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Volumn 69, Issue 4, 2012, Pages 641-650

Chromatin affinity-precipitation using a small metabolic molecule: Its application to analysis of O-acetyl-ADP-ribose

Author keywords

Chromatin affinity precipitation (ChAP); Chromatin immunoprecipitation (ChIP); O acetyl ADP ribose (AAR, OAADPR); Silent chromatin; Sir2

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE ACETATE; DNA FRAGMENT; SILENT INFORMATION REGULATOR PROTEIN 2;

EID: 84857054908     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-011-0771-x     Document Type: Article
Times cited : (11)

References (57)
  • 1
    • 0025900189 scopus 로고
    • Modifiers of position effect are shared between telomeric and silent mating-type loci in S. cerevisiae
    • Aparicio OM, Billington BL, Gottschling DE (1991) Modifiers of position effect are shared between telomeric and silent matingtype loci in S. cerevisiae. Cell 66:1279-1287 (Pubitemid 121001416)
    • (1991) Cell , vol.66 , Issue.6 , pp. 1279-1287
    • Aparicio, O.M.1    Billington, B.L.2    Gottschling, D.E.3
  • 2
    • 1642297558 scopus 로고    scopus 로고
    • Structural basis for the mechanism and regulation of Sir2 enzymes
    • DOI 10.1016/S1097-2765(04)00082-6, PII S1097276504000826
    • Avalos JL, Boeke JD, Wolberger C (2004) Structural basis for the mechanism and regulation of Sir2 enzymes. Mol Cell 13:639-648 (Pubitemid 38368122)
    • (2004) Molecular Cell , vol.13 , Issue.5 , pp. 639-648
    • Avalos, J.L.1    Boeke, J.D.2    Wolberger, C.3
  • 3
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast Sir2 and human SIRT1
    • DOI 10.1074/jbc.M205670200
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, Sinclair DA (2002) Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast Sir2 and human SIRT1. J Biol Chem 277:45099-45107 (Pubitemid 36159111)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 4
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • DOI 10.1146/annurev.biochem.73.011303.073651
    • Blander G, Guarente L (2004) The Sir2 family of protein deacetylases. Annu Rev Biochem 73:417-435 (Pubitemid 39050375)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 417-435
    • Blander, G.1    Guarente, L.2
  • 7
    • 0037085264 scopus 로고    scopus 로고
    • Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3
    • DOI 10.1074/jbc.M110532200
    • Carmen AA, Milne L, Grunstein M (2002) Acetylation of the yeast histone H4 N-terminus regulates its binding to heterochromatin protein SIR3. J Biol Chem 277:4778-4781 (Pubitemid 34968510)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.7 , pp. 4778-4781
    • Carmen, A.A.1    Milne, L.2    Grunstein, M.3
  • 8
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P, Allis CD, Sassone-Corsi P (2000) Signaling to chromatin through histone modifications. Cell 103:263-271
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 9
    • 50249084505 scopus 로고    scopus 로고
    • Bypassing Sir2 and O-acetyl-ADP-ribose in transcriptional silencing
    • Chou C-C, Li Y-C, Gartenberg MR (2008) Bypassing Sir2 and O-acetyl-ADP-ribose in transcriptional silencing. Mol Cell 31:650-659
    • (2008) Mol Cell , vol.31 , pp. 650-659
    • Chou, C.-C.1    Li, Y.-C.2    Gartenberg, M.R.3
  • 10
    • 0037221445 scopus 로고    scopus 로고
    • +-dependent deacetylases
    • DOI 10.1016/S0968-0004(02)00005-1, PII S0968000402000051
    • Denu JM (2003) Linking chromatin function with metabolic networks: Sir2 family of NAD?-dependent deacetylases. Trends Biochem Sci 28:41-48 (Pubitemid 36051005)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.1 , pp. 41-48
    • Denu, J.M.1
  • 11
    • 25144496904 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • DOI 10.1016/j.cbpa.2005.08.010, PII S1367593105001079, Mechanisms / Analytical Techniques
    • Denu JM (2005) The Sir2 family of protein deacetylases. Curr Opin Chem Biol 9:431-440 (Pubitemid 41338194)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.5 , pp. 431-440
    • Denu, J.M.1
  • 12
