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Volumn 55, Issue 37, 2016, Pages 5204-5217

A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A Partner and Regulator of Ferrochelatase

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CELL CULTURE; CELLS; CYTOLOGY; MASS SPECTROMETRY; PURIFICATION;

EID: 84988591400     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.6b00756     Document Type: Article
Times cited : (90)

References (110)
  • 1
    • 40049109300 scopus 로고    scopus 로고
    • Nuclear hormone receptors for heme: REV-ERBalpha and REV-ERBbeta are ligand-regulated components of the mammalian clock
    • Burris, T. P. (2008) Nuclear hormone receptors for heme: REV-ERBalpha and REV-ERBbeta are ligand-regulated components of the mammalian clock Mol. Endocrinol. 22, 1509-1520 10.1210/me.2007-0519
    • (2008) Mol. Endocrinol. , vol.22 , pp. 1509-1520
    • Burris, T.P.1
  • 7
    • 0141963861 scopus 로고    scopus 로고
    • Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels
    • Tang, X. D., Xu, R., Reynolds, M. F., Garcia, M. L., Heinemann, S. H., and Hoshi, T. (2003) Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels Nature 425, 531-535 10.1038/nature02003
    • (2003) Nature , vol.425 , pp. 531-535
    • Tang, X.D.1    Xu, R.2    Reynolds, M.F.3    Garcia, M.L.4    Heinemann, S.H.5    Hoshi, T.6
  • 8
    • 84864297704 scopus 로고    scopus 로고
    • One ring to rule them all: Trafficking of heme and heme synthesis intermediates in the metazoans
    • Hamza, I. and Dailey, H. A. (2012) One ring to rule them all: trafficking of heme and heme synthesis intermediates in the metazoans Biochim. Biophys. Acta, Mol. Cell Res. 1823, 1617-1632 10.1016/j.bbamcr.2012.04.009
    • (2012) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1823 , pp. 1617-1632
    • Hamza, I.1    Dailey, H.A.2
  • 9
    • 0028574776 scopus 로고
    • Oxidative crosslinking of LDL protein induced by hemin: Involvement of tyrosines
    • Miller, Y. I. and Shaklai, N. (1994) Oxidative crosslinking of LDL protein induced by hemin: involvement of tyrosines Biochem. Mol. Biol. Int. 34, 1121-1129
    • (1994) Biochem. Mol. Biol. Int. , vol.34 , pp. 1121-1129
    • Miller, Y.I.1    Shaklai, N.2
  • 12
    • 0018409237 scopus 로고
    • Heme biosynthesis in Friend erythroleukemia cells: Control by ferrochelatase
    • Rutherford, T., Thompson, G. G., and Moore, M. R. (1979) Heme biosynthesis in Friend erythroleukemia cells: control by ferrochelatase Proc. Natl. Acad. Sci. U. S. A. 76, 833-836 10.1073/pnas.76.2.833
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 833-836
    • Rutherford, T.1    Thompson, G.G.2    Moore, M.R.3
  • 13
    • 0034671586 scopus 로고    scopus 로고
    • Multiple regulatory steps in erythroid heme biosynthesis
    • Woodard, S. I. and Dailey, H. A. (2000) Multiple regulatory steps in erythroid heme biosynthesis Arch. Biochem. Biophys. 384, 375-378 10.1006/abbi.2000.2069
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 375-378
    • Woodard, S.I.1    Dailey, H.A.2
  • 14
    • 77956552982 scopus 로고    scopus 로고
    • Regulation of Mammalian Heme Biosynthesis
    • (Warren, M. J. and Smith, A. G. Eds.), Landes Bioscience and Springer Science+Business Media, New York
    • Medlock, A. E. and Dailey, H. A. (2009) Regulation of Mammalian Heme Biosynthesis. In Tetrapyrroles: Birth, Life and Death (Warren, M. J. and Smith, A. G., Eds.) pp 116-127, Landes Bioscience and Springer Science+Business Media, New York.
