메뉴 건너뛰기




Volumn 9, Issue , 2008, Pages

Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOGLUTARIC ACID; DIOXYGENASE; JUMONJI C DOMAIN CONTAINING 6 PROTEIN; OXIDOREDUCTASE; CELL SURFACE RECEPTOR; ISOPROTEIN; JMJD6 PROTEIN, HUMAN;

EID: 47249153638     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-9-293     Document Type: Article
Times cited : (40)

References (108)
  • 2
    • 0034212377 scopus 로고    scopus 로고
    • Evidence of domain swapping within the jumonji family of transcription factors
    • 10.1016/S0968-0004(00)01593-0 10838566
    • Balciunas D Ronne H Evidence of domain swapping within the jumonji family of transcription factors Trends Biochem Sci 2000, 25:274-276. 10.1016/S0968-0004(00)01593-0 10838566
    • (2000) Trends Biochem Sci , vol.25 , pp. 274-276
    • Balciunas, D.1    Ronne, H.2
  • 3
    • 0035150397 scopus 로고    scopus 로고
    • JmjC: Cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta
    • 10.1016/S0968-0004(00)01700-X 11165500
    • Clissold PM Ponting CP JmjC: Cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta Trends Biochem Sci 2001, 26:7-9. 10.1016/S0968-0004(00)01700-X 11165500
    • (2001) Trends Biochem Sci , vol.26 , pp. 7-9
    • Clissold, P.M.1    Ponting, C.P.2
  • 4
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • 10.1038/nrg1945 16983801
    • Klose RJ Kallin EM Zhang Y JmjC-domain-containing proteins and histone demethylation Nat Rev Genet 2006, 7:715-727. 10.1038/nrg1945 16983801
    • (2006) Nat Rev Genet , vol.7 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 5
    • 33748291758 scopus 로고    scopus 로고
    • Roles of jumonji and jumonji family genes in chromatin regulation and development
    • 10.1002/dvdy.20851 16715513
    • Takeuchi T Watanabe Y Takano-Shimizu T Kondo S Roles of jumonji and jumonji family genes in chromatin regulation and development Dev Dyn 2006, 235:2449-2459. 10.1002/dvdy.20851 16715513
    • (2006) Dev Dyn , vol.235 , pp. 2449-2459
    • Takeuchi, T.1    Watanabe, Y.2    Takano-Shimizu, T.3    Kondo, S.4
  • 6
    • 33645891676 scopus 로고    scopus 로고
    • Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins
    • 10.1016/j.jinorgbio.2006.01.024 16513174
    • Clifton IJ McDonough MA Ehrismann D Kershaw NJ Granatino N Schofield CJ Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins J Inorg Biochem 2006, 100:644-669. 10.1016/j.jinorgbio.2006.01.024 16513174
    • (2006) J Inorg Biochem , vol.100 , pp. 644-669
    • Clifton, I.J.1    McDonough, M.A.2    Ehrismann, D.3    Kershaw, N.J.4    Granatino, N.5    Schofield, C.J.6
  • 8
    • 0032760945 scopus 로고    scopus 로고
    • Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes
    • 10.1016/S0959-440X(99)00036-6 10607676
    • Schofield CJ Zhang Z Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes Curr Opin Struct Biol 1999, 9:722-731. 10.1016/S0959-440X(99)00036-6 10607676
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 722-731
    • Schofield, C.J.1    Zhang, Z.2
  • 9
    • 17644392469 scopus 로고    scopus 로고
    • Methylation: Lost in hydroxylation?
