메뉴 건너뛰기




Volumn 56, Issue 16, 2013, Pages 6512-6520

Erratum: Total synthesis and full histone deacetylase inhibitory profiling of azumamides A-E as well as β2-epi-azumaide e and β3-epi-azumaide e (Journal of Medicinal Chemistry (2013) 56:16 (6512-6520) DOI:10.1021/jm4008449);Total synthesis and full histone deacetylase inhibitory profiling of azumamides A-E as Well as β2- epi -Azumamide e and β3- epi -Azumamide e

Author keywords

[No Author keywords available]

Indexed keywords

AZUMAMIDE A; AZUMAMIDE B; AZUMAMIDE C; AZUMAMIDE D; AZUMAMIDE E; BETA2 EPIAZUMAMIDE E; BETA3 EPIAZUMAMIDE E; HISTONE DEACETYLASE INHIBITOR; TETRAPEPTIDE; UNCLASSIFIED DRUG;

EID: 84883180983     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm401223n     Document Type: Erratum
Times cited : (35)

References (36)
  • 1
    • 33846122993 scopus 로고    scopus 로고
    • Dimethyl sulfoxide to vorinostat: Development of this histone deacetylase inhibitor as an anticancer drug
    • Marks, P. A.; Breslow, R. Dimethyl sulfoxide to vorinostat: development of this histone deacetylase inhibitor as an anticancer drug Nat. Biotechnol. 2007, 25, 84-90
    • (2007) Nat. Biotechnol. , vol.25 , pp. 84-90
    • Marks, P.A.1    Breslow, R.2
  • 3
    • 0027378351 scopus 로고
    • Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase
    • Kijima, M.; Yoshida, M.; Sugita, K.; Horinouchi, S.; Beppu, T. Trapoxin, an antitumor cyclic tetrapeptide, is an irreversible inhibitor of mammalian histone deacetylase J. Biol. Chem. 1993, 268, 22429-22435
    • (1993) J. Biol. Chem. , vol.268 , pp. 22429-22435
    • Kijima, M.1    Yoshida, M.2    Sugita, K.3    Horinouchi, S.4    Beppu, T.5
  • 4
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton, J.; Hassig, C. A.; Schreiber, S. L. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p Science 1996, 272, 408-411
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 5
    • 0029795991 scopus 로고    scopus 로고
    • Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function
    • Taunton, J.; Collins, J. L.; Schreiber, S. L. Synthesis of natural and modified trapoxins, useful reagents for exploring histone deacetylase function J. Am. Chem. Soc. 1996, 118, 10412-10422
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10412-10422
    • Taunton, J.1    Collins, J.L.2    Schreiber, S.L.3
  • 6
    • 78649304686 scopus 로고    scopus 로고
    • Role of histone deacetylases and their inhibitors in cancer biology and treatment
    • Beumer, J. H.; Tawbi, H. Role of histone deacetylases and their inhibitors in cancer biology and treatment Curr. Clin. Pharmacol. 2010, 5, 196-208
    • (2010) Curr. Clin. Pharmacol. , vol.5 , pp. 196-208
    • Beumer, J.H.1    Tawbi, H.2
  • 7
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland, M.; Montgomery, R. L.; Olson, E. N. The many roles of histone deacetylases in development and physiology: implications for disease and therapy Nat. Rev. Genet. 2009, 10, 32-42
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 8
    • 53249130741 scopus 로고    scopus 로고
    • Therapeutic application of histone deacetylase inhibitors for central nervous system disorders
    • Kazantsev, A. G.; Thompson, L. M. Therapeutic application of histone deacetylase inhibitors for central nervous system disorders Nat. Rev. Drug Discovery 2008, 7, 854-868
    • (2008) Nat. Rev. Drug Discovery , vol.7 , pp. 854-868
    • Kazantsev, A.G.1    Thompson, L.M.2
