메뉴 건너뛰기




Volumn 67, Issue , 2011, Pages 69-90

Errors in erasure: Links between histone lysine methylation removal and disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA THALASSEMIA MENTAL RETARDATION SYNDROME X LINKED PROTEIN; CATHEPSIN L; CHROMATIN HELICASE DNA BINDING 1 PROTEIN; CHROMATIN HELICASE DNA BINDING 3 PROTEIN; CHROMATIN HELICASE DNA BINDING 4 PROTEIN; CHROMATIN HELICASE DNA BINDING 5 PROTEIN; CHROMATIN HELICASE DNA BINDING 7 PROTEIN; DNA BINDING PROTEIN; HIRA PROTEIN; HISTONE; HISTONE DEMETHYLASE; HISTONE H3; JARID1B PROTEIN; JUMONJI DOMAIN CONTAINING PROTEIN D3; LSD1 PROTEIN; NUCLEAR PROTEIN; ONCOPROTEIN; PROTEIN JMJD2C; REGULATOR PROTEIN; RETINOBLASTOMA BINDING PROTEIN 2; TUMOR SUPPRESSOR PROTEIN; UBIQUITOUS TRANSCRIBED X CHROMOSOME TETRATRICOPEPTIDE REPEAT PROTEIN; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; CHAPERONE; HIRA PROTEIN, HUMAN; LYSINE; TRANSCRIPTION FACTOR;

EID: 79952109209     PISSN: 0071786X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-7643-8989-5_4     Document Type: Article
Times cited : (17)

References (117)
  • 3
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey VG, Faulkner R, Mirsky AE (1964) Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA 51:786-794
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 4
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in polycomb-group silencing
    • DOI 10.1126/science.1076997
    • Cao R, Wang L, Wang H, Xia L, Erdjument-Bromage H, Tempst P, Jones RS, Zhang Y (2002) Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 298:1039-1043 (Pubitemid 35247314)
    • (2002) Science , vol.298 , Issue.5595 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3    Xia, L.4    Erdjument-Bromage, H.5    Tempst, P.6    Jones, R.S.7    Zhang, Y.8
  • 5
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • DOI 10.1016/S0959-437X(02)00287-3
    • Kouzarides T (2002) Histone methylation in transcriptional control. Curr Opin Genet Dev 12:198-209 (Pubitemid 34219493)
    • (2002) Current Opinion in Genetics and Development , vol.12 , Issue.2 , pp. 198-209
    • Kouzarides, T.1
  • 8
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • DOI 10.1016/j.cell.2007.02.005, PII S0092867407001845
    • Kouzarides T (2007) Chromatin modifications and their function. Cell 128:693-705 (Pubitemid 46273577)
    • (2007) Cell , vol.128 , Issue.4 , pp. 693-705
    • Kouzarides, T.1
  • 10
    • 23944509075 scopus 로고    scopus 로고
    • The SET-domain protein superfamily: Protein lysine methyltransferases
    • Dillon SC, Zhang X, Trievel RC, Cheng X (2005) The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biol 6:227
    • (2005) Genome Biol , vol.6 , pp. 227
    • Dillon, S.C.1    Zhang, X.2    Trievel, R.C.3    Cheng, X.4
  • 13
    • 0036683308 scopus 로고    scopus 로고
    • Unsafe SETs: Histone lysine methyltransferases and cancer
    • DOI 10.1016/S0968-0004(02)02141-2, PII S0968000402021412
    • Schneider R, Bannister AJ, Kouzarides T (2002) Unsafe SETs: histone lysine methyltransferases and cancer. Trends Biochem Sci 27:396-402 (Pubitemid 34874749)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.8 , pp. 396-402
    • Schneider, R.1    Bannister, A.J.2    Kouzarides, T.3
  • 15
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • DOI 10.1126/science.1063127
    • Jenuwein T, Allis CD (2001) Translating the histone code. Science 293:1074-1080 (Pubitemid 32758077)
    • (2001) Science , vol.293 , Issue.5532 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 16
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • DOI 10.1016/j.cell.2004.12.012, PII S0092867404011997
    • Shi Y, Lan F, Matson C, Mulligan P, Whetstine JR, Cole PA, Casero RA (2004) Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 119:941-953 (Pubitemid 40037608)
    • (2004) Cell , vol.119 , Issue.7 , pp. 941-953
    • Shi, Y.1    Lan, F.2    Matson, C.3    Mulligan, P.4    Whetstine, J.R.5    Cole, P.A.6    Casero, R.A.7    Shi, Y.8
  • 19
    • 33746332412 scopus 로고    scopus 로고
