메뉴 건너뛰기




Volumn 287, Issue 15, 2012, Pages 12405-12416

Regulation of poly(ADP-ribose) polymerase-1-dependent gene expression through promoter-directed recruitment of a nuclear NAD + synthase

Author keywords

[No Author keywords available]

Indexed keywords

ADP-RIBOSE; CELL-BASED; CELLULAR COMPARTMENTS; CODING GENES; ENZYMATIC ACTIVITIES; EXPRESSION MICROARRAY; FUNCTIONAL INTERACTION; GENE SETS; GENOMIC ASSAYS; KEY ENZYMES; MCF-7 CELLS; METABOLIC PATHWAYS; NUCLEAR PROCESS; SYNTHASES; TARGET GENES; TWO-PHOTON EXCITATION MICROSCOPIES;

EID: 84859506559     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.304469     Document Type: Article
Times cited : (91)

References (51)
  • 1
    • 44649130038 scopus 로고    scopus 로고
    • Transcriptional control by PARP-1: Chromatin modulation, enhancer-binding, coregulation, and insulation
    • Kraus, W. L. (2008) Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation. Curr. Opin. Cell Biol. 20, 294-302
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 294-302
    • Kraus, W.L.1
  • 2
    • 77954274504 scopus 로고    scopus 로고
    • The PARP side of the nucleus: Molecular actions, physiological outcomes, and clinical targets
    • Krishnakumar, R., and Kraus, W. L. (2010) The PARP side of the nucleus: molecular actions, physiological outcomes, and clinical targets. Mol. Cell 39, 8-24
    • (2010) Mol. Cell , vol.39 , pp. 8-24
    • Krishnakumar, R.1    Kraus, W.L.2
  • 3
    • 0033198919 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
    • DOI 10.1042/0264-6021:3420249
    • D'Amours, D., Desnoyers, S., D'Silva, I., and Poirier, G. G. (1999) Poly- (ADP-ribosyl)ation reactions in the regulation of nuclear functions. Biochem. J. 342, 249-268 (Pubitemid 29425344)
    • (1999) Biochemical Journal , vol.342 , Issue.2 , pp. 249-268
    • D'Amours, D.1    Desnoyers, S.2    D'Silva, I.3    Poirier, G.G.4
  • 5
    • 0037829279 scopus 로고    scopus 로고
    • Reconstructing eukaryotic NAD metabolism
    • DOI 10.1002/bies.10297
    • Rongvaux, A., Andris, F., Van Gool, F., and Leo, O. (2003) Reconstructing eukaryotic NAD metabolism. BioEssays 25, 683-690 (Pubitemid 36850796)
    • (2003) BioEssays , vol.25 , Issue.7 , pp. 683-690
    • Rongvaux, A.1    Andris, F.2    Van Gool, F.3    Leo, O.4
  • 7
    • 0036856578 scopus 로고    scopus 로고
    • Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAF biosynthesis
    • DOI 10.1002/1521-4141(200211)32:11<3225::AID-IMMU3225>3.0.CO;2-L
    • Rongvaux, A., Shea, R. J., Mulks, M. H., Gigot, D., Urbain, J., Leo, O., and Andris, F. (2002) Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis. Eur. J. Immunol. 32, 3225-3234 (Pubitemid 35414880)
    • (2002) European Journal of Immunology , vol.32 , Issue.11 , pp. 3225-3234
    • Rongvaux, A.1    She, R.J.2    Mulks, M.H.3    Gigot, D.4    Urbain, J.5    Leo, O.6    Andris, F.7
  • 8
    • 0038356712 scopus 로고    scopus 로고
    • Growth phase-dependent changes in the subcellular localization of pre-B-cell colony-enhancing factor
    • DOI 10.1016/S0014-5793(03)00476-9
    • Kitani, T., Okuno, S., and Fujisawa, H. (2003) Growth phase-dependent changes in the subcellular localization of pre-B-cell colony-enhancing factor. FEBS Lett. 544, 74-78 (Pubitemid 36628039)
    • (2003) FEBS Letters , vol.544 , Issue.1-3 , pp. 74-78
    • Kitani, T.1    Okuno, S.2    Fujisawa, H.3
