메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

A Molecular Mechanism for Direct Sirtuin Activation by Resveratrol

Author keywords

[No Author keywords available]

Indexed keywords

PICEATANNOL; RESVERATROL; SIRTUIN 1; SIRTUIN 2; SIRTUIN 3; SIRTUIN 5;

EID: 84869816787     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049761     Document Type: Article
Times cited : (229)

References (62)
  • 2
    • 13944253348 scopus 로고    scopus 로고
    • Calorie restriction - the SIR2 connection
    • Guarente L, Picard F, (2005) Calorie restriction- the SIR2 connection. Cell 120: 473-482.
    • (2005) Cell , vol.120 , pp. 473-482
    • Guarente, L.1    Picard, F.2
  • 3
    • 33845868198 scopus 로고    scopus 로고
    • Sirtuins as potential targets for metabolic syndrome
    • Guarente L, (2006) Sirtuins as potential targets for metabolic syndrome. Nature 444: 868-874.
    • (2006) Nature , vol.444 , pp. 868-874
    • Guarente, L.1
  • 4
    • 40849135481 scopus 로고    scopus 로고
    • The Sirtuin family: therapeutic targets to treat diseases of aging
    • Milne JC, Denu JM, (2008) The Sirtuin family: therapeutic targets to treat diseases of aging. Curr Opin Chem Biol 12: 11-17.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 11-17
    • Milne, J.C.1    Denu, J.M.2
  • 5
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: insights into their biological function
    • Michan S, Sinclair D, (2007) Sirtuins in mammals: insights into their biological function. Biochem J 404: 1-13.
    • (2007) Biochem J , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 6
    • 3142740860 scopus 로고    scopus 로고
    • Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase
    • Cohen HY, Miller C, Bitterman KJ, Wall NR, Hekking B, et al. (2004) Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase. Science 305: 390-392.
    • (2004) Science , vol.305 , pp. 390-392
    • Cohen, H.Y.1    Miller, C.2    Bitterman, K.J.3    Wall, N.R.4    Hekking, B.5
  • 7
    • 31044445366 scopus 로고    scopus 로고
    • Genomic instability and aging-like phenotype in the absence of mammalian SIRT6
    • Mostoslavsky R, Chua KF, Lombard DB, Pang WW, Fischer MR, et al. (2006) Genomic instability and aging-like phenotype in the absence of mammalian SIRT6. Cell 124: 315-329.
    • (2006) Cell , vol.124 , pp. 315-329
    • Mostoslavsky, R.1    Chua, K.F.2    Lombard, D.B.3    Pang, W.W.4    Fischer, M.R.5
  • 8
    • 84858000209 scopus 로고    scopus 로고
    • The sirtuin SIRT6 regulates lifespan in male mice
    • Kanfi Y, Naiman S, Amir G, Peshti V, Zinman G, et al. (2012) The sirtuin SIRT6 regulates lifespan in male mice. Nature 483: 218-221.
    • (2012) Nature , vol.483 , pp. 218-221
    • Kanfi, Y.1    Naiman, S.2    Amir, G.3    Peshti, V.4    Zinman, G.5
  • 9
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I, (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell 16: 4623-4635.
    • (2005) Mol Biol Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 10
    • 10744232772 scopus 로고    scopus 로고
    • Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly
    • Rose G, Dato S, Altomare K, Bellizzi D, Garasto S, et al. (2003) Variability of the SIRT3 gene, human silent information regulator Sir2 homologue, and survivorship in the elderly. Exp Gerontol 38: 1065-1070.
    • (2003) Exp Gerontol , vol.38 , pp. 1065-1070
    • Rose, G.1    Dato, S.2    Altomare, K.3    Bellizzi, D.4    Garasto, S.5
  • 11
    • 55749084738 scopus 로고    scopus 로고
    • A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis
    • Ahn BH, Kim HS, Song S, Lee IH, Liu J, et al. (2008) A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis. Proc Natl Acad Sci USA 105: 14447-14452.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14447-14452
    • Ahn, B.H.1    Kim, H.S.2    Song, S.3    Lee, I.H.4    Liu, J.5
  • 12
    • 50149103440 scopus 로고    scopus 로고
    • Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5
    • Schlicker C, Gertz M, Papatheodorou P, Kachholz B, Becker CF, et al. (2008) Substrates and regulation mechanisms for the human mitochondrial sirtuins Sirt3 and Sirt5. J Mol Biol 382: 790-801.
