메뉴 건너뛰기




Volumn 54, Issue 8, 2011, Pages 2933-2943

Utilization of nitrophenylphosphates and oxime-based ligation for the development of nanomolar affinity inhibitors of the Yersinia pestis outer protein H (YopH) phosphatase

Author keywords

[No Author keywords available]

Indexed keywords

NITROPHENYLPHOSPHATE DERIVATIVE; OUTER MEMBRANE PROTEIN; OXIME DERIVATIVE; PHENYL GROUP; PHOSPHATASE; PHOSPHATE; UNCLASSIFIED DRUG;

EID: 79955438388     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm200022g     Document Type: Article
Times cited : (44)

References (80)
  • 1
    • 70349897489 scopus 로고    scopus 로고
    • Physiological signaling specificity by protein tyrosine phosphatases
    • Soulsby, M.; Bennett, A. M. Physiological signaling specificity by protein tyrosine phosphatases Physiology 2009, 24, 281-289
    • (2009) Physiology , vol.24 , pp. 281-289
    • Soulsby, M.1    Bennett, A.M.2
  • 2
    • 63749113783 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: Thirty years and counting
    • Hunter, T. Tyrosine phosphorylation: thirty years and counting Curr. Opin. Cell Biol. 2009, 21, 140-146
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 140-146
    • Hunter, T.1
  • 3
    • 0037317489 scopus 로고    scopus 로고
    • PTP1B inhibitors as potential therapeutics in the treatment of type 2 diabetes and obesity
    • DOI 10.1517/13543784.12.2.223
    • Zhang, Z.-Y.; Lee, S.-Y. PTP1B inhibitors as potential therapeutics in the treatment of type 2 diabetes and obesity Expert Opin. Invest. Drugs 2003, 12, 223-233 (Pubitemid 36204601)
    • (2003) Expert Opinion on Investigational Drugs , vol.12 , Issue.2 , pp. 223-233
    • Zhang, Z.-Y.1    Lee, S.-Y.2
  • 5
    • 43049129579 scopus 로고    scopus 로고
    • Targeting PTPs with small molecule inhibitors in cancer treatment
    • Jiang, Z.-X.; Zhang, Z.-Y. Targeting PTPs with small molecule inhibitors in cancer treatment Cancer Metastasis Rev. 2008, 27, 263-272
    • (2008) Cancer Metastasis Rev. , vol.27 , pp. 263-272
    • Jiang, Z.-X.1    Zhang, Z.-Y.2
  • 6
    • 71049155822 scopus 로고    scopus 로고
    • Knowledge-based characterization of similarity relationships in the human protein-tyrosine phosphatase family for rational inhibitor design
    • Vidovic, D.; Schurer, S. C. Knowledge-based characterization of similarity relationships in the human protein-tyrosine phosphatase family for rational inhibitor design J. Med. Chem. 2009, 52, 6649-6659
    • (2009) J. Med. Chem. , vol.52 , pp. 6649-6659
    • Vidovic, D.1    Schurer, S.C.2
  • 9
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • DOI 10.1021/jm010533y
    • McGovern, S. L.; Caselli, E.; Grigorieff, N.; Shoichet, B. K. A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening J. Med. Chem. 2002, 45, 1712-1722 (Pubitemid 34293537)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.8 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 11
    • 0141923641 scopus 로고    scopus 로고
    • Identification and prediction of promiscuous aggregating inhibitors among known drugs
    • DOI 10.1021/jm030191r
    • Seidler, J.; McGovern, S. L.; Doman, T. N.; Shoichet, B. K. Identification and prediction of promiscuous aggregating inhibitors among known drugs J. Med. Chem. 2003, 46, 4477-4486 (Pubitemid 37238749)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.21 , pp. 4477-4486
    • Seidler, J.1    McGovern, S.L.2    Doman, T.N.3    Shoichet, B.K.4
  • 12
    • 0029015718 scopus 로고
    • Kinetic and mechanistic characterization of a mammalian protein-tyrosine phosphatase, PTP1
    • Zhang, Z.-Y. Kinetic and mechanistic characterization of a mammalian protein-tyrosine phosphatase, PTP1 J. Biol. Chem. 1995, 270, 11199-11204