    • The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3
    • DOI 10.1038/nature04837, PII NATURE04837
    • Cloos PA, Christensen J, Agger K, Maiolica A, Rappsilber J, Antal T, Hansen KH, Helin K (2006) The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3. Nature 442:307-311 (Pubitemid 44114906)
    • (2006) Nature , vol.442 , Issue.7100 , pp. 307-311
    • Cloos, P.A.C.1    Christensen, J.2    Agger, K.3    Maiolica, A.4    Rappsilber, J.5    Antal, T.6    Hansen, K.H.7    Helin, K.8
  • 20
    • 33745847680 scopus 로고    scopus 로고
    • The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
    • DOI 10.1038/nature04853, PII NATURE04853
    • Klose RJ, Yamane K, Bae Y, Zhang D, Erdjument-Bromage H, Tempst P, Wong J, Zhang Y (2006) The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature 442:312-316 (Pubitemid 44114907)
    • (2006) Nature , vol.442 , Issue.7100 , 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
  • 22
    • 70349272130 scopus 로고    scopus 로고
    • KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
    • Ciccone DN, Su H, Hevi S, Gay F, Lei H, Bajko J, Xu G, Li E, Chen T (2009) KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints. Nature 461:415-418
    • (2009) Nature , vol.461 , pp. 415-418
    • Ciccone, D.N.1    Su, H.2    Hevi, S.3    Gay, F.4    Lei, H.5    Bajko, J.6    Xu, G.7    Li, E.8    Chen, T.9
  • 24
    • 68749108259 scopus 로고    scopus 로고
    • LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer
    • Wang Y, Zhang H, Chen Y, Sun Y, Yang F, Yu W, Liang J, Sun L, Yang X, Shi L et al (2009) LSD1 is a subunit of the NuRD complex and targets the metastasis programs in breast cancer. Cell 138:660-672
    • (2009) Cell , vol.138 , pp. 660-672
    • Wang, Y.1    Zhang, H.2    Chen, Y.3    Sun, Y.4    Yang, F.5    Yu, W.6    Liang, J.7    Sun, L.8    Yang, X.9    Shi, L.10
  • 25
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor- dependent transcription
    • DOI 10.1038/nature04020, PII N04020
    • Metzger E, Wissmann M, Yin N, Muller JM, Schneider R, Peters AHFM, Günther T, Buettner R, Schule R (2005) LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 437:436-439 (Pubitemid 41613508)
    • (2005) Nature , vol.437 , Issue.7057 , pp. 436-439
    • Metzger, E.1    Wissmann, M.2    Yin, N.3    Muller, J.M.4    Schneider, R.5    Peters, A.H.F.M.6    Gunther, T.7    Buettner, R.8    Schule, R.9
  • 29
    • 33646826162 scopus 로고    scopus 로고
    • Molecular cytogenetic characterization of a metastatic lung sarcomatoid carcinoma: 9p23 neocentromere and 9p23∼p24 amplification including JAK2 and JMJD2C
    • DOI 10.1016/j.cancergencyto.2006.01.004, PII S0165460806000495
    • Italiano A, Attias R, Aurias A, Perot G, Burel-Vandenbos F, Otto J, Venissac N, Pedeutour F (2006) Molecular cytogenetic characterization of a metastatic lung sarcomatoid carcinoma: 9p23 neocentromere and 9p23-p24 amplification including JAK2 and JMJD2C. Cancer Genet Cytogenet 167:122-130 (Pubitemid 43776948)
    • (2006) Cancer Genetics and Cytogenetics , vol.167 , Issue.2 , pp. 122-130
    • Italiano, A.1    Attias, R.2    Aurias, A.3    Perot, G.4    Burel-Vandenbos, F.5    Otto, J.6    Venissac, N.7    Pedeutour, F.8
  • 36
    • 34249900454 scopus 로고    scopus 로고
    • The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation
    • DOI 10.1038/nature05823, PII NATURE05823
    • Tahiliani M, Mei P, Fang R, Leonor T, Rutenberg M, Shimizu F, Li J, Rao A, Shi Y (2007) The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation. Nature 447:601-605 (Pubitemid 46868038)
    • (2007) Nature , vol.447 , Issue.7144 , pp. 601-605
    • Tahiliani, M.1    Mei, P.2    Fang, R.3    Leonor, T.4    Rutenberg, M.5    Shimizu, F.6    Li, J.7    Rao, A.8    Shi, Y.9
  • 38
    • 33847383585 scopus 로고    scopus 로고
    • Physical and Functional Association of a Trimethyl H3K4 Demethylase and Ring6a/MBLR, a Polycomb-like Protein
    • DOI 10.1016/j.cell.2007.02.004, PII S0092867407001833