  • 9
    • 0942279500 scopus 로고    scopus 로고
    • Characterization of human brain nicotinamide 5′-mononucleotide adenylyltransferase-2 and expression in human pancreas
    • DOI 10.1042/BJ20030518
    • Yalowitz, J. A., Xiao, S., Biju, M. P., Antony, A. C., Cummings, O. W., Deeg, M. A., and Jayaram, H. N. (2004) Characterization of human brain nicotinamide 5′-mononucleotide adenylyltransferase-2 and expression in human pancreas. Biochem. J. 377, 317-326 (Pubitemid 38142187)
    • (2004) Biochemical Journal , vol.377 , Issue.2 , pp. 317-326
    • Yalowitz, J.A.1    Xiao, S.2    Biju, M.P.3    Antony, A.C.4    Cummings, O.W.5    Deeg, M.A.6    Jayaram, H.N.7
  • 11
    • 0035808313 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase
    • DOI 10.1074/jbc.M008700200
    • Emanuelli, M., Carnevali, F., Saccucci, F., Pierella, F., Amici, A., Raffaelli, N., and Magni, G. (2001) Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase. J. Biol. Chem. 276, 406-412 (Pubitemid 32050333)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.1 , pp. 406-412
    • Emanuelli, M.1    Carnevali, F.2    Saccucci, F.3    Pierella, F.4    Amici, A.5    Raffaelli, N.6    Magni, G.7
  • 12
    • 0035831109 scopus 로고    scopus 로고
    • Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis
    • DOI 10.1016/S0014-5793(01)02180-9, PII S0014579301021809
    • Schweiger, M., Hennig, K., Lerner, F., Niere, M., Hirsch-Kauffmann, M., Specht, T., Weise, C., Oei, S. L., and Ziegler, M. (2001) Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential forNADsynthesis. FEBS Lett. 492, 95-100 (Pubitemid 32206727)
    • (2001) FEBS Letters , vol.492 , Issue.1-2 , pp. 95-100
    • Schweiger, M.1    Hennig, K.2    Lerner, F.3    Niere, M.4    Hirsch-Kauffmann, M.5    Specht, T.6    Weise, C.7    Oei, S.L.8    Ziegler, M.9
  • 13
    • 27744501798 scopus 로고    scopus 로고
    • Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms
    • DOI 10.1074/jbc.M508660200
    • Berger, F., Lau, C., Dahlmann, M., and Ziegler, M. (2005) Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. J. Biol. Chem. 280, 36334-36341 (Pubitemid 41633907)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.43 , pp. 36334-36341
    • Berger, F.1    Lau, C.2    Dahlmann, M.3    Ziegler, M.4
  • 16
    • 27644591304 scopus 로고    scopus 로고
    • Axon degeneration mechanisms: Commonality amid diversity
    • Coleman, M. (2005) Axon degeneration mechanisms: commonality amid diversity. Nat. Rev. Neurosci. 6, 889-898
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 889-898
    • Coleman, M.1
  • 17
    • 23744474976 scopus 로고    scopus 로고
    • A local mechanism mediates NAD-dependent protection of axon degeneration
    • DOI 10.1083/jcb.200504028
    • Wang, J., Zhai, Q., Chen, Y., Lin, E., Gu, W., McBurney, M. W., and He, Z. (2005) A local mechanism mediates NAD-dependent protection of axon degeneration. J. Cell Biol. 170, 349-355 (Pubitemid 41126935)
    • (2005) Journal of Cell Biology , vol.170 , Issue.3 , pp. 349-355
    • Wang, J.1    Zhai, Q.2    Chen, Y.3    Lin, E.4    Gu, W.5    McBurney, M.W.6    He, Z.7
  • 18
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • DOI 10.1126/science.1098014
    • Araki, T., Sasaki, Y., and Milbrandt, J. (2004) Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305, 1010-1013 (Pubitemid 39071777)