    • (1995) J. Biol. Chem. , vol.270 , pp. 11199-11204
    • Zhang, Z.-Y.1
  • 13
    • 0029921630 scopus 로고    scopus 로고
    • Potent low molecular weight substrates for protein-tyrosine phosphatase
    • DOI 10.1074/jbc.271.13.7868
    • Montserat, J.; Chen, L.; Lawrence, D. S.; Zhang, Z.-Y. Potent low molecular weight substrates for protein-tyrosine phosphatase J. Biol. Chem. 1996, 271, 7868-7872 (Pubitemid 26107070)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.13 , pp. 7868-7872
    • Montserat, J.1    Chen, L.2    Lawrence, D.S.3    Zhang, Z.-Y.4
  • 14
    • 0029739468 scopus 로고    scopus 로고
    • VHR and PTP1 protein phosphatases exhibit remarkably different active site specificities toward low molecular weight nonpeptidic substrates
    • DOI 10.1021/bi960700+
    • Chen, L.; Montserat, J.; Lawrence, D. S.; Zhang, Z.-Y. VHR and PTP1 protein phosphatases exhibit remarkably different active site specificities toward low molecular weight nonpeptidic substrates Biochemistry 1996, 35, 9349-9354 (Pubitemid 26320039)
    • (1996) Biochemistry , vol.35 , Issue.29 , pp. 9349-9354
    • Chen, L.1    Montserat, J.2    Lawrence, D.S.3    Zhang, Z.-Y.4
  • 16
    • 27644555726 scopus 로고    scopus 로고
    • Substrate activity screening: A fragment-based method for the rapid identification of nonpeptidic protease inhibitors
    • DOI 10.1021/ja0547230
    • Wood, W. J. L.; Patterson, A. W.; Tsuruoka, H.; Jain, R. K.; Ellman, J. A. Substrate activity screening: a fragment-based method for the rapid identification of nonpeptidic protease inhibitors J. Am. Chem. Soc. 2005, 127, 15521-15527 (Pubitemid 41572526)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.44 , pp. 15521-15527
    • Wood, W.J.L.1    Patterson, A.W.2    Tsuruoka, H.3    Jain, R.K.4    Ellman, J.A.5
  • 17
    • 33745922373 scopus 로고    scopus 로고
    • Rapid identification of potent nonpeptidic serine protease inhibitors
    • DOI 10.1002/cbic.200600081
    • Salisbury, C. M.; Ellman, J. A. Rapid identification of potent nonpeptidic serine protease inhibitors ChemBioChem 2006, 7, 1034-1037 (Pubitemid 44049437)
    • (2006) ChemBioChem , vol.7 , Issue.7 , pp. 1034-1037
    • Salisbury, C.M.1    Ellman, J.A.2
  • 18
    • 34347226326 scopus 로고    scopus 로고
    • Substrate activity screening (SAS): A general procedure for the preparation and screening of a fragment-based non-peptidic protease substrate library for inhibitor discovery
    • DOI 10.1038/nprot.2007.28, PII NPROT.2007.28
    • Patterson, A. W.; Wood, W. J. L.; Ellman, J. A. Substrate activity screening (SAS): a general procedure for the preparation and screening of a fragment-based non-peptidic protease substrate library for inhibitor discovery Nat. Protoc. 2007, 2, 424-433 (Pubitemid 47040058)
    • (2007) Nature Protocols , vol.2 , Issue.2 , pp. 424-433
    • Patterson, A.W.1    Wood, W.J.L.2    Ellman, J.A.3
  • 19
    • 34250219213 scopus 로고    scopus 로고
    • Characterization and optimization of selective, nonpeptidic inhibitors of cathepsin S with an unprecedented binding mode
    • DOI 10.1021/jm070111+
    • Inagaki, H.; Tsuruoka, H.; Hornsby, M.; Lesley, S. A.; Spraggon, G.; Ellman, J. A. Characterization and optimization of selective, nonpeptidic inhibitors of cathepsin S with an unprecedented binding mode J. Med. Chem. 2007, 50, 2693-2699 (Pubitemid 46896077)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.11 , pp. 2693-2699
    • Inagaki, H.1    Tsuruoka, H.2    Hornsby, M.3    Lesley, S.A.4    Spraggon, G.5    Ellman, J.A.6
  • 21
    • 34547758886 scopus 로고    scopus 로고
