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Volumn 9, Issue 3, 2014, Pages 769-776

Development of accessible peptidic tool compounds to study the phosphatase PTP1B in intact cells

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; INSULIN RECEPTOR; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR; CELL PENETRATING PEPTIDE; CSK TYROSINE-PROTEIN KINASE; ENZYME INHIBITOR; PEPTIDE; POLYARGININE; PROTEIN BINDING; PROTEIN TYROSINE KINASE; PTPN1 PROTEIN, HUMAN;

EID: 84896958284     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/cb400903u     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling 2000 and beyond
    • Hunter, T. (2000) Signaling 2000 and beyond Cell 100, 113-127
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 3
    • 84872502581 scopus 로고    scopus 로고
    • Challenges and opportunities in the development of protein phosphatase-directed therapeutics
    • De Munter, S., Köhn, M., and Bollen, M. (2013) Challenges and opportunities in the development of protein phosphatase-directed therapeutics ACS Chem. Biol. 8, 36-45
    • (2013) ACS Chem. Biol. , vol.8 , pp. 36-45
    • De Munter, S.1    Köhn, M.2    Bollen, M.3
  • 5
    • 84872783533 scopus 로고    scopus 로고
    • Small molecule tools for functional interrogation of protein tyrosine phosphatases
    • He, R., Zeng, L.-F., He, Y., Zhang, S., and Zhang, Z.-Y. (2013) Small molecule tools for functional interrogation of protein tyrosine phosphatases FEBS J. 280, 731-750
    • (2013) FEBS J. , vol.280 , pp. 731-750
    • He, R.1    Zeng, L.-F.2    He, Y.3    Zhang, S.4    Zhang, Z.-Y.5
  • 6
    • 84877992759 scopus 로고    scopus 로고
    • Elucidating human phosphatase-substrate networks
    • Li, X., Wilmanns, M., Thornton, J., and Köhn, M. (2013) Elucidating human phosphatase-substrate networks Sci. Signaling 6, rs10
    • (2013) Sci. Signaling , vol.6 , pp. 10
    • Li, X.1    Wilmanns, M.2    Thornton, J.3    Köhn, M.4
  • 8
    • 21244444303 scopus 로고    scopus 로고
    • Inhibitors of protein tyrosine phosphatases: Next-generation drugs'
    • Bialy, L. and Waldmann, H. (2005) Inhibitors of protein tyrosine phosphatases: next-generation drugs' Angew. Chem., Int. Ed. 44, 3814-3839
    • (2005) Angew. Chem., Int. Ed. , vol.44 , pp. 3814-3839
    • Bialy, L.1    Waldmann, H.2
  • 10
    • 0032503030 scopus 로고    scopus 로고
    • Affinity selection from peptide libraries to determine substrate specificity of protein tyrosine phosphatases
    • Huyer, G., Kelly, J., Moffat, J., Zamboni, R., Jia, R., Gresser, M. J., and Ramachandran, C. (1998) Affinity selection from peptide libraries to determine substrate specificity of protein tyrosine phosphatases Anal. Biochem. 258, 19-30
    • (1998) Anal. Biochem. , vol.258 , pp. 19-30
    • Huyer, G.1    Kelly, J.2    Moffat, J.3    Zamboni, R.4    Jia, R.5    Gresser, M.J.6    Ramachandran, C.7
  • 11
  • 12
    • 0024287614 scopus 로고
    • Characterization of the major protein-tyrosine-phosphatases of human placenta
    • Tonks, N.K., Diltz, C. D., and Fischer, E. (1988) Characterization of the major protein-tyrosine-phosphatases of human placenta J. Biol. Chem. 263, 6731-6737
    • (1988) J. Biol. Chem. , vol.263 , pp. 6731-6737
    • Tonks . N, K.1    Diltz, C.D.2    Fischer, E.3
  • 13
    • 0023924803 scopus 로고
    • Purification of the major protein-tyrosine-phosphatases of human placenta
    • Tonks, N. K., Diltz, C. D., and Fischer, E. (1988) Purification of the major protein-tyrosine-phosphatases of human placenta J. Biol. Chem. 263, 6722-6730
    • (1988) J. Biol. Chem. , vol.263 , pp. 6722-6730
    • Tonks, N.K.1    Diltz, C.D.2    Fischer, E.3
  • 16
    • 33847202286 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B deficiency or inhibition delays ErbB2-induced mammary tumorigenesis and protects from lung metastasis
    • Julien, S. G., Dubé, N., Read, M., Penney, J., Paquet, M., Han, Y., Kennedy, B. P., Muller, W. J., and Tremblay, M. L. (2007) Protein tyrosine phosphatase 1B deficiency or inhibition delays ErbB2-induced mammary tumorigenesis and protects from lung metastasis Nat. Genet. 39, 338-346