    • (2008) J Mol Biol , vol.382 , pp. 790-801
    • Schlicker, C.1    Gertz, M.2    Papatheodorou, P.3    Kachholz, B.4    Becker, C.F.5
  • 13
    • 77950806433 scopus 로고    scopus 로고
    • SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation
    • Hirschey MD, Shimazu T, Goetzman E, Jing E, Schwer B, et al. (2010) SIRT3 regulates mitochondrial fatty-acid oxidation by reversible enzyme deacetylation. Nature 464: 121-125.
    • (2010) Nature , vol.464 , pp. 121-125
    • Hirschey, M.D.1    Shimazu, T.2    Goetzman, E.3    Jing, E.4    Schwer, B.5
  • 14
    • 32944479897 scopus 로고    scopus 로고
    • Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization
    • Mahlknecht U, Ho AD, Letzel S, Voelter-Mahlknecht S, (2006) Assignment of the NAD-dependent deacetylase sirtuin 5 gene (SIRT5) to human chromosome band 6p23 by in situ hybridization. Cytogenet Genome Res 112: 208-212.
    • (2006) Cytogenet Genome Res , vol.112 , pp. 208-212
    • Mahlknecht, U.1    Ho, A.D.2    Letzel, S.3    Voelter-Mahlknecht, S.4
  • 15
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • Nakagawa T, Lomb DJ, Haigis MC, Guarente L, (2009) SIRT5 Deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137: 560-570.
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 16
    • 77953285831 scopus 로고    scopus 로고
    • Function and regulation of the mitochondrial Sirtuin isoform Sirt5 in Mammalia
    • Gertz M, Steegborn C, (2009) Function and regulation of the mitochondrial Sirtuin isoform Sirt5 in Mammalia. Biochim Biophys Acta 1804: 1658-1665.
    • (2009) Biochim Biophys Acta , vol.1804 , pp. 1658-1665
    • Gertz, M.1    Steegborn, C.2
  • 17
    • 81055122671 scopus 로고    scopus 로고
    • Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase
    • Du J, Zhou Y, Su X, Yu JJ, Khan S, et al. (2011) Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase. Science 334: 806-809.
    • (2011) Science , vol.334 , pp. 806-809
    • Du, J.1    Zhou, Y.2    Su, X.3    Yu, J.J.4    Khan, S.5
  • 18
    • 77953289094 scopus 로고    scopus 로고
    • Structural basis for sirtuin function: What we know and what we don't
    • Sanders BD, Jackson B, Marmorstein R, (2010) Structural basis for sirtuin function: What we know and what we don't. Biochim Biophys Acta 1804: 1604-1616.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1604-1616
    • Sanders, B.D.1    Jackson, B.2    Marmorstein, R.3
  • 19
    • 42049113213 scopus 로고    scopus 로고
    • Inhibitors of NAD+ dependent histone deacetylases (sirtuins)
    • Neugebauer RC, Sippl W, Jung M, (2008) Inhibitors of NAD+ dependent histone deacetylases (sirtuins). Curr Pharm Des 14: 562-573.
    • (2008) Curr Pharm Des , vol.14 , pp. 562-573
    • Neugebauer, R.C.1    Sippl, W.2    Jung, M.3
  • 20
    • 77953292895 scopus 로고    scopus 로고
    • Sirtuins inhibitors: The approach to affinity and selectivity
    • Cen Y, (2010) Sirtuins inhibitors: The approach to affinity and selectivity. Biochim Biophys Acta 1804: 1635-1644.
    • (2010) Biochim Biophys Acta , vol.1804 , pp. 1635-1644
    • Cen, Y.1
  • 22
    • 13944258164 scopus 로고    scopus 로고
    • Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition
    • Sauve AA, Moir RD, Schramm VL, Willis IM, (2005) Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition. Mol Cell 17: 595-601.
    • (2005) Mol Cell , vol.17 , pp. 595-601
    • Sauve, A.A.1    Moir, R.D.2    Schramm, V.L.3    Willis, I.M.4
  • 23
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz KT, Bitterman KJ, Cohen HY, Lamming DW, Lavu S, et al. (2003) Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425: 191-196.