    • Fragment-based substrate activity screening method for the identification of potent inhibitors of the Mycobacterium tuberculosis phosphatase PtpB
    • DOI 10.1021/ja0727520
    • Soellner, M. B.; Rawls, K. A.; Grundner, C.; Alber, T.; Ellman, J. A. Fragment-based substrate activity screening method for the identification of potent inhibitors of the Mycobacterium tuberculosis phosphatase PTPB J. Am. Chem. Soc. 2007, 129, 9613-9615 (Pubitemid 47237472)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.31 , pp. 9613-9615
    • Soellner, M.B.1    Rawls, K.A.2    Grundner, C.3    Alber, T.4    Ellman, J.A.5
  • 22
    • 0021219614 scopus 로고
    • A modified direct phosphate assay for studying ATPases
    • Jenkins, W. T.; Marshall, M. M. A modified direct phosphate assay for studying ATPases Anal. Biochem. 1984, 141, 155-160 (Pubitemid 14043271)
    • (1984) Analytical Biochemistry , vol.141 , Issue.1 , pp. 155-160
    • Jenkins, W.T.1    Marshall, M.M.2
  • 23
    • 0021077311 scopus 로고
    • Inorganic phosphate determination in the presence of a labile organic phosphate: Assay for carbamyl phosphate phosphatase activity
    • Black, M. J.; Jones, M. E. Inorganic phosphate determination in the presence of a labile organic phosphate: assay for carbamyl phosphate phosphatase activity Anal. Biochem. 1983, 135, 233-238 (Pubitemid 14218269)
    • (1983) Analytical Biochemistry , vol.135 , Issue.1 , pp. 233-238
    • Black, M.J.1    Jones, M.E.2
  • 24
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb, M. R. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 4884-487
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4884-487
    • Webb, M.R.1
  • 25
    • 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. Stategies for developing protein tyrosine phosphatase inhibitors Methods 2007, 42, 250-260 (Pubitemid 46783589)
    • (2007) Methods , vol.42 , Issue.3 , pp. 250-260
    • Tautz, L.1    Mustelin, T.2
  • 26
    • 0025976707 scopus 로고
    • Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart
    • Zhang, Z.-Y. Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart J. Biol. Chem. 1991, 266, 1516-1525
    • (1991) J. Biol. Chem. , vol.266 , pp. 1516-1525
    • Zhang, Z.-Y.1
  • 27
    • 0031457541 scopus 로고    scopus 로고
    • Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design
    • Puius, Y. A.; Zhao, Y.; Sullivan, M.; Lawrence, D. S.; Almo, S. C.; Zhang, Z.-Y. Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 13420-13425
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13420-13425
    • Puius, Y.A.1    Zhao, Y.2    Sullivan, M.3    Lawrence, D.S.4    Almo, S.C.5    Zhang, Z.-Y.6
  • 28
    • 0037174872 scopus 로고    scopus 로고
    • Probing the molecular basis for potent and selective protein-tyrosine phosphatase 1B inhibition
    • DOI 10.1074/jbc.M207347200
    • Guo, X.-L.; Shen, K.; Wang, F.; Lawrence, D. S.; Zhang, Z.-Y. Probing the molecular basis for potent and selective protein-tyrosine phosphatase 1B inhibition J. Biol. Chem. 2002, 277, 41014-41022 (Pubitemid 35215691)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.43 , pp. 41014-41022
    • Guo, X.-L.1    Shen, K.2    Wang, F.3    Lawrence, D.S.4    Zhang, Z.-Y.5
  • 29
    • 0037194618 scopus 로고    scopus 로고
    • Divalent and trivalent α-ketocarboxylic acids as inhibitors of protein tyrosine phosphatases
    • DOI 10.1021/jm020093q
    • Chen, Y. T.; Seto, C. T. Divalent and trivalent alpha-ketocarboxylic acids as inhibitors of protein tyrosine phosphatases J. Med. Chem. 2002, 45, 3946-3952 (Pubitemid 35024296)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.18 , pp. 3946-3952
    • Chen, Y.T.1    Seto, C.T.2
  • 30
    • 2542479008 scopus 로고    scopus 로고