    • 1299289 15809658 10.1038/sj.embor.7400379
    • Trewick SC McLaughlin PJ Allshire RC Methylation: Lost in hydroxylation? EMBO Rep 2005, 6:315-320. 1299289 15809658 10.1038/sj.embor.7400379
    • (2005) EMBO Rep , vol.6 , pp. 315-320
    • Trewick, S.C.1    McLaughlin, P.J.2    Allshire, R.C.3
  • 10
    • 0034640295 scopus 로고    scopus 로고
    • Jumonji, a nuclear protein that is necessary for normal heart development
    • 10807864
    • Lee Y Song AJ Baker R Micales B Conway SJ Lyons GE Jumonji, a nuclear protein that is necessary for normal heart development Circ Res 2000, 86:932-938. 10807864
    • (2000) Circ Res , vol.86 , pp. 932-938
    • Lee, Y.1    Song, A.J.2    Baker, R.3    Micales, B.4    Conway, S.J.5    Lyons, G.E.6
  • 11
    • 0032772975 scopus 로고    scopus 로고
    • Jumonji gene is essential for the neurulation and cardiac development of mouse embryos with a C3H/He background
    • 10.1016/S0925-4773(99)00100-8 10446263
    • Takeuchi T Kojima M Nakajima K Kondo S jumonji gene is essential for the neurulation and cardiac development of mouse embryos with a C3H/He background Mech Dev 1999, 86:29-38. 10.1016/S0925-4773(99)00100-8 10446263
    • (1999) Mech Dev , vol.86 , pp. 29-38
    • Takeuchi, T.1    Kojima, M.2    Nakajima, K.3    Kondo, S.4
  • 12
    • 0034596260 scopus 로고    scopus 로고
    • Jumonji is a nuclear protein that participates in the negative regulation of cell growth
    • 10.1006/bbrc.2000.3138 10913339
    • Toyoda M Kojima M Takeuchi T Jumonji is a nuclear protein that participates in the negative regulation of cell growth Biochem Biophys Res Commun 2000, 274:332-336. 10.1006/bbrc.2000.3138 10913339
    • (2000) Biochem Biophys Res Commun , vol.274 , pp. 332-336
    • Toyoda, M.1    Kojima, M.2    Takeuchi, T.3
  • 13
    • 20444429760 scopus 로고    scopus 로고
    • Binding of pRB to the PHD protein RBP2 promotes cellular differentiation
    • 10.1016/j.molcel.2005.05.012 15949438
    • Benevolenskaya EV Murray HL Branton P Young RA Kaelin WG Jr Binding of pRB to the PHD protein RBP2 promotes cellular differentiation Mol Cell 2005, 18:623-635. 10.1016/j.molcel.2005.05.012 15949438
    • (2005) Mol Cell , vol.18 , pp. 623-635
    • Benevolenskaya, E.V.1    Murray, H.L.2    Branton, P.3    Young, R.A.4    Kaelin Jr., W.G.5
  • 14
    • 0141961566 scopus 로고    scopus 로고
    • Physical and functional interaction between the vitamin D receptor and hairless corepressor, two proteins required for hair cycling
    • 10.1074/jbc.M304886200 12847098
    • Hsieh JC Sisk JM Jurutka PW Haussler CA Slater SA Haussler MR Thompson CC Physical and functional interaction between the vitamin D receptor and hairless corepressor, two proteins required for hair cycling J Biol Chem 2003, 278:38665-38674. 10.1074/jbc.M304886200 12847098
    • (2003) J Biol Chem , vol.278 , pp. 38665-38674
    • Hsieh, J.C.1    Sisk, J.M.2    Jurutka, P.W.3    Haussler, C.A.4    Slater, S.A.5    Haussler, M.R.6    Thompson, C.C.7
  • 15
    • 0036786432 scopus 로고    scopus 로고
    • Novel mechanism of nuclear receptor corepressor interaction dictated by activation function 2 helix determinants
    • 134023 12215540 10.1128/MCB.22.19.6831-6841.2002
    • Moraitis: AN Giguere V Thompson CC Novel mechanism of nuclear receptor corepressor interaction dictated by activation function 2 helix determinants Mol Cell Biol 2002, 22:6831-6841. 134023 12215540 10.1128/ MCB.22.19.6831-6841.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 6831-6841
    • Moraitis, A.N.1    Giguere, V.2    Thompson, C.C.3
  • 16
    • 0035887252 scopus 로고    scopus 로고
    • The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressor
    • 312820 11641275 10.1101/gad.916701
    • Potter GB Beaudoin GM 3rd DeRenzo CL Zarach JM Chen SH Thompson CC The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressor Genes Dev 2001, 15:2687-2701. 312820 11641275 10.1101/gad.916701
    • (2001) Genes Dev , vol.15 , pp. 2687-2701
    • Potter, G.B.1    Beaudoin III, G.M.2    DeRenzo, C.L.3    Zarach, J.M.4    Chen, S.H.5    Thompson, C.C.6
  • 18
    • 7344229369 scopus 로고    scopus 로고
    • Cloning, genomic organization, alternative transcripts and mutational analysis of the gene responsible for autosomal recessive universal congenital alopecia
    • 10.1093/hmg/7.11.1671 9736769
    • Cichon S Anker M Vogt IR Rohleder H Putzstuck M Hillmer A Farooq SA Al-Dhafri KS Ahmad M Haque S Cloning, genomic organization, alternative transcripts and mutational analysis of the gene responsible for autosomal recessive universal congenital alopecia Hum Mol Genet 1998, 7:1671-1679. 10.1093/hmg/7.11.1671 9736769
    • (1998) Hum Mol Genet , vol.7 , pp. 1671-1679
    • Cichon, S.1    Anker, M.2    Vogt, I.R.3    Rohleder, H.4    Putzstuck, M.5    Hillmer, A.6    Farooq, S.A.7    Al-Dhafri, K.S.8    Ahmad, M.9    Haque, S.10
  • 19
    • 4644338642 scopus 로고    scopus 로고
    • The co-repressor hairless has a role in epithelial cell differentiation in the skin
    • 10.1242/dev.01303 15280217
    • Zarach JM Beaudoin GM 3rd Coulombe PA Thompson CC The co-repressor hairless has a role in epithelial cell differentiation in the skin Development 2004, 131:4189-4200. 10.1242/dev.01303 15280217
    • (2004) Development , vol.131 , pp. 4189-4200
    • Zarach, J.M.1    Beaudoin III, G.M.2    Coulombe, P.A.3    Thompson, C.C.4
  • 20
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • 10.1038/nrm1761 16261189
    • Martin C Zhang Y The diverse functions of histone lysine methylation Nat Rev Mol Cell Biol 2005, 6:838-849. 10.1038/nrm1761 16261189
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 24
    • 34347346108 scopus 로고    scopus 로고
    • Demethylation of histone H3K36 and H3K9 by Rph1: A vestige of an H3K9 methylation system in Saccharomyces cerevisiae?