  • 9
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci, S.; Pelicci, P. G. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer Nat. Rev. Cancer 2006, 6, 38-51
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 38-51
    • Minucci, S.1    Pelicci, P.G.2
  • 13
    • 34447340903 scopus 로고    scopus 로고
    • Zinc binding in HDAC inhibitors: A DFT study
    • Wang, D.; Helquist, P.; Wiest, O. Zinc binding in HDAC inhibitors: a DFT study J. Org. Chem. 2007, 72, 5446-5449
    • (2007) J. Org. Chem. , vol.72 , pp. 5446-5449
    • Wang, D.1    Helquist, P.2    Wiest, O.3
  • 15
    • 33947586979 scopus 로고    scopus 로고
    • Total synthesis of azumamide A and azumamide E, evaluation as histone deacetylase inhibitors, and design of a more potent analogue
    • Wen, S.; Carey, K. L.; Nakao, Y.; Fusetani, N.; Packham, G.; Ganesan, A. Total synthesis of azumamide A and azumamide E, evaluation as histone deacetylase inhibitors, and design of a more potent analogue Org. Lett. 2007, 9, 1105-1108
    • (2007) Org. Lett. , vol.9 , pp. 1105-1108
    • Wen, S.1    Carey, K.L.2    Nakao, Y.3    Fusetani, N.4    Packham, G.5    Ganesan, A.6
  • 19
    • 79959580534 scopus 로고    scopus 로고
    • Contemporary strategies for peptide macrocyclization
    • White, C. J.; Yudin, A. K. Contemporary strategies for peptide macrocyclization Nat. Chem. 2011, 3, 509-524
    • (2011) Nat. Chem. , vol.3 , pp. 509-524
    • White, C.J.1    Yudin, A.K.2
  • 20
    • 0036828151 scopus 로고    scopus 로고
    • Asymmetric synthesis of β-amino acid derivatives incorporating a broad range of substitution patterns by enolate additions to tert -butanesulfinyl imines
    • Tang, T. P.; Ellman, J. A. Asymmetric synthesis of β-amino acid derivatives incorporating a broad range of substitution patterns by enolate additions to tert -butanesulfinyl imines J. Org. Chem. 2002, 67, 7819-7832
    • (2002) J. Org. Chem. , vol.67 , pp. 7819-7832
    • Tang, T.P.1    Ellman, J.A.2
  • 21
    • 77953299014 scopus 로고    scopus 로고
    • Synthesis and applications of tert -butanesulfinamide
    • Robak, M. T.; Herbage, M. A.; Ellman, J. A. Synthesis and applications of tert -butanesulfinamide Chem. Rev. 2010, 110, 3600-3740
    • (2010) Chem. Rev. , vol.110 , pp. 3600-3740
    • Robak, M.T.1    Herbage, M.A.2    Ellman, J.A.3
  • 22
    • 33947468884 scopus 로고
    • The stereochemistry of the Ivanov and Reformatsky reactions. 1
    • Zimmerman, H. E.; Traxler, M. D. The stereochemistry of the Ivanov and Reformatsky reactions. 1 J. Am. Chem. Soc. 1957, 79, 1920-1923
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 1920-1923
    • Zimmerman, H.E.1    Traxler, M.D.2
  • 23
  • 24
    • 33847799798 scopus 로고
    • Ester enolate Claisen rearrangement: Stereochemical control through stereoselective enolate formation
    • Ireland, R. E.; Mueller, R. H.; Willard, A. K. Ester enolate Claisen rearrangement: Stereochemical control through stereoselective enolate formation J. Am. Chem. Soc. 1976, 98, 2868-2877
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 2868-2877
    • Ireland, R.E.1    Mueller, R.H.2    Willard, A.K.3
  • 25
    • 0001723738 scopus 로고
    • Acyclic stereoselection. 47. Stereochemistry of the Michael addition of ester and ketone enolates to α,β-unsaturated ketones
    • Oare, D. A.; Heathcock, C. H. Acyclic stereoselection. 47. Stereochemistry of the Michael addition of ester and ketone enolates to α,β-unsaturated ketones J. Org. Chem. 1990, 55, 157-172
