메뉴 건너뛰기




Volumn 55, Issue 18, 2012, Pages 8021-8027

Structural analysis of bengamide derivatives as inhibitors of methionine aminopeptidases

Author keywords

[No Author keywords available]

Indexed keywords

BENGAMIDE 1; BENGAMIDE 2; BENGAMIDE DERIVATIVE; ENZYME INHIBITOR; METHIONYL AMINOPEPTIDASE; NATURAL PRODUCT; UNCLASSIFIED DRUG;

EID: 84866863979     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm3008695     Document Type: Article
Times cited : (26)

References (37)
  • 1
    • 0022979685 scopus 로고
    • Bengamides, heterocyclic anthelmintics from a Jaspidae marine sponge
    • Quinoa, E.; Adamczeski, M.; Crews, P.; Bakus, G. J. Bengamides, heterocyclic anthelmintics from a Jaspidae marine sponge J. Org. Chem. 1986, 51, 4494-4497
    • (1986) J. Org. Chem. , vol.51 , pp. 4494-4497
    • Quinoa, E.1    Adamczeski, M.2    Crews, P.3    Bakus, G.J.4
  • 7
    • 0024347025 scopus 로고
    • Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
    • Chang, S. Y.; McGary, E. C.; Chang, S. Methionine aminopeptidase gene of Escherichia coli is essential for cell growth J. Bacteriol. 1989, 171, 4071-4072
    • (1989) J. Bacteriol. , vol.171 , pp. 4071-4072
    • Chang, S.Y.1    McGary, E.C.2    Chang, S.3
  • 8
    • 0024729628 scopus 로고
    • PepM is an essential gene in Salmonella typhimurium
    • Miller, C. G.; Kukral, A. M.; Miller, J. L.; Movva, N. R. pepM is an essential gene in Salmonella typhimurium J. Bacteriol. 1989, 171, 5215-5217
    • (1989) J. Bacteriol. , vol.171 , pp. 5215-5217
    • Miller, C.G.1    Kukral, A.M.2    Miller, J.L.3    Movva, N.R.4
  • 9
    • 0036230288 scopus 로고    scopus 로고
    • Methionine in and out of proteins: Targets for drug design
    • Vaughan, M. D.; Sampson, P. B.; Honek, J. F. Methionine in and out of proteins: targets for drug design Curr. Med. Chem. 2002, 9, 385-409
    • (2002) Curr. Med. Chem. , vol.9 , pp. 385-409
    • Vaughan, M.D.1    Sampson, P.B.2    Honek, J.F.3
  • 10
    • 0029585125 scopus 로고
    • Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases
    • Li, X.; Chang, Y. H. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 12357-12361
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 12357-12361
    • Li, X.1    Chang, Y.H.2
  • 11
    • 0031171961 scopus 로고    scopus 로고
    • Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin
    • Griffith, E. C.; Su, Z.; Turk, B. E.; Chen, S.; Chang, Y. H.; Wu, Z.; Biemann, K.; Liu, J. O. Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin Chem. Biol. 1997, 4, 461-471
    • (1997) Chem. Biol. , vol.4 , pp. 461-471
    • Griffith, E.C.1    Su, Z.2    Turk, B.E.3    Chen, S.4    Chang, Y.H.5    Wu, Z.6    Biemann, K.7    Liu, J.O.8
  • 12
    • 33845310513 scopus 로고    scopus 로고
    • Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression
    • Hu, X.; Addlagatta, A.; Lu, J.; Matthews, B. W.; Liu, J. O. Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 18148-18153
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 18148-18153
    • Hu, X.1    Addlagatta, A.2    Lu, J.3    Matthews, B.W.4    Liu, J.O.5
  • 13
    • 33745918935 scopus 로고    scopus 로고
    • Targeted gene disruption of methionine aminopeptidase 2 results in an embryonic gastrulation defect and endothelial cell growth arrest
    • Yeh, J. R.; Ju, R.; Brdlik, C. M.; Zhang, W.; Zhang, Y.; Matyskiela, M. E.; Shotwell, J. D.; Crews, C. M. Targeted gene disruption of methionine aminopeptidase 2 results in an embryonic gastrulation defect and endothelial cell growth arrest Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 10379-10384