    • 1900024 17371840 10.1128/MCB.02180-06
    • Klose RJ Gardner KE Liang G Erdjument-Bromage H Tempst P Zhang Y Demethylation of histone H3K36 and H3K9 by Rph1: A vestige of an H3K9 methylation system in Saccharomyces cerevisiae? Mol Cell Biol 2007, 27:3951-3961. 1900024 17371840 10.1128/MCB.02180-06
    • (2007) Mol Cell Biol , vol.27 , pp. 3951-3961
    • Klose, R.J.1    Gardner, K.E.2    Liang, G.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6
  • 27
    • 33746332412 scopus 로고    scopus 로고
    • The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3
    • 10.1038/nature04837 16732293
    • Cloos PA Christensen J Agger K Maiolica A Rappsilber J Antal T Hansen KH Helin K The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3 Nature 2006, 442:307-311. 10.1038/nature04837 16732293
    • (2006) Nature , vol.442 , pp. 307-311
    • Cloos, P.A.1    Christensen, J.2    Agger, K.3    Maiolica, A.4    Rappsilber, J.5    Antal, T.6    Hansen, K.H.7    Helin, K.8
  • 29
    • 33745847680 scopus 로고    scopus 로고
    • The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
    • 10.1038/nature04853 16732292
    • Klose RJ Yamane K Bae Y Zhang D Erdjument-Bromage H Tempst P Wong J Zhang Y The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36 Nature 2006, 442:312-316. 10.1038/ nature04853 16732292
    • (2006) Nature , vol.442 , pp. 312-316
    • Klose, R.J.1    Yamane, K.2    Bae, Y.3    Zhang, D.4    Erdjument-Bromage, H.5    Tempst, P.6    Wong, J.7    Zhang, Y.8
  • 33
  • 34
    • 33847383585 scopus 로고    scopus 로고
    • Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein
    • 10.1016/j.cell.2007.02.004 17320162
    • Lee MG Norman J Shilatifard A Shiekhattar R Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein Cell 2007, 128:877-887. 10.1016/j.cell.2007.02.004 17320162
    • (2007) Cell , vol.128 , pp. 877-887
    • Lee, M.G.1    Norman, J.2    Shilatifard, A.3    Shiekhattar, R.4
  • 35
    • 33847660838 scopus 로고    scopus 로고
    • Yeast Jhd2p is a histone H3 Lys4 trimethyl demethylase
    • 10.1038/nsmb1204 17310254
    • Liang G Klose RJ Gardner KE Zhang Y Yeast Jhd2p is a histone H3 Lys4 trimethyl demethylase Nat Struct Mol Biol 2007, 14:243-245. 10.1038/ nsmb1204 17310254
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 243-245
    • Liang, G.1    Klose, R.J.2    Gardner, K.E.3    Zhang, Y.4
  • 37
    • 34247253752 scopus 로고    scopus 로고
    • The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase
    • 10.1038/nsmb1217 17351630
    • Eissenberg JC Lee MG Schneider J Ilvarsonn A Shiekhattar R Shilatifard A The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase Nat Struct Mol Biol 2007, 14:344-346. 10.1038/nsmb1217 17351630
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 344-346
    • Eissenberg, J.C.1    Lee, M.G.2    Schneider, J.3    Ilvarsonn, A.4    Shiekhattar, R.5    Shilatifard, A.6
  • 39
    • 33947152396 scopus 로고    scopus 로고
    • The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth
    • 1820896 17311883 10.1101/gad.1523007
    • Secombe J Li L Carlos L Eisenman RN The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth Genes Dev 2007, 21:537-551. 1820896 17311883 10.1101/gad.1523007
    • (2007) Genes Dev , vol.21 , pp. 537-551
    • Secombe, J.1    Li, L.2    Carlos, L.3    Eisenman, R.N.4
  • 42
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • 10.1016/j.cell.2007.08.019 17825402
    • De Santa F Totaro MG Prosperini E Notarbartolo S Testa G Natoli G The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing Cell 2007, 130:1083-1094. 10.1016/ j.cell.2007.08.019 17825402
    • (2007) Cell , vol.130 , pp. 1083-1094
    • De Santa, F.1    Totaro, M.G.2    Prosperini, E.3    Notarbartolo, S.4    Testa, G.5    Natoli, G.6
  • 44
    • 35348993743 scopus 로고    scopus 로고
    • Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination
    • 10.1126/science.1149042 17761849
    • Lee MG Villa R Trojer P Norman J Yan KP Reinberg D Di Croce L Shiekhattar R Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination Science 2007, 318:447-450. 10.1126/science.1149042 17761849
    • (2007) Science , vol.318 , pp. 447-450
    • Lee, M.G.1    Villa, R.2    Trojer, P.3    Norman, J.4    Yan, K.P.5    Reinberg, D.6    Di Croce, L.7    Shiekhattar, R.8
  • 45
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • 10.1016/j.cell.2006.03.027 16603237
