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Volumn 365, Issue , 2007, Pages 9-22

A brief introduction to the protein phosphatase families

Author keywords

drug targets; HAD family; Protein phosphatases; PTPs, DSPs

Indexed keywords

PHOSPHOPROTEIN PHOSPHATASE;

EID: 34447280860     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1385/1-59745-267-X:9     Document Type: Article
Times cited : (37)

References (92)
  • 1
    • 0032227735 scopus 로고    scopus 로고
    • The role of tyrosine phosphorylation in cell growth and disease
    • Hunter, T. (1998) The role of tyrosine phosphorylation in cell growth and disease. Harvey Lect. 94, 81-119.
    • (1998) Harvey Lect. , vol.94 , pp. 81-119
    • Hunter, T.1
  • 2
    • 0347285350 scopus 로고    scopus 로고
    • A genomic perspective on PTPs: Gene structure, pseudogenes, and genetic disease linkage
    • Andersen, J. N., Jansen, P. G., Echwald, S. M., et al. (2004) A genomic perspective on PTPs: gene structure, pseudogenes, and genetic disease linkage. FASEB J. 18, 8-13.
    • (2004) FASEB J. , vol.18 , pp. 8-13
    • Andersen, J.N.1    Jansen, P.G.2    Echwald, S.M.3
  • 3
    • 2942581416 scopus 로고    scopus 로고
    • The PTPs in the human genome
    • Alonso, A., Sasin, J., Osterman, A., et al. (2004) The PTPs in the human genome. Cell 117, 699-711.
    • (2004) Cell , vol.117 , pp. 699-711
    • Alonso, A.1    Sasin, J.2    Osterman, A.3
  • 6
    • 0027962609 scopus 로고
    • Protein tyrosine phosphorylation in Mycobacterium tuberculosis
    • DOI 10.1016/0378-1097(94)90250-X
    • Chow, K., Ng, D., Stokes, R., and Johnson, P. (1994) Protein tyrosine phosphorylation in Mycobacterium tuberculosis. FEMS Microbiol. Lett. 124, 203-207. (Pubitemid 124012917)
    • (1994) FEMS Microbiology Letters , vol.124 , Issue.2 , pp. 203-207
    • Chow, K.1    Ng, D.2    Stokes, R.3    Johnson, P.4
  • 7
    • 0037335790 scopus 로고    scopus 로고
    • Archaeal protein kinases and protein phosphatases: Insights from genomics and biochemistry
    • DOI 10.1042/BJ20021547
    • Kennelly, P. J. (2003) Archaeal protein kinases and protein phosphatases: Insights from genomics and biochemistry. Biochem. J. 370, 373-389. (Pubitemid 36315125)
    • (2003) Biochemical Journal , vol.370 , Issue.2 , pp. 373-389
    • Kennelly, P.J.1
  • 8
    • 1542373523 scopus 로고    scopus 로고
    • Protein phosphorylation on tyrosine in bacteria
    • DOI 10.1007/s00203-003-0640-6
    • Cozzone, A. J., Grangeasse, C., Doublet, P., and Duclos, B. (2004) Protein phosphorylation on tyrosine in bacteria. Arch. Microbiol. 181, 171-181. (Pubitemid 38316642)
    • (2004) Archives of Microbiology , vol.181 , Issue.3 , pp. 171-181
    • Cozzone, A.J.1    Grangeasse, C.2    Doublet, P.3    Duclos, B.4
  • 10
    • 0030297552 scopus 로고    scopus 로고
    • From form to function: Signaling by PTPs
    • Tonks, N. K. and Neel, B. G. (1996) From form to function: signaling by PTPs. Cell 87, 365-368.