    • (2009) Tetrapyrroles: Birth, Life and Death , pp. 116-127
    • Medlock, A.E.1    Dailey, H.A.2
  • 15
    • 0025811624 scopus 로고
    • Human erythroid 5-aminolevulinate synthase: Promoter analysis and identification of an iron-responsive element in the mRNA
    • Cox, T. C., Bawden, M. J., Martin, A., and May, B. K. (1991) Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA EMBO J. 10, 1891-1902
    • (1991) EMBO J. , vol.10 , pp. 1891-1902
    • Cox, T.C.1    Bawden, M.J.2    Martin, A.3    May, B.K.4
  • 16
    • 0028047783 scopus 로고
    • Human ferrochelatase is an iron-sulfur protein
    • Dailey, H. A., Finnegan, M. G., and Johnson, M. K. (1994) Human ferrochelatase is an iron-sulfur protein Biochemistry 33, 403-407 10.1021/bi00168a003
    • (1994) Biochemistry , vol.33 , pp. 403-407
    • Dailey, H.A.1    Finnegan, M.G.2    Johnson, M.K.3
  • 17
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA
    • Dandekar, T., Stripecke, R., Gray, N. K., Goossen, B., Constable, A., Johansson, H. E., and Hentze, M. W. (1991) Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA EMBO J. 10, 1903-1909
    • (1991) EMBO J. , vol.10 , pp. 1903-1909
    • Dandekar, T.1    Stripecke, R.2    Gray, N.K.3    Goossen, B.4    Constable, A.5    Johansson, H.E.6    Hentze, M.W.7
  • 19
    • 70349419513 scopus 로고    scopus 로고
    • Product release rather than chelation determines metal specificity for ferrochelatase
    • Medlock, A. E., Carter, M., Dailey, T. A., Dailey, H. A., and Lanzilotta, W. N. (2009) Product release rather than chelation determines metal specificity for ferrochelatase J. Mol. Biol. 393, 308-319 10.1016/j.jmb.2009.08.042
    • (2009) J. Mol. Biol. , vol.393 , pp. 308-319
    • Medlock, A.E.1    Carter, M.2    Dailey, T.A.3    Dailey, H.A.4    Lanzilotta, W.N.5
  • 20
    • 34848852657 scopus 로고    scopus 로고
    • A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase
    • Medlock, A. E., Dailey, T. A., Ross, T. A., Dailey, H. A., and Lanzilotta, W. N. (2007) A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase J. Mol. Biol. 373, 1006-1016 10.1016/j.jmb.2007.08.040
    • (2007) J. Mol. Biol. , vol.373 , pp. 1006-1016
    • Medlock, A.E.1    Dailey, T.A.2    Ross, T.A.3    Dailey, H.A.4    Lanzilotta, W.N.5
  • 22
    • 34447333925 scopus 로고    scopus 로고
    • Direct measurement of metal ion chelation in the active site of human ferrochelatase
    • Hoggins, M., Dailey, H. A., Hunter, C. N., and Reid, J. D. (2007) Direct measurement of metal ion chelation in the active site of human ferrochelatase Biochemistry 46, 8121-8127 10.1021/bi602418e
    • (2007) Biochemistry , vol.46 , pp. 8121-8127
    • Hoggins, M.1    Dailey, H.A.2    Hunter, C.N.3    Reid, J.D.4
  • 23
    • 29244482593 scopus 로고    scopus 로고
    • Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p
    • Ghosh, K., Thompson, A. M., Goldbeck, R. A., Shi, X., Whitman, S., Oh, E., Zhiwu, Z., Vulpe, C., and Holman, T. R. (2005) Spectroscopic and biochemical characterization of heme binding to yeast Dap1p and mouse PGRMC1p Biochemistry 44, 16729-16736 10.1021/bi0511585
    • (2005) Biochemistry , vol.44 , pp. 16729-16736
    • Ghosh, K.1    Thompson, A.M.2    Goldbeck, R.A.3    Shi, X.4    Whitman, S.5    Oh, E.6    Zhiwu, Z.7    Vulpe, C.8    Holman, T.R.9
  • 24
    • 84923927415 scopus 로고    scopus 로고
    • Spectroscopic and mutagenesis studies of human PGRMC1
    • Kaluka, D., Batabyal, D., Chiang, B. Y., Poulos, T. L., and Yeh, S. R. (2015) Spectroscopic and mutagenesis studies of human PGRMC1 Biochemistry 54, 1638-1647 10.1021/bi501177e
    • (2015) Biochemistry , vol.54 , pp. 1638-1647
    • Kaluka, D.1    Batabyal, D.2    Chiang, B.Y.3    Poulos, T.L.4    Yeh, S.R.5
  • 25
    • 84874823951 scopus 로고    scopus 로고
    • Functions of MAPR (membrane-associated progesterone receptor) family members as heme/steroid-binding proteins
    • Kimura, I., Nakayama, Y., Konishi, M., Terasawa, K., Ohta, M., Itoh, N., and Fujimoto, M. (2012) Functions of MAPR (membrane-associated progesterone receptor) family members as heme/steroid-binding proteins Curr. Protein Pept. Sci. 13, 687-696 10.2174/138920312804142110
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 687-696
    • Kimura, I.1    Nakayama, Y.2    Konishi, M.3    Terasawa, K.4    Ohta, M.5    Itoh, N.6    Fujimoto, M.7
  • 27
    • 14044276944 scopus 로고    scopus 로고
    • Neudesin, a novel secreted protein with a unique primary structure and neurotrophic activity
    • Kimura, I., Yoshioka, M., Konishi, M., Miyake, A., and Itoh, N. (2005) Neudesin, a novel secreted protein with a unique primary structure and neurotrophic activity J. Neurosci. Res. 79, 287-294 10.1002/jnr.20356
    • (2005) J. Neurosci. Res. , vol.79 , pp. 287-294
    • Kimura, I.1    Yoshioka, M.2    Konishi, M.3    Miyake, A.4    Itoh, N.5
  • 28
    • 80054739593 scopus 로고    scopus 로고
