic properties and regulation of biliverdin reductase
    • Bell JE and Maines MD. Kinetic properties and regulation of biliverdin reductase. Arch Biochem Biophys 263: 1-9, 1988.
    • (1988) Arch Biochem Biophys , vol.263 , pp. 1-9
    • Bell, J.E.1    Maines, M.D.2
  • 10
    • 0029782604 scopus 로고    scopus 로고
    • A carboxy-terminal deletion mutant of protein kinase C beta II inhibits insulin-stimulated 2-deoxyglucose uptake in L6 rat skeletal muscle cells
    • Chalfant CE, Ohno S, Konno Y, Fisher AA, Bisnauth LD, Watson JE, and Cooper DR. A carboxy-terminal deletion mutant of protein kinase C beta II inhibits insulin-stimulated 2-deoxyglucose uptake in L6 rat skeletal muscle cells. Mol Endocrinol 10: 1273-1281, 1996.
    • (1996) Mol Endocrinol , vol.10 , pp. 1273-1281
    • Chalfant, C.E.1    Ohno, S.2    Konno, Y.3    Fisher, A.A.4    Bisnauth, L.D.5    Watson, J.E.6    Cooper, D.R.7
  • 11
    • 0035126796 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-induced cyclooxygenase-2 expression via sequential activation of ceramide-dependent mitogen-activated protein kinases, and IkappaB kinase 1/2 in human alveolar epithelial cells
    • Chen CC, Sun YT, Chen JJ, and Chang YJ. Tumor necrosis factor-alpha-induced cyclooxygenase-2 expression via sequential activation of ceramide-dependent mitogen-activated protein kinases, and IkappaB kinase 1/2 in human alveolar epithelial cells. Mol Pharmacol 59: 493-500, 2001.
    • (2001) Mol Pharmacol , vol.59 , pp. 493-500
    • Chen, C.C.1    Sun, Y.T.2    Chen, J.J.3    Chang, Y.J.4
  • 12
    • 33845640469 scopus 로고    scopus 로고
    • ho-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism
    • Converso DP, Taille C, Carreras MC, Jaitovich A, Poderoso JJ, and Boczkowski J. ho-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism. FASEB J 20: 1236-1238, 2006.
    • (2006) FASEB J , vol.20 , pp. 1236-1238
    • Converso, D.P.1    Taille, C.2    Carreras, M.C.3    Jaitovich, A.4    Poderoso, J.J.5    Boczkowski, J.6
  • 13
    • 0030941654 scopus 로고    scopus 로고
    • Mapping of the novel protein kinase catalytic domain of Dictyostelium myosin II heavy chain kinase A
    • Cote GP, Luo X, Murphy MB, and Egelhoff TT. Mapping of the novel protein kinase catalytic domain of Dictyostelium myosin II heavy chain kinase A. J Biol Chem 272: 6846-6849, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 6846-6849
    • Cote, G.P.1    Luo, X.2    Murphy, M.B.3    Egelhoff, T.T.4
  • 14
    • 0026641481 scopus 로고
    • Expression and characterization of a cDNA for rat kidney biliverdin reductase: Evidence suggesting the liver and kidney enzymes are the same transcript product
    • Fakhrai H and Maines MD. Expression and characterization of a cDNA for rat kidney biliverdin reductase: evidence suggesting the liver and kidney enzymes are the same transcript product. J Biol Chem 267: 4023-4029, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 4023-4029
    • Fakhrai, H.1    Maines, M.D.2
  • 15
    • 0021879854 scopus 로고
    • Interleukin-2 stimulates association of protein kinase C with plasma membrane
    • Farrar WL and Anderson WB. Interleukin-2 stimulates association of protein kinase C with plasma membrane. Nature 315: 233-235, 1985.
    • (1985) Nature , vol.315 , pp. 233-235
    • Farrar, W.L.1    Anderson, W.B.2
  • 16
    • 27744443713 scopus 로고    scopus 로고
    • A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization
    • Godoy-Ruiz R, Perez-Jimenez R, Ibarra-Molero B, and Sanchez-Ruiz JM. A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization. Biophys J 89: 3320-3331, 2005.