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 10379-10384
    • Yeh, J.R.1    Ju, R.2    Brdlik, C.M.3    Zhang, W.4    Zhang, Y.5    Matyskiela, M.E.6    Shotwell, J.D.7    Crews, C.M.8
  • 14
    • 0025204095 scopus 로고
    • Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth
    • Ingber, D.; Fujita, T.; Kishimoto, S.; Sudo, K.; Kanamaru, T.; Brem, H.; Folkman, J. Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth Nature 1990, 348, 555-557
    • (1990) Nature , vol.348 , pp. 555-557
    • Ingber, D.1    Fujita, T.2    Kishimoto, S.3    Sudo, K.4    Kanamaru, T.5    Brem, H.6    Folkman, J.7
  • 15
    • 0030924753 scopus 로고    scopus 로고
    • The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2
    • Sin, N.; Meng, L.; Wang, M. Q.; Wen, J. J.; Bornmann, W. G.; Crews, C. M. The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2 Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 6099-6103
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6099-6103
    • Sin, N.1    Meng, L.2    Wang, M.Q.3    Wen, J.J.4    Bornmann, W.G.5    Crews, C.M.6
  • 18
    • 0034901968 scopus 로고    scopus 로고
    • Phase i trial of the angiogenesis inhibitor TNP-470 for progressive androgen-independent prostate cancer
    • Logothetis, C. J.; Wu, K. K.; Finn, L. D.; Daliani, D.; Figg, W.; Ghaddar, H.; Gutterman, J. U. Phase I trial of the angiogenesis inhibitor TNP-470 for progressive androgen-independent prostate cancer Clin. Cancer Res. 2001, 7, 1198-1203
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1198-1203
    • Logothetis, C.J.1    Wu, K.K.2    Finn, L.D.3    Daliani, D.4    Figg, W.5    Ghaddar, H.6    Gutterman, J.U.7
  • 19
    • 0033564306 scopus 로고    scopus 로고
    • Escherichia coli methionine aminopeptidase: Implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis
    • Lowther, W. T.; Orville, A. M.; Madden, D. T.; Lim, S.; Rich, D. H.; Matthews, B. W. Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis Biochemistry 1999, 38, 7678-7688
    • (1999) Biochemistry , vol.38 , pp. 7678-7688
    • Lowther, W.T.1    Orville, A.M.2    Madden, D.T.3    Lim, S.4    Rich, D.H.5    Matthews, B.W.6
  • 20
    • 79957587056 scopus 로고    scopus 로고
    • Inhibition of Mycobacterium tuberculosis methionine aminopeptidases by bengamide derivatives
    • Lu, J. P.; Yuan, X. H.; Yuan, H.; Wang, W. L.; Wan, B.; Franzblau, S. G.; Ye, Q. Z. Inhibition of Mycobacterium tuberculosis methionine aminopeptidases by bengamide derivatives ChemMedChem 2011, 6, 1041-1048
    • (2011) ChemMedChem , vol.6 , pp. 1041-1048
    • Lu, J.P.1    Yuan, X.H.2    Yuan, H.3    Wang, W.L.4    Wan, B.5    Franzblau, S.G.6    Ye, Q.Z.7
  • 21
    • 33746265863 scopus 로고    scopus 로고
    • Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases
    • Hu, X.; Addlagatta, A.; Matthews, B. W.; Liu, J. O. Identification of pyridinylpyrimidines as inhibitors of human methionine aminopeptidases Angew. Chem., Int. Ed. 2006, 45, 3772-3775
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 3772-3775
    • Hu, X.1    Addlagatta, A.2    Matthews, B.W.3    Liu, J.O.4
  • 22
    • 33746496094 scopus 로고    scopus 로고
    • Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human type 1 methionine aminopeptidase
    • Addlagatta, A.; Matthews, B. W. Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human type 1 methionine aminopeptidase Protein Sci. 2006, 15, 1842-1848
    • (2006) Protein Sci. , vol.15 , pp. 1842-1848