    • Yamane K Toumazou C Tsukada Y Erdjument-Bromage H Tempst P Wong J Zhang Y JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor Cell 2006, 125:483-495. 10.1016/ j.cell.2006.03.027 16603237
    • (2006) Cell , vol.125 , pp. 483-495
    • Yamane, K.1    Toumazou, C.2    Tsukada, Y.3    Erdjument-Bromage, H.4    Tempst, P.5    Wong, J.6    Zhang, Y.7
  • 46
    • 33744552663 scopus 로고    scopus 로고
    • Swi6/HP1 recruits a JmjC domain protein to facilitate transcription of heterochromatic repeats
    • 10.1016/j.molcel.2006.05.010 16762840
    • Zofall M Grewal SI Swi6/HP1 recruits a JmjC domain protein to facilitate transcription of heterochromatic repeats Mol Cell 2006, 22:681-692. 10.1016/j.molcel.2006.05.010 16762840
    • (2006) Mol Cell , vol.22 , pp. 681-692
    • Zofall, M.1    Grewal, S.I.2
  • 47
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • 10.1126/science.1125162 16601153
    • Huang Y Fang J Bedford MT Zhang Y Xu RM Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A Science 2006, 312:748-751. 10.1126/science.1125162 16601153
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 48
    • 0037180452 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway
    • 137720 12432100 10.1073/pnas.202614999
    • Dann CE 3rd Bruick RK Deisenhofer J Structure of factor-inhibiting hypoxia-inducible factor 1: An asparaginyl hydroxylase involved in the hypoxic response pathway Proc Natl Acad Sci USA 2002, 99:15351-15356. 137720 12432100 10.1073/pnas.202614999
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15351-15356
    • Dann III, C.E.1    Bruick, R.K.2    Deisenhofer, J.3
  • 49
    • 0037449811 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha
    • 10.1074/jbc.C200644200 12446723
    • Elkins JM Hewitson KS McNeill LA Seibel JF Schlemminger I Pugh CW Ratcliffe PJ Schofield CJ Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha J Biol Chem 2003, 278:1802-1806. 10.1074/ jbc.C200644200 12446723
    • (2003) J Biol Chem , vol.278 , pp. 1802-1806
    • Elkins, J.M.1    Hewitson, K.S.2    McNeill, L.A.3    Seibel, J.F.4    Schlemminger, I.5    Pugh, C.W.6    Ratcliffe, P.J.7    Schofield, C.J.8
  • 50
    • 2342644926 scopus 로고    scopus 로고
    • Oxygen sensing by HIF hydroxylases
    • 10.1038/nrm1366 15122348
    • Schofield CJ Ratcliffe PJ Oxygen sensing by HIF hydroxylases Nat Rev Mol Cell Biol 2004, 5:343-354. 10.1038/nrm1366 15122348
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 343-354
    • Schofield, C.J.1    Ratcliffe, P.J.2
  • 51
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • 10.1038/nature01048 12226668
    • Falnes PO Johansen RF Seeberg E AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli Nature 2002, 419:178-182. 10.1038/nature01048 12226668
    • (2002) Nature , vol.419 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 52
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • 10.1038/nature00908 12226667
    • Trewick SC Henshaw TF Hausinger RP Lindahl T Sedgwick B Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage Nature 2002, 419:174-178. 10.1038/nature00908 12226667
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 53
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases
    • RESEARCH0007 30706 11276424 10.1186/gb-2001-2-3-research0007
    • Aravind L Koonin EV The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases Genome Biol 2001, 2. RESEARCH0007 30706 11276424 10.1186/ gb-2001-2-3-research0007
    • (2001) Genome Biol , pp. 2
    • Aravind, L.1    Koonin, E.V.2
  • 54
    • 23044433837 scopus 로고    scopus 로고
    • The phosphatidylserine receptor has essential functions during embryogenesis but not in apoptotic cell removal
    • 549712 15345036 10.1186/jbiol10
    • Böse J Gruber AD Helming L Schiebe S Wegener I Hafner M Beales M Kontgen F Lengeling A The phosphatidylserine receptor has essential functions during embryogenesis but not in apoptotic cell removal J Biol 2004, 3:15. 549712 15345036 10.1186/jbiol10
    • (2004) J Biol , vol.3 , pp. 15
    • Böse, J.1    Gruber, A.D.2    Helming, L.3    Schiebe, S.4    Wegener, I.5    Hafner, M.6    Beales, M.7    Kontgen, F.8    Lengeling, A.9
  • 55
    • 14644432528 scopus 로고    scopus 로고
    • Identification of cardiac malformations in mice lacking Ptdsr using a novel high-throughput magnetic resonance imaging technique
    • 545075 15615595 10.1186/1471-213X-4-16