    • (2005) Biophys J , vol.89 , pp. 3320-3331
    • Godoy-Ruiz, R.1    Perez-Jimenez, R.2    Ibarra-Molero, B.3    Sanchez-Ruiz, J.M.4
  • 17
    • 0025760121 scopus 로고
    • Protein kinase C activation by phorbol esters: Do cysteine-rich regions and pseudosubstrate motifs play a role?
    • Gschwendt M, Kittstein W, and Marks F. Protein kinase C activation by phorbol esters: do cysteine-rich regions and pseudosubstrate motifs play a role? Trends Biochem Sci 16: 167-169, 1991.
    • (1991) Trends Biochem Sci , vol.16 , pp. 167-169
    • Gschwendt, M.1    Kittstein, W.2    Marks, F.3
  • 18
    • 0029020282 scopus 로고
    • Protein kinases: The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification
    • Hanks SK and Hunter T. Protein kinases: the eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 9: 576-596, 1995.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 19
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks SK, Quinn AM, and Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241: 42-52, 1988.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 20
    • 33645984875 scopus 로고    scopus 로고
    • Hosseini M, Rose AY, Song K, Bohan C, Alexander JP, Kelley MJ, and Acott TS. IL-1 and TNF induction of matrix metalloproteinase-3 by c-Jun N-terminal kinase in trabecular meshwork. Invest Ophthalmol Vis Sci 47: 1469-1476, 2006.
    • Hosseini M, Rose AY, Song K, Bohan C, Alexander JP, Kelley MJ, and Acott TS. IL-1 and TNF induction of matrix metalloproteinase-3 by c-Jun N-terminal kinase in trabecular meshwork. Invest Ophthalmol Vis Sci 47: 1469-1476, 2006.
  • 21
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudosubstrate prototype in its regulatory domain
    • House C and Kemp BE. Protein kinase C contains a pseudosubstrate prototype in its regulatory domain. Science 238: 1726-1728, 1987.
    • (1987) Science , vol.238 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 22
    • 0024348120 scopus 로고
    • Detection of 10 variants of biliverdin reductase in rat liver by two-dimensional gel electrophoresis
    • Huang TJ, Trakshel GM, and Maines MD. Detection of 10 variants of biliverdin reductase in rat liver by two-dimensional gel electrophoresis. J Biol Chem 264: 7844-7849, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 7844-7849
    • Huang, T.J.1    Trakshel, G.M.2    Maines, M.D.3
  • 23
    • 0034614490 scopus 로고    scopus 로고
    • Signaling: 2000 and beyond
    • Hunter T. Signaling: 2000 and beyond. Cell 100: 113-127, 2000.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 25
    • 0036854481 scopus 로고    scopus 로고
    • Protein kinase C beta (PKC beta): Normal functions and diseases
    • Kawakami T, Kawakami Y, and Kitaura J. Protein kinase C beta (PKC beta): normal functions and diseases. J Biochem (Tokyo) 132: 677-682, 2002.
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 677-682
    • Kawakami, T.1    Kawakami, Y.2    Kitaura, J.3
  • 26
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • Keranen LM, Dutil EM, and Newton AC. Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. Curr Biol 5: 1394-1403, 1995.
    • (1995) Curr Biol , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 28
    • 0034604723 scopus 로고    scopus 로고
    • Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content
    • Knapp LT and Klann E. Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content. J Biol Chem 275: 24136-24145, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 24136-24145
    • Knapp, L.T.1    Klann, E.2
  • 29
    • 0035091209 scopus 로고    scopus 로고
    • The Arabidopsis HY2 gene encodes phytochromobilin synthase, a ferredoxin-dependent biliverdin reductase
    • Kohchi T, Mukougawa K, Frankenberg N, Masuda M, Yokota A, and Lagarias JC. The Arabidopsis HY2 gene encodes phytochromobilin synthase, a ferredoxin-dependent biliverdin reductase. Plant Cell 13: 425-436, 2001.