    • (2004) Science , vol.305 , Issue.5686 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 20
    • 34247278118 scopus 로고    scopus 로고
    • Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1
    • DOI 10.1073/pnas.0609211104
    • Berger, F., Lau, C., and Ziegler, M. (2007) Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyltransferase 1. Proc. Natl. Acad. Sci. U.S.A. 104, 3765-3770 (Pubitemid 47181528)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.10 , pp. 3765-3770
    • Berger, F.1    Lau, C.2    Ziegler, M.3
  • 21
    • 38949198773 scopus 로고    scopus 로고
    • Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes
    • DOI 10.1126/science.1149250
    • Krishnakumar, R., Gamble, M. J., Frizzell, K. M., Berrocal, J. G., Kininis, M., and Kraus, W. L. (2008) Reciprocal binding of PARP-1 and histone H1 at promoters specifies transcriptional outcomes. Science 319, 819-821 (Pubitemid 351225873)
    • (2008) Science , vol.319 , Issue.5864 , pp. 819-821
    • Krishnakumar, R.1    Gamble, M.J.2    Frizzell, K.M.3    Berrocal, J.G.4    Kininis, M.5    Kraus, W.L.6
  • 22
    • 10944227347 scopus 로고    scopus 로고
    • +- dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1
    • +- dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1. Cell 119, 803-814
    • (2004) Cell , vol.119 , pp. 803-814
    • Kim, M.Y.1    Mauro, S.2    Gévry, N.3    Lis, J.T.4    Kraus, W.L.5
  • 23
    • 35648955118 scopus 로고    scopus 로고
    • The DNA binding and catalytic domains of poly(ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription
    • DOI 10.1128/MCB.01314-07
    • Wacker, D. A., Ruhl, D. D., Balagamwala, E. H., Hope, K. M., Zhang, T., and Kraus, W. L. (2007) The DNA binding and catalytic domains of poly- (ADP-ribose) polymerase 1 cooperate in the regulation of chromatin structure and transcription. Mol. Cell. Biol. 27, 7475-7485 (Pubitemid 350033654)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.21 , pp. 7475-7485
    • Wacker, D.A.1    Ruhl, D.D.2    Balagamwala, E.H.3    Hope, K.M.4    Zhang, T.5    Kraus, W.L.6
  • 24
    • 33745255099 scopus 로고    scopus 로고
    • A topoisomerase IIβ-mediated dsDNA break required for regulated transcription
    • DOI 10.1126/science.1127196
    • Ju, B. G., Lunyak, V. V., Perissi, V., Garcia-Bassets, I., Rose, D. W., Glass, C. K., and Rosenfeld, M. G. (2006) A topoisomerase IIβ-mediated dsDNA break required for regulated transcription. Science 312, 1798-1802 (Pubitemid 43962898)
    • (2006) Science , vol.312 , Issue.5781 , pp. 1798-1802
    • Ju, B.-G.1    Lunyak, V.V.2    Perissi, V.3    Garcia-Bassets, I.4    Rose, D.W.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 25
    • 10944253639 scopus 로고    scopus 로고
    • Activating the PARP-1 sensor component of the groucho/ TLE1 corepressor complex mediates a CaMKinase IIδ-dependent neurogenic gene activation pathway
    • DOI 10.1016/j.cell.2004.11.017, PII S0092867404010931
    • Ju, B. G., Solum, D., Song, E. J., Lee, K. J., Rose, D. W., Glass, C. K., and Rosenfeld, M. G. (2004) Activating the PARP-1 sensor component of the groucho/ TLE1 corepressor complex mediates a CaMKinase IIδ-dependent neurogenic gene activation pathway. Cell 119, 815-829 (Pubitemid 40017688)
    • (2004) Cell , vol.119 , Issue.6 , pp. 815-829