    • Parallel synthesis of a library of bidentate protein tyrosine phosphatase inhibitors based on the α-ketoacid motif
    • DOI 10.1016/j.bmc.2004.03.058, PII S0968089604002639
    • Chen, Y. T.; Seto, C. T. Parallel synthesis of a library of bidentate protein tyrosine phosphatase inhibitors based on the alpha-ketoacid motif Bioor. Med. Chem. 2004, 12, 3289-3298 (Pubitemid 38680718)
    • (2004) Bioorganic and Medicinal Chemistry , vol.12 , Issue.12 , pp. 3289-3298
    • Chen, Y.T.1    Seto, C.T.2
  • 31
    • 15244355146 scopus 로고    scopus 로고
    • Investigations of linker structure on the potency of a series of bidentate protein tyrosine phosphatase inhibitors
    • DOI 10.1016/j.bmc.2005.02.001
    • Xie, J.; Seto, C. T. Investigations of linker structure on the potency of a series of bidentate protein tyrosine phosphatase inhibitors Bioorg. Med. Chem. 2005, 13, 2981-2991 (Pubitemid 40387506)
    • (2005) Bioorganic and Medicinal Chemistry , vol.13 , Issue.8 , pp. 2981-2991
    • Xie, J.1    Seto, C.T.2
  • 33
    • 77956747889 scopus 로고    scopus 로고
    • A focused library of protein tyrosine phosphatase inhibitors
    • Comeau, A. B.; Critton, D. A.; Page, R.; Seto, C. T. A focused library of protein tyrosine phosphatase inhibitors J. Med. Chem. 2010, 53, 6768-6772
    • (2010) J. Med. Chem. , vol.53 , pp. 6768-6772
    • Comeau, A.B.1    Critton, D.A.2    Page, R.3    Seto, C.T.4
  • 34
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb, H. C.; Finn, M. G.; Sharpless, K. B. Click chemistry: diverse chemical function from a few good reactions Angew. Chem., Int. Ed. 2001, 40, 2004-2021
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 35
    • 38749134860 scopus 로고    scopus 로고
    • Protected aminooxyprolines for expedited library synthesis: Application to Tsg101-directed proline-oxime containing peptides
    • DOI 10.1016/j.bmcl.2007.12.003, PII S0960894X07014461
    • Liu, F.; Stephen, A. G.; Fisher, R. J.; Burke, T. R., Jr. Protected aminooxyprolines for expedited library synthesis: application to Tsg101-directed proline-oxime containing peptides Bioorg. Med. Chem. Lett. 2008, 18, 1096-1101 (Pubitemid 351179331)
    • (2008) Bioorganic and Medicinal Chemistry Letters , vol.18 , Issue.3 , pp. 1096-1101
    • Liu, F.1    Stephen, A.G.2    Fisher, R.J.3    Burke Jr., T.R.4
  • 37
    • 49649128615 scopus 로고    scopus 로고
    • Synthesis of a homologous series of side-chain-extended orthogonally protected aminooxy-containing amino acids
    • Liu, F.; Thomas, J.; Burke, T. R., Jr. Synthesis of a homologous series of side-chain-extended orthogonally protected aminooxy-containing amino acids Synthesis 2008, 2432-2438
    • (2008) Synthesis , pp. 2432-2438
    • Liu, F.1    Thomas, J.2    Burke Jr., T.R.3
  • 38
    • 77950934522 scopus 로고    scopus 로고
    • A rapid oxime linker-based library approach to identification of bivalent inhibitors of the Yersinia pestis protein-tyrosine phosphatase, YopH
    • Liu, F.; Hakami, R. M.; Dyas, B.; Bahta, M.; Lountos, G. T.; Waugh, D. S.; Ulrich, R. G.; Burke, T. R., Jr. A rapid oxime linker-based library approach to identification of bivalent inhibitors of the Yersinia pestis protein-tyrosine phosphatase, YopH Bioor. Med. Chem. Lett. 2010, 20, 2813-2816
    • (2010) Bioor. Med. Chem. Lett. , vol.20 , pp. 2813-2816
    • Liu, F.1    Hakami, R.M.2    Dyas, B.3    Bahta, M.4    Lountos, G.T.5    Waugh, D.S.6    Ulrich, R.G.7    Burke Jr., T.R.8
  • 40
    • 29044441527 scopus 로고    scopus 로고
    • Uracil-directed ligand tethering: An efficient strategy for uracil DNA glycosylase (UNG) inhibitor development
    • DOI 10.1021/ja055846n