    • (1996) Cell , vol.87 , pp. 365-368
    • Tonks, N.K.1    Neel, B.G.2
  • 11
    • 11244277091 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases and the immune response
    • DOI 10.1038/nri1530
    • Mustelin, T., Vang, T., and Bottini, N. (2005) Protein tyrosine phosphatases and the immune response. Nat. Rev. Immunol. 5, 43-57. (Pubitemid 40070330)
    • (2005) Nature Reviews Immunology , vol.5 , Issue.1 , pp. 43-57
    • Mustelin, T.1    Vang, T.2    Bottini, N.3
  • 12
    • 17844403782 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases and signaling
    • Stoker, A. W. (2005) Protein tyrosine phosphatases and signaling. J. Endocrinol. 185, 19-33.
    • (2005) J. Endocrinol. , vol.185 , pp. 19-33
    • Stoker, A.W.1
  • 13
    • 12344290477 scopus 로고    scopus 로고
    • Tyrosine phosphatases in vessel wall signaling
    • DOI 10.1016/j.cardiores.2004.08.016, PII S0008636304003827
    • Kappert, K., Peters, K. G., Bohmer, F. D., and Ostman, A. (2005) Tyrosine phosphatases in vessel wall signaling. Cardiovasc. Res. 65, 587-598. (Pubitemid 40138979)
    • (2005) Cardiovascular Research , vol.65 , Issue.3 , pp. 587-598
    • Kappert, K.1    Peters, K.G.2    Bohmer, F.D.3    Ostman, A.4
  • 14
    • 13944254436 scopus 로고    scopus 로고
    • New vision from Eyes absent: Transcription factors as enzymes
    • DOI 10.1016/j.tig.2005.01.005
    • Rebay, I., Silver, S. J., and Tootle, T. L. (2005) New vision from Eyes absent: transcription factors as enzymes. Trends Genet. 21, 163-171. (Pubitemid 40269855)
    • (2005) Trends in Genetics , vol.21 , Issue.3 , pp. 163-171
    • Rebay, I.1    Silver, S.J.2    Tootle, T.L.3
  • 15
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • DOI 10.1038/nrm1527
    • Wong, W. and Scott, J. D. (2004) AKAP signalling complexes: focal points in space and time. Nat. Rev. Mol. Cell. Biol. 5, 959-970. (Pubitemid 39611533)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.12 , pp. 959-970
    • Wong, W.1    Scott, J.D.2
  • 16
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1 - Targeted in many directions
    • Cohen, P. T. (2002) Protein phosphatase 1: targeted in many directions. J. Cell. Sci. 115, 241-256. (Pubitemid 34145174)
    • (2002) Journal of Cell Science , vol.115 , Issue.2 , pp. 241-256
    • Cohen, P.T.W.1
  • 17
    • 0346728803 scopus 로고    scopus 로고
    • Functional Diversity of Protein Phosphatase-1, a Cellular Economizer and Reset Button
    • DOI 10.1152/physrev.00013.2003
    • Ceulemans, H. and Bollen, M. (2004) Functional diversity of protein phosphatase-1, a cellular economizer and reset button. Physiol. Rev. 84, 1-39. (Pubitemid 38049874)
    • (2004) Physiological Reviews , vol.84 , Issue.1 , pp. 1-39
    • Ceulemans, H.1    Bollen, M.2
  • 18
    • 0033604644 scopus 로고    scopus 로고
    • Shp-2 tyrosine phosphatase: Signaling one cell or many
    • Feng, G. S. (1999) Shp-2 tyrosine phosphatase: Signaling one cell or many. Exp. Cell Res. 253, 47-54
    • (1999) Exp. Cell Res. , vol.253 , pp. 47-54
    • Feng, G.S.1
  • 20
    • 0037025315 scopus 로고    scopus 로고
    • Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP)
    • DOI 10.1074/jbc.M202885200
