메뉴 건너뛰기




Volumn 111, Issue 6, 2002, Pages 771-778

Signaling network model of chromatin

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; HISTONE; MEMBRANE RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 0037074010     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)01196-0     Document Type: Review
Times cited : (341)

References (74)
  • 1
    • 0036850346 scopus 로고    scopus 로고
    • Deciphering the transcriptional histone acetylation code for a human gene
    • Agalioti T., Chen G., Thanos D. Deciphering the transcriptional histone acetylation code for a human gene. Cell. 111:2002;381-392.
    • (2002) Cell , vol.111 , pp. 381-392
    • Agalioti, T.1    Chen, G.2    Thanos, D.3
  • 2
    • 0036849262 scopus 로고    scopus 로고
    • Epigenetic consequences of nucleosome dynamics
    • Ahmad K., Henikoff S. Epigenetic consequences of nucleosome dynamics. Cell. 111:2002;281-284.
    • (2002) Cell , vol.111 , pp. 281-284
    • Ahmad, K.1    Henikoff, S.2
  • 3
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in regulation of RNA synthesis
    • Allfrey V.G., Faulkner R., Mirsky A.E. Acetylation and methylation of histones and their possible role in regulation of RNA synthesis. Proc. Natl. Acad. Sci. USA. 51:1964;786-794.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 6
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla U.S., Iyengar R. Emergent properties of networks of biological signaling pathways. Science. 283:1999;381-387.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 7
    • 0027192267 scopus 로고
    • Transcriptional silencing in yeast is associated with reduced nucleosome acetylation
    • Braunstein M., Rose A.B., Holmes S.G., Allis C.D., Broach J.R. Transcriptional silencing in yeast is associated with reduced nucleosome acetylation. Genes Dev. 7:1993;592-604.
    • (1993) Genes Dev. , vol.7 , pp. 592-604
    • Braunstein, M.1    Rose, A.B.2    Holmes, S.G.3    Allis, C.D.4    Broach, J.R.5
  • 8
    • 0029953722 scopus 로고    scopus 로고
    • Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern
    • Braunstein M., Sobel R.E., Allis C.D., Turner B.M., Broach J.R. Efficient transcriptional silencing in Saccharomyces cerevisiae requires a heterochromatin histone acetylation pattern. Mol. Cell. Biol. 16:1996;4349-4356.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4349-4356
    • Braunstein, M.1    Sobel, R.E.2    Allis, C.D.3    Turner, B.M.4    Broach, J.R.5
  • 9
    • 0035893240 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae
    • Briggs S.D., Bryk M., Strahl B.D., Cheung W.L., Davie J.K., Dent S.Y., Winston F., Allis C.D. Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev. 15:2001;3286-3295.
    • (2001) Genes Dev. , vol.15 , pp. 3286-3295
    • Briggs, S.D.1    Bryk, M.2    Strahl, B.D.3    Cheung, W.L.4    Davie, J.K.5    Dent, S.Y.6    Winston, F.7    Allis, C.D.8
  • 10
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell J.E., Zhou J., Ranalli T., Kobayashi R., Edmondson D.G., Roth S.Y., Allis C.D. Tetrahymena histone acetyltransferase A. a homolog to yeast Gcn5p linking histone acetylation to gene activation Cell. 84:1996;843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 12
    • 0037085264 scopus 로고    scopus 로고
    • Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3
    • Carmen A.A., Milne L., Grunstein M. Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3. J. Biol. Chem. 277:2002;4778-4781.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4778-4781
    • Carmen, A.A.1    Milne, L.2    Grunstein, M.3
  • 13
    • 0027515186 scopus 로고
    • Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast
    • Chan C.S., Botstein D. Isolation and characterization of chromosome-gain and increase-in-ploidy mutants in yeast. Genetics. 135:1993;677-691.