    • 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. 2005, 127, 17412-17420 (Pubitemid 41791060)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.49 , pp. 17412-17420
    • Jiang, Y.L.1    Krosky, D.J.2    Seiple, L.3    Stivers, J.T.4
  • 42
    • 67349171544 scopus 로고    scopus 로고
    • Impact of linker strain and flexibility in the design of a fragment-based inhibitor
    • Chung, S.; Parker, J. B.; Bianchet, M.; Amzel, L. M.; Stivers, J. T. Impact of linker strain and flexibility in the design of a fragment-based inhibitor Nat. Chem. Biol. 2009, 5, 407-413
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 407-413
    • Chung, S.1    Parker, J.B.2    Bianchet, M.3    Amzel, L.M.4    Stivers, J.T.5
  • 43
    • 33644759169 scopus 로고    scopus 로고
    • Rapid assembly and in situ screening of bidentate inhibitors of protein tyrosine phosphatases
    • DOI 10.1021/ol052895w
    • Srinivasan, R.; Uttamchandani, M.; Yao, S. Q. Rapid assembly and in situ screening of bidentate inhibitors of protein tyrosine phosphatases Org. Lett. 2006, 8, 713-716 (Pubitemid 43341997)
    • (2006) Organic Letters , vol.8 , Issue.4 , pp. 713-716
    • Srinivasan, R.1    Uttamchandani, M.2    Yao, S.Q.3
  • 44
    • 70749146770 scopus 로고    scopus 로고
    • High-throughput discovery of Mycobacterium tuberculosis protein tyrosine phosphatase B (MptpB) inhibitors using click chemistry
    • Tan, L. P.; Wu, H.; Yang, P. Y.; Kalesh, K. A.; Zhang, X.; Hu, M.; Srinivasan, R.; Yao, S. Q. High-throughput discovery of Mycobacterium tuberculosis protein tyrosine phosphatase B (MptpB) inhibitors using click chemistry Org. Lett. 2009, 11, 5102-5105
    • (2009) Org. Lett. , vol.11 , pp. 5102-5105
    • Tan, L.P.1    Wu, H.2    Yang, P.Y.3    Kalesh, K.A.4    Zhang, X.5    Hu, M.6    Srinivasan, R.7    Yao, S.Q.8
  • 46
    • 64549106489 scopus 로고    scopus 로고
    • High-throughput synthesis of azide libraries suitable for direct "click" chemistry and in situ screening
    • Srinivasan, R.; Tan, L. P.; Wu, H.; Yang, P. Y.; Kalesh, K. A.; Yao, S. Q. High-throughput synthesis of azide libraries suitable for direct "click" chemistry and in situ screening Org. Biomol. Chem. 2009, 7, 1821-1828
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 1821-1828
    • Srinivasan, R.1    Tan, L.P.2    Wu, H.3    Yang, P.Y.4    Kalesh, K.A.5    Yao, S.Q.6
  • 47
    • 0026703858 scopus 로고
    • A general method for the preparation of benzylic alpha,alpha- difluorophosphonic acids; Non-hydrolyzable mimetics of phosphotyrosine
    • Smyth, M. S.; Ford, H., Jr.; Burke, T. R., Jr. A general method for the preparation of benzylic alpha,alpha-difluorophosphonic acids; non-hydrolyzable mimetics of phosphotyrosine Tetrahedron Lett. 1992, 33, 4137-4140
    • (1992) Tetrahedron Lett. , vol.33 , pp. 4137-4140
    • Smyth, M.S.1    Ford Jr., H.2    Burke Jr., T.R.3
  • 49
    • 0031757577 scopus 로고    scopus 로고
    • Structure-based design and synthesis of small molecule protein-tyrosine phosphatase 1B inhibitors
    • DOI 10.1016/S0968-0896(98)00140-0, PII S0968089698001400
    • Yao, Z. J.; Ye, B.; Wu, X. W.; Wang, S. M.; Wu, L.; Zhang, Z. Y.; Burke, T. R., Jr. Structure-based design and synthesis of small molecule protein-tyrosine phosphatase 1B inhibitors Bioorg. Med. Chem. 1998, 6, 1799-1810 (Pubitemid 28524234)
    • (1998) Bioorganic and Medicinal Chemistry , vol.6 , Issue.10 , pp. 1799-1810
    • Yao, Z.-J.1    Ye, B.2    Wu, X.-W.3    Wang, S.4    Wu, L.5    Zhang, Z.-Y.6    Burke Jr., T.R.7
  • 50
    • 0041355319 scopus 로고    scopus 로고
    • Crystal structure of the Yersinia protein-tyrosine phosphatase YopH complexed with a specific small molecule inhibitor
    • DOI 10.1074/jbc.M304693200