    • Schneider JE Böse J Bamforth SD Gruber AD Broadbent C Clarke K Neubauer S Lengeling A Bhattacharya S Identification of cardiac malformations in mice lacking Ptdsr using a novel high-throughput magnetic resonance imaging technique BMC Dev Biol 2004, 4:16. 545075 15615595 10.1186/1471-213X-4-16
    • (2004) BMC Dev Biol , vol.4 , pp. 16
    • Schneider, J.E.1    Böse, J.2    Bamforth, S.D.3    Gruber, A.D.4    Broadbent, C.5    Clarke, K.6    Neubauer, S.7    Lengeling, A.8    Bhattacharya, S.9
  • 56
    • 0034604029 scopus 로고    scopus 로고
    • A receptor for phosphatidylserine-specific clearance of apoptotic cells
    • 10.1038/35011084 10811223
    • Fadok VA Bratton DL Rose DM Pearson A Ezekewitz RA Henson PM A receptor for phosphatidylserine-specific clearance of apoptotic cells Nature 2000, 405:85-90. 10.1038/35011084 10811223
    • (2000) Nature , vol.405 , pp. 85-90
    • Fadok, V.A.1    Bratton, D.L.2    Rose, D.M.3    Pearson, A.4    Ezekewitz, R.A.5    Henson, P.M.6
  • 57
    • 10144255178 scopus 로고    scopus 로고
    • The phosphatidylserine receptor from Hydra is a nuclear protein with potential Fe(II) dependent oxygenase activity
    • 442123 15193161 10.1186/1471-2121-5-26
    • Cikala M Alexandrova O David CN Proschel M Stiening B Cramer P Böttger A The phosphatidylserine receptor from Hydra is a nuclear protein with potential Fe(II) dependent oxygenase activity BMC Cell Biol 2004, 5:26. 442123 15193161 10.1186/1471-2121-5-26
    • (2004) BMC Cell Biol , vol.5 , pp. 26
    • Cikala, M.1    Alexandrova, O.2    David, C.N.3    Proschel, M.4    Stiening, B.5    Cramer, P.6    Böttger, A.7
  • 58
    • 0346690073 scopus 로고    scopus 로고
    • Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals
    • 10.1016/j.yexcr.2003.09.023 14729065
    • Cui P Qin B Liu N Pan G Pei D Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals Exp Cell Res 2004, 293:154-163. 10.1016/j.yexcr.2003.09.023 14729065
    • (2004) Exp Cell Res , vol.293 , pp. 154-163
    • Cui, P.1    Qin, B.2    Liu, N.3    Pan, G.4    Pei, D.5
  • 59
    • 34447527656 scopus 로고    scopus 로고
    • The Drosophila homolog of the putative phosphatidylserine receptor functions to inhibit apoptosis
    • 10.1242/dev.02860 17522160
    • Krieser RJ Moore FE Dresnek D Pellock BJ Patel R Huang A Brachmann C White K The Drosophila homolog of the putative phosphatidylserine receptor functions to inhibit apoptosis Development 2007, 134:2407-2414. 10.1242/dev.02860 17522160
    • (2007) Development , vol.134 , pp. 2407-2414
    • Krieser, R.J.1    Moore, F.E.2    Dresnek, D.3    Pellock, B.J.4    Patel, R.5    Huang, A.6    Brachmann, C.7    White, K.8
  • 60
  • 61
    • 34648828852 scopus 로고    scopus 로고
    • Characterization of the biochemical and biophysical properties of the phosphatidylserine receptor (PS-R) gene product
    • 10.1007/s11010-007-9492-8 17534701
    • Tibrewal N Liu T Li H Birge RB Characterization of the biochemical and biophysical properties of the phosphatidylserine receptor (PS-R) gene product Mol Cell Biochem 2007, 304:119-125. 10.1007/s11010-007-9492-8 17534701
    • (2007) Mol Cell Biochem , vol.304 , pp. 119-125
    • Tibrewal, N.1    Liu, T.2    Li, H.3    Birge, R.B.4
  • 62
    • 0345374586 scopus 로고    scopus 로고
    • Phosphatidylserine receptor is required for clearance of apoptotic cells
    • 10.1126/science.1087621 14645847
    • Li MO Sarkisian MR Mehal WZ Rakic P Flavell RA Phosphatidylserine receptor is required for clearance of apoptotic cells Science 2003, 302:1560-1563. 10.1126/science.1087621 14645847
    • (2003) Science , vol.302 , pp. 1560-1563
    • Li, M.O.1    Sarkisian, M.R.2    Mehal, W.Z.3    Rakic, P.4    Flavell, R.A.5
  • 63
    • 1942489369 scopus 로고    scopus 로고
    • Defective fetal liver erythropoiesis and T lymphopoiesis in mice lacking the phosphatidylserine receptor
    • 10.1182/blood-2003-09-3245 14715629
    • Kunisaki Y Masuko S Noda M Inayoshi A Sanui T Harada M Sasazuki T Fukui Y Defective fetal liver erythropoiesis and T lymphopoiesis in mice lacking the phosphatidylserine receptor Blood 2004, 103:3362-3364. 10.1182/blood-2003-09-3245 14715629
    • (2004) Blood , vol.103 , pp. 3362-3364
    • Kunisaki, Y.1    Masuko, S.2    Noda, M.3    Inayoshi, A.4    Sanui, T.5    Harada, M.6    Sasazuki, T.7    Fukui, Y.8
  • 64
    • 27944460430 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: Guardians of the Arg?