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1    Bitterman, K.J.2    Cohen, H.Y.3    Lamming, D.W.4    Lavu, S.5
  • 24
    • 36749087548 scopus 로고    scopus 로고
    • Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
    • Milne JC, Lambert PD, Schenk S, Carney DP, Smith JJ, et al. (2007) Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes. Nature 450: 712-716.
    • (2007) Nature , vol.450 , pp. 712-716
    • Milne, J.C.1    Lambert, P.D.2    Schenk, S.3    Carney, D.P.4    Smith, J.J.5
  • 25
    • 48349110303 scopus 로고    scopus 로고
    • A low dose of dietary resveratrol partially mimics caloric restriction and retards aging parameters in mice
    • Barger JL, Kayo T, Vann JM, Arias EB, Wang J, et al. (2008) A low dose of dietary resveratrol partially mimics caloric restriction and retards aging parameters in mice. PLoS ONE 3: e2264.
    • (2008) PLoS ONE , vol.3
    • Barger, J.L.1    Kayo, T.2    Vann, J.M.3    Arias, E.B.4    Wang, J.5
  • 26
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • Wood JG, Rogina B, Lavu S, Howitz K, Helfand SL, et al. (2004) Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature 430: 686-689.
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3    Howitz, K.4    Helfand, S.L.5
  • 27
    • 33745962138 scopus 로고    scopus 로고
    • Therapeutic potential of resveratrol: the in vivo evidence
    • Baur JA, Sinclair DA, (2006) Therapeutic potential of resveratrol: the in vivo evidence. Nat Rev Drug Discov 5: 493-506.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 493-506
    • Baur, J.A.1    Sinclair, D.A.2
  • 28
    • 33751072349 scopus 로고    scopus 로고
    • Resveratrol improves health and survival of mice on a high-calorie diet
    • Baur JA, Pearson KJ, Price NL, Jamieson HA, Lerin C, et al. (2006) Resveratrol improves health and survival of mice on a high-calorie diet. Nature 444: 337-342.
    • (2006) Nature , vol.444 , pp. 337-342
    • Baur, J.A.1    Pearson, K.J.2    Price, N.L.3    Jamieson, H.A.4    Lerin, C.5
  • 29
    • 33845399894 scopus 로고    scopus 로고
    • Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha
    • Lagouge M, Argmann C, Gerhart-Hines Z, Meziane H, Lerin C, et al. (2006) Resveratrol improves mitochondrial function and protects against metabolic disease by activating SIRT1 and PGC-1alpha. Cell 127: 1109-1122.
    • (2006) Cell , vol.127 , pp. 1109-1122
    • Lagouge, M.1    Argmann, C.2    Gerhart-Hines, Z.3    Meziane, H.4    Lerin, C.5
  • 30
    • 46749136505 scopus 로고    scopus 로고
    • Resveratrol: one molecule, many targets
    • Pirola L, Frojdo S, (2008) Resveratrol: one molecule, many targets. IUBMB Life 60: 323-332.
    • (2008) IUBMB Life , vol.60 , pp. 323-332
    • Pirola, L.1    Frojdo, S.2
  • 31
    • 77950246109 scopus 로고    scopus 로고
    • SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1
    • Pacholec M, Bleasdale JE, Chrunyk B, Cunningham D, Flynn D, et al. (2010) SRT1720, SRT2183, SRT1460, and resveratrol are not direct activators of SIRT1. J Biol Chem 285: 8340-8351.
    • (2010) J Biol Chem , vol.285 , pp. 8340-8351
    • Pacholec, M.1    Bleasdale, J.E.2    Chrunyk, B.3    Cunningham, D.4    Flynn, D.5
  • 32
    • 84863011114 scopus 로고    scopus 로고
    • Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases
    • Park SJ, Ahmad F, Philp A, Baar K, Williams T, et al. (2012) Resveratrol ameliorates aging-related metabolic phenotypes by inhibiting cAMP phosphodiesterases. Cell 148: 421-433.
    • (2012) Cell , vol.148 , pp. 421-433
    • Park, S.J.1    Ahmad, F.2    Philp, A.3    Baar, K.4    Williams, T.5
  • 33
    • 84865980711 scopus 로고    scopus 로고
    • Structures, substrates, and regulators of Mammalian sirtuins - opportunities and challenges for drug development
    • Moniot S, Weyand M, Steegborn C, (2012) Structures, substrates, and regulators of Mammalian sirtuins- opportunities and challenges for drug development. Front Pharmacol 3: 16.