    • Sun, J.-P.; Wu, L.; Fedorov, A. A.; Almo, S. C.; Zhang, Z.-Y. Crystal structure of the Yersinia protein-tyrosine phosphatase YopH complexed with a specific small molecule inhibitor J. Biol. Chem. 2003, 278, 33392-33399 (Pubitemid 37055792)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 33392-33399
    • Sun, J.-P.1    Wu, L.2    Fedorov, A.A.3    Almo, S.C.4    Zhang, Z.-Y.5
  • 51
    • 0031030669 scopus 로고    scopus 로고
    • Facile synthesis of aryl(difluoromethyl)phosphonates through CuBr-mediated cross coupling reactions of [(diethoxyphosphinyl)difluoromethyl] zinc bromide with aryl iodides
    • DOI 10.1016/S0040-4020(96)01063-0, PII S0040402096010630
    • Yokomatsu, T.; Murano, T.; Suemune, K.; Shibuya, S. Facile synthesis of aryl(difluoromethyl)phosphonates through CuBr-mediated cross coupling reactions of [(diethoxyphosphinyl)difluoromethyl]zinc bromide with aryl iodides Tetrahedron 1997, 53, 815-822 (Pubitemid 27006714)
    • (1997) Tetrahedron , vol.53 , Issue.3 , pp. 815-822
    • Yokomatsu, T.1    Murano, T.2    Suemune, K.3    Shibuya, S.4
  • 52
    • 0032558506 scopus 로고    scopus 로고
    • Solid-phase synthesis of potential protein tyrosine phosphatase inhibitors via the Ugi four-component condensation
    • DOI 10.1016/S0960-894X(98)00408-9, PII S0960894X98004089
    • Li, Z.; Yeo, S. L.; Pallen, C. J.; Ganesan, A. Solid-phase synthesis of potential protein tyrosine phosphatase inhibitors via the Ugi four-component condensation Bioorg. Med. Chem. Lett. 1998, 8, 2443-2446 (Pubitemid 28546749)
    • (1998) Bioorganic and Medicinal Chemistry Letters , vol.8 , Issue.18 , pp. 2443-2446
    • Li, Z.1    Yeo, S.L.2    Pallen, C.J.3    Ganesan, A.4
  • 53
    • 0242401865 scopus 로고    scopus 로고
    • High-Resolution Structure of the Yersinia pestis Protein Tyrosine Phosphatase YopH in Complex with a Phosphotyrosyl Mimetic-Containing Hexapeptide
    • DOI 10.1021/bi030156m
    • Phan, J.; Lee, K.; Cherry, S.; Tropea, J. E.; Burke, T. R., Jr.; Waugh, D. S. High-resolution structure of the Yersinia pestis protein tyrosine phosphatase YopH in complex with a phosphotyrosyl mimetic-containing hexapeptide Biochemistry 2003, 42, 13113-13121 (Pubitemid 37420663)
    • (2003) Biochemistry , vol.42 , Issue.45 , 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
  • 54
    • 0035827268 scopus 로고    scopus 로고
    • The catalytic mechanism of protein tyrosine phosphatases revisited
    • DOI 10.1016/S0014-5793(01)02479-6, PII S0014579301024796
    • Kolmodin, K.; Aqvist, J. The catalytic mechanism of protein tyrosine phosphatases revisited FEBS Lett. 2001, 498, 208-213 (Pubitemid 32539205)
    • (2001) FEBS Letters , vol.498 , Issue.2-3 , pp. 208-213
    • Kolmodin, K.1    Aqvist, J.2
  • 55
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Mechanisms of catalysis and regulation
    • Denu, J. M.; Dixon, J. E. Protein tyrosine phosphatases: mechanisms of catalysis and regulation Curr. Opin. Chem. Biol. 1998, 2, 633-641 (Pubitemid 128645721)
    • (1998) Current Opinion in Chemical Biology , vol.2 , Issue.5 , pp. 633-641
    • Denu, J.M.1    Dixon, J.E.2
  • 56
    • 0031893253 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases: Biological function, structural characteristics, and mechanism of catalysis
    • DOI 10.1080/10409239891204161
    • Zhang, Z.-Y. Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis Crit. Rev. Biochem. Mol. Biol. 1998, 33, 1-52 (Pubitemid 28124251)
    • (1998) Critical Reviews in Biochemistry and Molecular Biology , vol.33 , Issue.1 , pp. 1-52
    • Zhang, Z.-Y.1
  • 57
    • 79955372017 scopus 로고    scopus 로고
    • version 3.7-1f/MacOSX; MolSoft LLC: La Jolla, CA.