    • Lee MG, Norman J, Shilatifard A, Shiekhattar R (2007) Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein. Cell 128:877-887 (Pubitemid 46341414)
    • (2007) Cell , vol.128 , Issue.5 , pp. 877-887
    • Lee, M.G.1    Norman, J.2    Shilatifard, A.3    Shiekhattar, R.4
  • 39
    • 34547687916 scopus 로고    scopus 로고
    • The function and regulation of the JARID1 family of histone H3 lysine 4 demethylases: The Myc connection
    • Secombe J, Eisenman RN (2007) The function and regulation of the JARID1 family of histone H3 lysine 4 demethylases: the Myc connection. Cell Cycle 6:1324-1328 (Pubitemid 47327965)
    • (2007) Cell Cycle , vol.6 , Issue.11 , pp. 1324-1328
    • Secombe, J.1    Eisenman, R.N.2
  • 42
    • 20444429760 scopus 로고    scopus 로고
    • Binding of pRB to the PHD protein RBP2 promotes cellular differentiation
    • DOI 10.1016/j.molcel.2005.05.012, PII S1097276505013183
    • Benevolenskaya EV, Murray HL, Branton P, Young RA, Kaelin WG Jr (2005) Binding of pRB to the PHD protein RBP2 promotes cellular differentiation. Mol Cell 18:623-635 (Pubitemid 40804799)
    • (2005) Molecular Cell , vol.18 , Issue.6 , pp. 623-635
    • Benevolenskaya, E.V.1    Murray, H.L.2    Branton, P.3    Young, R.A.4    Kaelin Jr., W.G.5
  • 43
    • 0038748632 scopus 로고    scopus 로고
    • A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer
    • Lu PJ, Sundquist K, BaeckstromD, PoulsomR, Hanby A, Meier-Ewert S, Jones T, Mitchell M, Pitha-Rowe P, Freemont P et al (1999) A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer. J Biol Chem 274:15633-15645
    • (1999) J Biol Chem , vol.274 , pp. 15633-15645
    • Lu, P.J.1    Sundquist, K.2    Poulsomr, B.3    Hanby, A.4    Meier-Ewert, S.5    Jones, T.6    Mitchell, M.7    Pitha-Rowe, P.8    Freemont, P.9
  • 45
    • 33947152396 scopus 로고    scopus 로고
    • The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth
    • DOI 10.1101/gad.1523007
    • Secombe J, Li L, Carlos L, Eisenman RN (2007) The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth. Genes Dev 21:537-551 (Pubitemid 46409469)
    • (2007) Genes and Development , vol.21 , Issue.5 , pp. 537-551
    • Secombe, J.1    Li, L.2    Carlos, L.3    Eisenman, R.N.4
  • 46
    • 35348993743 scopus 로고    scopus 로고
    • Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination
    • DOI 10.1126/science.1149042
    • Lee MG, Villa R, Trojer P, Norman J, Yan K-P, Reinberg D, Di Croce L, Shiekhattar R (2007) Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination. Science 318:447-450 (Pubitemid 47614529)
    • (2007) Science , vol.318 , Issue.5849 , pp. 447-450
    • Min, G.L.1    Villa, R.2    Trojer, P.3    Norman, J.4    Yan, K.-P.5    Reinberg, D.6    Di Croce, L.7    Shiekhattar, R.8
  • 48
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • DOI 10.1016/j.cell.2007.08.019, PII S0092867407010823
    • Schones D.E.anta F, Totaro MG, Prosperini E, Notarbartolo S, Testa G, Natoli G (2007) The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 130:1083-1094 (Pubitemid 47410272)
    • (2007) Cell , vol.130 , Issue.6 , pp. 1083-1094
    • De Santa, F.1    Totaro, M.G.2    Prosperini, E.3    Notarbartolo, S.4    Testa, G.5    Natoli, G.6
  • 50
    • 35348826654 scopus 로고    scopus 로고
    • JMJD3 is a histone H3K27 demethylase
    • DOI 10.1038/cr.2007.83, PII CR200783
    • Xiang Y, Zhu Z, Han G, Lin H, Xu L, Chen CD (2007) JMJD3 is a histone H3K27 demethylase. Cell Res 17:850-857 (Pubitemid 47585113)
    • (2007) Cell Research , vol.17 , Issue.10 , pp. 850-857
    • Xiang, Y.1    Zhu, Z.2    Han, G.3    Lin, H.4    Xu, L.5    Chen, C.D.6
  • 52
    • 1342332096 scopus 로고    scopus 로고
    • Polycomb CBX7 has a unifying role in cellular lifespan
    • DOI 10.1038/ncb1077
    • Gil J, Bernard D, Martinez D, Beach D (2004) Polycomb CBX7 has a unifying role in cellular lifespan. Nat Cell Biol 6:67-72 (Pubitemid 38425732)
    • (2004) Nature Cell Biology , vol.6 , Issue.1 , pp. 67-72
    • Gil, J.1    Bernard, D.2    Martinez, D.3    Beach, D.4
  • 53
