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Volumn 363, Issue 1-2, 2005, Pages 15-23

Acetylation and deacetylation of non-histone proteins

Author keywords

HATs; HDACs; Post translational modification

Indexed keywords

ALPHA TUBULIN; ANDROGEN RECEPTOR; CELL NUCLEUS RECEPTOR; E1A PROTEIN; ERYTHROID KRUPPEL LIKE FACTOR; ESTROGEN RECEPTOR; HEAT SHOCK PROTEIN 90; HEPATITIS DELTA ANTIGEN; HISTONE ACETYLTRANSFERASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KARYOPHERIN ALPHA; KU ANTIGEN; MYC PROTEIN; MYOD PROTEIN; PROTEIN; PROTEIN P53; RNA BINDING PROTEIN; SMAD7 PROTEIN; STAT3 PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR E2F1; TRANSCRIPTION FACTOR E2F2; TRANSCRIPTION FACTOR E2F3; TRANSCRIPTION FACTOR GATA 1; TRANSCRIPTION FACTOR GATA 2; TRANSCRIPTION FACTOR GATA 3; TRANSCRIPTION FACTOR YY1; UNCLASSIFIED DRUG;

EID: 28044471827     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2005.09.010     Document Type: Review
Times cited : (1368)

References (93)
  • 1
    • 0013857650 scopus 로고    scopus 로고
    • Structural modifications of histones and their possible role in the regulation of ribonucleic acid synthesis
    • V.G. Allfrey Structural modifications of histones and their possible role in the regulation of ribonucleic acid synthesis Proc. Can. Cancer Res. Conf. 6 1996 313 335
    • (1996) Proc. Can. Cancer Res. Conf. , vol.6 , pp. 313-335
    • Allfrey, V.G.1
  • 2
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • V.G. Allfrey, R. Faulkner, and A.E. Mirsky Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis Proc. Natl. Acad. Sci. U. S. A. 51 1964 786 794
    • (1964) Proc. Natl. Acad. Sci. U. S. A. , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 3
    • 22844432021 scopus 로고    scopus 로고
    • Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: A novel basis of antileukemia activity of histone deacetylase inhibitors
    • P. Bali Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis of antileukemia activity of histone deacetylase inhibitors J. Biol. Chem. 280 2005 26729 26734
    • (2005) J. Biol. Chem. , vol.280 , pp. 26729-26734
    • Bali, P.1
  • 4
    • 0034177669 scopus 로고    scopus 로고
    • Acetylation of importin-alpha nuclear import factors by CBP/p300
    • A.J. Bannister, E.A. Miska, D. Gorlich, and T. Kouzarides Acetylation of importin-alpha nuclear import factors by CBP/p300 Curr. Biol. 10 2000 467 470
    • (2000) Curr. Biol. , vol.10 , pp. 467-470
    • Bannister, A.J.1    Miska, E.A.2    Gorlich, D.3    Kouzarides, T.4
  • 5
    • 2942657482 scopus 로고    scopus 로고
    • Ubiquitin-dependent degradation of p73 is inhibited by PML
    • F. Bernassola Ubiquitin-dependent degradation of p73 is inhibited by PML J. Exp. Med. 199 2004 1545 1557
    • (2004) J. Exp. Med. , vol.199 , pp. 1545-1557
    • Bernassola, F.1
  • 6
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • J. Boyes, P. Byfield, Y. Nakatani, and V. Ogryzko Regulation of activity of the transcription factor GATA-1 by acetylation Nature 396 1998 594 598
    • (1998) Nature , vol.396 , pp. 594-598
    • Boyes, J.1    Byfield, P.2    Nakatani, Y.3    Ogryzko, V.4
  • 7
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • J.E. Brownell 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
  • 8
    • 0032814140 scopus 로고    scopus 로고
    • Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins
    • M. Bustin Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins Mol. Cell. Biol. 19 1999 5237 5246
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5237-5246
    • Bustin, M.1
  • 9
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • M. Bustin, and R. Reeves High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function Prog. Nucleic Acid Res. Mol. Biol. 54 1996 35 100
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 10
    • 0025323711 scopus 로고
    • Structural features of the HMG chromosomal proteins and their genes
