메뉴 건너뛰기




Volumn 3 MAR, Issue , 2012, Pages

Biliverdin reductase: More than a namesake-the reductase, its peptide fragments, and biliverdin regulate activity of the three classes of protein kinase C

Author keywords

Biliverdin; Biliverdin reductase; Peptides; Protein kinase C; Signaling pathways

Indexed keywords

AUTOANTIGEN; BILIVERDIN; BILIVERDIN REDUCTASE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE KINASE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; LYSYLARGINYLASPARAGYLARGINYLTYROSYLLEUCYLSERYLPHENYLALANINE; LYSYLLYSYLARGINYLISOLEUCYLLEUCYLHISTIDYLCYSTEINE; LYSYLTYROSYLCYSTYLCYSTYLSERYLARGINYLLYSINE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; OXIDOREDUCTASE; PEPTIDE; PHENYLALANYLGLYCYLPHENYLALANYLPROLYLALANYLPHENYLALANINE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN KINASE C; PROTEIN KINASE C BETA II; PROTEIN KINASE C DELTA; PROTEIN KINASE C XI; PROTEIN TYROSINE KINASE; SOMATOMEDIN C; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 84865967131     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2012.00031     Document Type: Article
Times cited : (33)

References (66)
  • 1
    • 0037088596 scopus 로고    scopus 로고
    • Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase1 by oxidative stress
    • Ahmad, Z.,Salim, M., and Maines, M. D. (2002). Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase1 by oxidative stress. J. Biol. Chem. 277, 9226-9232.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9226-9232
    • Ahmad, Z.1    Salim, M.2    Maines, M.D.3
  • 2
    • 0036523088 scopus 로고    scopus 로고
    • Caspase-3-dependent proteolytic cleavage of protein kinase C delta is essential for oxidative stress-mediated dopaminergic cell death after exposure to methylcyclopentadienyl manganese tricarbonyl
    • Anantharam, V., Kitazawa, M., Wagner, J., Kaul, S., and Kanthasamy, A. G. (2002). Caspase-3-dependent proteolytic cleavage of protein kinase C delta is essential for oxidative stress-mediated dopaminergic cell death after exposure to methylcyclopentadienyl manganese tricarbonyl. J. Neurosci. 22, 1738-1751.
    • (2002) J. Neurosci. , vol.22 , pp. 1738-1751
    • Anantharam, V.1    Kitazawa, M.2    Wagner, J.3    Kaul, S.4    Kanthasamy, A.G.5
  • 4
    • 54049141728 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase/MAP kinase phosphatase regulation: roles in cell growth, death, and cancer
    • Boutros, T., Chevet, E., and Metrakos, P. (2008). Mitogen-activated protein (MAP) kinase/MAP kinase phosphatase regulation: roles in cell growth, death, and cancer. Pharmacol. Rev. 60, 261-310.
    • (2008) Pharmacol. Rev. , vol.60 , pp. 261-310
    • Boutros, T.1    Chevet, E.2    Metrakos, P.3
  • 5
    • 0028986075 scopus 로고
    • Control of I kappa B-alpha proteolysis by site-specific, signalinduced phosphorylation
    • Brown, K., Gerstberger, S., Carlson, L., Franzoso, G., and Siebenlist, U. (1995). Control of I kappa B-alpha proteolysis by site-specific, signalinduced phosphorylation. Science 267, 1485-1488.
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 6
    • 59649097080 scopus 로고    scopus 로고
    • A protein kinase C delta-dependent protein kinase D pathway modulates ERK1/2 and JNK1/2 phosphorylation and Bimassociated apoptosis by asbestos
    • Buder-Hoffmann, S. A., Shukla, A., Barrett, T. F., Macpherson, M. B., Lounsbury, K. M., and Mossman, B. T. (2009). A protein kinase C delta-dependent protein kinase D pathway modulates ERK1/2 and JNK1/2 phosphorylation and Bimassociated apoptosis by asbestos. Am. J. Pathol. 174, 449-459.