    • Ju, B.-G.1    Solum, D.2    Song, E.J.3    Lee, K.-J.4    Rose, D.W.5    Glass, C.K.6    Rosenfeld, M.G.7
  • 28
    • 71749119589 scopus 로고    scopus 로고
    • Global analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells
    • Frizzell, K. M., Gamble, M. J., Berrocal, J. G., Zhang, T., Krishnakumar, R., Cen, Y., Sauve, A. A., and Kraus, W. L. (2009) Global analysis of transcriptional regulation by poly(ADP-ribose) polymerase-1 and poly(ADP-ribose) glycohydrolase in MCF-7 human breast cancer cells. J. Biol. Chem. 284, 33926-33938
    • (2009) J. Biol. Chem. , vol.284 , pp. 33926-33938
    • Frizzell, K.M.1    Gamble, M.J.2    Berrocal, J.G.3    Zhang, T.4    Krishnakumar, R.5    Cen, Y.6    Sauve, A.A.7    Kraus, W.L.8
  • 29
    • 46149108345 scopus 로고    scopus 로고
    • Rapid, Transcription-Independent Loss of Nucleosomes over a Large Chromatin Domain at Hsp70 Loci
    • DOI 10.1016/j.cell.2008.05.029, PII S0092867408006892
    • Petesch, S. J., and Lis, J. T. (2008) Rapid, transcription-independent loss of nucleosomes over a large chromatin domain at Hsp70 loci. Cell 134, 74-84 (Pubitemid 351905736)
    • (2008) Cell , vol.134 , Issue.1 , pp. 74-84
    • Petesch, S.J.1    Lis, J.T.2
  • 30
    • 0037462597 scopus 로고    scopus 로고
    • Chromatin loosening by poly(ADP)-ribose polymerase (PARP) at Drosophila puff loci
    • DOI 10.1126/science.1078764
    • Tulin, A., and Spradling, A. (2003) Chromatin loosening by poly(ADP)- ribose polymerase (PARP) at Drosophila puff loci. Science 299, 560-562 (Pubitemid 36135152)
    • (2003) Science , vol.299 , Issue.5606 , pp. 560-562
    • Tulin, A.1    Spradling, A.2
  • 31
    • 0037102454 scopus 로고    scopus 로고
    • The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development
    • Tulin, A., Stewart, D., and Spradling, A. C. (2002) The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase (PARP) is required to modulate chromatin structure during development. Genes Dev. 16, 2108-2119
    • (2002) Genes Dev. , vol.16 , pp. 2108-2119
    • Tulin, A.1    Stewart, D.2    Spradling, A.C.3
  • 32
    • 77956526559 scopus 로고    scopus 로고
    • PARP-1 regulates chromatin structure and transcription through a KDM5B-dependent pathway
    • Krishnakumar, R., and Kraus, W. L. (2010) PARP-1 regulates chromatin structure and transcription through a KDM5B-dependent pathway. Mol. Cell 39, 736-749
    • (2010) Mol. Cell , vol.39 , pp. 736-749
    • Krishnakumar, R.1    Kraus, W.L.2
  • 33
    • 0346122893 scopus 로고    scopus 로고
    • PARP-1 binds E2F-1 independently of its DNA binding and catalytic domains, and acts as a novel coactivator of E2F-1-mediated transcription during re-entry of quiescent cells into S phase
    • DOI 10.1038/sj.onc.1206897
    • Simbulan-Rosenthal, C. M., Rosenthal, D. S., Luo, R., Samara, R., Espinoza, L. A., Hassa, P. O., Hottiger, M. O., and Smulson, M. E. (2003) PARP-1 binds E2F-1 independently of its DNA binding and catalytic domains, and acts as a novel coactivator of E2F-1-mediated transcription during reentry of quiescent cells into S phase. Oncogene 22, 8460-8471 (Pubitemid 37523898)
    • (2003) Oncogene , vol.22 , Issue.52 , pp. 8460-8471
    • Simbulan-Rosenthal, C.M.1    Rosenthal, D.S.2    Luo, R.3    Samara, R.4    Espinoza, L.A.5    Hassa, P.O.6    Hottiger, M.O.7    Smulson, M.E.8
  • 34
    • 0035824647 scopus 로고    scopus 로고