    • Progesterone receptor membrane component 1 modulates human cytochrome p450 activities in an isoform-dependent manner
    • Oda, S., Nakajima, M., Toyoda, Y., Fukami, T., and Yokoi, T. (2011) Progesterone receptor membrane component 1 modulates human cytochrome p450 activities in an isoform-dependent manner Drug Metab. Dispos. 39, 2057-2065 10.1124/dmd.111.040907
    • (2011) Drug Metab. Dispos. , vol.39 , pp. 2057-2065
    • Oda, S.1    Nakajima, M.2    Toyoda, Y.3    Fukami, T.4    Yokoi, T.5
  • 29
    • 79951960870 scopus 로고    scopus 로고
    • Progesterone receptor membrane component 1 inhibits the activity of drug-metabolizing cytochromes P450 and binds to cytochrome P450 reductase
    • Szczesna-Skorupa, E. and Kemper, B. (2011) Progesterone receptor membrane component 1 inhibits the activity of drug-metabolizing cytochromes P450 and binds to cytochrome P450 reductase Mol. Pharmacol. 79, 340-350 10.1124/mol.110.068478
    • (2011) Mol. Pharmacol. , vol.79 , pp. 340-350
    • Szczesna-Skorupa, E.1    Kemper, B.2
  • 31
    • 14044252188 scopus 로고    scopus 로고
    • Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae
    • Mallory, J. C., Crudden, G., Johnson, B. L., Mo, C., Pierson, C. A., Bard, M., and Craven, R. J. (2005) Dap1p, a heme-binding protein that regulates the cytochrome P450 protein Erg11p/Cyp51p in Saccharomyces cerevisiae Mol. Cell. Biol. 25, 1669-1679 10.1128/MCB.25.5.1669-1679.2005
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1669-1679
    • Mallory, J.C.1    Crudden, G.2    Johnson, B.L.3    Mo, C.4    Pierson, C.A.5    Bard, M.6    Craven, R.J.7
  • 32
    • 84885646346 scopus 로고    scopus 로고
    • Progesterone receptor membrane component 1/Sigma-2 receptor associates with MAP1LC3B and promotes autophagy
    • Mir, S. U., Schwarze, S. R., Jin, L., Zhang, J., Friend, W., Miriyala, S., St Clair, D., and Craven, R. J. (2013) Progesterone receptor membrane component 1/Sigma-2 receptor associates with MAP1LC3B and promotes autophagy Autophagy 9, 1566-1578 10.4161/auto.25889
    • (2013) Autophagy , vol.9 , pp. 1566-1578
    • Mir, S.U.1    Schwarze, S.R.2    Jin, L.3    Zhang, J.4    Friend, W.5    Miriyala, S.6    St Clair, D.7    Craven, R.J.8
  • 33
    • 0038397236 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Dap1p, a novel DNA damage response protein related to the mammalian membrane-associated progesterone receptor
    • Hand, R. A., Jia, N., Bard, M., and Craven, R. J. (2003) Saccharomyces cerevisiae Dap1p, a novel DNA damage response protein related to the mammalian membrane-associated progesterone receptor Eukaryotic Cell 2, 306-317 10.1128/EC.2.2.306-317.2003
    • (2003) Eukaryotic Cell , vol.2 , pp. 306-317
    • Hand, R.A.1    Jia, N.2    Bard, M.3    Craven, R.J.4
  • 34
    • 77955295885 scopus 로고    scopus 로고
    • Pgrmc1 (progesterone receptor membrane component 1) associates with epidermal growth factor receptor and regulates erlotinib sensitivity
    • Ahmed, I. S., Rohe, H. J., Twist, K. E., and Craven, R. J. (2010) Pgrmc1 (progesterone receptor membrane component 1) associates with epidermal growth factor receptor and regulates erlotinib sensitivity J. Biol. Chem. 285, 24775-24782 10.1074/jbc.M110.134585
    • (2010) J. Biol. Chem. , vol.285 , pp. 24775-24782
    • Ahmed, I.S.1    Rohe, H.J.2    Twist, K.E.3    Craven, R.J.4
  • 35
    • 37549014195 scopus 로고    scopus 로고
    • Regulation of iron homeostasis mediated by the heme-binding protein Dap1 (damage resistance protein 1) via the P450 protein Erg11/Cyp51
    • Craven, R. J., Mallory, J. C., and Hand, R. A. (2007) Regulation of iron homeostasis mediated by the heme-binding protein Dap1 (damage resistance protein 1) via the P450 protein Erg11/Cyp51 J. Biol. Chem. 282, 36543-36551 10.1074/jbc.M706770200
    • (2007) J. Biol. Chem. , vol.282 , pp. 36543-36551
    • Craven, R.J.1    Mallory, J.C.2    Hand, R.A.3
  • 38
    • 37249017475 scopus 로고    scopus 로고
    • Measurement of the heme affinity for yeast dap1p, and its importance in cellular function
    • Thompson, A. M., Reddi, A. R., Shi, X., Goldbeck, R. A., Moenne-Loccoz, P., Gibney, B. R., and Holman, T. R. (2007) Measurement of the heme affinity for yeast dap1p, and its importance in cellular function Biochemistry 46, 14629-14637 10.1021/bi7013739
    • (2007) Biochemistry , vol.46 , pp. 14629-14637
    • Thompson, A.M.1    Reddi, A.R.2    Shi, X.3    Goldbeck, R.A.4    Moenne-Loccoz, P.5    Gibney, B.R.6    Holman, T.R.7
  • 39
    • 0038313119 scopus 로고    scopus 로고
    • Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain
    • Mifsud, W. and Bateman, A. (2002) Membrane-bound progesterone receptors contain a cytochrome b5-like ligand-binding domain Genome Biol. 3, research0068.1 10.1186/gb-2002-3-12-research0068
    • (2002) Genome Biol. , vol.3
    • Mifsud, W.1    Bateman, A.2
  • 40
    • 0015462595 scopus 로고
    • The structure of cytochrome b 5 at 2.0 Angstrom resolution