    • 0033552813 scopus 로고    scopus 로고
    • The oncogene and Polycombgroup gene bmi-1 regulates cell proliferation and senescence through the ink4a locus
    • DOI 10.1038/16476
    • Jacobs JJ, Kieboom K, Marino S, DePinho RA, van Lohuizen M (1999) The oncogene and Polycomb-group gene bmi-1 regulates cell proliferation and senescence through the ink4a locus. Nature 397:164-168 (Pubitemid 29050921)
    • (1999) Nature , vol.397 , Issue.6715 , pp. 164-168
    • Jacobs, J.L.1    Kieboom, K.2    Marino, S.3    DePinho, R.A.4    Van Lohuizen, M.5
  • 54
    • 53249108053 scopus 로고    scopus 로고
    • Role of the lysinespecific demethylase 1 in the proinflammatory phenotype of vascular smooth muscle cells of diabetic mice
    • Reddy MA, Villeneuve LM, Wang M, Lanting L, Natarajan R (2008) Role of the lysinespecific demethylase 1 in the proinflammatory phenotype of vascular smooth muscle cells of diabetic mice. Circ Res 103:615-623
    • (2008) Circ Res , vol.103 , pp. 615-623
    • Reddy, M.A.1    Villeneuve, L.M.2    Wang, M.3    Lanting, L.4    Natarajan, R.5
  • 56
    • 55549140173 scopus 로고    scopus 로고
    • Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaBdependent inflammatory genes. Relevance to diabetes and inflammation
    • Li Y, Reddy MA, Miao F, Shanmugam N, Yee JK, Hawkins D, Ren B, Natarajan R (2008) Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaBdependent inflammatory genes. Relevance to diabetes and inflammation. J Biol Chem 283:26771-26781
    • (2008) J Biol Chem , vol.283 , pp. 26771-26781
    • Li, Y.1    Reddy, M.A.2    Miao, F.3    Shanmugam, N.4    Yee, J.K.5    Hawkins, D.6    Ren, B.7    Natarajan, R.8
  • 57
    • 0023404906 scopus 로고
    • Changes in histones H2A and H3 variant composition in differentiating and mature rat brain cortical neurons
    • Pina B, Suau P (1987) Changes in histones H2A and H3 variant composition in differentiating and mature rat brain cortical neurons. Dev Biol 123:51-58
    • (1987) Dev Biol , vol.123 , pp. 51-58
    • Pina, B.1    Suau, P.2
  • 58
    • 0023682238 scopus 로고
    • The production of tissue-specific histone complements during development
    • Lennox RW, Cohen LH (1988) The production of tissue-specific histone complements during development. Biochem Cell Biol 66:636-649
    • (1988) Biochem Cell Biol , vol.66 , pp. 636-649
    • Lennox, R.W.1    Cohen, L.H.2
  • 59
    • 0030881925 scopus 로고    scopus 로고
    • Constitutive expression, not a particular primary sequence, is the important feature of the H3 replacement variant HV2 in Tetrahymena thermophila
    • Yu L, Gorovsky MA (1997) Constitutive expression, not a particular primary sequence, is the important feature of the H3 replacement variant hv2 in Tetrahymena thermophila. Mol Cell Biol 17:6303-6310 (Pubitemid 27451174)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.11 , pp. 6303-6310
    • Yu, L.1    Gorovsky, M.A.2
  • 60
    • 0036299092 scopus 로고    scopus 로고
    • The histone variant H3.3 marks active chromatin by replication- independent nucleosome assembly
    • DOI 10.1016/S1097-2765(02)00542-7
    • Ahmad K, Henikoff S (2002) The histone variant H3.3 marks active chromatin by replicationindependent nucleosome assembly. Mol Cell 9:1191-1200 (Pubitemid 34722299)
    • (2002) Molecular Cell , vol.9 , Issue.6 , pp. 1191-1200
    • Ahmad, K.1    Henikoff, S.2
  • 61
    • 0742304304 scopus 로고    scopus 로고
    • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis
    • DOI 10.1016/S0092-8674(03)01064-X
    • Tagami H, Ray-Gallet D, Almouzni G, Nakatani Y (2004) Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis. Cell 116:51-61 (Pubitemid 38156183)
    • (2004) Cell , vol.116 , Issue.1 , pp. 51-61
    • Tagami, H.1    Ray-Gallet, D.2    Almouzni, G.3    Nakatani, Y.4
  • 62
    • 0036284794 scopus 로고    scopus 로고
    • HIRA is critical for a nucleosome assembly pathway independent of DNA synthesis
    • DOI 10.1016/S1097-2765(02)00526-9