    • M. Bustin, D.A. Lehn, and D. Landsman Structural features of the HMG chromosomal proteins and their genes Biochim. Biophys. Acta 1049 1990 231 243
    • (1990) Biochim. Biophys. Acta , vol.1049 , pp. 231-243
    • Bustin, M.1    Lehn, D.A.2    Landsman, D.3
  • 12
    • 0035048250 scopus 로고    scopus 로고
    • Unanticipated repression function linked to erythroid Kruppel-like factor
    • X. Chen, and J.J. Bieker Unanticipated repression function linked to erythroid Kruppel-like factor Mol. Cell. Biol. 21 2001 3118 3125
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3118-3125
    • Chen, X.1    Bieker, J.J.2
  • 13
    • 8644288177 scopus 로고    scopus 로고
    • Stage-specific repression by the EKLF transcriptional activator
    • X. Chen, and J.J. Bieker Stage-specific repression by the EKLF transcriptional activator Mol. Cell. Biol. 24 2004 10416 10424
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10416-10424
    • Chen, X.1    Bieker, J.J.2
  • 14
    • 0035979737 scopus 로고    scopus 로고
    • Duration of nuclear NF-kappaB action regulated by reversible acetylation
    • L. Chen, W. Fischle, E. Verdin, and W.C. Greene Duration of nuclear NF-kappaB action regulated by reversible acetylation Science 293 2001 1653 1657
    • (2001) Science , vol.293 , pp. 1653-1657
    • Chen, L.1    Fischle, W.2    Verdin, E.3    Greene, W.C.4
  • 15
    • 0037011056 scopus 로고    scopus 로고
    • Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB
    • L.F. Chen, Y. Mu, and W.C. Greene Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB EMBO J. 21 2002 6539 6548
    • (2002) EMBO J. , vol.21 , pp. 6539-6548
    • Chen, L.F.1    Mu, Y.2    Greene, W.C.3
  • 16
    • 12144286529 scopus 로고    scopus 로고
    • Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis
    • H.Y. Cohen Acetylation of the C terminus of Ku70 by CBP and PCAF controls Bax-mediated apoptosis Mol. Cell 13 2004 627 638
    • (2004) Mol. Cell , vol.13 , pp. 627-638
    • Cohen, H.Y.1
  • 18
    • 18244408596 scopus 로고    scopus 로고
    • DNA damage-dependent acetylation of p73 dictates the selective activation of apoptotic target genes
    • A. Costanzo DNA damage-dependent acetylation of p73 dictates the selective activation of apoptotic target genes Mol. Cell 9 2002 175 186
    • (2002) Mol. Cell , vol.9 , pp. 175-186
    • Costanzo, A.1
  • 19
    • 10844286471 scopus 로고    scopus 로고
    • Phosphorylation of estrogen receptor alpha blocks its acetylation and regulates estrogen sensitivity
    • Y. Cui, M. Zhang, R. Pestell, E.M. Curran, W.V. Welshons, and S.A. Fuqua Phosphorylation of estrogen receptor alpha blocks its acetylation and regulates estrogen sensitivity Cancer Res. 64 2004 9199 9208
    • (2004) Cancer Res. , vol.64 , pp. 9199-9208
    • Cui, Y.1    Zhang, M.2    Pestell, R.3    Curran, E.M.4    Welshons, W.V.5    Fuqua, S.A.6
  • 20
    • 4444277135 scopus 로고    scopus 로고
    • In vivo posttranslational modifications of the high mobility group A1a proteins in breast cancer cells of differing metastatic potential
    • D.D. Edberg, J.E. Bruce, W.F. Siems, and R. Reeves In vivo posttranslational modifications of the high mobility group A1a proteins in breast cancer cells of differing metastatic potential Biochemistry 43 2004 11500 11515
    • (2004) Biochemistry , vol.43 , pp. 11500-11515
    • Edberg, D.D.1    Bruce, J.E.2    Siems, W.F.3    Reeves, R.4
  • 21
    • 0034881964 scopus 로고    scopus 로고
    • Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment
    • J.M. Espinosa, and B.M. Emerson Transcriptional regulation by p53 through intrinsic DNA/chromatin binding and site-directed cofactor recruitment Mol. Cell 8 2001 57 69
    • (2001) Mol. Cell , vol.8 , pp. 57-69
    • Espinosa, J.M.1    Emerson, B.M.2
  • 22
    • 0034617058 scopus 로고    scopus 로고
    • P300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation
    • M. Fu p300 and p300/cAMP-response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation J. Biol. Chem. 275 2000 20853 20860