    • Mathews, F. S., Argos, P., and Levine, M. (1972) The structure of cytochrome b 5 at 2.0 Angstrom resolution Cold Spring Harbor Symp. Quant. Biol. 36, 387-395 10.1101/SQB.1972.036.01.050
    • (1972) Cold Spring Harbor Symp. Quant. Biol. , vol.36 , pp. 387-395
    • Mathews, F.S.1    Argos, P.2    Levine, M.3
  • 41
    • 0015505465 scopus 로고
    • Three-dimensional Fourier synthesis of calf liver cytochrome b 5 at 2-8 A resolution
    • Mathews, F. S., Levine, M., and Argos, P. (1972) Three-dimensional Fourier synthesis of calf liver cytochrome b 5 at 2-8 A resolution J. Mol. Biol. 64, 449-464 10.1016/0022-2836(72)90510-4
    • (1972) J. Mol. Biol. , vol.64 , pp. 449-464
    • Mathews, F.S.1    Levine, M.2    Argos, P.3
  • 43
    • 25444442560 scopus 로고    scopus 로고
    • Characterization of the periplasmic heme-binding protein shut from the heme uptake system of Shigella dysenteriae
    • Eakanunkul, S., Lukat-Rodgers, G. S., Sumithran, S., Ghosh, A., Rodgers, K. R., Dawson, J. H., and Wilks, A. (2005) Characterization of the periplasmic heme-binding protein shut from the heme uptake system of Shigella dysenteriae Biochemistry 44, 13179-13191 10.1021/bi050422r
    • (2005) Biochemistry , vol.44 , pp. 13179-13191
    • Eakanunkul, S.1    Lukat-Rodgers, G.S.2    Sumithran, S.3    Ghosh, A.4    Rodgers, K.R.5    Dawson, J.H.6    Wilks, A.7
  • 44
    • 34547422800 scopus 로고    scopus 로고
    • Cloning and characterization of a novel periplasmic heme-transport protein from the human pathogen Pseudomonas aeruginosa
    • Tong, Y. and Guo, M. (2007) Cloning and characterization of a novel periplasmic heme-transport protein from the human pathogen Pseudomonas aeruginosa JBIC, J. Biol. Inorg. Chem. 12, 735-750 10.1007/s00775-007-0226-x
    • (2007) JBIC, J. Biol. Inorg. Chem. , vol.12 , pp. 735-750
    • Tong, Y.1    Guo, M.2
  • 47
    • 42149149334 scopus 로고    scopus 로고
    • Identification of ZBP-89 as a novel GATA-1-associated transcription factor involved in megakaryocytic and erythroid development
    • Woo, A. J., Moran, T. B., Schindler, Y. L., Choe, S. K., Langer, N. B., Sullivan, M. R., Fujiwara, Y., Paw, B. H., and Cantor, A. B. (2008) Identification of ZBP-89 as a novel GATA-1-associated transcription factor involved in megakaryocytic and erythroid development Mol. Cell. Biol. 28, 2675-2689 10.1128/MCB.01945-07
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2675-2689
    • Woo, A.J.1    Moran, T.B.2    Schindler, Y.L.3    Choe, S.K.4    Langer, N.B.5    Sullivan, M.R.6    Fujiwara, Y.7    Paw, B.H.8    Cantor, A.B.9
  • 48
    • 0017157390 scopus 로고
    • Erythroid cell differentiation: Murine erythroleukemia cell variant with unique pattern of induction by polar compounds
    • Ohta, Y., Tanaka, M., Terada, M., Miller, O. J., Bank, A., Marks, P., and Rifkind, R. A. (1976) Erythroid cell differentiation: murine erythroleukemia cell variant with unique pattern of induction by polar compounds Proc. Natl. Acad. Sci. U. S. A. 73, 1232-1236 10.1073/pnas.73.4.1232
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 1232-1236
    • Ohta, Y.1    Tanaka, M.2    Terada, M.3    Miller, O.J.4    Bank, A.5    Marks, P.6    Rifkind, R.A.7
  • 49
  • 50
    • 0018612930 scopus 로고
    • Properties and usefulness of the original K-562 human myelogenous leukemia cell line
    • Lozzio, B. B. and Lozzio, C. B. (1979) Properties and usefulness of the original K-562 human myelogenous leukemia cell line Leuk. Res. 3, 363-370 10.1016/0145-2126(79)90033-X
    • (1979) Leuk. Res. , vol.3 , pp. 363-370
    • Lozzio, B.B.1    Lozzio, C.B.2
  • 51
    • 0016640079 scopus 로고
    • Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome
    • Lozzio, C. B. and Lozzio, B. B. (1975) Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome Blood 45, 321-334
    • (1975) Blood , vol.45 , pp. 321-334
    • Lozzio, C.B.1    Lozzio, B.B.2
  • 52
    • 0025896880 scopus 로고
    • Multiple mechanisms for the regulation of haem synthesis during erythroid cell differentiation. Possible role for coproporphyrinogen oxidase
    • Conder, L. H., Woodard, S. I., and Dailey, H. A. (1991) Multiple mechanisms for the regulation of haem synthesis during erythroid cell differentiation. Possible role for coproporphyrinogen oxidase Biochem. J. 275 (Part 2) 321-326 10.1042/bj2750321
    • (1991) Biochem. J. , vol.275 , Issue.PART 2 , pp. 321-326
    • Conder, L.H.1    Woodard, S.I.2    Dailey, H.A.3
  • 53
    • 0018395453 scopus 로고
    • Induction of erythroid differentiation in the human leukaemia cell line K562
    • Andersson, L. C., Jokinen, M., and Gahmberg, C. G. (1979) Induction of erythroid differentiation in the human leukaemia cell line K562 Nature 278, 364-365 10.1038/278364a0
    • (1979) Nature , vol.278 , pp. 364-365
    • Andersson, L.C.1    Jokinen, M.2    Gahmberg, C.G.3
  • 54
    • 0034176006 scopus 로고    scopus 로고