    • Ray-Gallet D, Quivy JP, Scamps C, Martini EM, Lipinski M, Almouzni G (2002) HIRA is critical for a nucleosome assembly pathway independent of DNA synthesis. Mol Cell 9:1091-1100 (Pubitemid 34626677)
    • (2002) Molecular Cell , vol.9 , Issue.5 , pp. 1091-1100
    • Ray-Gallet, D.1    Quivy, J.-P.2    Scamps, C.3    Martini, E.M.-D.4    Lipinski, M.5    Almouzni, G.6
  • 63
    • 0029038946 scopus 로고
    • A human homolog of the S. cerevisiae HIR1 and HIR2 transcriptional repressors cloned from the DiGeorge syndrome critical region
    • Lamour V, Lecluse Y, Desmaze C, Spector M, Bodescot M, Aurias A, Osley MA, Lipinski M (1995) A human homolog of the S. cerevisiae HIR1 and HIR2 transcriptional repressors cloned from the DiGeorge syndrome critical region. Hum Mol Genet 4:791-799
    • (1995) Hum Mol Genet , vol.4 , pp. 791-799
    • Lamour, V.1    Lecluse, Y.2    Desmaze, C.3    Spector, M.4    Bodescot, M.5    Aurias, A.6    Osley, M.A.7    Lipinski, M.8
  • 64
    • 0033753819 scopus 로고    scopus 로고
    • The 22q11 deletion syndromes
    • Scambler PJ (2000) The 22q11 deletion syndromes. Hum Mol Genet 9:2421-2426
    • (2000) Hum Mol Genet , vol.9 , pp. 2421-2426
    • Scambler, P.J.1
  • 67
    • 0036124470 scopus 로고    scopus 로고
    • Targeted mutagenesis of the Hira gene results in gastrulation defects and patterning abnormalities of mesoendodermal derivatives prior to early embryonic lethality
    • DOI 10.1128/MCB.22.7.2318-2328.2002
    • Roberts C, Sutherland HF, Farmer H, Kimber W, Halford S, Carey A, Brickman JM, Wynshaw-Boris A, Scambler PJ (2002) Targeted mutagenesis of the Hira gene results in gastrulation defects and patterning abnormalities of mesoendodermal derivatives prior to early embryonic lethality. Mol Cell Biol 22:2318-2328 (Pubitemid 34224636)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.7 , pp. 2318-2328
    • Roberts, C.1    Sutherland, H.F.2    Farmer, H.3    Kimber, W.4    Halford, S.5    Carey, A.6    Brickman, J.M.7    Wynshaw-Boris, A.8    Scambler, P.J.9
  • 68
    • 35948990898 scopus 로고    scopus 로고
    • The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization
    • DOI 10.1371/journal.pgen.0030182
    • Bonnefoy E, Orsi GA, Couble P, Loppin B (2007) The essential role of Drosophila HIRA for de novo assembly of paternal chromatin at fertilization. PLoS Genet 3:1991-2006 (Pubitemid 350072062)
    • (2007) PLoS Genetics , vol.3 , Issue.10 , pp. 1991-2006
    • Bonnefoy, E.1    Orsi, G.A.2    Couble, P.3    Loppin, B.4
  • 69
    • 27644515513 scopus 로고    scopus 로고
    • The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus
    • DOI 10.1038/nature04059, PII N04059
    • Loppin B, Bonnefoy E, Anselme C, Laurencon A, Karr TL, Couble P (2005) The histone H3.3 chaperone HIRA is essential for chromatin assembly in the male pronucleus. Nature 437:1386-1390 (Pubitemid 41568687)
    • (2005) Nature , vol.437 , Issue.7063 , pp. 1386-1390
    • Loppin, B.1    Bonnefoy, E.2    Anselme, C.3    Laurencon, A.4    Karr, T.L.5    Couble, P.6
  • 70
    • 67650960676 scopus 로고    scopus 로고
    • Transcription in the absence of histone H3.3
    • Hodl M, Basler K (2009) Transcription in the absence of histone H3.3. Curr Biol 19:1221-1226
    • (2009) Curr Biol , vol.19 , pp. 1221-1226
    • Hodl, M.1    Basler, K.2
  • 71
    • 71849103121 scopus 로고    scopus 로고
    • Transcriptional and developmental functions of the H3.3 histone variant in Drosophila
    • Sakai A, Schwartz BE, Goldstein S, Ahmad K (2009) Transcriptional and developmental functions of the H3.3 histone variant in Drosophila. Curr Biol 19(21):1816-1820
    • (2009) Curr Biol , vol.19 , Issue.21 , pp. 1816-1820
    • Sakai, A.1    Schwartz, B.E.2    Goldstein, S.3    Ahmad, K.4
  • 77
    • 0028787425 scopus 로고
    • Molecular analysis of a major antigenic region of the 240-kD protein of Mi-2 autoantigen
    • Ge Q, Nilasena DS, O'Brien CA, Frank MB, Targoff IN (1995) Molecular analysis of a major antigenic region of the 240-kD protein of Mi-2 autoantigen. J Clin Invest 96:1730-1737
    • (1995) J Clin Invest , vol.96 , pp. 1730-1737