    • The enzymatic and DNA binding activity of PARP-1 are not required for NF-κB coactivator function
    • Hassa, P. O., Covic, M., Hasan, S., Imhof, R., and Hottiger, M. O. (2001) The enzymatic and DNA binding activity of PARP-1 are not required for NF-κB coactivator function. J. Biol. Chem. 276, 45588-45597
    • (2001) J. Biol. Chem. , vol.276 , pp. 45588-45597
    • Hassa, P.O.1    Covic, M.2    Hasan, S.3    Imhof, R.4    Hottiger, M.O.5
  • 36
    • 0032006563 scopus 로고    scopus 로고
    • p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation
    • Kraus, W. L., and Kadonaga, J. T. (1998) p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation. Genes Dev. 12, 331-342 (Pubitemid 28084262)
    • (1998) Genes and Development , vol.12 , Issue.3 , pp. 331-342
    • Kraus, W.L.1    Kadonaga, J.T.2
  • 38
    • 0001732595 scopus 로고
    • Biochemical reconstitution of chromatin with physiological nucleosome spacing
    • Bulger, M., and Kadonaga, J. (1994) Biochemical reconstitution of chromatin with physiological nucleosome spacing. Methods Mol. Genet. 5, 241-262
    • (1994) Methods Mol. Genet. , vol.5 , pp. 241-262
    • Bulger, M.1    Kadonaga, J.2
  • 39
    • 0025696463 scopus 로고
    • Use of two-dimensional thin-layer chromatography for the components study of poly(adenosine diphosphate ribose)
    • Keith, G., Desgrès, J., and de Murcia, G. (1990) Use of two-dimensional thin-layer chromatography for the components study of poly(adenosine diphosphate ribose). Anal. Biochem. 191, 309-313
    • (1990) Anal. Biochem. , vol.191 , pp. 309-313
    • Keith, G.1    Desgrès, J.2    De Murcia, G.3
  • 40
    • 3042793425 scopus 로고    scopus 로고
    • Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis
    • DOI 10.1126/science.1096485
    • Kasischke, K. A., Vishwasrao, H. D., Fisher, P. J., Zipfel, W. R., and Webb, W. W. (2004) Neural activity triggers neuronal oxidative metabolism followed by astrocytic glycolysis. Science 305, 99-103 (Pubitemid 38869381)
    • (2004) Science , vol.305 , Issue.5680 , pp. 99-103
    • Kasischke, K.A.1    Vishwasrao, H.D.2    Fisher, P.J.3    Zipfel, W.R.4    Webb, W.W.5
  • 41
    • 33845432928 scopus 로고    scopus 로고
    • Adjusting batch effects in microarray expression data using empirical Bayes methods
    • DOI 10.1093/biostatistics/kxj037
    • Johnson, W. E., Li, C., and Rabinovic, A. (2007) Adjusting batch effects in microarray expression data using empirical Bayes methods. Biostatistics 8, 118-127 (Pubitemid 44906106)
    • (2007) Biostatistics , vol.8 , Issue.1 , pp. 118-127
    • Johnson, W.E.1    Li, C.2    Rabinovic, A.3
  • 42
    • 34447519218 scopus 로고    scopus 로고
    • Genomic analyses of transcription factor binding, histone acetylation, and gene expression reveal mechanistically distinct classes of estrogen-regulated promoters
    • DOI 10.1128/MCB.00083-07
    • Kininis, M., Chen, B. S., Diehl, A. G., Isaacs, G. D., Zhang, T., Siepel, A. C., Clark, A. G., and Kraus, W. L. (2007) Genomic analyses of transcription factor binding, histone acetylation, and gene expression reveal mechanistically distinct classes of estrogen-regulated promoters. Mol. Cell. Biol. 27, 5090-5104 (Pubitemid 47068284)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.14 , pp. 5090-5104
    • Kininis, M.1    Chen, B.S.2    Diehl, A.G.3    Isaacs, G.D.4    Zhang, T.5    Siepel, A.C.6    Clark, A.G.7    Kraus, W.L.8