    • ICM Chemist Pro Software, version 3.7-1f/MacOSX; MolSoft LLC: La Jolla, CA; https://www.molsoft.com/icm-chemist-pro.html.
    • ICM Chemist Pro Software
  • 59
    • 34247362854 scopus 로고    scopus 로고
    • PTP1B as a drug target: Recent developments in PTP1B inhibitor discovery
    • DOI 10.1016/j.drudis.2007.03.011, PII S1359644607001365
    • Zhang, S.; Zhang, Z.-Y. PTP1B as a drug target: recent developments in PTP1B inhibitor discovery Drug Discovery Today 2007, 12, 373-381 (Pubitemid 46636379)
    • (2007) Drug Discovery Today , vol.12 , Issue.9-10 , pp. 373-381
    • Zhang, S.1    Zhang, Z.-Y.2
  • 62
    • 0041842684 scopus 로고    scopus 로고
    • Effect of detergent on "promiscuous" inhibitors
    • Ryan, A. J.; Gray, N. M.; Lowe, P. N.; Chung, C. W. Effect of detergent on "promiscuous" inhibitors J. Med. Chem. 2003, 46, 3448-3451
    • (2003) J. Med. Chem. , vol.46 , pp. 3448-3451
    • Ryan, A.J.1    Gray, N.M.2    Lowe, P.N.3    Chung, C.W.4
  • 63
    • 0024211451 scopus 로고
    • A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen
    • DOI 10.1084/jem.168.5.1523
    • Streuli, M.; Krueger, N. X.; Hall, L. R.; Schlossman, S. F.; Saito, H. A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen J. Exp. Med. 1988, 168, 1523-1530 (Pubitemid 19023243)
    • (1988) Journal of Experimental Medicine , vol.168 , Issue.5 , pp. 1523-1530
    • Streuli, M.1    Krueger, N.X.2    Hall, L.R.3    Schlossman, S.F.4    Saito, H.5
  • 64
    • 62149114138 scopus 로고    scopus 로고
    • Dual-specificity phosphatases: Critical regulators with diverse cellular targets
    • Patterson, K. I.; Brummer, T.; O'Brien, P. M.; Daly, R. J. Dual-specificity phosphatases: critical regulators with diverse cellular targets Biochem. J. 2009, 418, 475-489
    • (2009) Biochem. J. , vol.418 , pp. 475-489
    • Patterson, K.I.1    Brummer, T.2    O'Brien, P.M.3    Daly, R.J.4
  • 65
    • 0035655578 scopus 로고    scopus 로고
    • IL-15-induced conversion of monocytes to mature dendritic cells
    • DOI 10.1046/j.1365-2249.2001.01672.x
    • Saikh, K. U.; Khan, A. S.; Kissner, T.; Ulrich, R. G. IL-15-induced conversion of monocytes to mature dendritic cells Clin. Exp. Immunol. 2001, 126, 447-455 (Pubitemid 34008717)
    • (2001) Clinical and Experimental Immunology , vol.126 , Issue.3 , pp. 447-455
    • Saikh, K.U.1    Khan, A.S.2    Kissner, T.3    Ulrich, R.G.4
  • 66
    • 0021992123 scopus 로고
    • Mechanism of action of gentamicin components. Characteristics of their binding to Escherichia coli ribosomes
    • DOI 10.1111/j.1432-1033.1985.tb08761.x
    • Tangy, F.; Moukkadem, M.; Vindimian, E.; Capmau, M. L.; Le Goffic, F. Mechanism of action of gentamicin components. Characteristics of their binding to Escherichia coli ribosomes Eur. J. Biochem. 1985, 147, 381-386 (Pubitemid 15137274)
    • (1985) European Journal of Biochemistry , vol.147 , Issue.2 , pp. 381-386
    • Tangy, F.1    Moukkadem, M.2    Vindimian, E.3
  • 67
    • 33750451937 scopus 로고    scopus 로고
    • Overproduction, purification, and biochemical characterization of the dual specificity H1 protein phosphatase encoded by variola major virus
    • DOI 10.1016/j.pep.2006.05.007, PII S1046592806001550
    • Tropea, J. E.; Phan, J.; Waugh, D. S. Overproduction, purification, and biochemical characterization of the dual specificity H1 protein phosphatase encoded by Variola major virus Protein Expression Purif 2006, 50, 31-36 (Pubitemid 44648742)