    • Bottini, N., Stefanini, L., Williams, S., et al. (2002) Activation of ZAP-70 through specific dephosphorylation at the inhibitory Tyr-292 by the low molecular weight phosphotyrosine phosphatase (LMPTP). J. Biol. Chem. 277, 24,220-24,224. (Pubitemid 34951938)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24220-24224
    • Bottini, N.1    Stefanini, L.2    Williams, S.3    Alonso, A.4    Jascur, T.5    Abraham, R.T.6    Couture, C.7    Mustelin, T.8
  • 21
    • 0040821207 scopus 로고    scopus 로고
    • Combination of gene targeting and substrate trapping to identify substrates of protein tyrosine phosphatases using PTP-PEST as a model
    • DOI 10.1021/bi981259l
    • Cote, J. F., Charest, A., Wagner, J., and Tremblay, M. L. (1998) Combination of gene targeting and substrate trapping to identify substrates of PTPs using PTPPEST as a model. Biochemistry 37, 13,128-13,137 . (Pubitemid 28449556)
    • (1998) Biochemistry , vol.37 , Issue.38 , pp. 13128-13137
    • Cote, J.-F.1    Charest, A.2    Wagner, J.3    Tremblay, M.L.4
  • 23
    • 0034802515 scopus 로고    scopus 로고
    • Hematopoietic protein tyrosine phosphatase suppresses extracellular stimulus-regulated kinase activation
    • DOI 10.1128/MCB.21.20.6851-6858.2001
    • Gronda, M., Arab, S., Iafrate, B., Suzuki, H., and Zanke, B. (2001) Hematopoietic PTP suppresses extracellular stimulus-regulated kinase activation. Mol. Cell. Biol. 21, 6851-6858. (Pubitemid 32911246)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.20 , pp. 6851-6858
    • Gronda, M.1    Arab, S.2    Iafrate, B.3    Suzuki, H.4    Zanke, B.W.5
  • 24
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the PTP-1B gene
    • Elchebly, M., Payette, P., Michaliszyn, E., et al. (1999) Increased insulin sensitivity and obesity resistance in mice lacking the PTP-1B gene. Science 283, 1544-1548.
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1    Payette, P.2    Michaliszyn, E.3
  • 27
    • 0033722475 scopus 로고    scopus 로고
    • Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate
    • Wharram, B. L., Goyal, M., Gillespie, P. J., et al. (2000) Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate. Clin. Invest. 106, 1281-1290.
    • (2000) Clin. Invest. , vol.106 , pp. 1281-1290
    • Wharram, B.L.1    Goyal, M.2    Gillespie, P.J.3
  • 29
    • 0031870959 scopus 로고    scopus 로고
    • Pten is essential for embryonic development and tumour suppression
    • DOI 10.1038/1235
    • Di Cristofano, A., Pesce, B., Cordon-Cardo, C., and Pandolfi, P. P. (1998) Pten is essential for embryonic development and tumour suppression. Nat. Genet. 19, 348-355. (Pubitemid 28357906)
    • (1998) Nature Genetics , vol.19 , Issue.4 , pp. 348-355
    • Di Cristofano, A.1    Pesce, B.2    Cordon-Cardo, C.3    Pandolfi, P.P.4
  • 31
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning, G., Whyte, D. B., Martinez, R., Hunter, T. and Sudarsanam, S. (2002) The protein kinase complement of the human genome. Science 298, 1912-1934. (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 32
    • 0032535169 scopus 로고    scopus 로고
    • Role of PP2A in intracellular signal transduction pathways
    • Schonthal, A. H. (1998) Role of PP2A in intracellular signal transduction pathways. Front. Biosci. 3, D1262-1273.