    • (2009) Am. J. Pathol. , vol.174 , pp. 449-459
    • Buder-Hoffmann, S.A.1    Shukla, A.2    Barrett, T.F.3    Macpherson, M.B.4    Lounsbury, K.M.5    Mossman, B.T.6
  • 8
    • 0037443030 scopus 로고    scopus 로고
    • Altered protein kinase C (PKC) isoforms in non-small cell lung cancer cells: PKC delta promotes cellular survival and chemotherapeutic resistance
    • Clark, A. S., West, K. A., Blumberg, P. M., and Dennis, P. A. (2003). Altered protein kinase C (PKC) isoforms in non-small cell lung cancer cells: PKC delta promotes cellular survival and chemotherapeutic resistance. Cancer Res. 63, 780-786.
    • (2003) Cancer Res , vol.63 , pp. 780-786
    • Clark, A.S.1    West, K.A.2    Blumberg, P.M.3    Dennis, P.A.4
  • 10
    • 0028129666 scopus 로고
    • Delta protein kinase-C in the rat ovary: estrogen regulation and localization
    • Cutler, R. E. Jr., Maizels, E. T., and Hunzicker-Dunn, M. (1994). Delta protein kinase-C in the rat ovary: estrogen regulation and localization. Endocrinology 135, 1669-1678.
    • (1994) Endocrinology , vol.135 , pp. 1669-1678
    • Cutler Jr., R.E.1    Maizels, E.T.2    Hunzicker-Dunn, M.3
  • 12
    • 35648987863 scopus 로고    scopus 로고
    • Biliverdin inhibits activation of NFkappaB: reversal of inhibition by human biliverdin reductase
    • Gibbs, P. E., and Maines, M. D. (2007). Biliverdin inhibits activation of NFkappaB: reversal of inhibition by human biliverdin reductase. Int. J. Cancer 121, 2567-2574.
    • (2007) Int. J. Cancer , vol.121 , pp. 2567-2574
    • Gibbs, P.E.1    Maines, M.D.2
  • 13
    • 84855481125 scopus 로고    scopus 로고
    • Formation of ternary complex of human biliverdin reductase-protein kinase C delta-ERK2 protein is essential for ERK2-mediated activation of Elk1 protein, nuclear factor-kappaB, and inducible nitric-oxidase synthase (iNOS)
    • Gibbs, P. E., Miralem, T., Lerner Marmarosh, N., Tudor, C., and Maines, M. D. (2012). Formation of ternary complex of human biliverdin reductase-protein kinase C delta-ERK2 protein is essential for ERK2-mediated activation of Elk1 protein, nuclear factor-kappaB, and inducible nitric-oxidase synthase (iNOS). J. Biol. Chem. 287, 1066-1079.
    • (2012) J. Biol. Chem. , vol.287 , pp. 1066-1079
    • Gibbs, P.E.1    Miralem, T.2    Lerner Marmarosh, N.3    Tudor, C.4    Maines, M.D.5
  • 14
    • 77956638427 scopus 로고    scopus 로고
    • Characterization of the human biliverdin reductase gene structure and regulatory elements: promoter activity is enhanced by hypoxia and suppressed by TNF{alpha}-activated NF-{kappa}B
    • Gibbs, P. E., Miralem, T., and Maines, M. D. (2010). Characterization of the human biliverdin reductase gene structure and regulatory elements: promoter activity is enhanced by hypoxia and suppressed by TNF{alpha}-activated NF-{kappa}B. FASEB J. 24, 3239-3254.
    • (2010) FASEB J , vol.24 , pp. 3239-3254
    • Gibbs, P.E.1    Miralem, T.2    Maines, M.D.3
  • 15
    • 38449104652 scopus 로고    scopus 로고
    • Impaired T cell protein kinase C delta activation decreases ERK pathway signaling in idiopathic and hydralazine-induced lupus
    • Gorelik, G., Fang, J. Y., Wu, A., Sawalha, A. H., and Richardson, B. (2007). Impaired T cell protein kinase C delta activation decreases ERK pathway signaling in idiopathic and hydralazine-induced lupus. J. Immunol. 179, 5553-5563.
    • (2007) J. Immunol. , vol.179 , pp. 5553-5563
    • Gorelik, G.1    Fang, J.Y.2    Wu, A.3    Sawalha, A.H.4    Richardson, B.5
  • 16
    • 27144490362 scopus 로고    scopus 로고
    • A humanspecific TNF-responsive promoter for Goodpasture antigen-binding protein
    • Granero, F., Revert, F., Revert-Ros, F., Lainez, S., Martinez-Martinez, P., and Saus, J. (2005). A humanspecific TNF-responsive promoter for Goodpasture antigen-binding protein. FEBS J. 272, 5291-5305.