    • (2007) Nat. Genet. , vol.39 , pp. 338-346
    • Julien, S.G.1    Dubé, N.2    Read, M.3    Penney, J.4    Paquet, M.5    Han, Y.6    Kennedy, B.P.7    Muller, W.J.8    Tremblay, M.L.9
  • 17
    • 33847375227 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B is required for Her2/Neu - Induced breast cancer
    • Bentires-Alj, M. and Neel, B. G. (2007) Protein tyrosine phosphatase 1B is required for Her2/Neu-induced breast cancer Cancer Res. 67, 2420-2424
    • (2007) Cancer Res. , vol.67 , pp. 2420-2424
    • Bentires-Alj, M.1    Neel, B.G.2
  • 18
    • 66349114704 scopus 로고    scopus 로고
    • Activation of Src by protein tyrosine phosphatase 1B is required for ErbB2 transformation of human breast epithelial cells
    • Arias-Romero, L. E., Saha, S., Villamar-Cruz, O., Yip, S.-C., Ethier, S. P., Zhang, Z.-Y., and Chernoff, J. (2009) Activation of Src by protein tyrosine phosphatase 1B is required for ErbB2 transformation of human breast epithelial cells Cancer Res. 69, 4582-4588
    • (2009) Cancer Res. , vol.69 , pp. 4582-4588
    • Arias-Romero, L.E.1    Saha, S.2    Villamar-Cruz, O.3    Yip, S.-C.4    Ethier, S.P.5    Zhang, Z.-Y.6    Chernoff, J.7
  • 19
    • 0029066496 scopus 로고
    • Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B
    • Jia, Z., Barford, D., Flint, A. J., and Tonks, N.K. (1995) Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B Science 268, 1754-1758
    • (1995) Science , vol.268 , pp. 1754-1758
    • Jia, Z.1    Barford, D.2    Flint, A.J.3    Tonks . N, K.4
  • 20
    • 0034507958 scopus 로고    scopus 로고
    • Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B
    • Salmeen, A., Andersen, J. N., Myers, M. P., Tonks, N. K., and Barford, D. (2000) Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B Mol. Cell 6, 1401-1412
    • (2000) Mol. Cell , vol.6 , pp. 1401-1412
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Tonks, N.K.4    Barford, D.5
  • 21
    • 10644292747 scopus 로고    scopus 로고
    • Applying the SPOT peptide synthesis procedure to the study of protein tyrosine phosphatase substrate specificity: Probing for the heavenly match in vitro
    • Espanel, X. and Hooft van Huijsduijnen, R. (2005) Applying the SPOT peptide synthesis procedure to the study of protein tyrosine phosphatase substrate specificity: probing for the heavenly match in vitro Methods 35, 64-72
    • (2005) Methods , vol.35 , pp. 64-72
    • Espanel, X.1    Hooft Van Huijsduijnen, R.2
  • 23
    • 58849085891 scopus 로고    scopus 로고
    • High-throughput screening of catalytic inactive mutants of protein tyrosine phosphatases (PTPs) in a phosphopeptide microarray
    • Sun, H., Tan, L. P., Gao, L., and Yao, S. Q. (2009) High-throughput screening of catalytic inactive mutants of protein tyrosine phosphatases (PTPs) in a phosphopeptide microarray Chem. Commun. 677-679
    • (2009) Chem. Commun. , pp. 677-679
    • Sun, H.1    Tan, L.P.2    Gao, L.3    Yao, S.Q.4
  • 24
    • 0345791528 scopus 로고    scopus 로고
    • Probing protein-tyrosine phosphatase substrate specificity using a phosphotyrosine-containing phage-library
    • Wälchli, S., Espanel, X., Harrenga, A., Rossi, M., Cesareni, G., and Hooft van Huijsduijnen, R. (2004) Probing protein-tyrosine phosphatase substrate specificity using a phosphotyrosine-containing phage-library J. Biol. Chem. 279, 311-318
    • (2004) J. Biol. Chem. , vol.279 , pp. 311-318
    • Wälchli, S.1    Espanel, X.2    Harrenga, A.3    Rossi, M.4    Cesareni, G.5    Hooft Van Huijsduijnen, R.6
  • 26
    • 0034723343 scopus 로고    scopus 로고
    • Assessment of protein-tyrosine phosphatase 1B substrate specificity using 'inverse alanine scanning'
    • Vetter, S. W., Keng, Y. F., Lawrence, D. S., and Zhang, Z.-Y. (2000) Assessment of protein-tyrosine phosphatase 1B substrate specificity using 'inverse alanine scanning' J. Biol. Chem. 275, 2265-2268
    • (2000) J. Biol. Chem. , vol.275 , pp. 2265-2268
