메뉴 건너뛰기




Volumn 76, Issue 1, 2010, Pages 10-16

NMR-based design and evaluation of novel bidentate inhibitors of the protein tyrosine phosphatase YopH

Author keywords

NMR screening; Protein tyrosine phosphatase; Spin label; Yersinia; YopH

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL PROTEIN; BIDENTATE DERIVATIVE; FURANYL SALICYLATE DERIVATIVE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; PROTEIN YOPH; UNCLASSIFIED DRUG; MOLECULAR LIBRARY; OUTER MEMBRANE PROTEIN; YOPH PROTEIN, YERSINIA;

EID: 77952976580     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2010.00982.x     Document Type: Article
Times cited : (21)

References (35)
  • 1
    • 0028802323 scopus 로고
    • Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell
    • Persson C., Nordfelth R., Holmstrom A., Hakansson S., Rosqvist R., Wolf-Watz H. (1995) Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell. Mol Microbiol 18 : 135 150.
    • (1995) Mol Microbiol , vol.18 , pp. 135-150
    • Persson, C.1    Nordfelth, R.2    Holmstrom, A.3    Hakansson, S.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 2
    • 0034085052 scopus 로고    scopus 로고
    • Yersinia enterocolitica TyeA, an intracellular regulator of the type III machinery, is required for specific targeting of YopE, YopH, YopM, and YopN into the cytosol of eukaryotic cells
    • Cheng L.W., Schneewind O. (2000) Yersinia enterocolitica TyeA, an intracellular regulator of the type III machinery, is required for specific targeting of YopE, YopH, YopM, and YopN into the cytosol of eukaryotic cells. J Bacteriol 182 : 3183 3190.
    • (2000) J Bacteriol , vol.182 , pp. 3183-3190
    • Cheng, L.W.1    Schneewind, O.2
  • 3
    • 0034729212 scopus 로고    scopus 로고
    • Type III secretion: A bacterial device for close combat with cells of their eukaryotic host
    • Cornelis G.R. (2000) Type III secretion: a bacterial device for close combat with cells of their eukaryotic host. Philos Trans R Soc Lond B Biol Sci 355 : 681 693.
    • (2000) Philos Trans R Soc Lond B Biol Sci , vol.355 , pp. 681-693
    • Cornelis, G.R.1
  • 4
    • 0034254928 scopus 로고    scopus 로고
    • Molecular and cell biology aspects of plague
    • Cornelis G.R. (2000) Molecular and cell biology aspects of plague. Proc Natl Acad Sci USA 97 : 8778 8783.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8778-8783
    • Cornelis, G.R.1
  • 5
    • 0242401865 scopus 로고    scopus 로고
    • High-resolution structure of the Yersinia pestis protein tyrosine phosphatase YopH in complex with a phosphotyrosyl mimetic-containing hexapeptide
    • Phan J., Lee K., Cherry S., Tropea J.E., Burke T.R. Jr., Waugh D.S. (2003) High-resolution structure of the Yersinia pestis protein tyrosine phosphatase YopH in complex with a phosphotyrosyl mimetic-containing hexapeptide. Biochemistry 42 : 13113 13121.
    • (2003) Biochemistry , vol.42 , pp. 13113-13121
    • Phan, J.1    Lee, K.2    Cherry, S.3    Tropea, J.E.4    Burke, Jr.T.R.5    Waugh, D.S.6
  • 6
    • 0033791898 scopus 로고    scopus 로고
    • The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages
    • Black D.S., Marie-Cardine A., Schraven B., Bliska J.B. (2000) The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages. Cell Microbiol 2 : 401 414.
    • (2000) Cell Microbiol , vol.2 , pp. 401-414
    • Black, D.S.1    Marie-Cardine, A.2    Schraven, B.3    Bliska, J.B.4
  • 7
    • 0031689503 scopus 로고    scopus 로고
    • Identification of an amino-terminal substrate-binding domain in the Yersinia tyrosine phosphatase that is required for efficient recognition of focal adhesion targets
    • Black D.S., Montagna L.G., Zitsmann S., Bliska J.B. (1998) Identification of an amino-terminal substrate-binding domain in the Yersinia tyrosine phosphatase that is required for efficient recognition of focal adhesion targets. Mol Microbiol 29 : 1263 1274.
    • (1998) Mol Microbiol , vol.29 , pp. 1263-1274
    • Black, D.S.1    Montagna, L.G.2    Zitsmann, S.3    Bliska, J.B.4
  • 8
    • 0037167585 scopus 로고    scopus 로고
    • Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: Comparison with a crystal structure
    • Khandelwal P., Keliikuli K., Smith C.L., Saper M.A., Zuiderweg E.R. (2002) Solution structure and phosphopeptide binding to the N-terminal domain of Yersinia YopH: comparison with a crystal structure. Biochemistry 41 : 11425 11437.