    • 16257219
    • Fackelmayer FO Protein arginine methyltransferases: Guardians of the Arg? Trends Biochem Sci 2005, 30:666-671. 16257219
    • (2005) Trends Biochem Sci , vol.30 , pp. 666-671
    • Fackelmayer, F.O.1
  • 67
    • 3242879520 scopus 로고    scopus 로고
    • e2g: An interactive web-based server for efficiently mapping large EST and cDNA sets to genomic sequences
    • 441616 15215398 10.1093/nar/gkh478
    • Krüger J Sczyrba A Kurtz S Giegerich R e2g: An interactive web-based server for efficiently mapping large EST and cDNA sets to genomic sequences Nucleic Acids Res 2004, 32:W301-304. 441616 15215398 10.1093/nar/gkh478
    • (2004) Nucleic Acids Res , vol.32
    • Krüger, J.1    Sczyrba, A.2    Kurtz, S.3    Giegerich, R.4
  • 68
    • 0031732094 scopus 로고    scopus 로고
    • A computer program for aligning a cDNA sequence with a genomic DNA sequence
    • 310774 9750195
    • Florea L Hartzell G Zhang Z Rubin GM Miller W A computer program for aligning a cDNA sequence with a genomic DNA sequence Genome Res 1998, 8:967-974. 310774 9750195
    • (1998) Genome Res , vol.8 , pp. 967-974
    • Florea, L.1    Hartzell, G.2    Zhang, Z.3    Rubin, G.M.4    Miller, W.5
  • 69
    • 0034949428 scopus 로고    scopus 로고
    • If phosphatidylserine is the death knell, a new phosphatidylserine-specific receptor is the bellringer
    • 10.1038/sj.cdd.4400856 11536008
    • Fadok VA Xue D Henson P If phosphatidylserine is the death knell, a new phosphatidylserine-specific receptor is the bellringer Cell Death Differ 2001, 8:582-587. 10.1038/sj.cdd.4400856 11536008
    • (2001) Cell Death Differ , vol.8 , pp. 582-587
    • Fadok, V.A.1    Xue, D.2    Henson, P.3
  • 70
    • 33749543416 scopus 로고    scopus 로고
    • Selection and slippage creating serine homopolymers
    • 10.1093/molbev/msl073 16877497
    • Huntley MA Golding GB Selection and slippage creating serine homopolymers Mol Biol Evol 2006, 23:2017-2025. 10.1093/molbev/msl073 16877497
    • (2006) Mol Biol Evol , vol.23 , pp. 2017-2025
    • Huntley, M.A.1    Golding, G.B.2
  • 71
    • 33745770062 scopus 로고    scopus 로고
    • Early nonsense: mRNA decay solves a translational problem
    • 10.1038/nrm1942 16723977
    • Amrani N Sachs MS Jacobson A Early nonsense: mRNA decay solves a translational problem Nat Rev Mol Cell Biol 2006, 7:415-425. 10.1038/ nrm1942 16723977
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 415-425
    • Amrani, N.1    Sachs, M.S.2    Jacobson, A.3
  • 72
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • 10.1126/science.278.5338.631 9381173
    • Tatusov RL Koonin EV Lipman DJ A genomic perspective on protein families Science 1997, 278:631-637. 10.1126/science.278.5338.631 9381173
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 74
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • 10.1093/bioinformatics/bti125 15531603
    • Söding J Protein homology detection by HMM-HMM comparison Bioinformatics 2005, 21:951-960. 10.1093/bioinformatics/bti125 15531603
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Söding, J.1
  • 75
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • 10.1006/jmbi.1993.1626 8254673
    • Sali A Blundell TL Comparative protein modelling by satisfaction of spatial restraints J Mol Biol 1993, 234:779-815. 10.1006/jmbi.1993.1626 8254673
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 76
    • 0027380612 scopus 로고
    • Molecular characterization of flavanone 3 beta-hydroxylases. Consensus sequence, comparison with related enzymes and the role of conserved histidine residues
    • 10.1111/j.1432-1033.1993.tb18301.x 8223617
    • Britsch L Dedio J Saedler H Forkmann G Molecular characterization of flavanone 3 beta-hydroxylases. Consensus sequence, comparison with related enzymes and the role of conserved histidine residues Eur J Biochem 1993, 217:745-754. 10.1111/j.1432-1033.1993.tb18301.x 8223617
    • (1993) Eur J Biochem , vol.217 , pp. 745-754
    • Britsch, L.1    Dedio, J.2    Saedler, H.3    Forkmann, G.4