    • Vetter, S.W.1    Keng, Y.F.2    Lawrence, D.S.3    Zhang, Z.-Y.4
  • 27
    • 84872770077 scopus 로고    scopus 로고
    • PTP1B and TCPTP - Nonredundant phosphatases in insulin signaling and glucose homeostasis
    • Tiganis, T. (2013) PTP1B and TCPTP-nonredundant phosphatases in insulin signaling and glucose homeostasis FEBS J. 280, 445-458
    • (2013) FEBS J. , vol.280 , pp. 445-458
    • Tiganis, T.1
  • 28
    • 0034731372 scopus 로고    scopus 로고
    • Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines
    • Bjorge, J. D., Pang, A., and Fujita, D. J. (2000) Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines J. Biol. Chem. 275, 41439-41446
    • (2000) J. Biol. Chem. , vol.275 , pp. 41439-41446
    • Bjorge, J.D.1    Pang, A.2    Fujita, D.J.3
  • 29
    • 14944349510 scopus 로고    scopus 로고
    • Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase
    • van Vliet, C., Bukczynska, P. E., Puryer, M. A., Sadek, C. M., Shields, B. J., Tremblay, M. L., and Tiganis, T. (2005) Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase Nat. Immunol. 6, 253-260
    • (2005) Nat. Immunol. , vol.6 , pp. 253-260
    • Van Vliet, C.1    Bukczynska, P.E.2    Puryer, M.A.3    Sadek, C.M.4    Shields, B.J.5    Tremblay, M.L.6    Tiganis, T.7
  • 30
    • 0028077830 scopus 로고
    • Potent inhibtion of insulin receptor dephosphorylation by a hexamer peptide containing the phosphotyrosyl mimetic F(2)Pmp
    • Burke, T. R., Kole, H. K., and Roller, P. P. (1994) Potent inhibtion of insulin receptor dephosphorylation by a hexamer peptide containing the phosphotyrosyl mimetic F(2)Pmp Biochem. Biophys. Res. Commun. 204, 129-134
    • (1994) Biochem. Biophys. Res. Commun. , vol.204 , pp. 129-134
    • Burke, T.R.1    Kole, H.K.2    Roller, P.P.3
  • 31
    • 80053901151 scopus 로고    scopus 로고
    • Efficient scaled-up synthesis of N -a-Fmoc-4-phosphono(difluoromethyl)-L- phenylalanine and its incorporation into peptides
    • Meyer, C. and Köhn, M. (2011) Efficient scaled-up synthesis of N -a-Fmoc-4-phosphono(difluoromethyl)-L-phenylalanine and its incorporation into peptides Synthesis 20, 3255-3260
    • (2011) Synthesis , vol.20 , pp. 3255-3260
    • Meyer, C.1    Köhn, M.2
  • 32
    • 0031031166 scopus 로고    scopus 로고
    • Potent inhibition of protein tyrosine phosphatase by phosphotyrosine- mimic containing cyclic peptides
    • Akamatsu, M., Roller, P. P., Chen, L., Zhang, Z.-Y., Ye, B., and Burke, T. R. (1997) Potent inhibition of protein tyrosine phosphatase by phosphotyrosine-mimic containing cyclic peptides Bioorg. Med. Chem. 5, 157-163
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 157-163
    • Akamatsu, M.1    Roller, P.P.2    Chen, L.3    Zhang, Z.-Y.4    Ye, B.5    Burke, T.R.6
  • 33
    • 0029015718 scopus 로고
    • Kinetic and mechanistic characterization of a mammalian protein-tyrosine phosphatase, PTP1
    • Zhang, Z.-Y. (1995) Kinetic and mechanistic characterization of a mammalian protein-tyrosine phosphatase, PTP1 J. Biol. Chem. 270, 11199-11204
    • (1995) J. Biol. Chem. , vol.270 , pp. 11199-11204
    • Zhang, Z.-Y.1
  • 34
    • 0242410531 scopus 로고    scopus 로고
    • Microcystine analogues comprised only of adda and a single additional amino acid retain moderate activity as PP1/PP2A inhibitors
    • Gulledge, B. M., Aggen, J. B., Eng, H., Sweimeh, K., and Chamberlin, A. R. (2003) Microcystine analogues comprised only of adda and a single additional amino acid retain moderate activity as PP1/PP2A inhibitors Bioorg. Med. Chem. Lett. 13, 2907-2911
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 2907-2911
    • Gulledge, B.M.1    Aggen, J.B.2    Eng, H.3    Sweimeh, K.4    Chamberlin, A.R.5
  • 35
    • 0028298024 scopus 로고
    • Protein tyrosine phosphatase substrate specificity: Size and phosphotyrosine positioning requirements in peptide substrates
    • Zhang, Z.-Y., Maclean, D., McNamara, D. J., Sawyer, T. K., and Dixon, J. E. (1994) Protein tyrosine phosphatase substrate specificity: size and phosphotyrosine positioning requirements in peptide substrates Biochemistry 33, 2285-2290