    • Ge, Q.1    Nilasena, D.S.2    O'brien, C.A.3    Frank, M.B.4    Targoff, I.N.5
  • 78
    • 0028788212 scopus 로고
    • The major dermatomyositis-specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation
    • Seelig HP, Moosbrugger I, Ehrfeld H, Fink T, Renz M, Genth E (1995) The major dermatomyositis-specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation. Arthritis Rheum 38:1389-1399
    • (1995) Arthritis Rheum , vol.38 , pp. 1389-1399
    • Seelig, H.P.1    Moosbrugger, I.2    Ehrfeld, H.3    Fink, T.4    Renz, M.5    Genth, E.6
  • 79
    • 0030266784 scopus 로고    scopus 로고
    • Two forms of the major antigenic protein of the dermatomyositis-specific Mi-2 autoantigen
    • Seelig HP, Renz M, Targoff IN, Ge Q, Frank MB (1996) Two forms of the major antigenic protein of the dermatomyositis-specific Mi-2 autoantigen. Arthritis Rheum 39:1769-1771
    • (1996) Arthritis Rheum , vol.39 , pp. 1769-1771
    • Seelig, H.P.1    Renz, M.2    Targoff, I.N.3    Ge, Q.4    Frank, M.B.5
  • 80
    • 0019981972 scopus 로고
    • Production of a monoclonal antibody specific for Hodgkin and Sternberg-Reed cells of Hodgkin's disease and a subset of normal lymphoid cells
    • DOI 10.1038/299065a0
    • Schwab U, Stein H, Gerdes J, Lemke H, Kirchner H, Schaadt M, Diehl V (1982) Production of a monoclonal antibody specific for Hodgkin and Sternberg-Reed cells of Hodgkin's disease and a subset of normal lymphoid cells. Nature 299:65-67 (Pubitemid 12049770)
    • (1982) Nature , vol.299 , Issue.5878 , pp. 65-67
    • Schwab, U.1    Stein, H.2    Gerdes, J.3
  • 82
    • 0037455722 scopus 로고    scopus 로고
    • CHD5, a new member of the chromodomain gene family, is preferentially expressed in the nervous system
    • DOI 10.1038/sj.onc.1206211
    • Thompson PM, Gotoh T, Kok M, White PS, Brodeur GM (2003) CHD5, a new member of the chromodomain gene family, is preferentially expressed in the nervous system. Oncogene 22:1002-1011 (Pubitemid 36313144)
    • (2003) Oncogene , vol.22 , Issue.7 , pp. 1002-1011
    • Thompson, P.M.1    Gotoh, T.2    Kok, M.3    White, P.S.4    Brodeur, G.M.5
  • 83
    • 0038824950 scopus 로고    scopus 로고
    • Progression of myelodysplastic syndrome: Allelic loss on chromosomal arm 1p
    • DOI 10.1046/j.1365-2141.2003.04434.x
    • Mori N, Morosetti R, Mizoguchi H, Koeffler HP (2003) Progression of myelodysplastic syndrome: allelic loss on chromosomal arm 1p. Br J Haematol 122:226-230 (Pubitemid 36859607)
    • (2003) British Journal of Haematology , vol.122 , Issue.2 , pp. 226-230
    • Mori, N.1    Morosetti, R.2    Mizoguchi, H.3    Koeffler, H.P.4
  • 84
    • 0032211176 scopus 로고    scopus 로고
    • Chromosome band 1p36 contains a putative tumor suppressor gene important in the evolution of chronic myelocytic leukemia
    • Mori N, Morosetti R, Spira S, Lee S, Ben-Yehuda D, Schiller G, Landolfi R, Mizoguchi H, Koeffler HP (1998) Chromosome band 1p36 contains a putative tumor suppressor gene important in the evolution of chronic myelocytic leukemia. Blood 92:3405-3409 (Pubitemid 28492351)
    • (1998) Blood , vol.92 , Issue.9 , pp. 3405-3409
    • Mori, N.1    Morosetti, R.2    Spira, S.3    Lee, S.4    Ben-Yehuda, D.5    Schiller, G.6    Landolfi, R.7    Mizoguchi, H.8    Koeffler, H.P.9
  • 87
  • 92
    • 0021830398 scopus 로고
    • Pathologic features of the CHARGE association: Support for involvement of the neural crest
    • DOI 10.1002/tera.1420310303
    • Siebert JR, Graham JM Jr, MacDonald C (1985) Pathologic features of the CHARGE association: support for involvement of the neural crest. Teratology 31:331-336 (Pubitemid 15000257)
    • (1985) Teratology , vol.31 , Issue.3 , pp. 331-336
    • Siebert, J.R.1    Graham Jr., J.M.2    MacDonald, C.3
  • 94
    • 0031040868 scopus 로고    scopus 로고
    • Cloning and developmental expression analysis of chick Hira (Chira), a candidate gene for DiGeorge syndrome
    • DOI 10.1093/hmg/6.2.237