    • Addlagatta, A.1    Matthews, B.W.2
  • 23
    • 84855816823 scopus 로고    scopus 로고
    • Structural analysis of inhibition of Mycobacterium tuberculosis methionine aminopeptidase by bengamide derivatives
    • Lu, J. P.; Yuan, X. H.; Ye, Q. Z. Structural analysis of inhibition of Mycobacterium tuberculosis methionine aminopeptidase by bengamide derivatives Eur. J. Med. Chem. 2012, 47, 479-484
    • (2012) Eur. J. Med. Chem. , vol.47 , pp. 479-484
    • Lu, J.P.1    Yuan, X.H.2    Ye, Q.Z.3
  • 25
    • 0028819132 scopus 로고
    • Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth
    • Zuo, S.; Guo, Q.; Ling, C.; Chang, Y. H. Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth Mol. Gen. Genet. 1995, 246, 247-253
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 247-253
    • Zuo, S.1    Guo, Q.2    Ling, C.3    Chang, Y.H.4
  • 26
    • 2942750310 scopus 로고    scopus 로고
    • Characterization of full length and truncated type i human methionine aminopeptidases expressed from Escherichia coli
    • Li, J. Y.; Chen, L. L.; Cui, Y. M.; Luo, Q. L.; Gu, M.; Nan, F. J.; Ye, Q. Z. Characterization of full length and truncated type I human methionine aminopeptidases expressed from Escherichia coli Biochemistry 2004, 43, 7892-7898
    • (2004) Biochemistry , vol.43 , pp. 7892-7898
    • Li, J.Y.1    Chen, L.L.2    Cui, Y.M.3    Luo, Q.L.4    Gu, M.5    Nan, F.J.6    Ye, Q.Z.7
  • 27
    • 27744565323 scopus 로고    scopus 로고
    • Structural basis for the functional differences between type i and type II human methionine aminopeptidases
    • Addlagatta, A.; Hu, X.; Liu, J. O.; Matthews, B. W. Structural basis for the functional differences between type I and type II human methionine aminopeptidases Biochemistry 2005, 44, 14741-14749
    • (2005) Biochemistry , vol.44 , pp. 14741-14749
    • Addlagatta, A.1    Hu, X.2    Liu, J.O.3    Matthews, B.W.4
  • 29
    • 35848950015 scopus 로고    scopus 로고
    • Kinetic and mutational studies of the number of interacting divalent cations required by bacterial and human methionine aminopeptidases
    • Hu, X. V.; Chen, X.; Han, K. C.; Mildvan, A. S.; Liu, J. O. Kinetic and mutational studies of the number of interacting divalent cations required by bacterial and human methionine aminopeptidases Biochemistry 2007, 46, 12833-12843
    • (2007) Biochemistry , vol.46 , pp. 12833-12843
    • Hu, X.V.1    Chen, X.2    Han, K.C.3    Mildvan, A.S.4    Liu, J.O.5
  • 30
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • Minor, W.; Cymborowski, M.; Otwinowski, Z.; Chruszcz, M. HKL-3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes Acta Crystallogr., Sect. D: Biol. Crystallogr. 2006, 62, 859-866
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 31
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A.; Teplyakov, A. MOLREP: an automated program for molecular replacement J. Appl. Crystallogr. 1997, 30, 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 32
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. 1994, D50, 760-763.
    • (1994) Acta Crystallogr. , vol.50 , pp. 760-763
  • 34
    • 77249109358 scopus 로고    scopus 로고
    • Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidase
    • Lu, J. P.; Chai, S. C.; Ye, Q. Z. Catalysis and inhibition of Mycobacterium tuberculosis methionine aminopeptidase J. Med. Chem. 2010, 53, 1329-1337
    • (2010) J. Med. Chem. , vol.53 , pp. 1329-1337
    • Lu, J.P.1    Chai, S.C.2    Ye, Q.Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.