    • (2012) Front Pharmacol , vol.3 , pp. 16
    • Moniot, S.1    Weyand, M.2    Steegborn, C.3
  • 34
    • 20444444649 scopus 로고    scopus 로고
    • Mechanism of human SIRT1 activation by resveratrol
    • Borra MT, Smith BC, Denu JM, (2005) Mechanism of human SIRT1 activation by resveratrol. J Biol Chem 280: 17187-17195.
    • (2005) J Biol Chem , vol.280 , pp. 17187-17195
    • Borra, M.T.1    Smith, B.C.2    Denu, J.M.3
  • 36
    • 33846449466 scopus 로고    scopus 로고
    • Design and synthesis of compounds that extend yeast replicative lifespan
    • Yang H, Baur JA, Chen A, Miller C, Adams JK, et al. (2007) Design and synthesis of compounds that extend yeast replicative lifespan. Aging Cell 6: 35-43.
    • (2007) Aging Cell , vol.6 , pp. 35-43
    • Yang, H.1    Baur, J.A.2    Chen, A.3    Miller, C.4    Adams, J.K.5
  • 37
    • 33745534953 scopus 로고    scopus 로고
    • Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide
    • Hoff KG, Avalos JL, Sens K, Wolberger C, (2006) Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide. Structure 14: 1231-1240.
    • (2006) Structure , vol.14 , pp. 1231-1240
    • Hoff, K.G.1    Avalos, J.L.2    Sens, K.3    Wolberger, C.4
  • 39
    • 55549119303 scopus 로고    scopus 로고
    • Does white wine qualify for French paradox? Comparison of the cardioprotective effects of red and white wines and their constituents: resveratrol, tyrosol, and hydroxytyrosol
    • Dudley JI, Lekli I, Mukherjee S, Das M, Bertelli AA, et al. (2008) Does white wine qualify for French paradox? Comparison of the cardioprotective effects of red and white wines and their constituents: resveratrol, tyrosol, and hydroxytyrosol. J Agric Food Chem 56: 9362-9373.
    • (2008) J Agric Food Chem , vol.56 , pp. 9362-9373
    • Dudley, J.I.1    Lekli, I.2    Mukherjee, S.3    Das, M.4    Bertelli, A.A.5
  • 40
    • 84866552404 scopus 로고    scopus 로고
    • Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition
    • Fischer F, Gertz M, Suenkel B, Lakshminarasimhan M, Schutkowski M, et al. (2012) Sirt5 deacylation activities show differential sensitivities to nicotinamide inhibition. PLoS ONE 7: e45098.
    • (2012) PLoS ONE , vol.7
    • Fischer, F.1    Gertz, M.2    Suenkel, B.3    Lakshminarasimhan, M.4    Schutkowski, M.5
  • 41
    • 77958488312 scopus 로고    scopus 로고
    • SIRT1 activation by small molecules: kinetic and biophysical evidence for direct interaction of enzyme and activator
    • Dai H, Kustigian L, Carney D, Case A, Considine T, et al. (2010) SIRT1 activation by small molecules: kinetic and biophysical evidence for direct interaction of enzyme and activator. J Biol Chem 285: 32695-32703.
    • (2010) J Biol Chem , vol.285 , pp. 32695-32703
    • Dai, H.1    Kustigian, L.2    Carney, D.3    Case, A.4    Considine, T.5
  • 42
    • 33847635635 scopus 로고    scopus 로고
    • Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin
    • Schuetz A, Min J, Antoshenko T, Wang CL, Allali-Hassani A, et al. (2007) Structural basis of inhibition of the human NAD+-dependent deacetylase SIRT5 by suramin. Structure 15: 377-389.
    • (2007) Structure , vol.15 , pp. 377-389
    • Schuetz, A.1    Min, J.2    Antoshenko, T.3    Wang, C.L.4    Allali-Hassani, A.5
  • 43
    • 69949151709 scopus 로고    scopus 로고
    • Crystal structures of human SIRT3 displaying substrate-induced conformational changes
    • Jin L, Wei W, Jiang Y, Peng H, Cai J, et al. (2009) Crystal structures of human SIRT3 displaying substrate-induced conformational changes. J Biol Chem 284: 24394-24405.