    • (1998) Front. Biosci. , vol.3
    • Schonthal, A.H.1
  • 33
    • 0033615538 scopus 로고    scopus 로고
    • Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association
    • DOI 10.1016/S0092-8674(00)81663-3
    • Lee, J. O. Yang, H., Georgescu, M. M., et al. (1999) Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Cell 99, 323-334. (Pubitemid 29519911)
    • (1999) Cell , vol.99 , Issue.3 , pp. 323-334
    • Lee, J.-O.1    Yang, H.2    Georgescu, M.-M.3    Cristofano, A.D.4    Maehama, T.5    Shi, Y.6    Dixon, J.E.7    Pandolfi, P.8    Pavletich, N.P.9
  • 34
    • 0346156077 scopus 로고    scopus 로고
    • Crystal Structure of a Phosphoinositide Phosphatase, MTMR2: Insights into Myotubular Myopathy and Charcot-Marie-Tooth Syndrome
    • DOI 10.1016/S1097-2765(03)00486-6
    • Begley, M. J. Taylor, G. S., Kim, S. A., Veine, D. M., Dixon, J. E., and Stuckey, J. A. (2003) Crystal structure of a phosphoinositide phosphatase, MTMR2: insights into myotubular myopathy and Charcot-Marie-Tooth Syndrome. Mol. Cell 12, 1391-1402. (Pubitemid 38037009)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1391-1402
    • Begley, M.J.1    Taylor, G.S.2    Kim, S.-A.3    Veine, D.M.4    Dixon, J.E.5    Stuckey, J.A.6
  • 35
    • 12144254762 scopus 로고    scopus 로고
    • Characterization of a plant, tyrosine-specific phosphatase of the aspartyl class
    • DOI 10.1021/bi0481794
    • Rayapureddi, J. P., Kattamuri, C., Chan, F. H., and Hegde, R. S. (2005) Characterization of a plant, tyrosine-specific phosphatase of the aspartyl class. Biochemistry 44, 751-8. (Pubitemid 40105506)
    • (2005) Biochemistry , vol.44 , Issue.2 , pp. 751-758
    • Rayapureddi, J.P.1    Kattamuri, C.2    Chan, F.H.3    Hegde, R.S.4
  • 37
    • 4344678787 scopus 로고    scopus 로고
    • Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities
    • DOI 10.1042/BJ20040511
    • Roberts, S. J., Stewart, A. J., Sadler, P. J., and Farquharson, C. (2004) Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities. Biochem. J. 382, 59-65. (Pubitemid 39141566)
    • (2004) Biochemical Journal , vol.382 , Issue.1 , pp. 59-65
    • Roberts, S.J.1    Stewart, A.J.2    Sadler, P.J.3    Farquharson, C.4
  • 39
    • 0033740573 scopus 로고    scopus 로고
    • Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants
    • Lunn, J. E., Ashton, A. R., Hatch, M. D., and Heldt, H. W. (2000) Purification, molecular cloning, and sequence analysis of sucrose-6F-phosphate phosphohydrolase from plants. Proc. Natl. Acad. Sci. USA 97, 12,914-12,919.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12914-12919
    • Lunn, J.E.1    Ashton, A.R.2    Hatch, M.D.3    Heldt, H.W.4
  • 41
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • DOI 10.1038/ncb1201
    • Gohla, A., Birkenfeld, J., and Bokoch, G. M. (2005) Chronophin, a novel HADtype serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 7, 21-29. (Pubitemid 40123379)
    • (2005) Nature Cell Biology , vol.7 , Issue.1 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 42
    • 0038168110 scopus 로고    scopus 로고
    • A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5
    • DOI 10.1074/jbc.M301791200
    • Yeo, M., Lin, P. S., Dahmus, M. E., and Gill, G. N. (2003) A novel RNA polymerase II C-terminal domain phosphatase that preferentially dephosphorylates serine 5. J. Biol. Chem. 278, 26,078-26,085. (Pubitemid 36835376)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 26078-26085
    • Yeo, M.1    Lin, P.S.2    Dahmus, M.E.3    Gill, G.N.4
  • 43
    • 4944254297 scopus 로고    scopus 로고
    • X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily
    • DOI 10.1021/bi0490688
    • Peisach, E., Selengut, J. D., Dunaway-Mariano, D., and Allen, K. N. (2004) X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily. Biochemistry 43, 12,770-12,779. (Pubitemid 39331796)