    • Roberts C, Daw SC, Halford S, Scambler PJ (1997) Cloning and developmental expression analysis of chick Hira (Chira), a candidate gene for DiGeorge syndrome. Hum Mol Genet 6:237-245 (Pubitemid 27078080)
    • (1997) Human Molecular Genetics , vol.6 , Issue.2 , pp. 237-245
    • Roberts, C.1    Daw, S.C.M.2    Halford, S.3    Scambler, P.J.4
  • 95
    • 0031058266 scopus 로고    scopus 로고
    • The murine homologue of HIRA, a DiGeorge syndrome candidate gene, is expressed in embryonic structures affected in human CATCH22 patients
    • DOI 10.1093/hmg/6.2.247
    • Wilming LG, Snoeren CA, van Rijswijk A, Grosveld F, Meijers C (1997) The murine homologue of HIRA, a DiGeorge syndrome candidate gene, is expressed in embryonic structures affected in human CATCH22 patients. Hum Mol Genet 6:247-258 (Pubitemid 27078081)
    • (1997) Human Molecular Genetics , vol.6 , Issue.2 , pp. 247-258
    • Wilming, L.G.1    Snoeren, C.A.S.2    Van Rijswijk, A.3    Grosveld, F.4    Meijers, C.5
  • 98
    • 0018903045 scopus 로고
    • Proteolytic processing of histone H3 in chromatin: A physiologically regulated event in Tetrahymena micronuclei
    • Allis CD, Bowen JK, Abraham GN, Glover CV, Gorovsky MA (1980) Proteolytic processing of histone H3 in chromatin: a physiologically regulated event in Tetrahymena micronuclei. Cell 20:55-64 (Pubitemid 10117300)
    • (1980) Cell , vol.20 , Issue.1 , pp. 55-64
    • Allis, C.D.1    Abraham, G.N.2    Bowen, J.K.3
  • 99
    • 0025190848 scopus 로고
    • Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3
    • Falk MM, Grigera PR, Bergmann IE, Zibert A, Multhaup G, Beck E (1990) Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3. J Virol 64:748-756 (Pubitemid 20032691)
    • (1990) Journal of Virology , vol.64 , Issue.2 , pp. 748-756
    • Falk, M.M.1    Grigera, P.R.2    Bergmann, I.E.3    Zibert, A.4    Multhaup, G.5    Beck, E.6
  • 103
    • 0023656232 scopus 로고
    • Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin
    • Troen BR, Gal S, Gottesman MM (1987) Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. Biochem J 246:731-735
    • (1987) Biochem J , vol.246 , pp. 731-735
    • Troen, B.R.1    Gal, S.2    Gottesman, M.M.3
  • 104
    • 0030032833 scopus 로고    scopus 로고
    • Nuclear localization of procathepsin L/MEP in ras-transformed mouse fibroblasts
    • DOI 10.1016/0304-3835(95)04041-2
    • Hiwasa T, Sakiyama S (1996) Nuclear localization of procathepsin L/MEP in rastransformed mouse fibroblasts. Cancer Lett 99:87-91 (Pubitemid 26030356)
    • (1996) Cancer Letters , vol.99 , Issue.1 , pp. 87-91
    • Hiwasa, T.1    Sakiyama, S.2
  • 105
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor
    • DOI 10.1016/S1097-2765(04)00209-6, PII S1097276504002096
    • Goulet B, Baruch A, Moon NS, Poirier M, Sansregret LL, Erickson A, Bogyo M, Nepveu A (2004) A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in S phase and processes the CDP/Cux transcription factor. Mol Cell 14:207-219 (Pubitemid 38515648)
    • (2004) Molecular Cell , vol.14 , Issue.2 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.-S.3    Poirier, M.4    Sansregret, L.L.5    Erickson, A.6    Bogyo, M.7    Nepveu, A.8
  • 107
    • 0023610145 scopus 로고
    • Cysteine proteinase cathepsin L expression correlates closely with the metastatic potential of H-ras-transformed murine fibroblasts
    • Denhardt DT, Greenberg AH, Egan SE, Hamilton RT, Wright JA (1987) Cysteine proteinase cathepsin L expression correlates closely with the metastatic potential of H-ras-transformed murine fibroblasts. Oncogene 2:55-59 (Pubitemid 18021071)
    • (1987) Oncogene , vol.2 , Issue.1 , pp. 55-59
    • Denhardt, D.T.1    Greenberg, A.H.2    Egan, S.E.3    Hamilton, R.T.4    Wright, J.A.5
  • 108
    • 0031932089 scopus 로고    scopus 로고
    • Cysteine proteinases in cancer progression and their clinical relevance for prognosis
    • Lah TT, Kos J (1998) Cysteine proteinases in cancer progression and their clinical relevance for prognosis. Biol Chem 379:125-130 (Pubitemid 28075971)
    • (1998) Biological Chemistry , vol.379 , Issue.2 , pp. 125-130