  • 43
    • 77953305213 scopus 로고    scopus 로고
    • The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction
    • Langelier, M. F., Ruhl, D. D., Planck, J. L., Kraus, W. L., and Pascal, J. M. (2010) The Zn3 domain of human poly(ADP-ribose) polymerase-1 (PARP-1) functions in both DNA-dependent poly(ADP-ribose) synthesis activity and chromatin compaction. J. Biol. Chem. 285, 18877-18887
    • (2010) J. Biol. Chem. , vol.285 , pp. 18877-18887
    • Langelier, M.F.1    Ruhl, D.D.2    Planck, J.L.3    Kraus, W.L.4    Pascal, J.M.5
  • 44
    • 0028102269 scopus 로고
    • Two-photon molecular excitation provides intrinsic 3-dimensional resolution for laser-based microscopy and microphotochemistry
    • Williams, R. M., Piston, D. W., and Webb, W. W. (1994) Two-photon molecular excitation provides intrinsic 3-dimensional resolution for laserbased microscopy and microphotochemistry. FASEB J. 8, 804-813 (Pubitemid 24268871)
    • (1994) FASEB Journal , vol.8 , Issue.11 , pp. 804-813
    • Williams, R.M.1    Piston, D.W.2    Webb, W.W.3
  • 45
    • 0037040581 scopus 로고    scopus 로고
    • Regulation of corepressor function by nuclear NADH
    • DOI 10.1126/science.1069300
    • Zhang, Q., Piston, D. W., and Goodman, R. H. (2002) Regulation of corepressor function by nuclear NADH. Science 295, 1895-1897 (Pubitemid 34214127)
    • (2002) Science , vol.295 , Issue.5561 , pp. 1895-1897
    • Zhang, Q.1    Piston, D.W.2    Goodman, R.H.3
  • 46
    • 21644450243 scopus 로고    scopus 로고
    • Conformational dependence of intracellular NADH on metabolic state revealed by associated fluorescence anisotropy
    • DOI 10.1074/jbc.M502475200
    • Vishwasrao, H. D., Heikal, A. A., Kasischke, K. A., and Webb, W. W. (2005) Conformational dependence of intracellular NADH on metabolic state revealed by associated fluorescence anisotropy. J. Biol. Chem. 280, 25119-25126 (Pubitemid 40934604)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 25119-25126
    • Vishwasrao, H.D.1    Heikal, A.A.2    Kasischke, K.A.3    Webb, W.W.4
  • 47
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere, P. A. (1987) Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56, 89-124
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 48
    • 25444484672 scopus 로고    scopus 로고
    • Small molecule regulation of Sir2 protein deacetylases
    • DOI 10.1111/j.1742-4658.2005.04862.x
    • Grubisha, O., Smith, B. C., and Denu, J. M. (2005) Small molecule regulation of Sir2 protein deacetylases. FEBS J. 272, 4607-4616 (Pubitemid 41366985)
    • (2005) FEBS Journal , vol.272 , Issue.18 , pp. 4607-4616
    • Grubisha, O.1    Smith, B.C.2    Denu, J.M.3
  • 50
    • 0041589716 scopus 로고    scopus 로고
    • Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked?
    • Zhang, J. (2003) Are poly(ADP-ribosyl)ation by PARP-1 and deacetylation by Sir2 linked? BioEssays 25, 808-814
    • (2003) BioEssays , vol.25 , pp. 808-814
    • Zhang, J.1
  • 51
    • 77953290752 scopus 로고    scopus 로고
    • + metabolism and signaling to the control of cellular functions
    • + metabolism and signaling to the control of cellular functions. Biochim. Biophys. Acta 1804, 1666-1675
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1666-1675
    • Zhang, T.1    Kraus, W.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.