    • (2004) Biochemistry , vol.43 , Issue.40 , pp. 12770-12779
    • Peisach, E.1    Selengut, J.D.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 44
    • 1442310583 scopus 로고    scopus 로고
    • Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily
    • Stewart, A. J., Schmid, R., Blindauer, C. A., Paisey, S. J., and Farquharson, C. (2003) Comparative modelling of human PHOSPHO1 reveals a new group of phosphatases within the haloacid dehalogenase superfamily. Protein Eng. 16, 889-895. (Pubitemid 38281738)
    • (2003) Protein Engineering , vol.16 , Issue.12 , pp. 889-895
    • Stewart, A.J.1    Schmid, R.2    Blindauer, C.A.3    Paisey, S.J.4    Farquharson, C.5
  • 45
    • 4344585269 scopus 로고    scopus 로고
    • Phosphoryl group transfer: Evolution of a catalytic scaffold
    • DOI 10.1016/j.tibs.2004.07.008, PII S0968000404001793
    • Allen, K. N. and Dunaway-Mariano, D. (2004) Phosphoryl group transfer: evolution of a catalytic scaffold. Trends Biochem. Sci. 29, 495-503. (Pubitemid 39158873)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.9 , pp. 495-503
    • Allen, K.N.1    Dunaway-Mariano, D.2
  • 46
    • 1542267779 scopus 로고    scopus 로고
    • Analysis of the substrate specificity loop of the had superfamily cap domain
    • DOI 10.1021/bi0356810
    • Lahiri, S. D., Zhang, G., Dai, J., Dunaway-Mariano, D., and Allen, K. N. (2004) Analysis of the substrate specificity loop of the HAD superfamily cap domain. Biochemistry 43, 2812-2820. (Pubitemid 38327812)
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2812-2820
    • Lahiri, S.D.1    Zhang, G.2    Dai, J.3    Dunaway-Mariano, D.4    Allen, K.N.5
  • 48
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • DOI 10.1074/jbc.273.22.13375
    • Maehama, T. and Dixon, J. E. (1998) The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273, 13,375-13,378. (Pubitemid 28268370)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.22 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 49
    • 0036899518 scopus 로고    scopus 로고
    • PTEN and myotubularin phosphatases: From 3-phosphoinositide dephosphorylation to disease
    • DOI 10.1016/S0962-8924(02)02412-1, PII S0962892402024121
    • Wishart, M. J. and Dixon, J. E. (2002) PTEN and myotubularins phosphatases: from 3-phosphoinositide dephosphorylation to disease. Trends Cell Biol. 12, 579-585. (Pubitemid 35461856)
    • (2002) Trends in Cell Biology , vol.12 , Issue.12 , pp. 579-585
    • Wishart, M.J.1    Dixon, J.E.2
  • 51
    • 0036668633 scopus 로고    scopus 로고
    • The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations
    • DOI 10.1093/embo-reports/kvf150
    • Bordo, D. and Bork, P. (2002) The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations. EMBO Rep. 3, 741-746. (Pubitemid 34966012)
    • (2002) EMBO Reports , vol.3 , Issue.8 , pp. 741-746
    • Bordo, D.1    Bork, P.2
  • 53
    • 0034405696 scopus 로고    scopus 로고
    • Relationship between exopolysaccharide production and protein-tyrosine phosphorylation in Gramnegative bacteria
    • Vincent, C., Duclos, B., Grangeasse, C., et al. (2000) Relationship between exopolysaccharide production and protein-tyrosine phosphorylation in Gramnegative bacteria. J. Mol. Biol. 304, 311-321.
    • (2000) J. Mol. Biol. , vol.304 , pp. 311-321
    • Vincent, C.1    Duclos, B.2    Grangeasse, C.3
  • 54
    • 33144469653 scopus 로고    scopus 로고
    • Characterization of the YfkJ protein tyrosine phosphatase of Bacillus subtilis and Bacillus anthracis
    • Musumeci, L., Tautz, L., Perego, M., Mustelin, T., and Bottini, N. (2005) Characterization of the YfkJ protein tyrosine phosphatase of Bacillus subtilis and Bacillus anthracis. J. Bacteriol., in press.