    • (2001) Plant Cell , vol.13 , pp. 425-436
    • Kohchi, T.1    Mukougawa, K.2    Frankenberg, N.3    Masuda, M.4    Yokota, A.5    Lagarias, J.C.6
  • 30
    • 0037113925 scopus 로고    scopus 로고
    • Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen
    • Korichneva I, Hoyos B, Chua R, Levi E, and Hammerling U. Zinc release from protein kinase C as the common event during activation by lipid second messenger or reactive oxygen. J Biol Chem 277: 44327-44331, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 44327-44331
    • Korichneva, I.1    Hoyos, B.2    Chua, R.3    Levi, E.4    Hammerling, U.5
  • 31
    • 2442594982 scopus 로고    scopus 로고
    • Biliverdin reductase: A novel regulator for Induction of activating transcription factor-2 and heme oxygenase-1
    • Kravets A, Hu Z, Miralem T, Torno MD, and Maines MD. Biliverdin reductase: a novel regulator for Induction of activating transcription factor-2 and heme oxygenase-1. J Biol Chem 279: 19916-19923, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 19916-19923
    • Kravets, A.1    Hu, Z.2    Miralem, T.3    Torno, M.D.4    Maines, M.D.5
  • 32
    • 0019887888 scopus 로고
    • Purification and characterization of biliverdin reductase from rat liver
    • Kutty RK and Maines MD. Purification and characterization of biliverdin reductase from rat liver. J Biol Chem 256: 3956-3962, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 3956-3962
    • Kutty, R.K.1    Maines, M.D.2
  • 33
    • 18844371482 scopus 로고    scopus 로고
    • Human biliverdin reductase: A member of the insulin receptor substrate family with serine/threonine/tyrosine kinase activity
    • Lerner-Marmarosh N, Shen J, Torno MD, Kravets A, Hu Z, and Maines MD. Human biliverdin reductase: a member of the insulin receptor substrate family with serine/threonine/tyrosine kinase activity. Proc Natl Acad Sci U S A 102: 7109-7114, 2005.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 7109-7114
    • Lerner-Marmarosh, N.1    Shen, J.2    Torno, M.D.3    Kravets, A.4    Hu, Z.5    Maines, M.D.6
  • 34
    • 0034980906 scopus 로고    scopus 로고
    • Liu JK, Maria B, Liu Yaping, Lu, Tong; Qu, Wei; Waalkes, Michael P. Stress-related gene expression in mice treated with inorganic arsenicals. Toxicol Sci 61: 314-320, 2001.
    • Liu JK, Maria B, Liu Yaping, Lu, Tong; Qu, Wei; Waalkes, Michael P. Stress-related gene expression in mice treated with inorganic arsenicals. Toxicol Sci 61: 314-320, 2001.
  • 36
    • 28844493391 scopus 로고    scopus 로고
    • New insights into biliverdin reductase functions: Linking heme metabolism to cell signaling
    • Maines MD. New insights into biliverdin reductase functions: linking heme metabolism to cell signaling. Physiology (Bethesda) 20: 382-389, 2005.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 382-389
    • Maines, M.D.1
  • 37
    • 0035123138 scopus 로고    scopus 로고
    • Nuclear localization of biliverdin reductase in the rat kidney: Response to nephrotoxins that induce heme oxygenase-1
    • Maines MD, Ewing JF, Huang TJ, and Panahian N. Nuclear localization of biliverdin reductase in the rat kidney: response to nephrotoxins that induce heme oxygenase-1. J Pharmacol Exp Ther 296: 1091-1097, 2001.
    • (2001) J Pharmacol Exp Ther , vol.296 , pp. 1091-1097
    • Maines, M.D.1    Ewing, J.F.2    Huang, T.J.3    Panahian, N.4
  • 38
    • 34247259885 scopus 로고    scopus 로고
    • Human biliverdin reductase: A previously unknown activator of protein kinase C βII
    • Maines MD, Miralem T, Lerner-Marmarosh N, Shen J, and Gibbs PE. Human biliverdin reductase: a previously unknown activator of protein kinase C βII. J Biol Chem 282: 8110-8122, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 8110-8122
    • Maines, M.D.1    Miralem, T.2    Lerner-Marmarosh, N.3    Shen, J.4    Gibbs, P.E.5
  • 39
    • 0029671237 scopus 로고    scopus 로고
    • Human biliverdin IXalpha reductase is a zinc-metalloprotein: Characterization of purified and Escherichia coli expressed enzymes
    • Maines MD, Polevoda BV, Huang TJ, and McCoubrey WK Jr. Human biliverdin IXalpha reductase is a zinc-metalloprotein: characterization of purified and Escherichia coli expressed enzymes. Eur J Biochem 235: 372-381, 1996.