    • (2000) J. Biol. Chem. , vol.275 , pp. 20853-20860
    • Fu, M.1
  • 23
    • 18344371150 scopus 로고    scopus 로고
    • Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function
    • M. Fu Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function Mol. Cell. Biol. 22 2002 3373 3388
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3373-3388
    • Fu, M.1
  • 24
    • 0043244921 scopus 로고    scopus 로고
    • Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
    • M. Fulco Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state Mol. Cell 12 2003 51 62
    • (2003) Mol. Cell , vol.12 , pp. 51-62
    • Fulco, M.1
  • 25
    • 0037205476 scopus 로고    scopus 로고
    • Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions
    • S.C. Galasinski, K.A. Resing, J.A. Goodrich, and N.G. Ahn Phosphatase inhibition leads to histone deacetylases 1 and 2 phosphorylation and disruption of corepressor interactions J. Biol. Chem. 277 2002 19618 19626
    • (2002) J. Biol. Chem. , vol.277 , pp. 19618-19626
    • Galasinski, S.C.1    Resing, K.A.2    Goodrich, J.A.3    Ahn, N.G.4
  • 26
    • 0037135566 scopus 로고    scopus 로고
    • Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor
    • L. Gaughan, I.R. Logan, S. Cook, D.E. Neal, and C.N. Robson Tip60 and histone deacetylase 1 regulate androgen receptor activity through changes to the acetylation status of the receptor J. Biol. Chem. 277 2002 25904 25913
    • (2002) J. Biol. Chem. , vol.277 , pp. 25904-25913
    • Gaughan, L.1    Logan, I.R.2    Cook, S.3    Neal, D.E.4    Robson, C.N.5
  • 27
    • 13744257306 scopus 로고    scopus 로고
    • Regulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylation
    • L. Gaughan, I.R. Logan, D.E. Neal, and C.N. Robson Regulation of androgen receptor and histone deacetylase 1 by Mdm2-mediated ubiquitylation Nucleic Acids Res. 33 2005 13 26
    • (2005) Nucleic Acids Res. , vol.33 , pp. 13-26
    • Gaughan, L.1    Logan, I.R.2    Neal, D.E.3    Robson, C.N.4
  • 28
    • 0037444225 scopus 로고    scopus 로고
    • Acetylation regulates subcellular localization of the Wnt signaling nuclear effector POP-1
    • F. Gay Acetylation regulates subcellular localization of the Wnt signaling nuclear effector POP-1 Genes Dev. 17 2003 717 722
    • (2003) Genes Dev. , vol.17 , pp. 717-722
    • Gay, F.1
  • 30
    • 0036753547 scopus 로고    scopus 로고
    • Control of Smad7 stability by competition between acetylation and ubiquitination
    • E. Gronroos, U. Hellman, C.H. Heldin, and J. Ericsson Control of Smad7 stability by competition between acetylation and ubiquitination Mol. Cell 10 2002 483 493
    • (2002) Mol. Cell , vol.10 , pp. 483-493
    • Gronroos, E.1    Hellman, U.2    Heldin, C.H.3    Ericsson, J.4
  • 31
    • 0030797585 scopus 로고    scopus 로고
    • Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
    • W. Gu, and R.G. Roeder Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain Cell 90 1997 595 606
    • (1997) Cell , vol.90 , pp. 595-606
    • Gu, W.1    Roeder, R.G.2
  • 33
    • 0037161744 scopus 로고    scopus 로고
    • HDAC6 is a microtubule-associated deacetylase
    • C. Hubbert HDAC6 is a microtubule-associated deacetylase Nature 417 2002 455 458
    • (2002) Nature , vol.417 , pp. 455-458
    • Hubbert, C.1
  • 34
    • 3142711538 scopus 로고    scopus 로고
    • Specific role for p300/CREB-binding protein-associated factor activity in E2F1 stabilization in response to DNA damage
    • A. Ianari, R. Gallo, M. Palma, E. Alesse, and A. Gulino Specific role for p300/CREB-binding protein-associated factor activity in E2F1 stabilization in response to DNA damage J. Biol. Chem. 279 2004 30830 30835
    • (2004) J. Biol. Chem. , vol.279 , pp. 30830-30835
    • Ianari, A.1    Gallo, R.2    Palma, M.3    Alesse, E.4    Gulino, A.5
  • 35
    • 0037112901 scopus 로고    scopus 로고
    • MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation
    • A. Ito MDM2-HDAC1-mediated deacetylation of p53 is required for its degradation EMBO J. 21 2002 6236 6245
    • (2002) EMBO J. , vol.21 , pp. 6236-6245
    • Ito, A.1
  • 36
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation
    • J.W. Jeong Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation Cell 111 2002 709 720
    • (2002) Cell , vol.111 , pp. 709-720
    • Jeong, J.W.1
  • 37
    • 0034617261 scopus 로고    scopus 로고
    • Histone deacetylases specifically down-regulate p53-dependent gene activation
    • L.J. Juan Histone deacetylases specifically down-regulate p53-dependent gene activation J. Biol. Chem. 275 2000 20436 20443
    • (2000) J. Biol. Chem. , vol.275 , pp. 20436-20443
    • Juan, L.J.1
  • 38
    • 0142122363 scopus 로고    scopus 로고
    • Overexpression of histone deacetylase HDAC1 modulates breast cancer progression by negative regulation of estrogen receptor alpha
    • H. Kawai, H. Li, S. Avraham, S. Jiang, and H.K. Avraham Overexpression of histone deacetylase HDAC1 modulates breast cancer progression by negative regulation of estrogen receptor alpha Int. J. Cancer 107 2003 353 358
    • (2003) Int. J. Cancer , vol.107 , pp. 353-358
    • Kawai, H.1    Li, H.2    Avraham, S.3    Jiang, S.4    Avraham, H.K.5
  • 39
    • 0037462725 scopus 로고    scopus 로고
    • Post-activation turn-off of NF-kappaB-dependent transcription is regulated by acetylation of p65
    • R. Kiernan Post-activation turn-off of NF-kappaB-dependent transcription is regulated by acetylation of p65 J. Biol. Chem. 278 2003 2758 2766
    • (2003) J. Biol. Chem. , vol.278 , pp. 2758-2766
    • Kiernan, R.1
  • 40
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • T. Kouzarides Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19 2000 1176 1179
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 41
    • 21144444486 scopus 로고    scopus 로고
    • HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor
    • J.J. Kovacs HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor Mol. Cell 18 2005 601 607
    • (2005) Mol. Cell , vol.18 , pp. 601-607
    • Kovacs, J.J.1
  • 42
    • 0021993649 scopus 로고
    • Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine
    • S.W. L'Hernault, and J.L. Rosenbaum Chlamydomonas alpha-tubulin is posttranslationally modified by acetylation on the epsilon-amino group of a lysine Biochemistry 24 1985 473 478
    • (1985) Biochemistry , vol.24 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 43
    • 0029004774 scopus 로고
    • Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300
    • J.S. Lee Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300 Genes Dev. 9 1995 1188 1198
    • (1995) Genes Dev. , vol.9 , pp. 1188-1198
    • Lee, J.S.1
  • 44
    • 0037050744 scopus 로고    scopus 로고
    • Modulation of HMG-N2 binding to chromatin by butyrate-induced acetylation in human colon adenocarcinoma cells
    • H. Luhrs Modulation of HMG-N2 binding to chromatin by butyrate-induced acetylation in human colon adenocarcinoma cells Int. J. Cancer 97 2002 567 573
    • (2002) Int. J. Cancer , vol.97 , pp. 567-573
    • Luhrs, H.1
  • 45
    • 0034676439 scopus 로고    scopus 로고
    • Deacetylation of p53 modulates its effect on cell growth and apoptosis
    • J. Luo, F. Su, D. Chen, A. Shiloh, and W. Gu Deacetylation of p53 modulates its effect on cell growth and apoptosis Nature 408 2000 377 381
    • (2000) Nature , vol.408 , pp. 377-381
    • Luo, J.1    Su, F.2    Chen, D.3    Shiloh, A.4    Gu, W.5
  • 46
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • J. Luo Negative control of p53 by Sir2alpha promotes cell survival under stress Cell 107 2001 137 148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1
  • 48
    • 0037064068 scopus 로고    scopus 로고
    • Acetylation of the adenovirus-transforming protein E1A determines nuclear localization by disrupting association with importin-alpha