    • (2005) FEBS J , vol.272 , pp. 5291-5305
    • Granero, F.1    Revert, F.2    Revert-Ros, F.3    Lainez, S.4    Martinez-Martinez, P.5    Saus, J.6
  • 17
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification
    • Hanks, S. K.,and Hunter, T. (1995). Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 18
    • 0024348120 scopus 로고
    • Detection of 10 variants of biliverdin reductase in rat liver by two-dimensional gel electrophoresis
    • Huang, T. J., Trakshel, G. M., and Maines, M. D. (1989). Detection of 10 variants of biliverdin reductase in rat liver by two-dimensional gel electrophoresis. J. Biol. Chem. 264, 7844-7849.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7844-7849
    • Huang, T.J.1    Trakshel, G.M.2    Maines, M.D.3
  • 20
    • 1842454982 scopus 로고    scopus 로고
    • The enigmatic protein kinase C delta: complex roles in cell proliferation and survival
    • Jackson, D. N., and Foster, D. A. (2004). The enigmatic protein kinase C delta: complex roles in cell proliferation and survival. FASEB J. 18, 627-636.
    • (2004) FASEB J , vol.18 , pp. 627-636
    • Jackson, D.N.1    Foster, D.A.2
  • 21
    • 0033555229 scopus 로고    scopus 로고
    • Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase
    • Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., and Kornfeld, K. (1999). Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase. Genes Dev. 13, 163-175.
    • (1999) Genes Dev , vol.13 , pp. 163-175
    • Jacobs, D.1    Glossip, D.2    Xing, H.3    Muslin, A.J.4    Kornfeld, K.5
  • 23
    • 61549122310 scopus 로고    scopus 로고
    • Pleiotropic functions of biliverdin reductase: cellular signaling and generation of cytoprotective and cytotoxic bilirubin
    • Kapitulnik, J., and Maines, M. D. (2009). Pleiotropic functions of biliverdin reductase: cellular signaling and generation of cytoprotective and cytotoxic bilirubin. Trends Pharmacol. Sci. 30, 129-137.
    • (2009) Trends Pharmacol. Sci. , vol.30 , pp. 129-137
    • Kapitulnik, J.1    Maines, M.D.2
  • 25
    • 76749088358 scopus 로고    scopus 로고
    • Pathological roles of MAPK signaling pathways in human diseases
    • Kim, E. K., and Choi, E. J. (2010). Pathological roles of MAPK signaling pathways in human diseases. Biochim. Biophys. Acta 1802, 396-405.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 396-405
    • Kim, E.K.1    Choi, E.J.2
  • 26
    • 3042737456 scopus 로고    scopus 로고
    • Caveolae compartmentalization of heme oxygenase-1 in endothelial cells
    • Kim, H. P., Wang, X., Galbiati, F., Ryter, S. W., and Choi, A. M. (2004). Caveolae compartmentalization of heme oxygenase-1 in endothelial cells. FASEB J. 18, 1080-1089.
    • (2004) FASEB J , vol.18 , pp. 1080-1089
    • Kim, H.P.1    Wang, X.2    Galbiati, F.3    Ryter, S.W.4    Choi, A.M.5
  • 27
    • 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, M. D., and Maines, M. D. (2004). Biliverdin reductase, a novel regulator for induction of activating transcription factor-2 and heme oxygenase-1. J. Biol. Chem. 279, 19916-19923.
    • (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
  • 28
    • 0019887888 scopus 로고
    • Purification and characterization of biliverdin reductase from rat liver
    • Kutty, R. K., and Maines, M. D. (1981). Purification and characterization of biliverdin reductase from rat liver. J. Biol. Chem. 256, 3956-3962.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3956-3962
    • Kutty, R.K.1    Maines, M.D.2
  • 29
    • 36849045105 scopus 로고    scopus 로고
    • Regulation of TNF-alphaactivated PKC-zeta signaling by the human biliverdin reductase: identification of activating and inhibitory domains of the reductase
    • Lerner-Marmarosh, N., Miralem, T., Gibbs, P. E., and Maines, M. D. (2007). Regulation of TNF-alphaactivated PKC-zeta signaling by the human biliverdin reductase: identification of activating and inhibitory domains of the reductase. FASEB J. 21, 3949-3962.