    • (1996) Eur J Biochem , vol.235 , pp. 372-381
    • Maines, M.D.1    Polevoda, B.V.2    Huang, T.J.3    McCoubrey Jr., W.K.4
  • 40
    • 0029123921 scopus 로고
    • The structure, organization and differential expression of the rat gene encoding biliverdin reductase
    • McCoubrey WK Jr, Cooklis MA, and Maines MD. The structure, organization and differential expression of the rat gene encoding biliverdin reductase. Gene 160: 235-240, 1995.
    • (1995) Gene , vol.160 , pp. 235-240
    • McCoubrey Jr, W.K.1    Cooklis, M.A.2    Maines, M.D.3
  • 42
    • 0036077325 scopus 로고    scopus 로고
    • TNF-alpha inhibits SP-A gene expression in lung epithelial cells via p38 MAPK
    • Miakotina OL and Snyder JM. TNF-alpha inhibits SP-A gene expression in lung epithelial cells via p38 MAPK. Am J Physiol Lung Cell Mol Physiol 283: L418-L427, 2002.
    • (2002) Am J Physiol Lung Cell Mol Physiol , vol.283
    • Miakotina, O.L.1    Snyder, J.M.2
  • 43
    • 20444445069 scopus 로고    scopus 로고
    • Small interference RNA-mediated gene silencing of human biliverdin reductase, but not that of heme oxygenase-1, attenuates arsenite-mediated induction of the oxygenase and increases apoptosis in 293A kidney cells
    • Miralem T, Hu Z, Torno MD, Lelli KM, and Maines MD. Small interference RNA-mediated gene silencing of human biliverdin reductase, but not that of heme oxygenase-1, attenuates arsenite-mediated induction of the oxygenase and increases apoptosis in 293A kidney cells. J Biol Chem 280: 17084-17092, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 17084-17092
    • Miralem, T.1    Hu, Z.2    Torno, M.D.3    Lelli, K.M.4    Maines, M.D.5
  • 44
    • 0028938152 scopus 로고
    • Localization of protein kinases by anchoring proteins: A theme in signal transduction
    • Mochly-Rosen D. Localization of protein kinases by anchoring proteins: a theme in signal transduction. Science 268: 247-251, 1995.
    • (1995) Science , vol.268 , pp. 247-251
    • Mochly-Rosen, D.1
  • 45
    • 0026733246 scopus 로고
    • p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C
    • Mochly-Rosen D, Miller KG, Scheller RH, Khaner H, Lopez J, and Smith BL. p65 fragments, homologous to the C2 region of protein kinase C, bind to the intracellular receptors for protein kinase C. Biochemistry 31: 8120-8124, 1992.
    • (1992) Biochemistry , vol.31 , pp. 8120-8124
    • Mochly-Rosen, D.1    Miller, K.G.2    Scheller, R.H.3    Khaner, H.4    Lopez, J.5    Smith, B.L.6
  • 46
    • 33645960166 scopus 로고    scopus 로고
    • PKCzeta at the crossroad of NF-kappaB and Jak1/Stat6 signaling pathways
    • Moscat J, Rennert P, and Diaz-Meco MT. PKCzeta at the crossroad of NF-kappaB and Jak1/Stat6 signaling pathways. Cell Death Differ 13: 702-711, 2006.
    • (2006) Cell Death Differ , vol.13 , pp. 702-711
    • Moscat, J.1    Rennert, P.2    Diaz-Meco, M.T.3
  • 47
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton AC. Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem Rev 101: 2353-2364, 2001.
    • (2001) Chem Rev , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 48
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton AC. Regulation of protein kinase C. Curr Opin Cell Biol 9: 161-167, 1997.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 49
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka Y. Studies and perspectives of protein kinase C. Science 233: 305-312, 1986.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 50
    • 30044442866 scopus 로고    scopus 로고
    • How Toll-like receptors signal: What we know and what we don't know
    • O'Neill LA. How Toll-like receptors signal: what we know and what we don't know. Curr Opin Immunol 18: 3-9, 2006.
    • (2006) Curr Opin Immunol , vol.18 , pp. 3-9
    • O'Neill, L.A.1
  • 51
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh DB, Ziegler W, and Parker PJ. Multiple pathways control protein kinase C phosphorylation. EMBO J 19: 496-503, 2000.