    • (2006) Protein Expression and Purification , vol.50 , Issue.1 , pp. 31-36
    • Tropea, J.E.1    Phan, J.2    Waugh, D.S.3
  • 68
    • 70349582984 scopus 로고    scopus 로고
    • Overproduction, purification and structure determination of human dual-specificity phosphatase 14
    • Lountos, G. T.; Tropea, J. E.; Cherry, S.; Waugh, D. S. Overproduction, purification and structure determination of human dual-specificity phosphatase 14 Acta Crystallog., Sect. D 2009, 65, 1013-1020
    • (2009) Acta Crystallog., Sect. D , vol.65 , pp. 1013-1020
    • Lountos, G.T.1    Tropea, J.E.2    Cherry, S.3    Waugh, D.S.4
  • 69
    • 33847247484 scopus 로고    scopus 로고
    • A generic method for the production of recombinant proteins in Escherichia coli using a dual hexahistidine-maltose-binding protein affinity tag
    • DOI 10.1385/1-59745-209-2:1, Macromolecular Crystallography Protocols, Volume 1: Preparation and Crystallizationof Macromolecules
    • Tropea, J. E.; Cherry, S.; Nallamsetty, S.; Bignon, C.; Waugh, D. S. A generic method for the production of recombinant proteins in Escherichia coli using a dual hexahistidine-maltose-binding protein affinity tag Methods Mol. Biol. (Totowa, NJ, U. S.) 2007, 363, 1-19 (Pubitemid 350183142)
    • (2007) Methods in Molecular Biology , vol.363 , pp. 1-19
    • Tropea, J.E.1    Cherry, S.2    Nallamsetty, S.3    Bignon, C.4    Waugh, D.S.5
  • 70
    • 0037157257 scopus 로고    scopus 로고
    • Determination of the virulence of the pigmentation-deficient and pigmentation-/plasminogen activator-deficient strains of Yersinia pestis in non-human primate and mouse models of pneumonic plague
    • DOI 10.1016/S0264-410X(02)00119-6, PII S0264410X02001196
    • Welkos, S.; Pitt, M. L.; Martinez, M.; Friedlander, A.; Vogel, P.; Tammariello, R. Determination of the virulence of the pigmentation-deficient and pigmentation-/plasminogen activator-deficient strains of Yersinia pestis in non-human primate and mouse models of pneumonic plague Vaccine 2002, 20, 2206-2214 (Pubitemid 34497029)
    • (2002) Vaccine , vol.20 , Issue.17-18 , pp. 2206-2214
    • Welkos, S.1    Pitt, M.L.M.2    Martinez, M.3    Friedlander, A.4    Vogel, P.5    Tammariello, R.6
  • 71
    • 70449768051 scopus 로고    scopus 로고
    • The MORPHEUS protein crystallization screen
    • Gorrec, F. The MORPHEUS protein crystallization screen J. Appl. Cryst. 2009, 42, 1035-1042
    • (2009) J. Appl. Cryst. , vol.42 , pp. 1035-1042
    • Gorrec, F.1
  • 72
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • DOI 10.1107/S0907444906019949
    • 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 (Pubitemid 44125661)
    • (2006) Acta Crystallographica Section D: Biological Crystallography , vol.62 , Issue.8 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 74
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 763.
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, 50, 760 - 763.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760
  • 77
    • 0030768649 scopus 로고    scopus 로고
    • Model phases: Probabilities and bias
    • DOI 10.1016/S0076-6879(97)77009-5
    • Read, R. J. Model phases: probabilities and bias Methods Enzymol. 1997, 277, 110-128 (Pubitemid 27390919)
    • (1997) Methods in Enzymology , vol.277 , pp. 110-128
    • Read, R.J.1
  • 79
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures Nature 1992, 355, 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.