    • Butyrate-induced erythroid differentiation of human K562 leukemia cells involves inhibition of ERK and activation of p38 MAP kinase pathways
    • Witt, O., Sand, K., and Pekrun, A. (2000) Butyrate-induced erythroid differentiation of human K562 leukemia cells involves inhibition of ERK and activation of p38 MAP kinase pathways Blood 95, 2391-2396
    • (2000) Blood , vol.95 , pp. 2391-2396
    • Witt, O.1    Sand, K.2    Pekrun, A.3
  • 56
    • 77951084376 scopus 로고    scopus 로고
    • Progesterone receptor membrane component 1 (Pgrmc1): A heme-1 domain protein that promotes tumorigenesis and is inhibited by a small molecule
    • Ahmed, I. S., Rohe, H. J., Twist, K. E., Mattingly, M. N., and Craven, R. J. (2010) Progesterone receptor membrane component 1 (Pgrmc1): a heme-1 domain protein that promotes tumorigenesis and is inhibited by a small molecule J. Pharmacol. Exp. Ther. 333, 564-573 10.1124/jpet.109.164210
    • (2010) J. Pharmacol. Exp. Ther. , vol.333 , pp. 564-573
    • Ahmed, I.S.1    Rohe, H.J.2    Twist, K.E.3    Mattingly, M.N.4    Craven, R.J.5
  • 57
    • 17844374364 scopus 로고    scopus 로고
    • A structure-based strategy for discovery of small ligands binding to functionally unknown proteins: Combination of in silico screening and surface plasmon resonance measurements
    • Yoshitani, N., Satou, K., Saito, K., Suzuki, S., Hatanaka, H., Seki, M., Shinozaki, K., Hirota, H., and Yokoyama, S. (2005) A structure-based strategy for discovery of small ligands binding to functionally unknown proteins: combination of in silico screening and surface plasmon resonance measurements Proteomics 5, 1472-1480 10.1002/pmic.200401032
    • (2005) Proteomics , vol.5 , pp. 1472-1480
    • Yoshitani, N.1    Satou, K.2    Saito, K.3    Suzuki, S.4    Hatanaka, H.5    Seki, M.6    Shinozaki, K.7    Hirota, H.8    Yokoyama, S.9
  • 61
    • 35448950792 scopus 로고    scopus 로고
    • Regulated expression of microRNAs in normal and polycythemia vera erythropoiesis
    • Bruchova, H., Yoon, D., Agarwal, A. M., Mendell, J., and Prchal, J. T. (2007) Regulated expression of microRNAs in normal and polycythemia vera erythropoiesis Exp. Hematol. 35, 1657-1667 10.1016/j.exphem.2007.08.021
    • (2007) Exp. Hematol. , vol.35 , pp. 1657-1667
    • Bruchova, H.1    Yoon, D.2    Agarwal, A.M.3    Mendell, J.4    Prchal, J.T.5
  • 62
    • 84982221024 scopus 로고    scopus 로고
    • Rapid and sensitive quantitation of heme in hemoglobinized cells
    • Marcero, J. R., Piel Iii, R. B., Burch, J. S., and Dailey, H. A. (2016) Rapid and sensitive quantitation of heme in hemoglobinized cells BioTechniques 61, 83-91 10.2144/000114444
    • (2016) BioTechniques , vol.61 , pp. 83-91
    • Marcero, J.R.1    Piel, R.B.2    Burch, J.S.3    Dailey, H.A.4
  • 63
    • 0032322648 scopus 로고    scopus 로고
    • Mitochondrial ABC transporters
    • Leighton, J. (1998) Mitochondrial ABC transporters Methods Enzymol. 292, 776-787 10.1016/S0076-6879(98)92059-6
    • (1998) Methods Enzymol. , vol.292 , pp. 776-787
    • Leighton, J.1
  • 64
    • 0034213588 scopus 로고    scopus 로고
    • ABC-me: A novel mitochondrial transporter induced by GATA-1 during erythroid differentiation
    • Shirihai, O. S., Gregory, T., Yu, C., Orkin, S. H., and Weiss, M. J. (2000) ABC-me: a novel mitochondrial transporter induced by GATA-1 during erythroid differentiation EMBO J. 19, 2492-2502 10.1093/emboj/19.11.2492
    • (2000) EMBO J. , vol.19 , pp. 2492-2502
    • Shirihai, O.S.1    Gregory, T.2    Yu, C.3    Orkin, S.H.4    Weiss, M.J.5
  • 66
    • 84883481556 scopus 로고    scopus 로고
    • The Protein Model Portal - A comprehensive resource for protein structure and model information
    • Haas, J., Roth, S., Arnold, K., Kiefer, F., Schmidt, T., Bordoli, L., and Schwede, T. (2013) The Protein Model Portal - a comprehensive resource for protein structure and model information Database 2013, bat031 10.1093/database/bat031
    • (2013) Database , vol.2013 , pp. bat031
    • Haas, J.1    Roth, S.2    Arnold, K.3    Kiefer, F.4    Schmidt, T.5    Bordoli, L.6    Schwede, T.7
  • 67
    • 84864448769 scopus 로고    scopus 로고
    • Template-based protein structure modeling using the RaptorX web server
    • Kallberg, M., Wang, H., Wang, S., Peng, J., Wang, Z., Lu, H., and Xu, J. (2012) Template-based protein structure modeling using the RaptorX web server Nat. Protoc. 7, 1511-1522 10.1038/nprot.2012.085
    • (2012) Nat. Protoc. , vol.7 , pp. 1511-1522
    • Kallberg, M.1    Wang, H.2    Wang, S.3    Peng, J.4    Wang, Z.5    Lu, H.6    Xu, J.7
  • 68
    • 84979859950 scopus 로고    scopus 로고
    • IntFOLD: An integrated server for modelling protein structures and functions from amino acid sequences
    • McGuffin, L. J., Atkins, J. D., Salehe, B. R., Shuid, A. N., and Roche, D. B. (2015) IntFOLD: an integrated server for modelling protein structures and functions from amino acid sequences Nucleic Acids Res. 43, W169-173 10.1093/nar/gkv236