    • (2009) J Biol Chem , vol.284 , pp. 24394-24405
    • Jin, L.1    Wei, W.2    Jiang, Y.3    Peng, H.4    Cai, J.5
  • 45
    • 2942534101 scopus 로고    scopus 로고
    • Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases
    • Zhao K, Harshaw R, Chai X, Marmorstein R, (2004) Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases. Proc Natl Acad Sci USA 101: 8563-8568.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8563-8568
    • Zhao, K.1    Harshaw, R.2    Chai, X.3    Marmorstein, R.4
  • 46
    • 33846709501 scopus 로고    scopus 로고
    • Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes
    • Sanders BD, Zhao K, Slama JT, Marmorstein R, (2007) Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes. Mol Cell 25: 463-472.
    • (2007) Mol Cell , vol.25 , pp. 463-472
    • Sanders, B.D.1    Zhao, K.2    Slama, J.T.3    Marmorstein, R.4
  • 47
    • 33845476236 scopus 로고    scopus 로고
    • Adenosine mimetics as inhibitors of NAD+-dependent histone deacetylases, from kinase to sirtuin inhibition
    • Trapp J, Jochum A, Meier R, Saunders L, Marshall B, et al. (2006) Adenosine mimetics as inhibitors of NAD+-dependent histone deacetylases, from kinase to sirtuin inhibition. J Med Chem 49: 7307-7316.
    • (2006) J Med Chem , vol.49 , pp. 7307-7316
    • Trapp, J.1    Jochum, A.2    Meier, R.3    Saunders, L.4    Marshall, B.5
  • 48
    • 27644585190 scopus 로고    scopus 로고
    • A role for SIR-2.1 regulation of ER stress response genes in determining C. elegans life span
    • Viswanathan M, Kim SK, Berdichevsky A, Guarente L, (2005) A role for SIR-2.1 regulation of ER stress response genes in determining C. elegans life span. Dev Cell 9: 605-615.
    • (2005) Dev Cell , vol.9 , pp. 605-615
    • Viswanathan, M.1    Kim, S.K.2    Berdichevsky, A.3    Guarente, L.4
  • 49
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W, (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 50
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • Vaguine AA, Richelle J, Wodak SJ, (1999) SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D Biol Crystallogr 55: 191-205.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 52
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 54
    • 0031059039 scopus 로고    scopus 로고
    • Detecting and overcoming crystal twinning
    • Yeates TO, (1997) Detecting and overcoming crystal twinning. Methods Enzymol 276: 344-358.
    • (1997) Methods Enzymol , vol.276 , pp. 344-358
    • Yeates, T.O.1
  • 55
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • Vagin AA, Isupov MN, (2001) Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps. Acta Crystallogr D Biol Crystallogr 57: 1451-1456.
    • (2001) Acta Crystallogr D Biol Crystallogr , vol.57 , pp. 1451-1456
    • Vagin, A.A.1    Isupov, M.N.2
  • 57
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-Building Tools for Molecular Graphics
    • Emsley P, Cowtan K, (2004) Coot: Model-Building Tools for Molecular Graphics. Acta Cryst Section D 60: 2126-2132.
    • (2004) Acta Cryst Section D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 58
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf AW, van Aalten DM, (2004) PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr D Biol Crystallogr 60: 1355-1363.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    van Aalten, D.M.2
  • 59
    • 0038003142 scopus 로고    scopus 로고
    • Nonisotopic substrate for assaying both human zinc and NAD+-dependent histone deacetylases
    • Heltweg B, Dequiedt F, Verdin E, Jung M, (2003) Nonisotopic substrate for assaying both human zinc and NAD+-dependent histone deacetylases. Anal Biochem 319: 42-48.
    • (2003) Anal Biochem , vol.319 , pp. 42-48
    • Heltweg, B.1    Dequiedt, F.2    Verdin, E.3    Jung, M.4
  • 60
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski RA, Moss DS, Thornton JM, (1993) Main-chain bond lengths and bond angles in protein structures. J Mol Biol 231: 1049-1067.
    • (1993) J Mol Biol , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 61
    • 0033397980 scopus 로고    scopus 로고
    • Python: a programming language for software integration and development
    • Sanner MF, (1999) Python: a programming language for software integration and development. J Mol Graph Model 17: 57-61.
    • (1999) J Mol Graph Model , vol.17 , pp. 57-61
    • Sanner, M.F.1
  • 62
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • Diederichs K, Karplus PA, (1997) Improved R-factors for diffraction data analysis in macromolecular crystallography. Nat Struct Biol 4: 269-275.
    • (1997) Nat Struct Biol , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.