메뉴 건너뛰기




Volumn 68, Issue 9, 2004, Pages 1807-1814

Using yeast to screen for inhibitors of protein tyrosine phosphatase 1B

Author keywords

Biological assay; Enzyme inhibitors; Protein tyrosine phosphatase; PTP1B; Saccharomyces cerevisiae; v Src

Indexed keywords

2,3 BIPHENYL 1 [3 BROMO 4 [PHOSPHONO(DIFLUOROMETHYL)]PHENYL]PROPAN 3 ONE; 3 (4 CHLOROPHENYL) 1 [3 BROMO 4 [PHOSPHONO(DIFLUOROMETHYL)]PHENYL] 2 THIAPROPANE; 7 BROMO 6 PHOSPHONO(DIFLUOROMETHYL) 3 NAPHTHALENONITRILE; N BENZOYLGLUTAMYL [4 PHOSPHONO(DIFLUOROMETHYL)]PHENYLALANYL [4 PHOSPHONO(DIFLUOROMETHYL)]PHENYLALANINAMIDE; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR; UNCLASSIFIED DRUG; VANADIC ACID;

EID: 4644349812     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2004.06.024     Document Type: Article
Times cited : (20)

References (32)
  • 1
    • 1542603144 scopus 로고    scopus 로고
    • Recent advances in protein tyrosine phosphatase 1B inhibitors
    • S.D. Taylor, and B. Hill Recent advances in protein tyrosine phosphatase 1B inhibitors Expert Opin. Investig. Drugs. 13 2004 199 214
    • (2004) Expert Opin. Investig. Drugs. , vol.13 , pp. 199-214
    • Taylor, S.D.1    Hill, B.2
  • 2
    • 0037317489 scopus 로고    scopus 로고
    • PTP1B inhibitors as potential therapeutics in the treatment of Type 2 diabetes and obesity
    • Z.Y. Zhang, and S.Y. Lee PTP1B inhibitors as potential therapeutics in the treatment of Type 2 diabetes and obesity Expert Opin Investig. Drugs. 12 2003 223 233
    • (2003) Expert Opin Investig. Drugs. , vol.12 , pp. 223-233
    • Zhang, Z.Y.1    Lee, S.Y.2
  • 3
    • 0037376001 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: The quest for negative regulators of insulin action
    • E. Asante-Appiah, and B.P. Kennedy Protein tyrosine phosphatases: the quest for negative regulators of insulin action Am J Physiol Endocrinol. Metab. 284 2003 E663 E670
    • (2003) Am J Physiol Endocrinol. Metab. , vol.284
    • Asante-Appiah, E.1    Kennedy, B.P.2
  • 4
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • M. Elchebly, P. Payette, E. Michaliszyn, W. Cromlish, S. Collins, and A.L. Loy Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene Science. 283 1999 1544 1548
    • (1999) Science. , vol.283 , pp. 1544-1548
    • Elchebly, M.1    Payette, P.2    Michaliszyn, E.3    Cromlish, W.4    Collins, S.5    Loy, A.L.6
  • 5
    • 0033942614 scopus 로고    scopus 로고
    • Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice
    • L.D. Klaman, O. Boss, O.D. Peroni, J.K. Kim, J.L. Martino, and J.M. Zabolotny Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice Mol. Cell. Biol. 20 2000 5479 5489
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5479-5489
    • Klaman, L.D.1    Boss, O.2    Peroni, O.D.3    Kim, J.K.4    Martino, J.L.5    Zabolotny, J.M.6
  • 6
    • 0037143754 scopus 로고    scopus 로고
    • PTP1B antisense oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitivity in diabetic mice
    • B.A. Zinker, C.M. Rondinone, J.M. Trevillyan, R.J. Gum, J.E. Clampit, and J.F. Waring PTP1B antisense oligonucleotide lowers PTP1B protein, normalizes blood glucose, and improves insulin sensitivity in diabetic mice Proc. Natl. Acad. Sci. U.S.A. 99 2002 11357 11362
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 11357-11362
    • Zinker, B.A.1    Rondinone, C.M.2    Trevillyan, J.M.3    Gum, R.J.4    Clampit, J.E.5    Waring, J.F.6
  • 7
    • 0036329620 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B reduction regulates adiposity and expression of genes involved in lipogenesis
    • C.M. Rondinone, J.M. Trevillyan, J. Clampit, R.J. Gum, C. Berg, and P. Kroeger Protein tyrosine phosphatase 1B reduction regulates adiposity and expression of genes involved in lipogenesis Diabetes. 51 2002 2405 2411
    • (2002) Diabetes. , vol.51 , pp. 2405-2411
    • Rondinone, C.M.1    Trevillyan, J.M.2    Clampit, J.3    Gum, R.J.4    Berg, C.5    Kroeger, P.6
  • 8
    • 0037221179 scopus 로고    scopus 로고
    • Reduction of protein tyrosine phosphatase 1B increases insulin-dependent signaling in ob/ob mice
    • R.J. Gum, L.L. Gaede, S.L. Koterski, M. Heindel, J.E. Clampit, and B.A. Zinker Reduction of protein tyrosine phosphatase 1B increases insulin-dependent signaling in ob/ob mice Diabetes. 52 2003 21 28
    • (2003) Diabetes. , vol.52 , pp. 21-28