    • (1993) Genetics , vol.135 , pp. 677-691
    • Chan, C.S.1    Botstein, D.2
  • 15
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P., Allis C.D., Sassone-Corsi P. Signaling to chromatin through histone modifications. Cell. 103:2000;263-271.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 16
    • 0028589148 scopus 로고
    • Platelet-derived growth factor receptor signals
    • Claesson-Welsh L. Platelet-derived growth factor receptor signals. J. Biol. Chem. 269:1994;32023-32026.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32023-32026
    • Claesson-Welsh, L.1
  • 17
    • 0033617334 scopus 로고    scopus 로고
    • Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter
    • Cosma M.P., Tanaka T., Nasmyth K. Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter. Cell. 97:1999;299-311.
    • (1999) Cell , vol.97 , pp. 299-311
    • Cosma, M.P.1    Tanaka, T.2    Nasmyth, K.3
  • 18
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila Enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V. Drosophila Enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell. 111:2002;185-196.
    • (2002) Cell , vol.111 , pp. 185-196
    • Czermin, B.1    Melfi, R.2    McCabe, D.3    Seitz, V.4    Imhof, A.5    Pirrotta, V.6
  • 19
    • 0035890134 scopus 로고    scopus 로고
    • The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation
    • de la Barre A.E., Angelov D., Molla A., Dimitrov S. The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation. EMBO J. 20:2001;6383-6393.
    • (2001) EMBO J. , vol.20 , pp. 6383-6393
    • De la Barre, A.E.1    Angelov, D.2    Molla, A.3    Dimitrov, S.4
  • 21
    • 0025736044 scopus 로고
    • Yeast histone H4 N-terminal sequence is required for promoter activation in vivo
    • Durrin L.K., Mann R.K., Kayne P.S., Grunstein M. Yeast histone H4 N-terminal sequence is required for promoter activation in vivo. Cell. 65:1991;1023-1031.
    • (1991) Cell , vol.65 , pp. 1023-1031
    • Durrin, L.K.1    Mann, R.K.2    Kayne, P.S.3    Grunstein, M.4
  • 22
    • 0033001953 scopus 로고    scopus 로고
    • Diverse signaling pathways activated by growth factor receptors induce broadly overlapping, rather than independent, sets of genes
    • Fambrough D., McClure K., Kazlauskas A., Lander E.S. Diverse signaling pathways activated by growth factor receptors induce broadly overlapping, rather than independent, sets of genes. Cell. 97:1999;727-741.
    • (1999) Cell , vol.97 , pp. 727-741
    • Fambrough, D.1    McClure, K.2    Kazlauskas, A.3    Lander, E.S.4
  • 23
    • 0036532226 scopus 로고    scopus 로고
    • Self-perpetuating states in signal transduction: Positive feedback, double-negative feedback and bistability
    • Ferrell J.E. Jr. Self-perpetuating states in signal transduction. positive feedback, double-negative feedback and bistability Curr. Opin. Cell Biol. 14:2002;140-148.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 140-148
    • Ferrell J.E., Jr.1
  • 25
    • 0034676456 scopus 로고    scopus 로고
    • Feedback control of intercellular signalling in development
    • Freeman M. Feedback control of intercellular signalling in development. Nature. 408:2000;313-319.
    • (2000) Nature , vol.408 , pp. 313-319
    • Freeman, M.1
  • 26
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye R.A. Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273:2000;793-798.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 27
    • 0036532235 scopus 로고    scopus 로고
    • Heterochromatin: New possibilities for the inheritance of structure
    • Grewal S.I., Elgin S.C. Heterochromatin. new possibilities for the inheritance of structure Curr. Opin. Genet. Dev. 12:2002;178-187.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 178-187
    • Grewal, S.I.1    Elgin, S.C.2
  • 28
    • 0033609055 scopus 로고    scopus 로고
    • Three proteins define a class of human histone deacetylases related to yeast Hda1p
    • Grozinger C.M., Hassig C.A., Schreiber S.L. Three proteins define a class of human histone deacetylases related to yeast Hda1p. Proc. Natl. Acad. Sci. USA. 96:1999;4868-4873.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4868-4873
    • Grozinger, C.M.1    Hassig, C.A.2    Schreiber, S.L.3
  • 29
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature. 389:1997;349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 30
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • Hassan A.H., Prochasson P., Neely K.E., Galasinski S.C., Chandy M., Carrozza M.J., Workman J.L. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell. 111:2002;369-379.