    • (1990) J. Org. Chem. , vol.55 , pp. 157-172
    • Oare, D.A.1    Heathcock, C.H.2
  • 26
    • 67749142082 scopus 로고    scopus 로고
    • Design, synthesis, biological evaluation, and structural characterization of potent histone deacetylase inhibitors based on cyclic α/β- tetrapeptide architectures
    • Montero, A.; Beierle, J. M.; Olsen, C. A.; Ghadiri, M. R. Design, synthesis, biological evaluation, and structural characterization of potent histone deacetylase inhibitors based on cyclic α/β-tetrapeptide architectures J. Am. Chem. Soc. 2009, 131, 3033-3041
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 3033-3041
    • Montero, A.1    Beierle, J.M.2    Olsen, C.A.3    Ghadiri, M.R.4
  • 27
    • 72249094958 scopus 로고    scopus 로고
    • Discovery of potent and selective histone deacetylase inhibitors via focused combinatorial libraries of cyclic α3β-tetrapeptides
    • Olsen, C. A.; Ghadiri, M. R. Discovery of potent and selective histone deacetylase inhibitors via focused combinatorial libraries of cyclic α3β-tetrapeptides J. Med. Chem. 2009, 52, 7836-7846
    • (2009) J. Med. Chem. , vol.52 , pp. 7836-7846
    • Olsen, C.A.1    Ghadiri, M.R.2
  • 29
    • 84866367304 scopus 로고    scopus 로고
    • Macrocyclic peptoid-peptide hybrids as inhibitors of class i histone deacetylases
    • Olsen, C. A.; Montero, A.; Leman, L. J.; Ghadiri, M. R. Macrocyclic peptoid-peptide hybrids as inhibitors of class I histone deacetylases ACS Med. Chem. Lett. 2012, 3, 749-753
    • (2012) ACS Med. Chem. Lett. , vol.3 , pp. 749-753
    • Olsen, C.A.1    Montero, A.2    Leman, L.J.3    Ghadiri, M.R.4
  • 30
    • 84862271824 scopus 로고    scopus 로고
    • Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme
    • Madsen, A. S.; Olsen, C. A. Substrates for efficient fluorometric screening employing the NAD-dependent sirtuin 5 lysine deacylase (KDAC) enzyme J. Med. Chem. 2012, 55, 5582-5590
    • (2012) J. Med. Chem. , vol.55 , pp. 5582-5590
    • Madsen, A.S.1    Olsen, C.A.2
  • 31
    • 84865848261 scopus 로고    scopus 로고
    • Profiling of substrates for zinc-dependent lysine deacylase enzymes: HDAC3 exhibits decrotonylase activity in vitro
    • Madsen, A. S.; Olsen, C. A. Profiling of substrates for zinc-dependent lysine deacylase enzymes: HDAC3 exhibits decrotonylase activity in vitro Angew. Chem., Int. Ed. 2012, 51, 9083-9087
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 9083-9087
    • Madsen, A.S.1    Olsen, C.A.2
  • 34
    • 78650111987 scopus 로고    scopus 로고
    • Probing the biology of natural products: Molecular editing by diverted total synthesis
    • Szpilman, A. M.; Carreira, E. M. Probing the biology of natural products: Molecular editing by diverted total synthesis Angew. Chem., Int. Ed. 2010, 49, 9592-9628
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 9592-9628
    • Szpilman, A.M.1    Carreira, E.M.2
  • 36
    • 77956034361 scopus 로고    scopus 로고
    • On the reach of chemical synthesis: Creation of a mini-pipeline from an academic laboratory
    • Wilson, R. M.; Danishefsky, S. J. On the reach of chemical synthesis: creation of a mini-pipeline from an academic laboratory Angew. Chem., Int. Ed. 2010, 49, 6032-6056
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 60326056
    • Wilson, R.M.1    Danishefsky, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.