    • (2015) Nucleic Acids Res. , vol.43 , pp. W169-W173
    • McGuffin, L.J.1    Atkins, J.D.2    Salehe, B.R.3    Shuid, A.N.4    Roche, D.B.5
  • 69
    • 79959564695 scopus 로고    scopus 로고
    • The IntFOLD server: An integrated web resource for protein fold recognition, 3D model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction
    • Roche, D. B., Buenavista, M. T., Tetchner, S. J., and McGuffin, L. J. (2011) The IntFOLD server: an integrated web resource for protein fold recognition, 3D model quality assessment, intrinsic disorder prediction, domain prediction and ligand binding site prediction Nucleic Acids Res. 39, W171-176 10.1093/nar/gkr184
    • (2011) Nucleic Acids Res. , vol.39 , pp. W171-W176
    • Roche, D.B.1    Buenavista, M.T.2    Tetchner, S.J.3    McGuffin, L.J.4
  • 70
    • 84930074657 scopus 로고    scopus 로고
    • The Phyre2 web portal for protein modeling, prediction and analysis
    • Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N., and Sternberg, M. J. (2015) The Phyre2 web portal for protein modeling, prediction and analysis Nat. Protoc. 10, 845-858 10.1038/nprot.2015.053
    • (2015) Nat. Protoc. , vol.10 , pp. 845-858
    • Kelley, L.A.1    Mezulis, S.2    Yates, C.M.3    Wass, M.N.4    Sternberg, M.J.5
  • 71
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER: a unified platform for automated protein structure and function prediction Nat. Protoc. 5, 725-738 10.1038/nprot.2010.5
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 72
    • 84925156346 scopus 로고    scopus 로고
    • The I-TASSER Suite: Protein structure and function prediction
    • Yang, J., Yan, R., Roy, A., Xu, D., Poisson, J., and Zhang, Y. (2014) The I-TASSER Suite: protein structure and function prediction Nat. Methods 12, 7-8 10.1038/nmeth.3213
    • (2014) Nat. Methods , vol.12 , pp. 7-8
    • Yang, J.1    Yan, R.2    Roy, A.3    Xu, D.4    Poisson, J.5    Zhang, Y.6
  • 73
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. (2008) I-TASSER server for protein 3D structure prediction BMC Bioinf. 9, 40 10.1186/1471-2105-9-40
    • (2008) BMC Bioinf. , vol.9 , pp. 40
    • Zhang, Y.1
  • 74
    • 84979850726 scopus 로고    scopus 로고
    • I-TASSER server: New development for protein structure and function predictions
    • Yang, J. and Zhang, Y. (2015) I-TASSER server: new development for protein structure and function predictions Nucleic Acids Res. 43, W174-181 10.1093/nar/gkv342
    • (2015) Nucleic Acids Res. , vol.43 , pp. W174-W181
    • Yang, J.1    Zhang, Y.2
  • 75
    • 84965109856 scopus 로고    scopus 로고
    • version 1.2r2, Schrodinger, LLC, Portland, OR
    • The PyMOL Molecular Graphics System, version 1.2r2 (2015) Schrodinger, LLC, Portland, OR.
    • (2015) The PyMOL Molecular Graphics System
  • 76
    • 0021100163 scopus 로고
    • Bovine ferrochelatase. Kinetic analysis of inhibition by N-methylprotoporphyrin, manganese, and heme
    • Dailey, H. A. and Fleming, J. E. (1983) Bovine ferrochelatase. Kinetic analysis of inhibition by N-methylprotoporphyrin, manganese, and heme J. Biol. Chem. 258, 11453-11459
    • (1983) J. Biol. Chem. , vol.258 , pp. 11453-11459
    • Dailey, H.A.1    Fleming, J.E.2
  • 77
    • 23044452883 scopus 로고    scopus 로고
    • Production and characterization of erythropoietic protoporphyric heterodimeric ferrochelatases
    • Najahi-Missaoui, W. and Dailey, H. A. (2005) Production and characterization of erythropoietic protoporphyric heterodimeric ferrochelatases Blood 106, 1098-1104 10.1182/blood-2004-12-4661
    • (2005) Blood , vol.106 , pp. 1098-1104
    • Najahi-Missaoui, W.1    Dailey, H.A.2
  • 78
    • 0030946074 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition
    • Izadi, N., Henry, Y., Haladjian, J., Goldberg, M. E., Wandersman, C., Delepierre, M., and Lecroisey, A. (1997) Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition Biochemistry 36, 7050-7057 10.1021/bi962577s
    • (1997) Biochemistry , vol.36 , pp. 7050-7057
    • Izadi, N.1    Henry, Y.2    Haladjian, J.3    Goldberg, M.E.4    Wandersman, C.5    Delepierre, M.6    Lecroisey, A.7
  • 79
    • 0021328935 scopus 로고
    • Specific indication of hemoproteins in polyacrylamide gels using a double-staining process
    • Francis, R. T., Jr. and Becker, R. R. (1984) Specific indication of hemoproteins in polyacrylamide gels using a double-staining process Anal. Biochem. 136, 509-514 10.1016/0003-2697(84)90253-7
    • (1984) Anal. Biochem. , vol.136 , pp. 509-514
    • Francis, R.T.1    Becker, R.R.2
  • 80
    • 0032830130 scopus 로고    scopus 로고
    • The transferrin receptor: Role in health and disease
    • Ponka, P. and Lok, C. N. (1999) The transferrin receptor: role in health and disease Int. J. Biochem. Cell Biol. 31, 1111-1137 10.1016/S1357-2725(99)00070-9
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 1111-1137