  • 77
    • 0034724670 scopus 로고    scopus 로고
    • Site-directed mutagenesis of 2,4-dichlorophenoxyacetic acid/ alpha-ketoglutarate dioxygenase. Identification of residues involved in metallocenter formation and substrate binding
    • 10.1074/jbc.275.17.12400 10777523
    • Hogan DA Smith SR Saari EA McCracken J Hausinger RP Site-directed mutagenesis of 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase. Identification of residues involved in metallocenter formation and substrate binding J Biol Chem 2000, 275:12400-12409. 10.1074/jbc.275.17.12400 10777523
    • (2000) J Biol Chem , vol.275 , pp. 12400-12409
    • Hogan, D.A.1    Smith, S.R.2    Saari, E.A.3    McCracken, J.4    Hausinger, R.P.5
  • 78
    • 28244466886 scopus 로고    scopus 로고
    • Repair of methylation damage in DNA and RNA by mammalian AlkB homologues
    • 10.1074/jbc.M509881200 16174769
    • Lee DH Jin SG Cai S Chen Y Pfeifer GP O'Connor TR Repair of methylation damage in DNA and RNA by mammalian AlkB homologues J Biol Chem 2005, 280:39448-39459. 10.1074/jbc.M509881200 16174769
    • (2005) J Biol Chem , vol.280 , pp. 39448-39459
    • Lee, D.H.1    Jin, S.G.2    Cai, S.3    Chen, Y.4    Pfeifer, G.P.5    O'Connor, T.R.6
  • 79
    • 32844455577 scopus 로고    scopus 로고
    • Crystal structures of catalytic complexes of the oxidative DNA/RNA repair enzyme AlkB
    • 10.1038/nature04561 16482161
    • Yu B Edstrom WC Benach J Hamuro Y Weber PC Gibney BR Hunt JF Crystal structures of catalytic complexes of the oxidative DNA/RNA repair enzyme AlkB Nature 2006, 439:879-884. 10.1038/nature04561 16482161
    • (2006) Nature , vol.439 , pp. 879-884
    • Yu, B.1    Edstrom, W.C.2    Benach, J.3    Hamuro, Y.4    Weber, P.C.5    Gibney, B.R.6    Hunt, J.F.7
  • 80
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • 10.1038/nrm2143 17342184
    • Klose RJ Zhang Y Regulation of histone methylation by demethylimination and demethylation Nat Rev Mol Cell Biol 2007, 8:307-318. 10.1038/nrm2143 17342184
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 307-318
    • Klose, R.J.1    Zhang, Y.2
  • 81
    • 33847050240 scopus 로고    scopus 로고
    • Non-heme dioxygenases: Cellular sensors and regulators jelly rolled into one?
    • 10.1038/nchembio863 17301803
    • Ozer A Bruick RK Non-heme dioxygenases: Cellular sensors and regulators jelly rolled into one? Nat Chem Biol 2007, 3:144-153. 10.1038/ nchembio863 17301803
    • (2007) Nat Chem Biol , vol.3 , pp. 144-153
    • Ozer, A.1    Bruick, R.K.2
  • 82
    • 24344487927 scopus 로고    scopus 로고
    • The curious world of apoptotic cell clearance
    • 10.1186/jbiol13
    • Weitzman JB The curious world of apoptotic cell clearance J Biol 2004, 3:13. 10.1186/jbiol13
    • (2004) J Biol , vol.3 , pp. 13
    • Weitzman, J.B.1
  • 83
    • 27744556005 scopus 로고    scopus 로고
    • Hide and seek: The secret identity of the phosphatidylserine receptor
    • 549716 15453906 10.1186/jbiol14
    • Williamson P Schlegel RA Hide and seek: The secret identity of the phosphatidylserine receptor J Biol 2004, 3:14. 549716 15453906 10.1186/ jbiol14
    • (2004) J Biol , vol.3 , pp. 14
    • Williamson, P.1    Schlegel, R.A.2
  • 84
    • 34247890161 scopus 로고    scopus 로고
    • Changing story of the receptor for phosphatidylserine-dependent clearance of apoptotic cells
    • 1866200 17471263 10.1038/sj.embor.7400956
    • Wolf A Schmitz C Bottger A Changing story of the receptor for phosphatidylserine-dependent clearance of apoptotic cells EMBO Rep 2007, 8:465-469. 1866200 17471263 10.1038/sj.embor.7400956
    • (2007) EMBO Rep , vol.8 , pp. 465-469
    • Wolf, A.1    Schmitz, C.2    Bottger, A.3
  • 85
    • 0032190230 scopus 로고    scopus 로고
    • AT-hook motifs identified in a wide variety of DNA-binding proteins
    • 147871 9742243 10.1093/nar/26.19.4413
    • Aravind L Landsman D AT-hook motifs identified in a wide variety of DNA-binding proteins Nucleic Acids Res 1998, 26:4413-4421. 147871 9742243 10.1093/nar/26.19.4413