    • (2002) Cell , vol.111 , pp. 369-379
    • Hassan, A.H.1    Prochasson, P.2    Neely, K.E.3    Galasinski, S.C.4    Chandy, M.5    Carrozza, M.J.6    Workman, J.L.7
  • 31
    • 0036312462 scopus 로고    scopus 로고
    • Trans-tail histone modifications: Wedge or bridge?
    • Henry K.W., Berger S.L. Trans-tail histone modifications. wedge or bridge? Nat. Struct. Biol. 9:2002;565-566.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 565-566
    • Henry, K.W.1    Berger, S.L.2
  • 32
    • 0034604354 scopus 로고    scopus 로고
    • Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes
    • Hsu J.Y., Sun Z.W., Li X., Reuben M., Tatchell K., Bishop D.K., Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F.et al. Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase and Glc7/PP1 phosphatase in budding yeast and nematodes. Cell. 102:2000;279-291.
    • (2000) Cell , vol.102 , pp. 279-291
    • Hsu, J.Y.1    Sun, Z.W.2    Li, X.3    Reuben, M.4    Tatchell, K.5    Bishop, D.K.6    Grushcow, J.M.7    Brame, C.J.8    Caldwell, J.A.9    Hunt, D.F.10
  • 34
    • 0034387879 scopus 로고    scopus 로고
    • Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
    • Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E. Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J. Mol. Biol. 304:2000;355-370.
    • (2000) J. Mol. Biol. , vol.304 , pp. 355-370
    • Hudson, B.P.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 35
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAFII250 double bromodomain module
    • Jacobson R.H., Ladurner A.G., King D.S., Tjian R. Structure and function of a human TAFII250 double bromodomain module. Science. 288:2000;1422-1425.
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H.1    Ladurner, A.G.2    King, D.S.3    Tjian, R.4
  • 36
    • 0034995566 scopus 로고    scopus 로고
    • Evolutionary correlation between linker histones and microtubular structures
    • Kaczanowski S., Jerzmanowski A. Evolutionary correlation between linker histones and microtubular structures. J. Mol. Evol. 53:2001;19-30.
    • (2001) J. Mol. Evol. , vol.53 , pp. 19-30
    • Kaczanowski, S.1    Jerzmanowski, A.2
  • 37
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer R.A., Sachsenmaier C., Cooper J.A., Soriano P. Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 18:1999;2459-2471.
    • (1999) EMBO J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 38
    • 0016211838 scopus 로고
    • Chromatin structure; Oligomers of the histones
    • Kornberg R.D., Thomas J.O. Chromatin structure; oligomers of the histones. Science. 184:1974;865-868.
    • (1974) Science , vol.184 , pp. 865-868
    • Kornberg, R.D.1    Thomas, J.O.2
  • 39
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides T. Acetylation. a regulatory modification to rival phosphorylation? EMBO J. 19:2000;1176-1179.
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 40
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein
    • Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D. Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 16:2002;2893-2905.
    • (2002) Genes Dev. , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 41
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature. 410:2001;116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 42
    • 0037163016 scopus 로고    scopus 로고
    • Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase
    • Lacoste N., Utley R.T., Hunter J., Poirier G.G., Cote J. Disruptor of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase. J. Biol. Chem. 277:2002;30421-30424.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30421-30424
    • Lacoste, N.1    Utley, R.T.2    Hunter, J.3    Poirier, G.G.4    Cote, J.5
  • 43
    • 0035964869 scopus 로고    scopus 로고
    • Correlation between histone lysine methylation and developmental changes at the chicken beta-globin locus
    • Litt M.D., Simpson M., Gaszner M., Allis C.D., Felsenfeld G. Correlation between histone lysine methylation and developmental changes at the chicken beta-globin locus. Science. 293:2001;2453-2455.