    • (2005) J. Bacteriol., in Press
    • Musumeci, L.1    Tautz, L.2    Perego, M.3    Mustelin, T.4    Bottini, N.5
  • 55
    • 0032509472 scopus 로고    scopus 로고
    • The second domain of the CD45 protein tyrosine phosphatase is critical for interleukin-2 secretion and substrate recruitment of TCRζ in vivo
    • Kashio, N., Matsumoto, W., Parker, S., and Rothstein, D.M. (1998). The second domain of the CD45 protein tyrosine phosphatase is critical for interleukin-2 secretion and substrate recruitment of TCRζ in vivo. J. Biol. Chem. 273, 33856-33863.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33856-33863
    • Kashio, N.1    Matsumoto, W.2    Parker, S.3    Rothstein, D.M.4
  • 58
    • 0037082201 scopus 로고    scopus 로고
    • Meeting at mitosis: Cell cycle-specific regulation of c-Src by RPTPα
    • Mustelin, T. and Hunter, T. (2002) Meeting at mitosis: cell cycle-specific regulation of c-Src by RPTPα Science's STKE. http://stke.sciencemag.org/cgi/content/full/OC-sigtrans;2002/115/pe3.
    • (2002) Science's STKE
    • Mustelin, T.1    Hunter, T.2
  • 59
    • 0031048053 scopus 로고    scopus 로고
    • Regulation of the low molecular weight phosphotyrosine phosphatase (LMPTP) by phosphorylation at tyrosines 131 and 132
    • Tailor, P., Williams, S., Gilman, J., Couture, C., and Mustelin, T. (1997) Regulation of the low molecular weight phosphotyrosine phosphatase (LMPTP) by phosphorylation at tyrosines 131 and 132. J. Biol. Chem. 272, 5371-5376.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5371-5376
    • Tailor, P.1    Williams, S.2    Gilman, J.3    Couture, C.4    Mustelin, T.5
  • 61
    • 0029757347 scopus 로고    scopus 로고
    • Disruption of the erp/mkp-1 gene does not affect mouse development: Normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts
    • Dorfman, K., Carrasco, D., Gruda, M., Ryan, C., Lira, S. A., and Bravo, R. (1996) Disruption of the erp/mkp-1 gene does not affect mouse development: normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts. Oncogene 13, 925-931. (Pubitemid 26329078)
    • (1996) Oncogene , vol.13 , Issue.5 , pp. 925-931
    • Dorfman, K.1    Carrasco, D.2    Gruda, M.3    Ryan, C.4    Lira, S.A.5    Bravo, R.6
  • 62
    • 0942279640 scopus 로고    scopus 로고
    • PEST Domain-Enriched Tyrosine Phosphatase (PEP) Regulation of Effector/Memory T Cells
    • DOI 10.1126/science.1092138
    • Hasegawa, K., Martin, F., Huang, G., Tumas, D., Diehl, L., and Chan, A. C. (2004) PEST domain-enriched tyrosine phosphatase (PEP) regulation of effector/memory T cells. Science 303, 685-689. (Pubitemid 38141637)
    • (2004) Science , vol.303 , Issue.5658 , pp. 685-689
    • Hasegawa, K.1    Martin, F.2    Huang, G.3    Tumas, D.4    Diehl, L.5    Chan, A.C.6
  • 71
    • 11144266638 scopus 로고    scopus 로고
    • Association of the single nucleotide polymorphism C1858T of the PTPN22 gene with type 1 diabetes
    • DOI 10.1016/j.humimm.2004.09.016, PII S0198885904006421
    • Ladner, M. B., Bottini, N., Valdes, A. M., and Noble, J. A. (2005) Association of the single-nucleotide polymorphism C1858T of the PTPN22 gene with type 1 diabetes. Hum. Immunol. 66, 60-64. (Pubitemid 40037712)
    • (2005) Human Immunology , vol.66 , Issue.1 , pp. 60-64
    • Ladner, M.B.1    Bottini, N.2    Valdes, A.M.3    Noble, J.A.4
  • 72
    • 0030583596 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the human transmembrane protein tyrosine phosphatase homologue, phogrin, an autoantigen of type 1 diabetes
    • DOI 10.1006/bbrc.1996.1526
    • Kawasaki, E., Hutton, J. C., and Eisenbarth, G. S (1996) Molecular cloning and characterization of the human transmembrane PTP homologue, phogrin, an autoantigen of type I diabetes. Biochem. Biophys. Res. Commun. 227, 440-447. (Pubitemid 26362823)
    • (1996) Biochemical and Biophysical Research Communications , vol.227 , Issue.2 , pp. 440-447
    • Kawasaki, E.1    Hutton, J.C.2    Eisenbarth, G.S.3
  • 77
    • 0026356617 scopus 로고
    • Partial trisomy 1q. A nonrandom primary chromosomal abnormality in myelodysplastic syndromes?
