메뉴 건너뛰기




Volumn 5, Issue 6, 2009, Pages 407-413

Impact of linker strain and flexibility in the design of a fragment-based inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

AMINE; BINDING PROTEIN; URACIL DNA GLYCOSIDASE;

EID: 67349171544     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.163     Document Type: Article
Times cited : (97)

References (25)
  • 2
    • 0035324944 scopus 로고    scopus 로고
    • Molecular complexity and its impact on the probability of finding leads for drug discovery
    • Hann, M.M., Leach, A.R. & Harper, G. Molecular complexity and its impact on the probability of finding leads for drug discovery. J. Chem. Inf. Comput. Sci. 41, 856-864 (2001).
    • (2001) J. Chem. Inf. Comput. Sci , vol.41 , pp. 856-864
    • Hann, M.M.1    Leach, A.R.2    Harper, G.3
  • 3
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W.P. On the attribution and additivity of binding energies. Proc. Natl. Acad. Sci. USA 78, 4046-4050 (1981).
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 4
    • 0036821028 scopus 로고    scopus 로고
    • The consequences of translational and rotational entropy lost by small molecules on binding to proteins
    • Murray, C.W. & Verdonk, M.L. The consequences of translational and rotational entropy lost by small molecules on binding to proteins. J. Comput. Aided Mol. Des. 16, 741-753 (2002).
    • (2002) J. Comput. Aided Mol. Des , vol.16 , pp. 741-753
    • Murray, C.W.1    Verdonk, M.L.2
  • 5
    • 29044441527 scopus 로고    scopus 로고
    • Uracil-directed ligand tethering: An efficient strategy for uracil DNA glycosylase (UNG) inhibitor development
    • Jiang, Y.L., Krosky, D.J., Seiple, L. & Stivers, J.T. Uracil-directed ligand tethering: an efficient strategy for uracil DNA glycosylase (UNG) inhibitor development. J. Am. Chem. Soc. 127, 17412-17420 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 17412-17420
    • Jiang, Y.L.1    Krosky, D.J.2    Seiple, L.3    Stivers, J.T.4
  • 6
    • 33845601247 scopus 로고    scopus 로고
    • Mimicking damaged DNA with a small molecule inhibitor of human UNG2
    • Krosky, D.J. et al. Mimicking damaged DNA with a small molecule inhibitor of human UNG2. Nucleic Acids Res. 34, 5872-5879 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 5872-5879
    • Krosky, D.J.1
  • 7
    • 33745590702 scopus 로고    scopus 로고
    • Synthesis and high-throughput evaluation of triskelion uracil libraries for inhibition of human dUTPase and UNG2
    • Jiang, Y.L., Chung, S., Krosky, D.J. & Stivers, J.T. Synthesis and high-throughput evaluation of triskelion uracil libraries for inhibition of human dUTPase and UNG2. Bioorg. Med. Chem. 14, 5666-5672 (2006).
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 5666-5672
    • Jiang, Y.L.1    Chung, S.2    Krosky, D.J.3    Stivers, J.T.4
  • 8
    • 33644910731 scopus 로고    scopus 로고
    • Uracils as a cellular weapon against viruses and mechanisms of viral escape
    • Priet, S., Sire, J. & Querat, G. Uracils as a cellular weapon against viruses and mechanisms of viral escape. Curr. HIV Res. 4, 31-42 (2006).
    • (2006) Curr. HIV Res , vol.4 , pp. 31-42
    • Priet, S.1    Sire, J.2    Querat, G.3
  • 10
    • 31644442238 scopus 로고    scopus 로고
    • Linking uracil base excision repair and 5-fluorouracil toxicity in yeast
    • Seiple, L., Jaruga, P., Dizdaroglu, M. & Stivers, J.T. Linking uracil base excision repair and 5-fluorouracil toxicity in yeast. Nucleic Acids Res. 34, 140-151 (2006).
    • (2006) Nucleic Acids Res , vol.34 , pp. 140-151
    • Seiple, L.1    Jaruga, P.2    Dizdaroglu, M.3    Stivers, J.T.4
  • 11
    • 0032763166 scopus 로고    scopus 로고
    • Expression of deoxyuridine triphosphatase (dUTPase) in colorectal tumours
    • Fleischmann, J. et al. Expression of deoxyuridine triphosphatase (dUTPase) in colorectal tumours. Int. J. Cancer 84, 614-617 (1999).
    • (1999) Int. J. Cancer , vol.84 , pp. 614-617
    • Fleischmann, J.1
  • 12
    • 33746683717 scopus 로고    scopus 로고
    • Genomic uracil and human disease
    • Hagen, L. et al. Genomic uracil and human disease. Exp. Cell Res. 312, 2666-2672 (2006).
    • (2006) Exp. Cell Res , vol.312 , pp. 2666-2672
    • Hagen, L.1
  • 13
    • 8644241815 scopus 로고    scopus 로고
    • Expression of the AID Protein in normal and neoplastic B-cells
    • Pasqualucci, L. et al. Expression of the AID Protein in normal and neoplastic B-cells. Blood 104, 3318-3325 (2004).
    • (2004) Blood , vol.104 , pp. 3318-3325