    • (1998) Nucleic Acids Res , vol.26 , pp. 4413-4421
    • Aravind, L.1    Landsman, D.2
  • 86
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • 10.1126/science.1145801 17947579
    • Chang B Chen Y Zhao Y Bruick RK JMJD6 is a histone arginine demethylase Science 2007, 318:444-447. 10.1126/science.1145801 17947579
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.1    Chen, Y.2    Zhao, Y.3    Bruick, R.K.4
  • 87
    • 35349030188 scopus 로고    scopus 로고
    • Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive
    • 10.1038/nature06166 17898714
    • Guccione E Bassi C Casadio F Martinato F Cesaroni M Schuchlautz H Luscher B Amati B Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive Nature 2007, 449:933-937. 10.1038/ nature06166 17898714
    • (2007) Nature , vol.449 , pp. 933-937
    • Guccione, E.1    Bassi, C.2    Casadio, F.3    Martinato, F.4    Cesaroni, M.5    Schuchlautz, H.6    Luscher, B.7    Amati, B.8
  • 91
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • 10.1038/nature05020 16728978
    • Li H Ilin S Wang W Duncan EM Wysocka J Allis CD Patel DJ Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF Nature 2006, 442:91-95. 10.1038/nature05020 16728978
    • (2006) Nature , vol.442 , pp. 91-95
    • Li, H.1    Ilin, S.2    Wang, W.3    Duncan, E.M.4    Wysocka, J.5    Allis, C.D.6    Patel, D.J.7
  • 95
    • 9444237436 scopus 로고    scopus 로고
    • Phosphatidylserine receptor is required for the engulfment of dead apoptotic cells and for normal embryonic development in zebrafish
    • 10.1242/dev.01409 15469976
    • Hong JR Lin GH Lin CJ Wang WP Lee CC Lin TL Wu JL Phosphatidylserine receptor is required for the engulfment of dead apoptotic cells and for normal embryonic development in zebrafish Development 2004, 131:5417-5427. 10.1242/dev.01409 15469976
    • (2004) Development , vol.131 , pp. 5417-5427
    • Hong, J.R.1    Lin, G.H.2    Lin, C.J.3    Wang, W.P.4    Lee, C.C.5    Lin, T.L.6    Wu, J.L.7
  • 97
    • 47249138693 scopus 로고    scopus 로고
    • RepeatMasker http://www.repeatmasker.org
  • 98
    • 47249157236 scopus 로고    scopus 로고
    • NCBI-BLAST http://www.ncbi.nlm.nih.gov/BLAST
  • 99
    • 47249109828 scopus 로고    scopus 로고
    • SMART http://smart.embl-heidelberg.de
  • 100
    • 0033625531 scopus 로고    scopus 로고
    • TEXshade: Shading and labeling of multiple sequence alignments using LATEX2 epsilon
    • 10.1093/bioinformatics/16.2.135 10842735
    • Beitz E TEXshade: Shading and labeling of multiple sequence alignments using LATEX2 epsilon Bioinformatics 2000, 16:135-139. 10.1093/ bioinformatics/16.2.135 10842735
    • (2000) Bioinformatics , vol.16 , pp. 135-139
    • Beitz, E.1
  • 101
    • 33747856166 scopus 로고    scopus 로고
    • The MPI Bioinformatics Toolkit for protein sequence analysis
    • 1538786 16845021 10.1093/nar/gkl217
    • Biegert A Mayer C Remmert M Soding J Lupas AN The MPI Bioinformatics Toolkit for protein sequence analysis Nucleic Acids Res 2006, 34:W335-339. 1538786 16845021 10.1093/nar/gkl217
    • (2006) Nucleic Acids Res , vol.34
    • Biegert, A.1    Mayer, C.2    Remmert, M.3    Soding, J.4    Lupas, A.N.5
  • 102
    • 47249132075 scopus 로고    scopus 로고
    • Swiss-Pdb-Viewer http://expasy.org/spdbv
  • 103
    • 47249158097 scopus 로고    scopus 로고
    • PyMOL http://pymol.sourceforge.net/
  • 104
    • 47249129909 scopus 로고    scopus 로고
    • PHYLIP http://evolution.genetics.washington.edu/phylip.html
  • 105
    • 47249123677 scopus 로고    scopus 로고
    • SUMOplot http://www.abgent.com.cn/doc/sumoplot/login.asp
  • 106
    • 47249165176 scopus 로고    scopus 로고
    • NetNES http://www.cbs.dtu.dk/services/NetNES
  • 107
    • 47249097078 scopus 로고    scopus 로고
    • Jpred-3 http://www.compbio.dundee.ac.uk/~www-jpred
  • 108
    • 47249163727 scopus 로고    scopus 로고
    • NCBI-Taxonomy http://www.ncbi.nlm.nih.gov/Taxonomy/


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.