    • 27644520989 scopus 로고    scopus 로고
    • Ribosome occupancy of the yeast CPA1 upstream open reading frame termination codon modulates nonsense-mediated mRNA decay
    • DOI 10.1016/j.molcel.2005.09.019, PII S1097276505016400
    • Gaba A, Jacobson A, Schs MS (2005) Ribosome occupancy of the yeast CPA1 upstream open reading frame termination codon modulates nonsense-mediated mRNA decay. Mol Cell 20:449-460 (Pubitemid 41572301)
    • (2005) Molecular Cell , vol.20 , Issue.3 , pp. 449-460
    • Gaba, A.1    Jacobson, A.2    Sachs, M.S.3
  • 13
    • 0035861202 scopus 로고    scopus 로고
    • The molecular biology of the SIR proteins
    • DOI 10.1016/S0378-1119(01)00741-7, PII S0378111901007417
    • Gasser SM, Cockell MM (2001) The molecular biology of the SIR proteins. Gene 279:1-16 (Pubitemid 33145178)
    • (2001) Gene , vol.279 , Issue.1 , pp. 1-16
    • Gasser, S.M.1    Cockell, M.M.2
  • 14
    • 0025201982 scopus 로고
    • Position effect at S. cerevisiae telomeres: Reversible repression of pol II transcription
    • Gottschling DE, Aparicio OM, Billington BL, Zakian VA (1990) Position effect at S. cerevisiae telomeres: reversible repression of pol II transcription. Cell 63:751-762 (Pubitemid 120035048)
    • (1990) Cell , vol.63 , Issue.4 , pp. 751-762
    • Gottschling, D.E.1    Aparicio, O.M.2    Billington, B.L.3    Zakian, V.A.4
  • 16
    • 0012567905 scopus 로고    scopus 로고
    • The T box and S box transcription termination control systems
    • a1-d305
    • Grundy FJ, Henkin TM (2003) The T box and S box transcription termination control system. Fornt Biosci 8:d20-d31 (Pubitemid 39069960)
    • (2003) Frontiers in Bioscience , vol.8
    • Grundy, F.J.1    Henkin, T.M.2
  • 17
    • 25444440088 scopus 로고    scopus 로고
    • Second messenger function and the structure-activity relationship of cyclic adenosine diphosphoribose (cADPR)
    • DOI 10.1111/j.1742-4658.2005.04863.x
    • Guse AH (2005) Second messenger function and the structureactivity relationship of cyclic adenosine diphosphoribose (cADPR). FEBS J 272:4590-4597 (Pubitemid 41366983)
    • (2005) FEBS Journal , vol.272 , Issue.18 , pp. 4590-4597
    • Guse, A.H.1
  • 18
    • 0029817763 scopus 로고    scopus 로고
    • Spreading of transcriptional repressor SIR3 from telomeric heterochromatin
    • DOI 10.1038/383092a0
    • Hecht A, Strahl-Bolsinger S, Grunstein M (1996) Spreading of transcriptional represser SIR3 from telomeric heterochromatin. Nature 383:92-96 (Pubitemid 26296468)
    • (1996) Nature , vol.383 , Issue.6595 , pp. 92-96
    • Hecht, A.1    Strahl-Bolsinger, S.2    Grunstein, M.3
  • 19
    • 0033289860 scopus 로고    scopus 로고
    • Mapping DNA interaction sites of chromosomal proteins crosslinking studies in yeast
    • Hecht A, Strahl-Bolsinger S, Grunstein M (1999) Mapping DNA interaction sites of chromosomal proteins crosslinking studies in yeast. Methods Mol Biol 119:469-479
    • (1999) Methods Mol Biol , vol.119 , pp. 469-479
    • Hecht, A.1    Strahl-Bolsinger, S.2    Grunstein, M.3
  • 20
    • 0042822279 scopus 로고    scopus 로고
    • Association of the RENT complex with nontranscribed and coding regions of rDNA and a regional requirement for the replication fork block protein Fob1 in rDNA silencing
    • DOI 10.1101/gad.1108403
    • Huang J, Moazed D (2003) Association of the RENT complex with nontranscribed and coding regions of rDNA and a regional requirement for the replication fork block protein Fob1 in rDNA silencing. Genes Dev 17:2162-2176 (Pubitemid 37052295)
    • (2003) Genes and Development , vol.17 , Issue.17 , pp. 2162-2176
    • Huang, J.1    Moazed, D.2
  • 21
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • DOI 10.1038/35001622
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NADdependent histone deacetylase. Nature 403:795-800 (Pubitemid 30111843)
    • (2000) Nature , vol.403 , Issue.6771 , pp. 795-800
    • Imai, S.-I.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 22
    • 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
  • 23