    • Lah, T.T.1    Kos, J.2
  • 109
    • 34548689404 scopus 로고    scopus 로고
    • Increased expression and activity of nuclear cathepsin L in cancer cells suggests a novel mechanism of cell transformation
    • DOI 10.1158/1541-7786.MCR-07-0160
    • Goulet B, Sansregret L, Leduy L, Bogyo M, Weber E, Chauhan SS, Nepveu A (2007) Increased expression and activity of nuclear cathepsin L in cancer cells suggests a novel mechanism of cell transformation. Mol Cancer Res 5:899-907 (Pubitemid 47416667)
    • (2007) Molecular Cancer Research , vol.5 , Issue.9 , pp. 899-907
    • Goulet, B.1    Sansregret, L.2    Leduy, L.3    Bogyo, M.4    Weber, E.5    Chauhan, S.S.6    Nepveu, A.7
  • 110
    • 1842328054 scopus 로고    scopus 로고
    • Identification of a cysteine protease responsible for degradation of sperm histones during male pronucleus remodeling in sea urchins
    • DOI 10.1002/(SICI)1097-4644(19971201)67:3<304::AID-JCB3>3.0.CO;2-#
    • Imschenetzky M, Diaz F, Montecino M, Sierra F, Puchi M(1997) Identification of a cysteine protease responsible for degradation of sperm histones during male pronucleus remodeling in sea urchins. J Cell Biochem 67:304-315 (Pubitemid 27509467)
    • (1997) Journal of Cellular Biochemistry , vol.67 , Issue.3 , pp. 304-315
    • Imschenetzky, M.1    Diaz, F.2    Montecino, M.3    Sierra, F.4    Puchi, M.5
  • 111
    • 21644456725 scopus 로고    scopus 로고
    • Inhibition of cysteine protease activity disturbs DNA replication and prevents mitosis in the early mitotic cell cycles of sea urchin embryos
    • DOI 10.1002/jcp.20338
    • Concha C, Monardes A, Even Y, Morin V, Puchi M, Imschenetzky M, Geneviere AM (2005) Inhibition of cysteine protease activity disturbs DNA replication and prevents mitosis in the early mitotic cell cycles of sea urchin embryos. J Cell Physiol 204:693-703 (Pubitemid 40934666)
    • (2005) Journal of Cellular Physiology , vol.204 , Issue.2 , pp. 693-703
    • Concha, C.1    Monardes, A.2    Even, Y.3    Morin, V.4    Puchi, M.5    Imschenetzky, M.6    Geneviere, A.M.7
  • 113
    • 67651148170 scopus 로고    scopus 로고
    • Histone H3 N-terminal peptide binds directly to its own mRNA: A possible mode of feedback inhibition to control translation
    • Lee KH, Lee NJ, Hyun S, Park YK, Yang EG, Lee J-K, Jeong S, Yu J (2009) Histone H3 N-terminal peptide binds directly to its own mRNA: a possible mode of feedback inhibition to control translation. Chembiochem 10:1313-1316
    • (2009) Chembiochem , vol.10 , pp. 1313-1316
    • Lee, K.H.1    Lee, N.J.2    Hyun, S.3    Park, Y.K.4    Yang, E.G.5    Lee, J.-K.6    Jeong, S.7    Yu, J.8
  • 114
    • 0032705821 scopus 로고    scopus 로고
    • Isolation of mitogenically active C-terminal truncated pentapeptide of osteogenic growth peptide from human plasma and culture medium of murine osteoblastic cells
    • DOI 10.1034/j.1399-3011.1999.00135.x
    • Bab I, Gavish H, Namdar-Attar M, Muhlrad A, Greenberg Z, Chen Y, Mansur N, Shteyer A, Chorev M (1999) Isolation of mitogenically active C-terminal truncated pentapeptide of osteogenic growth peptide from human plasma and culture medium of murine osteoblastic cells. J Pept Res 54:408-414 (Pubitemid 29498135)
    • (1999) Journal of Peptide Research , vol.54 , Issue.5 , pp. 408-414
    • Bab, I.1    Gavish, H.2    Namdar-Attar, M.3    Muhlrad, A.4    Greenberg, Z.5    Chen, Y.6    Mansur, N.7    Shteyer, A.8    Chorev, M.9
  • 115
    • 0026552958 scopus 로고
    • Histone H4-related osteogenic growth peptide (OGP): A novel circulating stimulator of osteoblastic activity
    • Bab I, Gazit D, Chorev M, Muhlrad A, Shteyer A, Greenberg Z, Namdar M, Kahn A (1992) Histone H4-related osteogenic growth peptide (OGP): a novel circulating stimulator of osteoblastic activity. EMBO J 11:1867-1873
    • (1992) EMBO J , vol.11 , pp. 1867-1873
    • Bab, I.1    Gazit, D.2    Chorev, M.3    Muhlrad, A.4    Shteyer, A.5    Greenberg, Z.6    Namdar, M.7    Kahn, A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.