    • Ponka, P.1    Lok, C.N.2
  • 81
    • 84942450672 scopus 로고    scopus 로고
    • Further Elucidation of the Mechanism of Iron Transport Form Plasma Transferrin to Mitochondrial Ferrochelatase: Further Evidence for the, ÄúKiss and Run,Äù Hypothesis
    • Hamdi, A., Roshan, T., Sheftel, A., and Ponka, P. (2014) Further Elucidation of the Mechanism of Iron Transport Form Plasma Transferrin to Mitochondrial Ferrochelatase: Further Evidence for the, ÄúKiss and Run,Äù Hypothesis Blood 124, 4023-4023
    • (2014) Blood , vol.124 , pp. 4023
    • Hamdi, A.1    Roshan, T.2    Sheftel, A.3    Ponka, P.4
  • 85
    • 52449090487 scopus 로고    scopus 로고
    • Adenine nucleotide translocator transports haem precursors into mitochondria
    • Azuma, M., Kabe, Y., Kuramori, C., Kondo, M., Yamaguchi, Y., and Handa, H. (2008) Adenine nucleotide translocator transports haem precursors into mitochondria PLoS One 3, e3070 10.1371/journal.pone.0003070
    • (2008) PLoS One , vol.3 , pp. e3070
    • Azuma, M.1    Kabe, Y.2    Kuramori, C.3    Kondo, M.4    Yamaguchi, Y.5    Handa, H.6
  • 88
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., and Lenaers, G. (2003) Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis J. Biol. Chem. 278, 7743-7746 10.1074/jbc.C200677200
    • (2003) J. Biol. Chem. , vol.278 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6    Lenaers, G.7
  • 89
    • 84877966571 scopus 로고    scopus 로고
    • APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria
    • Weber, T. A., Koob, S., Heide, H., Wittig, I., Head, B., van der Bliek, A., Brandt, U., Mittelbronn, M., and Reichert, A. S. (2013) APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria PLoS One 8, e63683 10.1371/journal.pone.0063683
    • (2013) PLoS One , vol.8 , pp. e63683
    • Weber, T.A.1    Koob, S.2    Heide, H.3    Wittig, I.4    Head, B.5    Van Der Bliek, A.6    Brandt, U.7    Mittelbronn, M.8    Reichert, A.S.9
  • 91
    • 84878472256 scopus 로고    scopus 로고
    • Stat and interferon genes identified by network analysis differentially regulate primitive and definitive erythropoiesis
    • Greenfest-Allen, E., Malik, J., Palis, J., and Stoeckert, C. J., Jr. (2013) Stat and interferon genes identified by network analysis differentially regulate primitive and definitive erythropoiesis BMC Syst. Biol. 7, 38 10.1186/1752-0509-7-38
    • (2013) BMC Syst. Biol. , vol.7 , pp. 38
    • Greenfest-Allen, E.1    Malik, J.2    Palis, J.3    Stoeckert, C.J.4
  • 93
    • 0022425318 scopus 로고
    • Orientation of ferrochelatase in bovine liver mitochondria
    • Harbin, B. M. and Dailey, H. A. (1985) Orientation of ferrochelatase in bovine liver mitochondria Biochemistry 24, 366-370 10.1021/bi00323a019
    • (1985) Biochemistry , vol.24 , pp. 366-370
    • Harbin, B.M.1    Dailey, H.A.2
  • 94
    • 0014545574 scopus 로고
    • The structural organization of haem synthesis in rat liver mitochondria
    • Jones, M. S. and Jones, O. T. (1969) The structural organization of haem synthesis in rat liver mitochondria Biochem. J. 113, 507-514 10.1042/bj1130507
    • (1969) Biochem. J. , vol.113 , pp. 507-514
    • Jones, M.S.1    Jones, O.T.2
  • 95
    • 0023677784 scopus 로고
    • The synthesis of murine ferrochelatase in vitro and in vivo
    • Karr, S. R. and Dailey, H. A. (1988) The synthesis of murine ferrochelatase in vitro and in vivo Biochem. J. 254, 799-803 10.1042/bj2540799
    • (1988) Biochem. J. , vol.254 , pp. 799-803
    • Karr, S.R.1    Dailey, H.A.2
  • 97
    • 15244348605 scopus 로고    scopus 로고
    • Hypothetical protein At2g24940.1 from Arabidopsis thaliana has a cytochrome b5 like fold
    • Song, J., Vinarov, D., Tyler, E. M., Shahan, M. N., Tyler, R. C., and Markley, J. L. (2004) Hypothetical protein At2g24940.1 from Arabidopsis thaliana has a cytochrome b5 like fold J. Biomol. NMR 30, 215-218 10.1023/B:JNMR.0000048943.34504.29
    • (2004) J. Biomol. NMR , vol.30 , pp. 215-218
    • Song, J.1    Vinarov, D.2    Tyler, E.M.3    Shahan, M.N.4    Tyler, R.C.5    Markley, J.L.6
  • 99
    • 0027377723 scopus 로고
    • Biphasic ordered induction of heme synthesis in differentiating murine erythroleukemia cells: Role of erythroid 5-aminolevulinate synthase
    • Lake-Bullock, H. and Dailey, H. A. (1993) Biphasic ordered induction of heme synthesis in differentiating murine erythroleukemia cells: role of erythroid 5-aminolevulinate synthase Mol. Cell. Biol. 13, 7122-7132 10.1128/MCB.13.11.7122
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7122-7132
    • Lake-Bullock, H.1    Dailey, H.A.2
  • 100
    • 79952278488 scopus 로고    scopus 로고
    • Measurement of uroporphyrinogen decarboxylase activity
    • Chapter 8, Unit 8, 4, Wiley, New York
    • Phillips, J. D. and Kushner, J. P. (2001) Measurement of uroporphyrinogen decarboxylase activity. Current Protocols in Toxicology, Chapter 8, Unit 8, 4, Wiley, New York.