    • (2002) Biochemistry , vol.41 , pp. 11425-11437
    • Khandelwal, P.1    Keliikuli, K.2    Smith, C.L.3    Saper, M.A.4    Zuiderweg, E.R.5
  • 9
    • 0025024995 scopus 로고
    • Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia
    • Guan K.L., Dixon J.E. (1990) Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 249 : 553 556.
    • (1990) Science , vol.249 , pp. 553-556
    • Guan, K.L.1    Dixon, J.E.2
  • 10
    • 34948904919 scopus 로고    scopus 로고
    • Yersinia pestis CO92 delta yopH is a potent live, attenuated plague vaccine
    • Bubeck S.S., Dube P.H. (2007) Yersinia pestis CO92 delta yopH is a potent live, attenuated plague vaccine. Clin Vaccine Immunol 14 : 1235 1238.
    • (2007) Clin Vaccine Immunol , vol.14 , pp. 1235-1238
    • Bubeck, S.S.1    Dube, P.H.2
  • 11
    • 34247592309 scopus 로고    scopus 로고
    • Development of molecular probes for second-site screening and design of protein tyrosine phosphatase inhibitors
    • Vazquez J., Tautz L., Ryan J.J., Vuori K., Mustelin T., Pellecchia M. (2007) Development of molecular probes for second-site screening and design of protein tyrosine phosphatase inhibitors. J Med Chem 50 : 2137 2143.
    • (2007) J Med Chem , vol.50 , pp. 2137-2143
    • Vazquez, J.1    Tautz, L.2    Ryan, J.J.3    Vuori, K.4    Mustelin, T.5    Pellecchia, M.6
  • 12
    • 0034822661 scopus 로고    scopus 로고
    • Spin label enhanced NMR screening
    • Jahnke W., Rudisser S., Zurini M. (2001) Spin label enhanced NMR screening. J Am Chem Soc 123 : 3149 3150.
    • (2001) J Am Chem Soc , vol.123 , pp. 3149-3150
    • Jahnke, W.1    Rudisser, S.2    Zurini, M.3
  • 14
    • 0036523375 scopus 로고    scopus 로고
    • Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy
    • Jahnke W. (2002) Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy. Chembiochem 3 : 167 173.
    • (2002) Chembiochem , vol.3 , pp. 167-173
    • Jahnke, W.1
  • 15
    • 45749113037 scopus 로고    scopus 로고
    • Development of paramagnetic probes for molecular recognition studies in protein kinases
    • Vazquez J., De S.K., Chen L.H., Riel-Mehan M., Emdadi A., Cellitti J. et al. (2008) Development of paramagnetic probes for molecular recognition studies in protein kinases. J Med Chem 51 : 3460 3465.
    • (2008) J Med Chem , vol.51 , pp. 3460-3465
    • Vazquez, J.1    De, S.K.2    Chen, L.H.3    Riel-Mehan, M.4    Emdadi, A.5    Cellitti, J.6
  • 17
    • 15744388307 scopus 로고    scopus 로고
    • Inhibition of Yersinia tyrosine phosphatase by furanyl salicylate compounds
    • Tautz L., Bruckner S., Sareth S., Alonso A., Bogetz J., Bottini N. et al. (2005) Inhibition of Yersinia tyrosine phosphatase by furanyl salicylate compounds. J Biol Chem 280 : 9400 9408.
    • (2005) J Biol Chem , vol.280 , pp. 9400-9408
    • Tautz, L.1    Bruckner, S.2    Sareth, S.3    Alonso, A.4    Bogetz, J.5    Bottini, N.6
  • 18
    • 34249052551 scopus 로고    scopus 로고
    • Strategies for developing protein tyrosine phosphatase inhibitors
    • DOI 10.1016/j.ymeth.2007.02.014, PII S1046202307000424, Emerging New Techniques for Studying Protein Phosphatases
    • Tautz L., Mustelin T. (2007) Strategies for developing protein tyrosine phosphatase inhibitors. Methods 42 : 250 260. (Pubitemid 46783589)
    • (2007) Methods , vol.42 , Issue.3 , pp. 250-260
    • Tautz, L.1    Mustelin, T.2
  • 19
    • 0034740867 scopus 로고    scopus 로고
    • 1H, 15N and 13C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptide
    • Khandelwal P., Keliikuli K., Smit C.L., Saper M.A., Zuiderweg E.R. (2001) 1H, 15N and 13C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptide. J Biomol NMR 21 : 69 70.
    • (2001) J Biomol NMR , vol.21 , pp. 69-70
    • Khandelwal, P.1    Keliikuli, K.2    Smit, C.L.3    Saper, M.A.4    Zuiderweg, E.R.5
  • 20
    • 1042266623 scopus 로고    scopus 로고
    • Lck dephosphorylation at Tyr-394 and inhibition of T cell antigen receptor signaling by Yersinia phosphatase YopH
    • Alonso A., Bottini N., Bruckner S., Rahmouni S., Williams S., Schoenberger S.P. et al. (2004) Lck dephosphorylation at Tyr-394 and inhibition of T cell antigen receptor signaling by Yersinia phosphatase YopH. J Biol Chem 279 : 4922 4928.