    • D.L. Madison, P. Yaciuk, R.P. Kwok, and J.R. Lundblad Acetylation of the adenovirus-transforming protein E1A determines nuclear localization by disrupting association with importin-alpha J. Biol. Chem. 277 2002 38755 38763
    • (2002) J. Biol. Chem. , vol.277 , pp. 38755-38763
    • Madison, D.L.1    Yaciuk, P.2    Kwok, R.P.3    Lundblad, J.R.4
  • 49
    • 0037452764 scopus 로고    scopus 로고
    • MyoD is functionally linked to the silencing of a muscle-specific regulatory gene prior to skeletal myogenesis
    • A. Mal, and M.L. Harter MyoD is functionally linked to the silencing of a muscle-specific regulatory gene prior to skeletal myogenesis Proc. Natl. Acad. Sci. U. S. A. 100 2003 1735 1739
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1735-1739
    • Mal, A.1    Harter, M.L.2
  • 50
    • 0035794552 scopus 로고    scopus 로고
    • A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: Inhibition of the myogenic program
    • A. Mal, M. Sturniolo, R.L. Schiltz, M.K. Ghosh, and M.L. Harter A role for histone deacetylase HDAC1 in modulating the transcriptional activity of MyoD: inhibition of the myogenic program EMBO J. 20 2001 1739 1753
    • (2001) EMBO J. , vol.20 , pp. 1739-1753
    • Mal, A.1    Sturniolo, M.2    Schiltz, R.L.3    Ghosh, M.K.4    Harter, M.L.5
  • 52
    • 0022452231 scopus 로고
    • The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules
    • H. Maruta, K. Greer, and J.L. Rosenbaum The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules J. Cell Biol. 103 1986 571 579
    • (1986) J. Cell Biol. , vol.103 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 54
    • 12244295468 scopus 로고    scopus 로고
    • In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation
    • A. Matsuyama In vivo destabilization of dynamic microtubules by HDAC6-mediated deacetylation EMBO J. 21 2002 6820 6831
    • (2002) EMBO J. , vol.21 , pp. 6820-6831
    • Matsuyama, A.1
  • 55
    • 84983719289 scopus 로고    scopus 로고
    • The small delta antigen of hepatitis delta virus is an acetylated protein and acetylation of lysine 72 may influence its cellular localization and viral RNA synthesis
    • J.J. Mu The small delta antigen of hepatitis delta virus is an acetylated protein and acetylation of lysine 72 may influence its cellular localization and viral RNA synthesis Virology 319 2004 60 70
    • (2004) Virology , vol.319 , pp. 60-70
    • Mu, J.J.1
  • 56
    • 0032186185 scopus 로고    scopus 로고
    • Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome
    • N. Munshi, M. Merika, J. Yie, K. Senger, G. Chen, and D. Thanos Acetylation of HMG I(Y) by CBP turns off IFN beta expression by disrupting the enhanceosome Mol. Cell 2 1998 457 467
    • (1998) Mol. Cell , vol.2 , pp. 457-467
    • Munshi, N.1    Merika, M.2    Yie, J.3    Senger, K.4    Chen, G.5    Thanos, D.6
  • 58
    • 0033215387 scopus 로고    scopus 로고
    • Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a
    • M. Murphy Transcriptional repression by wild-type p53 utilizes histone deacetylases, mediated by interaction with mSin3a Genes Dev. 13 1999 2490 2501
    • (1999) Genes Dev. , vol.13 , pp. 2490-2501
    • Murphy, M.1
  • 59
    • 2342569733 scopus 로고    scopus 로고
    • Acetylation regulates the differentiation-specific functions of the retinoblastoma protein
    • D.X. Nguyen, L.A. Baglia, S.M. Huang, C.M. Baker, and D.J. McCance Acetylation regulates the differentiation-specific functions of the retinoblastoma protein EMBO J. 23 2004 1609 1618
    • (2004) EMBO J. , vol.23 , pp. 1609-1618
    • Nguyen, D.X.1    Baglia, L.A.2    Huang, S.M.3    Baker, C.M.4    McCance, D.J.5
  • 60
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • B.J. North, B.L. Marshall, M.T. Borra, J.M. Denu, and E. Verdin The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase Mol. Cell 11 2003 437 444
    • (2003) Mol. Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 61