    • 0018644035 scopus 로고
    • Mar1 - A regulator of the HMa and HMα loci in Saccharomyces cerevisiae
    • Klar AJS, Fogel S, MacLeod K (1979) MAR1-a regulator of the HMa and HMa loci in Saccharomyces cerevisiae. Genetics 93:37-50 (Pubitemid 10154116)
    • (1979) Genetics , vol.93 , Issue.1 , pp. 37-50
    • Klar, A.J.S.1    Fogel, S.2    Macleod, K.3
  • 25
    • 33749052511 scopus 로고    scopus 로고
    • Rheostat Control of Gene Expression by Metabolites
    • DOI 10.1016/j.molcel.2006.09.002, PII S1097276506006307
    • Ladurner AG (2006) Rheostate control of gene expression by metabolites. Mol Cell 24:1-11 (Pubitemid 44466685)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 1-11
    • Ladurner, A.G.1
  • 27
    • 54249140416 scopus 로고    scopus 로고
    • Quantification of endogenous sirtuin metabolite O-acetyl-ADP-ribose
    • Lee S,TongL,Denu JM(2008)Quantification of endogenous sirtuin metabolite O-acetyl-ADP-ribose. Anal Biochem 15:174-179
    • (2008) Anal Biochem , vol.15 , pp. 174-179
    • Lee, S.1    Tongl2    Denu, J.M.3
  • 28
    • 0034934774 scopus 로고    scopus 로고
    • Promoter-specific binding of Rap1 revealed by genome-wide maps of protein-DNA association
    • DOI 10.1038/ng569
    • Lieb JD, Liu X, Botstein D, Brown PO (2001) Promoter-specific binding of Rap1 revealed by genome-wide maps of protein-DNA association. Nat Genet 28:327-334 (Pubitemid 32702421)
    • (2001) Nature Genetics , vol.28 , Issue.4 , pp. 327-334
    • Lieb, J.D.1    Liu, X.2    Botstein, D.3    Brown, P.O.4
  • 29
    • 0037174922 scopus 로고    scopus 로고
    • Dead box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E
    • DOI 10.1074/jbc.M206618200
    • Liou G-G, Chang HY, Lin CS, Lin-Chao S (2002) DEAD box RhlB RNAhelicase physically associateswith exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosomeassembling region of RNase E. J Biol Chem 277:41157-41162 (Pubitemid 35215707)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41157-41162
    • Liou, G.-G.1    Chang, H.-Y.2    Lin, C.-S.3    Lin-Chao, S.4
  • 30
    • 19344377042 scopus 로고    scopus 로고
    • Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation
    • DOI 10.1016/j.cell.2005.03.035, PII S0092867405003545
    • Liou G-G, Tanny JC, Kruger RG, Walz T, Moazed D (2005) Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. Cell 121:515-527 (Pubitemid 40720006)
    • (2005) Cell , vol.121 , Issue.4 , pp. 515-527
    • Liou, G.-G.1    Tanny, J.C.2    Kruger, R.G.3    Walz, T.4    Moazed, D.5
  • 32
    • 0031961672 scopus 로고    scopus 로고
    • Lactose repressor protein: Functional properties and struccture
    • Matthews KS, Nichols JC (1998) Lactose repressor protein: functional properties and struccture. Prog Nucleic Acid Res Mol Biol 58:127-164
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.58 , pp. 127-164
    • Matthews, K.S.1    Nichols, J.C.2
  • 33
    • 0034791301 scopus 로고    scopus 로고
    • Common themes in mechanisms of gene silencing
    • DOI 10.1016/S1097-2765(01)00340-9
    • Moazed D (2001) Common themes in mechanisms of gene silencing. Mol Cell 8:489-498 (Pubitemid 32946927)
    • (2001) Molecular Cell , vol.8 , Issue.3 , pp. 489-498
    • Moazed, D.1
  • 34
    • 0030598895 scopus 로고    scopus 로고
    • A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae
    • DOI 10.1016/S0092-8674(00)80139-7
    • Moazed D, Johnson D (1996) A deubiquitinating enzyme interacts with SIR4 and regulates silencing in S. cerevisiae. Cell 86:667-677 (Pubitemid 26299497)
    • (1996) Cell , vol.86 , Issue.4 , pp. 667-677
    • Moazed, D.1    Johnson, A.D.2
  • 35
    • 0030951007 scopus 로고    scopus 로고
    • Silent information regulator protein complexes in Saccharomyces cerevisiae: A SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3
    • DOI 10.1073/pnas.94.6.2186
    • Moazed D, Kistler A, Axelrod A, Rine J, Johnson AD (1997) Silent information regulator protein complexes in Saccharomyces cerevisiae: a SIR2/SIR4 complex and evidence for a regulatory domain in SIR4 that inhibits its interaction with SIR3. Proc Natl Acad Sci 94:2186-2191 (Pubitemid 27136849)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.6 , pp. 2186-2191