    • (2004) J Biol Chem , vol.279 , pp. 4922-4928
    • Alonso, A.1    Bottini, N.2    Bruckner, S.3    Rahmouni, S.4    Williams, S.5    Schoenberger, S.P.6
  • 21
    • 71049126149 scopus 로고    scopus 로고
    • Multidentate small-molecule inhibitors of vaccinia H1-related (VHR) phosphatase decrease proliferation of cervix cancer cells
    • Wu S., Vossius S., Rahmouni S., Miletic A.V., Vang T., Vazquez-Rodriguez J. et al. (2009) Multidentate small-molecule inhibitors of vaccinia H1-related (VHR) phosphatase decrease proliferation of cervix cancer cells. J Med Chem 52 : 6716 6723.
    • (2009) J Med Chem , vol.52 , pp. 6716-6723
    • Wu, S.1    Vossius, S.2    Rahmouni, S.3    Miletic, A.V.4    Vang, T.5    Vazquez-Rodriguez, J.6
  • 23
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • Eldridge M.D., Murray C.W., Auton T.R., Paolini G.V., Mee R.P. (1997) Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes. J Comput Aided Mol Des 11 : 425 445.
    • (1997) J Comput Aided Mol des , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5
  • 24
    • 61849109430 scopus 로고    scopus 로고
    • Discovery and binding studies on a series of novel Pin1 ligands
    • Wu B., Rega M.F., Wei J., Yuan H., Dahl R., Zhang Z. et al. (2009) Discovery and binding studies on a series of novel Pin1 ligands. Chem Biol Drug Des 73 : 369 379.
    • (2009) Chem Biol Drug des , vol.73 , pp. 369-379
    • Wu, B.1    Rega, M.F.2    Wei, J.3    Yuan, H.4    Dahl, R.5    Zhang, Z.6
  • 25
    • 0036893660 scopus 로고    scopus 로고
    • Genetic requirements for salmonella-induced cytopathology in human monocyte-derived macrophages
    • Browne S.H., Lesnick M.L., Guiney D.G. (2002) Genetic requirements for salmonella-induced cytopathology in human monocyte-derived macrophages. Infect Immun 70 : 7126 7135.
    • (2002) Infect Immun , vol.70 , pp. 7126-7135
    • Browne, S.H.1    Lesnick, M.L.2    Guiney, D.G.3
  • 26
    • 33747595206 scopus 로고    scopus 로고
    • Structure-activity relationships by interligand NOE-based design and synthesis of antiapoptotic compounds targeting Bid
    • Becattini B., Culmsee C., Leone M., Zhai D., Zhang X., Crowell K.J. et al. (2006) Structure-activity relationships by interligand NOE-based design and synthesis of antiapoptotic compounds targeting Bid. Proc Natl Acad Sci USA 103 : 12602 12606.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 12602-12606
    • Becattini, B.1    Culmsee, C.2    Leone, M.3    Zhai, D.4    Zhang, X.5    Crowell, K.J.6
  • 27
    • 33645302925 scopus 로고    scopus 로고
    • SAR by ILOEs: An NMR-based approach to reverse chemical genetics
    • Becattini B., Pellecchia M. (2006) SAR by ILOEs: an NMR-based approach to reverse chemical genetics. Chemistry 12 : 2658 2662.
    • (2006) Chemistry , vol.12 , pp. 2658-2662
    • Becattini, B.1    Pellecchia, M.2
  • 29
    • 25144456011 scopus 로고    scopus 로고
    • Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions
    • Pellecchia M. (2005) Solution nuclear magnetic resonance spectroscopy techniques for probing intermolecular interactions. Chem Biol 12 : 961 971.
    • (2005) Chem Biol , vol.12 , pp. 961-971
    • Pellecchia, M.1
  • 30
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C., Xia T.H., Billeter M., Güntert P., Wüthrich K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomol NMR 5 : 1 10.
    • (1995) J Biomol NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 32
    • 9844252882 scopus 로고    scopus 로고
    • NMR-based discovery of lead inhibitors that block DNA binding of the human papillomavirus E2 protein
    • Hajduk P.J., Dinges J., Miknis G.F., Merlock M., Middleton T., Kempf D.J. et al. (1997) NMR-based discovery of lead inhibitors that block DNA binding of the human papillomavirus E2 protein. J Med Chem 40 : 3144 3150.
    • (1997) J Med Chem , vol.40 , pp. 3144-3150
    • Hajduk, P.J.1    Dinges, J.2    Miknis, G.F.3    Merlock, M.4    Middleton, T.5    Kempf, D.J.6
  • 33
    • 33749659675 scopus 로고    scopus 로고
    • SAR by NMR: Putting the pieces together
    • Hajduk P.J. (2006) SAR by NMR: putting the pieces together. Mol Interv 6 : 266 272.
    • (2006) Mol Interv , vol.6 , pp. 266-272
    • Hajduk, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.