    • (2007) FASEB J , vol.21 , pp. 3949-3962
    • Lerner-Marmarosh, N.1    Miralem, T.2    Gibbs, P.E.3    Maines, M.D.4
  • 30
    • 44349190488 scopus 로고    scopus 로고
    • Human biliverdin reductase is an ERK activator; hBVR is an ERK nuclear transporter and is required for MAPK signaling
    • Lerner-Marmarosh, N., Miralem, T., Gibbs, P. E., and Maines, M. D. (2008). Human biliverdin reductase is an ERK activator; hBVR is an ERK nuclear transporter and is required for MAPK signaling. Proc. Natl. Acad. Sci. U.S.A. 105, 6870-6875.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 6870-6875
    • Lerner-Marmarosh, N.1    Miralem, T.2    Gibbs, P.E.3    Maines, M.D.4
  • 31
    • 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, M. D., Kravets, A., Hu, Z., and Maines, M. D. (2005). 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) 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
  • 32
    • 0026597280 scopus 로고
    • Phosphorylation by cAMPdependent protein kinase inhibits the degradation of tau by calpain
    • Litersky, J. M., and Johnson, G. V. (1992). Phosphorylation by cAMPdependent protein kinase inhibits the degradation of tau by calpain. J. Biol. Chem. 267, 1563-1568.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1563-1568
    • Litersky, J.M.1    Johnson, G.V.2
  • 33
    • 28844493391 scopus 로고    scopus 로고
    • New insights into biliverdin reductase functions: linking heme metabolism to cell signaling
    • Maines, M. D. (2005). New insights into biliverdin reductase functions: linking heme metabolism to cell signaling. Physiology (Bethesda) 20, 382-389.
    • (2005) Physiology (Bethesda) , vol.20 , pp. 382-389
    • Maines, M.D.1
  • 34
    • 35848965713 scopus 로고    scopus 로고
    • Biliverdin reductase: PKC interaction at the crosstalk of MAPK and PI3K signaling pathways
    • Maines, M. D. (2007). Biliverdin reductase: PKC interaction at the crosstalk of MAPK and PI3K signaling pathways. Antioxid. Redox Signal. 9, 2187-2195.
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2187-2195
    • Maines, M.D.1
  • 35
    • 34247259885 scopus 로고    scopus 로고
    • Human biliverdin reductase, a previously unknown activator of protein kinase C betaII
    • Maines, M. D., Miralem, T., Lerner Marmarosh, N., Shen, J., and Gibbs, P. E. (2007). Human biliverdin reductase, a previously unknown activator of protein kinase C betaII. J. Biol. Chem. 282, 8110-8122.
    • (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
  • 36
    • 0029671237 scopus 로고    scopus 로고
    • Human biliverdin IX alpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes
    • Maines, M. D., Polevoda, B. V., Huang, T. J., and Mccoubrey, W. K. Jr. (1996). Human biliverdin IX alpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes. Eur. J. Biochem. 235, 372-381.
    • (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
  • 37
    • 0348231006 scopus 로고    scopus 로고
    • Protein kinase C delta is a prosurvival factor in human breast tumor cell lines
    • McCracken, M. A., Miraglia, L. J., Mckay, R. A., and Strobl, J. S. (2003). Protein kinase C delta is a prosurvival factor in human breast tumor cell lines. Mol. Cancer Ther. 2, 273-281.
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 273-281
    • McCracken, M.A.1    Miraglia, L.J.2    Mckay, R.A.3    Strobl, J.S.4
  • 38
    • 0030703604 scopus 로고    scopus 로고
    • Regulation and function of the JNK subgroup of MAP kinases
    • Minden, A., and Karin, M. (1997). Regulation and function of the JNK subgroup of MAP kinases. Biochim. Biophys. Acta 1333, F85-F104.