    • Moazed, D.1    Kistler, A.2    Axelrod, A.3    Rine, J.4    Johnson, A.D.5
  • 36
    • 0028004378 scopus 로고
    • Evidence that a complex of SIR proteins interacts with the silencer and telomere-binding protein RAP1
    • Moretti P, Freeman K, Coodly L, Shore D (1994) Evidence that a complex of SIR proteins interacts with the silencer and telomerebinding protein RAP1. Genes Dev 8:2257-2269 (Pubitemid 24314288)
    • (1994) Genes and Development , vol.8 , Issue.19 , pp. 2257-2269
    • Moretti, P.1    Freeman, K.2    Coodly, L.3    Shore, D.4
  • 38
    • 0037291214 scopus 로고    scopus 로고
    • +-dependent tubulin deacetylase
    • DOI 10.1016/S1097-2765(03)00038-8
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (2003) The human Sir2 ortholog, SIRT2, is an NAD ?-dependent tubulin deacetylase. Mol Cell 11:437-444 (Pubitemid 36293837)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 39
    • 37349033583 scopus 로고    scopus 로고
    • Role of the Conserved Sir3-BAH Domain in Nucleosome Binding and Silent Chromatin Assembly
    • DOI 10.1016/j.molcel.2007.12.004, PII S1097276507008416
    • Onishi M, Liou G-G, Buchberger JR, Walz T, Moazed D (2007) Role of the conserved Sir3-BAH domain in nucleosome binding and silent chromatin assembly. Mol Cell 28:1015-1028 (Pubitemid 350297032)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 1015-1028
    • Onishi, M.1    Liou, G.-G.2    Buchberger, J.R.3    Walz, T.4    Moazed, D.5
  • 40
    • 0037154972 scopus 로고    scopus 로고
    • Epigenetic codes for heterochromatin formation and silencing: Rounding up the usual suspects
    • DOI 10.1016/S0092-8674(02)00644-X
    • Richards EJ, Elgin SC (2002) Epigenetic codes for heterochromatin formation and silencing rounding up the usual suspects. Cell 108:489-500 (Pubitemid 34260874)
    • (2002) Cell , vol.108 , Issue.4 , pp. 489-500
    • Richards, E.J.1    Elgin, S.C.R.2
  • 41
    • 0023340731 scopus 로고
    • Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae
    • Rine J, Herskowitz I (1987) Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae. Genetics 116:9-22
    • (1987) Genetics , vol.116 , pp. 9-22
    • Rine, J.1    Herskowitz, I.2
  • 42
    • 18944384374 scopus 로고    scopus 로고
    • A nonhistone protein-protein interaction required for assembly of the SIR complex and silent chromatin
    • DOI 10.1128/MCB.25.11.4514-4528.2005
    • Rudner AD, Hall BE, Ellenberger T, Moazed D (2005) A nonhistone protein-protein interaction required for assembly of the SIR complex and silent chromatin. Mol Cell Biol 25:4514-4528 (Pubitemid 40705757)
    • (2005) Molecular and Cellular Biology , vol.25 , Issue.11 , pp. 4514-4528
    • Rudner, A.D.1    Hall, B.E.2    Ellenberger, T.3    Moazed, D.4
  • 43
    • 0037636027 scopus 로고    scopus 로고
    • The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae
    • DOI 10.1146/annurev.biochem.72.121801.161547
    • Rusche LN, Kirchmaier AL, Rine J (2003) The establishment, inheritance, and function of silenced chromatin in Saccharomyces cerevisiae. Annu Rev Biochem 72:481-516 (Pubitemid 36930453)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 481-516
    • Rusche, L.N.1    Kirchmaier, A.L.2    Rine, J.3
  • 45
    • 0031056907 scopus 로고    scopus 로고
    • An unusual form of transcriptional silencing in yeast ribosomal DNA
    • Smith JS, Boeke JD (1997) An unusual form of transcriptional silencing in yeast ribosomal DNA. Genes Dev 11:241-254 (Pubitemid 27081899)
    • (1997) Genes and Development , vol.11 , Issue.2 , pp. 241-254
    • Smith, J.S.1    Boeke, J.D.2
  • 47
    • 0031027431 scopus 로고    scopus 로고
    • SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast
    • Strahl-Bolsinger S, Hecht A, Luo K, Grunstein M (1997) SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast. Genes Dev 11:83-93 (Pubitemid 27043826)
    • (1997) Genes and Development , vol.11 , Issue.1 , pp. 83-93