    • Gum, R.J.1    Gaede, L.L.2    Koterski, S.L.3    Heindel, M.4    Clampit, J.E.5    Zinker, B.A.6
  • 10
    • 10744223631 scopus 로고    scopus 로고
    • Cellular effects of small molecule PTP1B inhibitors on insulin signaling
    • L. Xie, S.Y. Lee, J.N. Andersen, S. Waters, K. Shen, and X.L. Guo Cellular effects of small molecule PTP1B inhibitors on insulin signaling Biochemistry. 42 2003 12792 12804
    • (2003) Biochemistry. , vol.42 , pp. 12792-12804
    • Xie, L.1    Lee, S.Y.2    Andersen, J.N.3    Waters, S.4    Shen, K.5    Guo, X.L.6
  • 11
    • 0036890871 scopus 로고    scopus 로고
    • From genetics and genomics to drug discovery: Yeast rises to the challenge
    • T. Melese, and P. Hieter From genetics and genomics to drug discovery: yeast rises to the challenge Trends Pharmacol. Sci. 23 2002 544 547
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 544-547
    • Melese, T.1    Hieter, P.2
  • 13
    • 0023377484 scopus 로고
    • Characterization of avian and viral p60src proteins expressed in yeast
    • S. Kornbluth, R. Jove, and H. Hanafusa Characterization of avian and viral p60src proteins expressed in yeast Proc. Natl. Acad. Sci. U.S.A. 84 1987 4455 4459
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 4455-4459
    • Kornbluth, S.1    Jove, R.2    Hanafusa, H.3
  • 14
    • 0027337893 scopus 로고
    • Expression of p60v-src in Saccharomyces cerevisiae results in elevation of p34CDC28 kinase activity and release of the dependence of DNA replication on mitosis
    • F. Boschelli Expression of p60v-src in Saccharomyces cerevisiae results in elevation of p34CDC28 kinase activity and release of the dependence of DNA replication on mitosis Mol. Cell. Biol. 13 1993 5112 5121
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5112-5121
    • Boschelli, F.1
  • 15
    • 0028065135 scopus 로고
    • Expression of p60v-src in Saccharomyces cerevisiae results in elevation of p34CDC28 kinase activity and release of the dependence of DNA replication on mitosis
    • F. Boschelli Expression of p60v-src in Saccharomyces cerevisiae results in elevation of p34CDC28 kinase activity and release of the dependence of DNA replication on mitosis Mol Cell Biol. 14 1994 6409
    • (1994) Mol Cell Biol. , vol.14 , pp. 6409
    • Boschelli, F.1
  • 16
    • 0028327357 scopus 로고
    • Aberrant protein phosphorylation at tyrosine is responsible for the growth-inhibitory action of pp60v-src expressed in the yeast Saccharomyces cerevisiae
    • M. Florio, L.K. Wilson, J.B. Trager, J. Thorner, and G.S. Martin Aberrant protein phosphorylation at tyrosine is responsible for the growth-inhibitory action of pp60v-src expressed in the yeast Saccharomyces cerevisiae Mol. Biol. Cell. 5 1994 283 296
    • (1994) Mol. Biol. Cell. , vol.5 , pp. 283-296
    • Florio, M.1    Wilson, L.K.2    Trager, J.B.3    Thorner, J.4    Martin, G.S.5
  • 17
    • 0030920621 scopus 로고    scopus 로고
    • The role of the Src homology-2 domain in the lethal effect of Src expression in the yeast Saccharomyces cerevisiae
    • J.B. Trager, and G.S. Martin The role of the Src homology-2 domain in the lethal effect of Src expression in the yeast Saccharomyces cerevisiae Int. J. Biochem. Cell Biol. 29 1997 635 648
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 635-648
    • Trager, J.B.1    Martin, G.S.2
  • 18
    • 0031022433 scopus 로고    scopus 로고
    • Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate
    • G. Huyer, S. Liu, J. Kelly, J. Moffat, P. Payette, and B. Kennedy Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate J. Biol. Chem. 272 1997 843 851
    • (1997) J. Biol. Chem. , vol.272 , pp. 843-851
    • Huyer, G.1    Liu, S.2    Kelly, J.3    Moffat, J.4    Payette, P.5    Kennedy, B.6
  • 19
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: Comparison of transcriptional activity and their use for heterologous expression
    • D. Mumberg, R. Muller, and M. Funk Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression Nucleic Acids Res. 22 1994 5767 5768
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 21
    • 0031956485 scopus 로고    scopus 로고
    • Use of a rapid throughput in vivo screen to investigate inhibitors of eukaryotic topoisomerase II enzymes
    • T.R. Hammonds, A. Maxwell, and J.R. Jenkins Use of a rapid throughput in vivo screen to investigate inhibitors of eukaryotic topoisomerase II enzymes Antimicrob. Agents Chemother. 42 1998 889 894