    • (1997) Biochim. Biophys. Acta , vol.1333
    • Minden, A.1    Karin, M.2
  • 39
    • 77951248544 scopus 로고    scopus 로고
    • Human biliverdin reductase suppresses Goodpasture antigenbinding protein (GPBP) kinase activity: the reductase regulates tumor necrosis factor-alphaNF-kappaB-dependent GPBP expression
    • Miralem, T., Gibbs, P. E., Revert, F., Saus, J., and Maines, M. D. (2010). Human biliverdin reductase suppresses Goodpasture antigenbinding protein (GPBP) kinase activity: the reductase regulates tumor necrosis factor-alphaNF-kappaB-dependent GPBP expression. J. Biol. Chem. 285, 12551-12558.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12551-12558
    • Miralem, T.1    Gibbs, P.E.2    Revert, F.3    Saus, J.4    Maines, M.D.5
  • 40
    • 20444445069 scopus 로고    scopus 로고
    • Small interference RNAmediated 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, M. D., Lelli, K. M., and Maines, M. D. (2005). Small interference RNAmediated 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) 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
  • 41
    • 18844427567 scopus 로고    scopus 로고
    • Upregulation of PKC-delta contributes to antiestrogen resistance in mammary tumor cells
    • Nabha, S. M., Glaros, S., Hong, M., Lykkesfeldt, A. E., Schiff, R., Osborne, K., and Reddy, K. B. (2005). Upregulation of PKC-delta contributes to antiestrogen resistance in mammary tumor cells. Oncogene 24, 3166-3176.
    • (2005) Oncogene , vol.24 , pp. 3166-3176
    • Nabha, S.M.1    Glaros, S.2    Hong, M.3    Lykkesfeldt, A.E.4    Schiff, R.5    Osborne, K.6    Reddy, K.B.7
  • 44
    • 3142723480 scopus 로고    scopus 로고
    • ERK1/2 associates with the c-Met-binding domain of growth factor receptor-bound protein 2 (Grb2)-associated binder-1 (Gab1): role in ERK1/2 and early growth response factor-1 (Egr-1) nuclear accumulation
    • Osawa, M., Itoh, S., Ohta, S., Huang, Q., Berk, B. C., Marmarosh, N. L., Che, W., Ding, B.,Yan, C., and Abe, J. (2004). ERK1/2 associates with the c-Met-binding domain of growth factor receptor-bound protein 2 (Grb2)-associated binder-1 (Gab1): role in ERK1/2 and early growth response factor-1 (Egr-1) nuclear accumulation. J. Biol. Chem. 279, 29691-29699.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29691-29699
    • Osawa, M.1    Itoh, S.2    Ohta, S.3    Huang, Q.4    Berk, B.C.5    Marmarosh, N.L.6    Che, W.7    Ding, B.8    Yan, C.9    Abe, J.10
  • 45
    • 35349023691 scopus 로고    scopus 로고
    • Heme-oxygenase1-induced protection against hypoxia/reoxygenation is dependent on biliverdin reductase and its interaction with PI3K/Akt pathway
    • Pachori, A. S., Smith, A., Mcdonald, P., Zhang, L., Dzau, V. J., and Melo, L. G. (2007). Heme-oxygenase1-induced protection against hypoxia/reoxygenation is dependent on biliverdin reductase and its interaction with PI3K/Akt pathway. J. Mol. Cell. Cardiol. 43, 580-592.
    • (2007) J. Mol. Cell. Cardiol. , vol.43 , pp. 580-592
    • Pachori, A.S.1    Smith, A.2    Mcdonald, P.3    Zhang, L.4    Dzau, V.J.5    Melo, L.G.6
  • 46
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Pawson, T., and Scott, J. D. (1997). Signaling through scaffold, anchoring, and adaptor proteins. Science 278, 2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Pawson, T.1    Scott, J.D.2
  • 47
    • 0026730649 scopus 로고
    • Exon/intron structure of the human alpha 3(IV) gene encompassing the Goodpasture antigen (alpha 3(IV)NC1). Identification of a potentially antigenic region at the triple helix/NC1 domain junction
    • Quinones, S., Bernal, D., GarciaSogo, M., Elena, S. F., and Saus, J. (1992). Exon/intron structure of the human alpha 3(IV) gene encompassing the Goodpasture antigen (alpha 3(IV)NC1). Identification of a potentially antigenic region at the triple helix/NC1 domain junction. J. Biol. Chem. 267, 19780-19784.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19780-19784
    • Quinones, S.1    Bernal, D.2    GarciaSogo, M.3    Elena, S.F.4    Saus, J.5
  • 48
    • 33744941875 scopus 로고    scopus 로고
    • The nuclear localization of ERK2 occurs by mechanisms both independent of and dependent on energy