    • Strahl-Bolsinger, S.1    Hecht, A.2    Luo, K.3    Grunstein, M.4
  • 48
    • 0035895275 scopus 로고    scopus 로고
    • Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product
    • DOI 10.1073/pnas.031563798
    • Tanny JC, Moazed D (2001) Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: evidence for acetyl transfer from substrate to an NAD breakdown product. Proc Natl Acad Sci 98:415-420 (Pubitemid 32105055)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.2 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 49
    • 3543038804 scopus 로고    scopus 로고
    • Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions
    • DOI 10.1128/MCB.24.16.6931-6946.2004
    • Tanny JC, Kirkpatrick DS, Gerber SA, Gygi SP, Moazed D (2004) Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions. Mol Cell Biol 24:6931-6946 (Pubitemid 39014422)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.16 , pp. 6931-6946
    • Tanny, J.C.1    Kirkpatrick, D.S.2    Gerber, S.A.3    Gygi, S.P.4    Moazed, D.5
  • 50
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J, Hassig CA, Schreiber ST (1996) A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408-411 (Pubitemid 26138177)
    • (1996) Science , vol.272 , Issue.5260 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 51
    • 66449123334 scopus 로고    scopus 로고
    • Hydrolase regulates NAD? metabolites and modulates cellular REDOX
    • Tong L, Lee S, Denu JM (2009) Hydrolase regulates NAD? metabolites and modulates cellular REDOX. J Biol Chem 284:11256-11266
    • (2009) J Biol Chem , vol.284 , pp. 11256-11266
    • Tong, L.1    Lee, S.2    Denu, J.M.3
  • 52
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner BM (2000) Histone acetylation and an epigenetic code. BioEssays 22:836-845
    • (2000) BioEssays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 53
    • 27144527479 scopus 로고    scopus 로고
    • Regulation of bacterial gene expression by riboswitches
    • DOI 10.1146/annurev.micro.59.030804.121336
    • Winkler WC, Breaker RR (2005) Regulation of bacterial gene expression by riboswitches. Annu Rev Microbiol 59:487-517 (Pubitemid 41507440)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 487-517
    • Winkler, W.C.1    Breaker, R.R.2
  • 54
    • 33845393998 scopus 로고    scopus 로고
    • Bypassing the catalytic activity of SIR2 for SIR protein spreading in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E06-08-0669
    • Yang B, Kirchmaier L (2006) Bypassing the catalytic activity of SIR2 for SIR protein spreading in Saccharomyces cerevisiae. Mol Biol Cell 17:5287-5297 (Pubitemid 44907369)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.12 , pp. 5287-5297
    • Yang, B.1    Kirchmaier, A.L.2
  • 55
    • 31144434817 scopus 로고    scopus 로고
    • Constant darkness is a circadian metabolic signal in mammals
    • DOI 10.1038/nature04368, PII NATURE04368
    • Zhang J, Kaasik K, Blackburn MR, Lee CC (2006) Constant darkness is a circadian metabolic signal in mammals. Nature 439:340-343 (Pubitemid 43128859)
    • (2006) Nature , vol.439 , Issue.7074 , pp. 340-343
    • Zhang, J.1    Kaasik, K.2    Blackburn, M.R.3    Cheng, C.L.4
  • 56
    • 0141618441 scopus 로고    scopus 로고
    • Structure and autoregulation of the yeast Hst2 homolog of Sir2
    • DOI 10.1038/nsb978
    • Zhao K, Chai X, Clements A, Marmorstein R (2003) Structure and autoregulation of the yeast Hst2 homolog of Sir2. Nat Struct Biol 10:864-871 (Pubitemid 37187660)
    • (2003) Nature Structural Biology , vol.10 , Issue.10 , pp. 864-871
    • Zhao, K.1    Chai, X.2    Clements, A.3    Marmorstein, R.4
  • 57
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide
    • DOI 10.1016/j.str.2003.09.016
    • Zhao K, Chai X, Marmorstein R (2003) Structure of the yeast Hst2 protein deacetylase in ternary complex with 20-O-acetyl ADP ribose and histone peptide. Structure 11:1403-1411 (Pubitemid 37412422)
    • (2003) Structure , vol.11 , Issue.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.