    • (2001) Science , vol.293 , pp. 2453-2455
    • Litt, M.D.1    Simpson, M.2    Gaszner, M.3    Allis, C.D.4    Felsenfeld, G.5
  • 44
    • 0036787812 scopus 로고    scopus 로고
    • The tail does not always wag the dog
    • Luger K. The tail does not always wag the dog. Nat. Genet. 32:2002;221-222.
    • (2002) Nat. Genet. , vol.32 , pp. 221-222
    • Luger, K.1
  • 45
    • 0033214772 scopus 로고    scopus 로고
    • Chromosomal elements conferring epigenetic inheritance
    • Lyko F., Paro R. Chromosomal elements conferring epigenetic inheritance. Bioessays. 21:1999;824-832.
    • (1999) Bioessays , vol.21 , pp. 824-832
    • Lyko, F.1    Paro, R.2
  • 46
    • 0035854382 scopus 로고    scopus 로고
    • Accounting for specificity in receptor tyrosine kinase signaling
    • Madhani H.D. Accounting for specificity in receptor tyrosine kinase signaling. Cell. 106:2001;9-11.
    • (2001) Cell , vol.106 , pp. 9-11
    • Madhani, H.D.1
  • 48
    • 0030027488 scopus 로고    scopus 로고
    • Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction
    • Mohammadi M., Dikic I., Sorokin A., Burgess W.H., Jaye M., Schlessinger J. Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction. Mol. Cell. Biol. 16:1996;977-989.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 977-989
    • Mohammadi, M.1    Dikic, I.2    Sorokin, A.3    Burgess, W.H.4    Jaye, M.5    Schlessinger, J.6
  • 50
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng H.H., Feng Q., Wang H., Erdjument-Bromage H., Tempst P., Zhang Y., Struhl K. Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev. 16:2002;1518-1527.
    • (2002) Genes Dev. , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 51
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • Nishioka K., Chuikov S., Sarma K., Erdjument-Bromage H., Allis C.D., Tempst P., Reinberg D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev. 16:2002;479-489.
    • (2002) Genes Dev. , vol.16 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3    Erdjument-Bromage, H.4    Allis, C.D.5    Tempst, P.6    Reinberg, D.7
  • 52
    • 0030668324 scopus 로고    scopus 로고
    • SET1, a yeast member of the trithorax family, functions in transcriptional silencing and diverse cellular processes
    • Nislow C., Ray E., Pillus L. SET1, a yeast member of the trithorax family, functions in transcriptional silencing and diverse cellular processes. Mol. Biol. Cell. 8:1997;2421-2436.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2421-2436
    • Nislow, C.1    Ray, E.2    Pillus, L.3
  • 53
    • 0035839110 scopus 로고    scopus 로고
    • Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries
    • Noma K., Allis C.D., Grewal S.I. Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries. Science. 293:2001;1150-1155.
    • (2001) Science , vol.293 , pp. 1150-1155
    • Noma, K.1    Allis, C.D.2    Grewal, S.I.3
  • 54
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p
    • Owen D.J., Ornaghi P., Yang J.C., Lowe N., Evans P.R., Ballario P., Neuhaus D., Filetici P., Travers A.A. The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p. EMBO J. 19:2000;6141-6149.