    • Ranganathan, A., Yazicioglu, M. N., and Cobb, M. H. (2006). The nuclear localization of ERK2 occurs by mechanisms both independent of and dependent on energy. J. Biol. Chem. 281, 15645-15652.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15645-15652
    • Ranganathan, A.1    Yazicioglu, M.N.2    Cobb, M.H.3
  • 49
    • 0033617196 scopus 로고    scopus 로고
    • Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen
    • Raya, A., Revert, F., Navarro, S., and Saus, J. (1999). Characterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen. J. Biol. Chem. 274, 12642-12649.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12642-12649
    • Raya, A.1    Revert, F.2    Navarro, S.3    Saus, J.4
  • 51
    • 0028036338 scopus 로고
    • Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins
    • Ron, D., Chen, C. H., Caldwell, J., Jamieson, L., Orr, E., and Mochly Rosen, D. (1994). 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) 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
  • 52
    • 0035815611 scopus 로고    scopus 로고
    • Human biliverdin reductase is autophosphorylated, and phosphorylation is required for bilirubin formation
    • Salim, M., Brown-Kipphut, B. A., and Maines, M. D. (2001). Human biliverdin reductase is autophosphorylated, and phosphorylation is required for bilirubin formation. J. Biol. Chem. 276, 10929-10934.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10929-10934
    • Salim, M.1    Brown-Kipphut, B.A.2    Maines, M.D.3
  • 56
    • 0037051553 scopus 로고    scopus 로고
    • Dephosphorylation of PKC delta by protein phosphatase 2Ac and its inhibition by nucleotides
    • Srivastava, J., Goris, J., Dilworth, S. M., and Parker, P. J. (2002). Dephosphorylation of PKC delta by protein phosphatase 2Ac and its inhibition by nucleotides. FEBS Lett. 516, 265-269.
    • (2002) FEBS Lett , vol.516 , pp. 265-269
    • Srivastava, J.1    Goris, J.2    Dilworth, S.M.3    Parker, P.J.4
  • 57
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • Steinberg, S. F. (2008). Structural basis of protein kinase C isoform function. Physiol. Rev. 88, 1341-1378.
    • (2008) Physiol. Rev. , vol.88 , pp. 1341-1378
    • Steinberg, S.F.1
  • 58
    • 0028023002 scopus 로고
    • Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling
    • Tanti, J. F., Gremeaux, T., Van Obberghen, E., and Le Marchand Brustel, Y. (1994). Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling. J. Biol. Chem. 269, 6051-6057.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6051-6057
    • Tanti, J.F.1    Gremeaux, T.2    Van Obberghen, E.3    Le Marchand Brustel, Y.4
  • 59
    • 48249153856 scopus 로고    scopus 로고
    • Biliverdin reductase is a transporter of haem into the nucleus and is essential for regulation of HO-1 gene expression by haematin
    • Tudor, C., Lerner-Marmarosh, N., Engelborghs, Y., Gibbs, P. E., and Maines, M. D. (2008). Biliverdin reductase is a transporter of haem into the nucleus and is essential for regulation of HO-1 gene expression by haematin. Biochem. J. 413, 405-416.
    • (2008) Biochem. J. , vol.413 , pp. 405-416
    • Tudor, C.1    Lerner-Marmarosh, N.2    Engelborghs, Y.3    Gibbs, P.E.4    Maines, M.D.5
  • 62
    • 0036304792 scopus 로고    scopus 로고
    • Crystal structure of a biliverdin IX alpha reductase enzyme-cofactor complex
    • Whitby, F. G., Phillips, J. D., Hill, C. P., Mccoubrey, W., and Maines, M. D. (2002). Crystal structure of a biliverdin IX alpha reductase enzyme-cofactor complex. J. Mol. Biol. 319, 1199-1210.
    • (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
  • 65
    • 0038237433 scopus 로고    scopus 로고
    • Protein kinase C delta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9
    • Yoshida, K., Wang, H. G., Miki, Y., and Kufe, D. (2003). Protein kinase C delta is responsible for constitutive and DNA damage-induced phosphorylation of Rad9. EMBO J. 22, 1431-1441.
    • (2003) EMBO J , vol.22 , pp. 1431-1441
    • Yoshida, K.1    Wang, H.G.2    Miki, Y.3    Kufe, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.