    • Fonatsch, C., Haase, D., Freund, M., Bartels, H., and Tesch, H. (1991) Partial trisomy 1q. A nonrandom primary chromosomal abnormality in myelodysplastic syndromes? Cancer Genet. Cytogenet. 56, 243-253.
    • (1991) Cancer Genet. Cytogenet. , vol.56 , pp. 243-253
    • Fonatsch, C.1    Haase, D.2    Freund, M.3    Bartels, H.4    Tesch, H.5
  • 78
    • 0027957970 scopus 로고
    • A hematopoietic protein tyrosine phosphatase (HePTP) gene that is amplified and overexpressed in myeloid malignancies maps to chromosome 1q32.1
    • Zanke, B., Squire, J. Griesser, H. et al. (1994) A hematopoietic PTP (HePTP) gene that is amplified and overexpressed in myeloid malignancies maps to chromosome 1q32.1. Leukemia 8, 236-244. (Pubitemid 24057536)
    • (1994) Leukemia , vol.8 , Issue.2 , pp. 236-244
    • Zanke, B.1    Squire, J.2    Griesser, H.3    Henry, M.4    Suzuki, H.5    Patterson, B.6    Minden, M.7    Mak, T.W.8
  • 79
    • 0037390203 scopus 로고    scopus 로고
    • The MID1/PP2A complex: A key to the pathogenesis of Opitz BBB/G syndrome
    • DOI 10.1002/bies.10256
    • Schweiger, S. and Schneider, R. (2003) The MID1/PP2A complex: a key to the pathogenesis of Opitz BBB/G syndrome. Bioessays 25, 356-366. (Pubitemid 36433182)
    • (2003) BioEssays , vol.25 , Issue.4 , pp. 356-366
    • Schweiger, S.1    Schneider, R.2
  • 80
    • 0142031099 scopus 로고    scopus 로고
    • A mutation in protein phosphatase type 2A as a cause of melanoma progression
    • Ito, A., Koma, Y.-I., and Watabe, K. (2003) A mutation in protein phosphatase type 2A as a cause of melanoma progression. Histol. Histopathol. 18, 1313-1319. (Pubitemid 37265031)
    • (2003) Histology and Histopathology , vol.18 , Issue.4 , pp. 1313-1319
    • Ito, A.1    Koma, Y.-I.2    Watabe, K.3
  • 81
    • 1442310493 scopus 로고    scopus 로고
    • Identification of specific PP2A complexes involved in human cell transformation
    • DOI 10.1016/S1535-6108(04)00026-1, PII S1535610804000261
    • Chen, W., Possemato, R., Campbell, K. T., Plattner, C. A., Pallas, D. C., and Hahn, W. C. (2004) Identification of specific PP2A complexes involved in human cell transformation. Cancer Cell 5, 127-136. (Pubitemid 38283799)
    • (2004) Cancer Cell , vol.5 , Issue.2 , pp. 127-136
    • Chen, W.1    Possemato, R.2    Campbell, K.T.3    Plattner, C.A.4    Pallas, D.C.5    Hahn, W.C.6
  • 84
    • 0038499543 scopus 로고    scopus 로고
    • Small molecule regulation of phosphatasedependent cell signaling pathways
    • Lazo, J. S. and Wipf, P. (2003) Small molecule regulation of phosphatasedependent cell signaling pathways. Oncol. Res. 13, 347-352.