    • 0035496915 scopus 로고    scopus 로고
    • Histone deacetylase 3 associates with and represses the transcription factor GATA-2
    • Y. Ozawa Histone deacetylase 3 associates with and represses the transcription factor GATA-2 Blood 98 2001 2116 2123
    • (2001) Blood , vol.98 , pp. 2116-2123
    • Ozawa, Y.1
  • 62
    • 1542297718 scopus 로고    scopus 로고
    • In vitro acetylation of HMGB-1 and -2 proteins by CBP: The role of the acidic tail
    • E. Pasheva In vitro acetylation of HMGB-1 and -2 proteins by CBP: the role of the acidic tail Biochemistry 43 2004 2935 2940
    • (2004) Biochemistry , vol.43 , pp. 2935-2940
    • Pasheva, E.1
  • 63
    • 10044262126 scopus 로고    scopus 로고
    • The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60
    • J.H. Patel The c-MYC oncoprotein is a substrate of the acetyltransferases hGCN5/PCAF and TIP60 Mol. Cell. Biol. 24 2004 10826 10834
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10826-10834
    • Patel, J.H.1
  • 64
    • 0038142184 scopus 로고    scopus 로고
    • Differential regulation of E2F1 apoptotic target genes in response to DNA damage
    • N. Pediconi Differential regulation of E2F1 apoptotic target genes in response to DNA damage Nat. Cell Biol. 5 2003 552 558
    • (2003) Nat. Cell Biol. , vol.5 , pp. 552-558
    • Pediconi, N.1
  • 65
    • 0035977014 scopus 로고    scopus 로고
    • Acetylation of MyoD by p300 requires more than its histone acetyltransferase domain
    • A. Polesskaya, and A. Harel-Bellan Acetylation of MyoD by p300 requires more than its histone acetyltransferase domain J. Biol. Chem. 276 2001 44502 44503
    • (2001) J. Biol. Chem. , vol.276 , pp. 44502-44503
    • Polesskaya, A.1    Harel-Bellan, A.2
  • 66
    • 0034602180 scopus 로고    scopus 로고
    • CREB-binding Protein/p300 activates MyoD by acetylation
    • A. Polesskaya CREB-binding Protein/p300 activates MyoD by acetylation J. Biol. Chem. 275 2000 34359 34364
    • (2000) J. Biol. Chem. , vol.275 , pp. 34359-34364
    • Polesskaya, A.1
  • 67
    • 0034711184 scopus 로고    scopus 로고
    • N-alpha -terminal acetylation of eukaryotic proteins
    • B. Polevoda, and F. Sherman N-alpha -terminal acetylation of eukaryotic proteins J. Biol. Chem. 275 2000 36479 36482
    • (2000) J. Biol. Chem. , vol.275 , pp. 36479-36482
    • Polevoda, B.1    Sherman, F.2
  • 68
    • 0034724166 scopus 로고    scopus 로고
    • Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis
    • S.E. Salghetti, M. Muratani, H. Wijnen, B. Futcher, and W.P. Tansey Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis Proc. Natl. Acad. Sci. U. S. A. 97 2000 3118 3123
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3118-3123
    • Salghetti, S.E.1    Muratani, M.2    Wijnen, H.3    Futcher, B.4    Tansey, W.P.5
  • 69
    • 0033231604 scopus 로고    scopus 로고
    • Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program
    • V. Sartorelli Acetylation of MyoD directed by PCAF is necessary for the execution of the muscle program Mol. Cell 4 1999 725 734
    • (1999) Mol. Cell , vol.4 , pp. 725-734
    • Sartorelli, V.1
  • 70
    • 0023608861 scopus 로고
    • Posttranslational modification and microtubule stability
    • E. Schulze, D.J. Asai, J.C. Bulinski, and M. Kirschner Posttranslational modification and microtubule stability J. Cell Biol. 105 1987 2167 2177
    • (1987) J. Cell Biol. , vol.105 , pp. 2167-2177
    • Schulze, E.1    Asai, D.J.2    Bulinski, J.C.3    Kirschner, M.4
  • 72
    • 0030941901 scopus 로고    scopus 로고
    • Everything you have ever wanted to know about Yin Yang 1
    • Y. Shi, J.S. Lee, and K.M. Galvin Everything you have ever wanted to know about Yin Yang 1 Biochim. Biophys. Acta 1332 1997 F49 F66
    • (1997) Biochim. Biophys. Acta , vol.1332
    • Shi, Y.1    Lee, J.S.2    Galvin, K.M.3
  • 73
    • 20444474176 scopus 로고    scopus 로고
    • The balance between acetylation and deacetylation controls Smad7 stability