    • (2000) EMBO J , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 52
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature 373: 573-580, 1995.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 53
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling: 50 years and counting
    • Pawson T and Scott JD. Protein phosphorylation in signaling: 50 years and counting. Trends Biochem Sci 30: 286-290, 2005.
    • (2005) Trends Biochem Sci , vol.30 , pp. 286-290
    • Pawson, T.1    Scott, J.D.2
  • 54
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson T and Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science 278: 2075-2080, 1997.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 55
    • 18844380660 scopus 로고    scopus 로고
    • Signaling in B cells via Toll-like receptors
    • Peng SL. Signaling in B cells via Toll-like receptors. Curr Opin Immunol 17: 230-236, 2005.
    • (2005) Curr Opin Immunol , vol.17 , pp. 230-236
    • Peng, S.L.1
  • 56
    • 0033582431 scopus 로고    scopus 로고
    • Molecular mechanism of the regulation of glutathione synthesis by tumor necrosis factor-alpha and dexamethasone in human alveolar epithelial cells
    • Rahman I, Antonicelli F, and MacNee W. Molecular mechanism of the regulation of glutathione synthesis by tumor necrosis factor-alpha and dexamethasone in human alveolar epithelial cells. J Biol Chem 274: 5088-5096, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 5088-5096
    • Rahman, I.1    Antonicelli, F.2    MacNee, W.3
  • 57
    • 0028036338 scopus 로고
    • Cloning of an intracellular receptor for protein kinase C: A homolog of the beta subunit of G proteins
    • Ron D, Chen CH, Caldwell J, Jamieson L, Orr E, and Mochly-Rosen D. Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins. Proc Natl Acad Sci U S A 91: 839-843, 1994.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 839-843
    • Ron, D.1    Chen, C.H.2    Caldwell, J.3    Jamieson, L.4    Orr, E.5    Mochly-Rosen, D.6
  • 58
    • 0028801624 scopus 로고
    • An autoregulatory region in protein kinase C: The pseudoanchoring site
    • Ron D and Mochly-Rosen D. An autoregulatory region in protein kinase C: the pseudoanchoring site. Proc Natl Acad Sci U S A 92: 492-496, 1995.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 492-496
    • Ron, D.1    Mochly-Rosen, D.2
  • 59
    • 0035815611 scopus 로고    scopus 로고
    • Human biliverdin reductase is autophosphorylated, and phosphorylation is required for bilirubin formation
    • Salim M, Brown-Kipphut BA, and Maines MD. Human biliverdin reductase is autophosphorylated, and phosphorylation is required for bilirubin formation. J Biol Chem 276: 10929-10934, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 10929-10934
    • Salim, M.1    Brown-Kipphut, B.A.2    Maines, M.D.3
  • 61
    • 0030921502 scopus 로고    scopus 로고
    • Rossi, Fouad Shalaby, Gen-Sheng Feng, and Tony Pawson. Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2
    • Saxton TM, Mark Henkemeyer, Stéphan Gasca, Randy Shen, Derrick J. Rossi, Fouad Shalaby, Gen-Sheng Feng, and Tony Pawson. Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp-2. EMBO J 16: 2352-2364, 1997.
    • (1997) EMBO J , vol.16 , pp. 2352-2364
    • Saxton, T.M.1    Henkemeyer, M.2    Gasca, S.3    Shen, R.4    Derrick, J.5
  • 62
    • 0030925429 scopus 로고    scopus 로고
    • Characterization of cyanobacterial biliverdin reductase: Conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis
    • Schluchter WM and Glazer AN. Characterization of cyanobacterial biliverdin reductase: conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis. J Biol Chem 272: 13562-13569, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 13562-13569
    • Schluchter, W.M.1    Glazer, A.N.2
  • 63
    • 21844443602 scopus 로고    scopus 로고
    • Differentiation of immature oligodendrocytes is regulated by phosphorylation of cyclic AMP-response element binding protein by a protein kinase C signaling cascade
    • Shiga H, Yamane Y, Kubo M, Sakurai Y, Asou H, and Ito E. Differentiation of immature oligodendrocytes is regulated by phosphorylation of cyclic AMP-response element binding protein by a protein kinase C signaling cascade. J Neurosci Res 80: 767-776, 2005.