    • (2000) EMBO J. , vol.19 , pp. 6141-6149
    • Owen, D.J.1    Ornaghi, P.2    Yang, J.C.3    Lowe, N.4    Evans, P.R.5    Ballario, P.6    Neuhaus, D.7    Filetici, P.8    Travers, A.A.9
  • 56
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell. 103:2000;211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 58
    • 0029079038 scopus 로고
    • Src phosphorylation of the epidermal growth factor receptor at novel sites mediates receptor interaction with Src and P85α
    • Stover D.R., Becker M., Liebetanz J., Lydon N.B. Src phosphorylation of the epidermal growth factor receptor at novel sites mediates receptor interaction with Src and P85α J. Biol. Chem. 270:1995;15591-15597.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15591-15597
    • Stover, D.R.1    Becker, M.2    Liebetanz, J.3    Lydon, N.B.4
  • 59
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., Allis C.D. The language of covalent histone modifications. Nature. 403:2000;41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 60
    • 0034839973 scopus 로고    scopus 로고
    • Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin
    • Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M. Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Mol. Cell. 8:2001;473-479.
    • (2001) Mol. Cell , vol.8 , pp. 473-479
    • Suka, N.1    Suka, Y.2    Carmen, A.A.3    Wu, J.4    Grunstein, M.5
  • 61
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun Z.W., Allis C.D. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature. 418:2002;104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 62
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J., Hassig C.A., Schreiber S.L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science. 272:1996;408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 63
    • 0035694785 scopus 로고    scopus 로고
    • Independent dynamic regulation of histone phosphorylation and acetylation during immediate-early gene induction
    • Thomson S., Clayton A.L., Mahadevan L.C. Independent dynamic regulation of histone phosphorylation and acetylation during immediate-early gene induction. Mol. Cell. 8:2001;1231-1241.
    • (2001) Mol. Cell , vol.8 , pp. 1231-1241
    • Thomson, S.1    Clayton, A.L.2    Mahadevan, L.C.3
  • 64
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner B.M. Histone acetylation and an epigenetic code. Bioessays. 22:2000;836-845.
    • (2000) Bioessays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 65
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner B.M. Cellular memory and the histone code. Cell. 111:2002;285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 66
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner B.M., Birley A.J., Lavender J. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell. 69:1992;375-384.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 67
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F., Gafken P.R., Gottschling D.E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell. 109:2002;745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 68
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P., Zhang Y. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol. Cell. 8:2001;1207-1217.
    • (2001) Mol. Cell , vol.8 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6    Zhang, Y.7
  • 69
    • 0033515426 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 is required for proper chromosome condensation and segregation
    • Wei Y., Yu L., Bowen J., Gorovsky M.A., Allis C.D. Phosphorylation of histone H3 is required for proper chromosome condensation and segregation. Cell. 97:1999;99-109.
    • (1999) Cell , vol.97 , pp. 99-109
    • Wei, Y.1    Yu, L.2    Bowen, J.3    Gorovsky, M.A.4    Allis, C.D.5
  • 70
    • 0033569641 scopus 로고    scopus 로고
    • Epigenetics: Regulation through repression
    • Wolffe A.P., Matzke M.A. Epigenetics. regulation through repression Science. 286:1999;481-486.
    • (1999) Science , vol.286 , pp. 481-486
    • Wolffe, A.P.1    Matzke, M.A.2
  • 71
    • 0037023681 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
    • Zegerman P., Canas B., Pappin D., Kouzarides T. Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J. Biol. Chem. 277:2002;11621-11624.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4
  • 72
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: An acetyl-lysine binding domain
    • Zeng L., Zhou M.M. Bromodomain. an acetyl-lysine binding domain FEBS Lett. 513:2002;124-128.
    • (2002) FEBS Lett. , vol.513 , pp. 124-128
    • Zeng, L.1    Zhou, M.M.2
  • 73
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang Y., Reinberg D. Transcription regulation by histone methylation. interplay between different covalent modifications of the core histone tails Genes Dev. 15:2001;2343-2360.
    • (2001) Genes Dev. , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 74
    • 0028875162 scopus 로고
    • Recognition and specificity in protein tyrosine kinase-mediated signalling
    • Zhou S., Cantley L.C. Recognition and specificity in protein tyrosine kinase-mediated signalling. Trends Biochem. Sci. 20:1995;470-475.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 470-475
    • Zhou, S.1    Cantley, L.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.