    • M. Simonsson, C.H. Heldin, J. Ericsson, and E. Gronroos The balance between acetylation and deacetylation controls Smad7 stability J. Biol. Chem. 280 2005 21797 21803
    • (2005) J. Biol. Chem. , vol.280 , pp. 21797-21803
    • Simonsson, M.1    Heldin, C.H.2    Ericsson, J.3    Gronroos, E.4
  • 74
    • 0018801554 scopus 로고
    • Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1
    • R. Sterner, G. Vidali, and V.G. Allfrey Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in HMG-1 J. Biol. Chem. 254 1979 11577 11583
    • (1979) J. Biol. Chem. , vol.254 , pp. 11577-11583
    • Sterner, R.1    Vidali, G.2    Allfrey, V.G.3
  • 75
    • 20844447169 scopus 로고    scopus 로고
    • Regulation of human SRY subcellular distribution by its acetylation/deacetylation
    • L. Thevenet Regulation of human SRY subcellular distribution by its acetylation/deacetylation EMBO J. 23 2004 3336 3345
    • (2004) EMBO J. , vol.23 , pp. 3336-3345
    • Thevenet, L.1
  • 76
    • 0032819331 scopus 로고    scopus 로고
    • Unlocking the mechanisms of transcription factor YY1: Are chromatin modifying enzymes the key?
    • M.J. Thomas, and E. Seto Unlocking the mechanisms of transcription factor YY1: are chromatin modifying enzymes the key? Gene 236 1999 197 208
    • (1999) Gene , vol.236 , pp. 197-208
    • Thomas, M.J.1    Seto, E.2
  • 77
    • 0035281548 scopus 로고    scopus 로고
    • HMG1 and 2, and related 'architectural' DNA-binding proteins
    • J.O. Thomas, and A.A. Travers HMG1 and 2, and related 'architectural' DNA-binding proteins Trends Biochem. Sci. 26 2001 167 174
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 167-174
    • Thomas, J.O.1    Travers, A.A.2
  • 78
    • 0035913903 scopus 로고    scopus 로고
    • HSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
    • H. Vaziri hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase Cell 107 2001 149 159
    • (2001) Cell , vol.107 , pp. 149-159
    • Vaziri, H.1
  • 79
    • 0014430407 scopus 로고
    • Chemical studies of histone acetylation. the distribution of epsilon-N-acetyllysine in calf thymus histones
    • G. Vidali, E.L. Gershey, and V.G. Allfrey Chemical studies of histone acetylation. The distribution of epsilon-N-acetyllysine in calf thymus histones J. Biol. Chem. 243 1968 6361 6366
    • (1968) J. Biol. Chem. , vol.243 , pp. 6361-6366
    • Vidali, G.1    Gershey, E.L.2    Allfrey, V.G.3
  • 80
    • 0242637101 scopus 로고    scopus 로고
    • Direct acetylation of the estrogen receptor alpha hinge region by p300 regulates transactivation and hormone sensitivity
    • C. Wang Direct acetylation of the estrogen receptor alpha hinge region by p300 regulates transactivation and hormone sensitivity J. Biol. Chem. 276 2001 18375 18383
    • (2001) J. Biol. Chem. , vol.276 , pp. 18375-18383
    • Wang, C.1
  • 81
    • 9144266386 scopus 로고    scopus 로고
    • AMP-activated protein kinase-regulated phosphorylation and acetylation of importin alpha1: Involvement in the nuclear import of RNA-binding protein HuR
    • W. Wang AMP-activated protein kinase-regulated phosphorylation and acetylation of importin alpha1: involvement in the nuclear import of RNA-binding protein HuR J. Biol. Chem. 279 2004 48376 48388
    • (2004) J. Biol. Chem. , vol.279 , pp. 48376-48388
    • Wang, W.1
  • 82
    • 15744385061 scopus 로고    scopus 로고
    • Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation
    • R. Wang, P. Cherukuri, and J. Luo Activation of Stat3 sequence-specific DNA binding and transcription by p300/CREB-binding protein-mediated acetylation J. Biol. Chem. 280 2005 11528 11534
    • (2005) J. Biol. Chem. , vol.280 , pp. 11528-11534
    • Wang, R.1    Cherukuri, P.2    Luo, J.3
  • 83
    • 0346688568 scopus 로고    scopus 로고
    • Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation
    • K. Watamoto Altered interaction of HDAC5 with GATA-1 during MEL cell differentiation Oncogene 22 2003 9176 9184
    • (2003) Oncogene , vol.22 , pp. 9176-9184