    • (2005) J Neurosci Res , vol.80 , pp. 767-776
    • Shiga, H.1    Yamane, Y.2    Kubo, M.3    Sakurai, Y.4    Asou, H.5    Ito, E.6
  • 64
    • 0036855827 scopus 로고    scopus 로고
    • Activation mechanisms of protein kinase C: Maturation, catalytic activation, and targeting
    • Shirai Y and Saito N. Activation mechanisms of protein kinase C: maturation, catalytic activation, and targeting. J Biochem (Tokyo) 132: 663-668, 2002.
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 663-668
    • Shirai, Y.1    Saito, N.2
  • 65
    • 0013830660 scopus 로고
    • Biliverdin reductase of guinea pig liver
    • Singleton JW and Laster L. Biliverdin reductase of guinea pig liver. J Biol Chem 240: 4780-4789, 1965.
    • (1965) J Biol Chem , vol.240 , pp. 4780-4789
    • Singleton, J.W.1    Laster, L.2
  • 67
    • 0036134050 scopus 로고    scopus 로고
    • High glucose-induced activation of protein kinase signaling pathways in vascular smooth muscle cells: A potential role in the pathogenesis of vascular dysfunction in diabetes (review)
    • Srivastava AK. High glucose-induced activation of protein kinase signaling pathways in vascular smooth muscle cells: a potential role in the pathogenesis of vascular dysfunction in diabetes (review). Int J Mol Med 9: 85-89, 2002.
    • (2002) Int J Mol Med , vol.9 , pp. 85-89
    • Srivastava, A.K.1
  • 68
    • 0028818886 scopus 로고
    • How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase
    • Taylor SS, Radzio-Andzelm E, and Hunter T. How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase. FASEB J 9: 1255-1266, 1995.
    • (1995) FASEB J , vol.9 , pp. 1255-1266
    • Taylor, S.S.1    Radzio-Andzelm, E.2    Hunter, T.3
  • 69
    • 0033961822 scopus 로고    scopus 로고
    • Protein kinase Ce is required for the induction of mitogen-activated protein kinase phophatase-1 in lipopolysaccharide-stimulated macrophages
    • Valledor AF, Xaus J, Comalada M, Soler C, and Celada A. Protein kinase Ce is required for the induction of mitogen-activated protein kinase phophatase-1 in lipopolysaccharide-stimulated macrophages. J Immunol 164: 29-37, 2000.
    • (2000) J Immunol , vol.164 , pp. 29-37
    • Valledor, A.F.1    Xaus, J.2    Comalada, M.3    Soler, C.4    Celada, A.5
  • 70
    • 0038165531 scopus 로고    scopus 로고
    • The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase
    • Wang J and de Montellano PR. The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase. J Biol Chem 278: 20069-20076, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 20069-20076
    • Wang, J.1    de Montellano, P.R.2
  • 71
    • 0036304792 scopus 로고    scopus 로고
    • Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex
    • Whitby FG, Phillips JD, Hill CP, McCoubrey W, and Maines MD. Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex. J Mol Biol 319: 1199-1210, 2002.
    • (2002) J Mol Biol , vol.319 , pp. 1199-1210
    • Whitby, F.G.1    Phillips, J.D.2    Hill, C.P.3    McCoubrey, W.4    Maines, M.D.5
  • 72
    • 0035193041 scopus 로고    scopus 로고
    • Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase Cs via src kinase pathway
    • Wooten MW, Vandenplas ML, Seibenhener ML, Geetha T, Diaz-Meco MT. Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase Cs via src kinase pathway. Mol Cell Biol 21: 8414-8427, 2001.
    • (2001) Mol Cell Biol , vol.21 , pp. 8414-8427
    • Wooten, M.W.1    Vandenplas, M.L.2    Seibenhener, M.L.3    Geetha, T.4    Diaz-Meco, M.T.5
  • 73
    • 33749270530 scopus 로고    scopus 로고
    • Stimulation of protein kinase C activity by tumor necrosis factor-alpha in bovine bronchial epithelial cells
    • Wyatt TA, Ito H, Veys TJ, and Spurzem JR. Stimulation of protein kinase C activity by tumor necrosis factor-alpha in bovine bronchial epithelial cells. Am J Physiol 273: L1007-1012, 1997.
    • (1997) Am J Physiol , vol.273
    • Wyatt, T.A.1    Ito, H.2    Veys, T.J.3    Spurzem, J.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.