    • Pasqualucci, L.1
  • 14
    • 33644643189 scopus 로고    scopus 로고
    • Role of genomic instability and p53 in AID-induced c-myc-Igh translocations
    • Ramiro, A.R. et al. Role of genomic instability and p53 in AID-induced c-myc-Igh translocations. Nature 440, 105-109 (2006).
    • (2006) Nature , vol.440 , pp. 105-109
    • Ramiro, A.R.1
  • 15
    • 0034646370 scopus 로고    scopus 로고
    • Combinatorial target-guided ligand assembly: Identification of potent subtype-selective c-Src inhibitors
    • Maly, D.J., Choong, I.C. & Ellman, J.A. Combinatorial target-guided ligand assembly: identification of potent subtype-selective c-Src inhibitors. Proc. Natl. Acad. Sci. USA 97, 2419-2424 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2419-2424
    • Maly, D.J.1    Choong, I.C.2    Ellman, J.A.3
  • 16
    • 0033120232 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: Structure and glycosylase mechanism revisited
    • Xiao, G. et al. Crystal structure of Escherichia coli uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited. Proteins 35, 13-24 (1999).
    • (1999) Proteins , vol.35 , pp. 13-24
    • Xiao, G.1
  • 17
    • 0030592680 scopus 로고    scopus 로고
    • Aminolysis of sulfinamoyl-esters, -sulfonamides and -sulfones. Thiooxamate and thiourea formation via a suifine intermediate. Thiophilic or carbo-philic reaction?
    • Baltas, M. et al. Aminolysis of sulfinamoyl-esters, -sulfonamides and -sulfones. Thiooxamate and thiourea formation via a suifine intermediate. Thiophilic or carbo-philic reaction? Tetrahedron 52, 14865-14876 (1996).
    • (1996) Tetrahedron , vol.52 , pp. 14865-14876
    • Baltas, M.1
  • 18
    • 0015101706 scopus 로고
    • Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect
    • Page, M.I. & Jencks, W.P. Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect. Proc. Natl. Acad. Sci. USA 68, 1678-1683 (1971).
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1678-1683
    • Page, M.I.1    Jencks, W.P.2
  • 19
    • 0028454828 scopus 로고
    • The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure
    • Böhm, H.J. The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure. J. Comput. Aided Mol. Des. 8, 243-256 (1994).
    • (1994) J. Comput. Aided Mol. Des , vol.8 , pp. 243-256
    • Böhm, H.J.1
  • 20
    • 0032112137 scopus 로고    scopus 로고
    • Prediction of binding constants of protein ligands: A fast method for the prioritization of hits obtained from de novo design or 3D database search programs
    • Böhm, H.J. Prediction of binding constants of protein ligands: a fast method for the prioritization of hits obtained from de novo design or 3D database search programs. J. Comput. Aided Mol. Des. 12, 309-323 (1998).
    • (1998) J. Comput. Aided Mol. Des , vol.12 , pp. 309-323
    • Böhm, H.J.1
  • 21
    • 33751204422 scopus 로고    scopus 로고
    • Fragment-based lead discovery: A chemical update
    • Erlanson, D.A. Fragment-based lead discovery: a chemical update. Curr. Opin. Biotechnol. 17, 643-652 (2006).
    • (2006) Curr. Opin. Biotechnol , vol.17 , pp. 643-652
    • Erlanson, D.A.1
  • 22
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S.B., Hajduk, P.J., Meadows, R.P. & Fesik, S.W. Discovering high-affinity ligands for proteins: SAR by NMR. Science 274, 1531-1534 (1996).
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 23
    • 33751076241 scopus 로고    scopus 로고
    • Deconstructing fragment-based inhibitor discovery
    • Babaoglu, K. & Shoichet, B.K. Deconstructing fragment-based inhibitor discovery. Nat. Chem. Biol. 2, 720-723 (2006).
    • (2006) Nat. Chem. Biol , vol.2 , pp. 720-723
    • Babaoglu, K.1    Shoichet, B.K.2
  • 24
    • 0024745871 scopus 로고
    • The price of lost freedom: Entropy of bimolecular complex formation
    • Finkelstein, A.V. & Janin, J. The price of lost freedom: entropy of bimolecular complex formation. Protein Eng. 3, 1-3 (1989).
    • (1989) Protein Eng , vol.3 , pp. 1-3
    • Finkelstein, A.V.1    Janin, J.2
  • 25
    • 0031058541 scopus 로고    scopus 로고
    • The statistical-thermody-namic basis for computation of binding affinities: A critical review
    • Gilson, M.K., Given, J.A., Bush, B.L. & McCammon, J.A. The statistical-thermody-namic basis for computation of binding affinities: a critical review. Biophys. J 72, 1047-1069 (1997).
    • (1997) Biophys. J , vol.72 , pp. 1047-1069
    • Gilson, M.K.1    Given, J.A.2    Bush, B.L.3    McCammon, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.