    • (2003) Oncol. Res. , vol.13 , pp. 347-352
    • Lazo, J.S.1    Wipf, P.2
  • 85
    • 13844312725 scopus 로고    scopus 로고
    • Dual specificity protein phosphatases: Therapeutic targets for cancer and Alzheimer's disease
    • DOI 10.1146/annurev.pharmtox.45.120403.100040
    • Ducruet, A. P., Vogt, A., Wipf, P., and Lazo, J. (2005) Dual specificity protein phosphatases: therapeutic targets for cancer and Alzheimer's disease. Annu. Rev. Pharmacol. Toxicol. 45, 725-750. (Pubitemid 40261823)
    • (2005) Annual Review of Pharmacology and Toxicology , vol.45 , pp. 725-750
    • Ducraet, A.P.1    Vogt, A.2    Wipf, P.3    Lazo, J.S.4
  • 87
    • 0038201764 scopus 로고    scopus 로고
    • Molecular design and biological activities of protein-tyrosine phosphatase inhibitors
    • DOI 10.1016/S0163-7258(03)00050-0
    • Umezawa, K., Kawakami, M., and Watanabe, T. (2003) Molecular design and biological activities of protein-tyrosine phosphatase inhibitors. Pharmacol. Ther. 99, 15-24. (Pubitemid 36694747)
    • (2003) Pharmacology and Therapeutics , vol.99 , Issue.1 , pp. 15-24
    • Umezawa, K.1    Kawakami, M.2    Watanabe, T.3
  • 88
    • 3142763040 scopus 로고    scopus 로고
    • α,α-Difluoro-β-ketophosphonates as potent inhibitors of protein tyrosine phosphatase 1B
    • DOI 10.1016/j.bmcl.2004.05.082, PII S0960894X04007358
    • Li, X., Bhandari, A., Holmes, C. P., and Szardenings, A. K. (2004) Alpha,alphadifluoro-beta-ketophosphonates as potent inhibitors of protein tyrosine phosphatase 1B. Bioorg. Med. Chem. Lett. 14, 4301-4306. (Pubitemid 38916954)
    • (2004) Bioorganic and Medicinal Chemistry Letters , vol.14 , Issue.16 , pp. 4301-4306
    • Li, X.1    Bhandari, A.2    Holmes, C.P.3    Szardenings, A.K.4
  • 89
    • 21244444303 scopus 로고    scopus 로고
    • Inhibitors of protein tyrosine phosphatases: Next-generation drugs?
    • DOI 10.1002/anie.200461517
    • Bialy, L. and Waldmann, H. (2005) Inhibitors of protein tyrosine phosphatases: next-generation drugs? Angew. Chem. Int. Ed. Engl., 44, 3814-3839. (Pubitemid 40885689)
    • (2005) Angewandte Chemie - International Edition , vol.44 , Issue.25 , pp. 3814-3839
    • Bialy, L.1    Waldmann, H.2
  • 90
    • 5744220107 scopus 로고    scopus 로고
    • Inhibition of protein tyrosine phosphatase 1B as a potential treatment of diabetes and obesity
    • DOI 10.2174/1381612043382954
    • Pei, Z., Liu, G., Lubben, T. H., and Szczepankiewicz, B. G. (2004) Inhibition of protein tyrosine phosphatase 1B as a potential treatment of diabetes and obesity. Curr. Pharm. Des. 10, 3481-3504. (Pubitemid 39378329)
    • (2004) Current Pharmaceutical Design , vol.10 , Issue.28 , pp. 3481-3504
    • Pei, Z.1    Liu, G.2    Lubben, T.H.3    Szczepankiewicz, B.G.4


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