    • (2001) Current Protocols in Toxicology
    • Phillips, J.D.1    Kushner, J.P.2
  • 101
    • 0037407929 scopus 로고    scopus 로고
    • The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase
    • Wu, C. K., Dailey, T. A., Dailey, H. A., Wang, B. C., and Rose, J. P. (2003) The crystal structure of augmenter of liver regeneration: A mammalian FAD-dependent sulfhydryl oxidase Protein Sci. 12, 1109-1118 10.1110/ps.0238103
    • (2003) Protein Sci. , vol.12 , pp. 1109-1118
    • Wu, C.K.1    Dailey, T.A.2    Dailey, H.A.3    Wang, B.C.4    Rose, J.P.5
  • 102
    • 84876678901 scopus 로고    scopus 로고
    • PGRMC2, a yet uncharacterized protein with potential as tumor suppressor, migration inhibitor, and regulator of cytochrome P450 enzyme activity
    • Wendler, A. and Wehling, M. (2013) PGRMC2, a yet uncharacterized protein with potential as tumor suppressor, migration inhibitor, and regulator of cytochrome P450 enzyme activity Steroids 78, 555-558 10.1016/j.steroids.2012.12.002
    • (2013) Steroids , vol.78 , pp. 555-558
    • Wendler, A.1    Wehling, M.2
  • 103
    • 84930509896 scopus 로고    scopus 로고
    • Progesterone receptor membrane component-1 (PGRMC1) and PGRMC-2 interact to suppress entry into the cell cycle in spontaneously immortalized rat granulosa cells
    • Peluso, J. J., Griffin, D., Liu, X., and Horne, M. (2014) Progesterone receptor membrane component-1 (PGRMC1) and PGRMC-2 interact to suppress entry into the cell cycle in spontaneously immortalized rat granulosa cells Biol. Reprod. 91, 104 10.1095/biolreprod.114.122986
    • (2014) Biol. Reprod. , vol.91 , pp. 104
    • Peluso, J.J.1    Griffin, D.2    Liu, X.3    Horne, M.4
  • 105
    • 84876720152 scopus 로고    scopus 로고
    • The hemophore HasA from Yersinia pestis (HasAyp) coordinates hemin with a single residue, Tyr75, and with minimal conformational change
    • Kumar, R., Lovell, S., Matsumura, H., Battaile, K. P., Moenne-Loccoz, P., and Rivera, M. (2013) The hemophore HasA from Yersinia pestis (HasAyp) coordinates hemin with a single residue, Tyr75, and with minimal conformational change Biochemistry 52, 2705-2707 10.1021/bi400280z
    • (2013) Biochemistry , vol.52 , pp. 2705-2707
    • Kumar, R.1    Lovell, S.2    Matsumura, H.3    Battaile, K.P.4    Moenne-Loccoz, P.5    Rivera, M.6
  • 106
    • 34547668765 scopus 로고    scopus 로고
    • Progesterone receptor membrane component 1: An integrative review
    • Cahill, M. A. (2007) Progesterone receptor membrane component 1: an integrative review J. Steroid Biochem. Mol. Biol. 105, 16-36 10.1016/j.jsbmb.2007.02.002
    • (2007) J. Steroid Biochem. Mol. Biol. , vol.105 , pp. 16-36
    • Cahill, M.A.1
  • 107
    • 84928716915 scopus 로고    scopus 로고
    • Pathways driving the endocytosis of mutant and wild-type EGFR in cancer
    • Hampton, K. K. and Craven, R. J. (2014) Pathways driving the endocytosis of mutant and wild-type EGFR in cancer Oncoscience 1, 504-512 10.18632/oncoscience.67
    • (2014) Oncoscience , vol.1 , pp. 504-512
    • Hampton, K.K.1    Craven, R.J.2
  • 108
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: Examination of the intermediates involved in iron metabolism
    • Richardson, D. R., Ponka, P., and Vyoral, D. (1996) Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: examination of the intermediates involved in iron metabolism Blood 87, 3477-3488
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1    Ponka, P.2    Vyoral, D.3
  • 109
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • Sheftel, A. D., Zhang, A. S., Brown, C., Shirihai, O. S., and Ponka, P. (2007) Direct interorganellar transfer of iron from endosome to mitochondrion Blood 110, 125-132 10.1182/blood-2007-01-068148
    • (2007) Blood , vol.110 , pp. 125-132
    • Sheftel, A.D.1    Zhang, A.S.2    Brown, C.3    Shirihai, O.S.4    Ponka, P.5
  • 110
    • 11144226961 scopus 로고    scopus 로고
    • Intracellular kinetics of iron in reticulocytes: Evidence for endosome involvement in iron targeting to mitochondria
    • Zhang, A. S., Sheftel, A. D., and Ponka, P. (2005) Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria Blood 105, 368-375 10.1182/blood-2004-06-2226
    • (2005) Blood , vol.105 , pp. 368-375
    • Zhang, A.S.1    Sheftel, A.D.2    Ponka, P.3


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