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 889-894
    • Hammonds, T.R.1    Maxwell, A.2    Jenkins, J.R.3
  • 22
    • 0033555247 scopus 로고    scopus 로고
    • [Difluro(phosphono)methyl]phenylalanine-containing peptide inhibitors of protein tyrosine phosphatases
    • S. Desmarais, R.W. Friesen, R. Zamboni, and C. Ramachandran [Difluro(phosphono)methyl]phenylalanine-containing peptide inhibitors of protein tyrosine phosphatases Biochem. J. 337 Pt 2 1999 219 223
    • (1999) Biochem. J. , vol.337 , Issue.2 , pp. 219-223
    • Desmarais, S.1    Friesen, R.W.2    Zamboni, R.3    Ramachandran, C.4
  • 24
    • 0035854750 scopus 로고    scopus 로고
    • The YRD motif is a major determinant of substrate and inhibitor specificity in T-cell protein-tyrosine phosphatase
    • E. Asante-Appiah, K. Ball, K. Bateman, K. Skorey, R. Friesen, and C. Desponts The YRD motif is a major determinant of substrate and inhibitor specificity in T-cell protein-tyrosine phosphatase J. Biol. Chem. 276 2001 26036 26043
    • (2001) J. Biol. Chem. , vol.276 , pp. 26036-26043
    • Asante-Appiah, E.1    Ball, K.2    Bateman, K.3    Skorey, K.4    Friesen, R.5    Desponts, C.6
  • 25
    • 0025024995 scopus 로고
    • Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia
    • K.L. Guan, and J.E. Dixon Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia Science. 249 1990 553 556
    • (1990) Science. , vol.249 , pp. 553-556
    • Guan, K.L.1    Dixon, J.E.2
  • 26
    • 0031055324 scopus 로고    scopus 로고
    • Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases
    • A.J. Flint, T. Tiganis, D. Barford, and N.K. Tonks Development of "substrate-trapping" mutants to identify physiological substrates of protein tyrosine phosphatases Proc. Natl. Acad. Sci. U.S.A. 94 1997 1680 1685
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4
  • 27
    • 0020463759 scopus 로고
    • Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate
    • G. Swarup, S. Cohen, and D.L. Garbers Inhibition of membrane phosphotyrosyl-protein phosphatase activity by vanadate Biochem. Biophys. Res. Commun. 107 1982 1104 1109
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 1104-1109
    • Swarup, G.1    Cohen, S.2    Garbers, D.L.3
  • 28
    • 0035870820 scopus 로고    scopus 로고
    • Development of a robust scintillation proximity assay for protein tyrosine phosphatase 1B using the catalytically inactive (C215S) mutant
    • K.I. Skorey, B.P. Kennedy, R.W. Friesen, and C. Ramachandran Development of a robust scintillation proximity assay for protein tyrosine phosphatase 1B using the catalytically inactive (C215S) mutant Anal. Biochem. 291 2001 269 278
    • (2001) Anal. Biochem. , vol.291 , pp. 269-278
    • Skorey, K.I.1    Kennedy, B.P.2    Friesen, R.W.3    Ramachandran, C.4
  • 29
    • 0032524855 scopus 로고    scopus 로고
    • Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases
    • Y.L. Zhang, Y.F. Keng, Y. Zhao, L. Wu, and Z.Y. Zhang Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases J. Biol. Chem. 273 1998 12281 12287
    • (1998) J. Biol. Chem. , vol.273 , pp. 12281-12287
    • Zhang, Y.L.1    Keng, Y.F.2    Zhao, Y.3    Wu, L.4    Zhang, Z.Y.5
  • 30
    • 0025688139 scopus 로고
    • Tyrosine phosphorylation in T cells is regulated by phosphatase activity: Studies with phenylarsine oxide
    • P. Garcia-Morales, Y. Minami, E. Luong, R.D. Klausner, and L.E. Samelson Tyrosine phosphorylation in T cells is regulated by phosphatase activity: studies with phenylarsine oxide Proc. Natl. Acad. Sci U.S.A. 87 1990 9255 9259
    • (1990) Proc. Natl. Acad. Sci U.S.A. , vol.87 , pp. 9255-9259
    • Garcia-Morales, P.1    Minami, Y.2    Luong, E.3    Klausner, R.D.4    Samelson, L.E.5
  • 32
    • 0032880903 scopus 로고    scopus 로고
    • Development and validation of an intact cell assay for protein tyrosine phosphatases using recombinant baculoviruses
    • W.A. Cromlish, P. Payette, and B.P. Kennedy Development and validation of an intact cell assay for protein tyrosine phosphatases using recombinant baculoviruses Biochem. Pharmacol. 58 1999 1539 1546
    • (1999) Biochem. Pharmacol. , vol.58 , pp. 1539-1546
    • Cromlish, W.A.1    Payette, P.2    Kennedy, B.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.