    • Watamoto, K.1
  • 84
    • 0034282480 scopus 로고    scopus 로고
    • Acetylation of GATA-3 affects T-cell survival and homing to secondary lymphoid organs
    • T. Yamagata Acetylation of GATA-3 affects T-cell survival and homing to secondary lymphoid organs EMBO J. 19 2000 4676 4687
    • (2000) EMBO J. , vol.19 , pp. 4676-4687
    • Yamagata, T.1
  • 85
    • 0029850458 scopus 로고    scopus 로고
    • Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3
    • W.M. Yang, C. Inouye, Y. Zeng, D. Bearss, and E. Seto Transcriptional repression by YY1 is mediated by interaction with a mammalian homolog of the yeast global regulator RPD3 Proc. Natl. Acad. Sci. U. S. A. 93 1996 12845 12850
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12845-12850
    • Yang, W.M.1    Inouye, C.2    Zeng, Y.3    Bearss, D.4    Seto, E.5
  • 86
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • W.M. Yang, Y.L. Yao, J.M. Sun, J.R. Davie, and E. Seto Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family J. Biol. Chem. 272 1997 28001 28007
    • (1997) J. Biol. Chem. , vol.272 , pp. 28001-28007
    • Yang, W.M.1    Yao, Y.L.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5
  • 87
    • 0034905085 scopus 로고    scopus 로고
    • Regulation of transcription factor YY1 by acetylation and deacetylation
    • Y.L. Yao, W.M. Yang, and E. Seto Regulation of transcription factor YY1 by acetylation and deacetylation Mol. Cell. Biol. 21 2001 5979 5991
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5979-5991
    • Yao, Y.L.1    Yang, W.M.2    Seto, E.3
  • 88
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • F. Yeung Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase EMBO J. 23 2004 2369 2380
    • (2004) EMBO J. , vol.23 , pp. 2369-2380
    • Yeung, F.1
  • 89
    • 12244251445 scopus 로고    scopus 로고
    • Stat3 dimerization regulated by reversible acetylation of a single lysine residue
    • Z.L. Yuan, Y.J. Guan, D. Chatterjee, and Y.E. Chin Stat3 dimerization regulated by reversible acetylation of a single lysine residue Science 307 2005 269 273
    • (2005) Science , vol.307 , pp. 269-273
    • Yuan, Z.L.1    Guan, Y.J.2    Chatterjee, D.3    Chin, Y.E.4
  • 90
    • 0032544123 scopus 로고    scopus 로고
    • Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases
    • W. Zhang, and J.J. Bieker Acetylation and modulation of erythroid Kruppel-like factor (EKLF) activity by interaction with histone acetyltransferases Proc. Natl. Acad. Sci. U. S. A. 95 1998 9855 9860
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 9855-9860
    • Zhang, W.1    Bieker, J.J.2
  • 91
    • 0034687687 scopus 로고    scopus 로고
    • Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP
    • Q. Zhang, H. Yao, N. Vo, and R.H. Goodman Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP Proc. Natl. Acad. Sci. U. S. A. 97 2000 14323 14328
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14323-14328
    • Zhang, Q.1    Yao, H.2    Vo, N.3    Goodman, R.H.4
  • 92
    • 0035099483 scopus 로고    scopus 로고
    • Site-specific acetylation by p300 or CREB binding protein regulates erythroid Kruppel-like factor transcriptional activity via its interaction with the SWI-SNF complex
    • W. Zhang, S. Kadam, B.M. Emerson, and J.J. Bieker Site-specific acetylation by p300 or CREB binding protein regulates erythroid Kruppel-like factor transcriptional activity via its interaction with the SWI-SNF complex Mol. Cell. Biol. 21 2001 2413 2422
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2413-2422
    • Zhang, W.1    Kadam, S.2    Emerson, B.M.3    Bieker, J.J.4
  • 93
    • 0037416151 scopus 로고    scopus 로고
    • HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo
    • Y. Zhang HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo EMBO J. 22 2003 1168 1179
    • (2003) EMBO J. , vol.22 , pp. 1168-1179
    • Zhang, Y.1


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