    • (1994) Biochemistry , vol.33 , pp. 2285-2290
    • Zhang, Z.-Y.1    Maclean, D.2    McNamara, D.J.3    Sawyer, T.K.4    Dixon, J.E.5
  • 36
    • 0028815228 scopus 로고
    • Radio frequency tag encoded combinatorial library method for the discovery of tripeptide-substituted cinnamic acid inhibitors of the protein tyrosine phosphatase
    • Moran, E., Sarshar, S., and Cargill, J. (1995) Radio frequency tag encoded combinatorial library method for the discovery of tripeptide-substituted cinnamic acid inhibitors of the protein tyrosine phosphatase J. Am. Chem. Soc. 117, 10787-10788
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10787-10788
    • Moran, E.1    Sarshar, S.2    Cargill, J.3
  • 37
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Wenqing, X. and Harrison, S. (1997) Three-dimensional structure of the tyrosine kinase c-Src Nature 385, 595-602
    • (1997) Nature , vol.385 , pp. 595-602
    • Wenqing, X.1    Harrison, S.2
  • 38
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
    • Zheng, X. M., Resnick, R. J., and Shalloway, D. (2000) A phosphotyrosine displacement mechanism for activation of Src by PTPalpha EMBO J. 19, 964-978
    • (2000) EMBO J. , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 40
    • 0032559056 scopus 로고    scopus 로고
    • Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics
    • Groves, M. R., Yao, Z. J., Roller, P. P., Burke, T. R., Jr., and Barford, D. (1998) Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics Biochemistry 37, 17773-17783
    • (1998) Biochemistry , vol.37 , pp. 17773-17783
    • Groves, M.R.1    Yao, Z.J.2    Roller, P.P.3    Burke Jr., T.R.4    Barford, D.5
  • 42
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • Wender, P. A., Mitchell, D. J., Pattabiraman, K., Pelkey, E. T., Steinman, L., and Rothbard, J. B. (2000) The design, synthesis and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters Proc. Natl. Acad. Sci. U.S.A. 97, 13003-13008
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 43
    • 53849084442 scopus 로고    scopus 로고
    • In vitro evaluation of reversible and irreversible cytochrome P450 inhibition: Current status on methodologies and their utility for predicting drug-drug interactions
    • Fowler, S. and Zhang, H. (2008) In vitro evaluation of reversible and irreversible cytochrome P450 inhibition: Current status on methodologies and their utility for predicting drug-drug interactions AAPS J. 10, 410-424
    • (2008) AAPS J. , vol.10 , pp. 410-424
    • Fowler, S.1    Zhang, H.2
  • 44
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni, J. V., Beahm, P. H., Shifrin, V., Jost, C. A., and Neel, B. G. (1992) The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence Cell 68, 545-560
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 45
    • 54749122331 scopus 로고    scopus 로고
    • Exploiting cross-amyloid interactions to inhibit protein aggregation but not function: Nanomolar affinity inhibition of insulin aggregation by an IAPP mimic
    • Velkova, A., Tatarek-Nossol, M., Andreetto, E., and Kapurniotu, A. (2008) Exploiting cross-amyloid interactions to inhibit protein aggregation but not function: nanomolar affinity inhibition of insulin aggregation by an IAPP mimic Angew. Chem., Int. Ed. 47, 7114-7118
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 7114-7118
    • Velkova, A.1    Tatarek-Nossol, M.2    Andreetto, E.3    Kapurniotu, A.4
  • 46
    • 79959981040 scopus 로고    scopus 로고
    • Rosetta FlexPepDock web server-high resolution modeling of peptide-protein interactions
    • London, N., Raveh, B., Cohen, E., Fathi, G., and Schueler-Furman, O. (2011) Rosetta FlexPepDock web server-high resolution modeling of peptide-protein interactions Nucleic Acids Res. 39, W249-253
    • (2011) Nucleic Acids Res. , vol.39 , pp. 249-253
    • London, N.1    Raveh, B.2    Cohen, E.3    Fathi, G.4    Schueler-Furman, O.5


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