Protein tyrosine phosphatases: Strategies for distinguishing proteins in a family containing multiple drug targets and anti-targets

Current Pharmaceutical Design

Volumn 10, Issue 10, 2004, Pages 1161-1181

  Hoffman, Brian T ^a   Nelson, Melanie R ^a   Burdick, Keith ^a   Baxter, Susan M ^a  

^a Cengent Therapeutics Inc   (United States)

Author keywords

Cdc25; Dual specificity phosphatases; Inhibitor; Protein tyrosine phosphatases; Pten; PTP; Specificity; Structure based drug design

Indexed keywords

1,2 NAPHTHOQUINONE DERIVATIVE; 2 (OXALYLAMINO)BENZOIC ACID; ALENDRONIC ACID; ANTINEOPLASTIC AGENT; BENZIMIDAZOLE DERIVATIVE; CD45 ANTIGEN; CINNAMIC ACID DERIVATIVE; DIFLUOROMETHYLPHOSPHONOMETHYLPHENYLALANINE; HYDROLASE INHIBITOR; MALONIC ACID DERIVATIVE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; OXAMIC ACID; PENTAMIDINE DERIVATIVE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR AGONIST; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHONIC ACID DERIVATIVE; PHOSPHONOMETHYLPHENYLALANINE; PROTEIN INHIBITOR; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE 1B; PROTEIN TYROSINE PHOSPHATASE 1B INHIBITOR; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; QUINONE DERIVATIVE; RK 682; SULFONAMIDE; SULFONE DERIVATIVE; SULFONIC ACID DERIVATIVE; TETRAZOLE DERIVATIVE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

ANTINEOPLASTIC ACTIVITY; CLINICAL TRIAL; DRUG DESIGN; DRUG POTENCY; DRUG SCREENING; DRUG SELECTIVITY; DRUG STRUCTURE; DRUG TARGETING; ENZYME ACTIVE SITE; ENZYME INHIBITION; ENZYME SPECIFICITY; HUMAN; IN VITRO STUDY; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN MOTIF; REVIEW; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; DRUG DESIGN; ENZYME INHIBITORS; HUMANS; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN-TYROSINE-PHOSPHATASE; SUBSTRATE SPECIFICITY;

EID: 1842431386     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/1381612043452659     Document Type: Review

References (204)

1. Flint AJ, Tiganis T, Barford D, Tonks NK. Development of "sUbstrate-trMpping" mutants to identify physiological substrates of protein tyrosine phosphatases. Proc Natl Acad Sci USA 1997; 94: 1680-5.
2. Theodosiou A, Ashworth A. MAP kinase phosphatases. Genome Biol 2002; 3: REVIEWS3009.
3. Elchebly, MPP, Michaliszyn, E, Cromlish W, Collins S, Loy AL, Normandin D, Cheng A, Himms-Hagen J, Chan CC, Ramachandran C, Gresser MJ, Tremblay, ME, Kennedy. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science 2000; 283: 1423-1425.
4. Klaman, L.D., Boss, O., Peroni, O.D., J.K., K., Martino, J.L., Zabolotny, J.M., et al. Increased energy expenditure, decreased adiposity, and tissue-specific insulin sensitivity in protein-tyrosine phosphatase 1B-deficient mice. Molecular Cell Biology 2000; 20: 5479-89.
5. van Huijsduijnen RHBA, Swinnen D. Selecting protein tyrosine phosphatases as drug targets. Drug Discovery Today 2002; 7: 1013-1019.
6. Zhang ZY, Wang Y, Dixon JE. Dissecting the catalytic mechanism of protein-tyrosine phosphatases. Proc Natl Acad Sci USA 1994; 91: 1624-7.
7. Denu JM, Tanner KG. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 1998; 37: 5633-42.
8. Zhang ZY. Chemical and mechanistic approaches to the study of protein tyrosine phosphatases. Acc Chem Res 2003; 36: 385-92.
9. Camps M, Nichols AA, rkinstall S. Dual specificity phosphatases: A gene family for control of MAP kinase function. FASEB J 2000; 14: 6-16.
10. Guan KL, Broyles SS, Dixon JE. A Tyr/Ser protein phosphatase encoded by vaccinia virus. Nature 1991; 350: 359-62.
11. Denu JM, Dixon JE. A catalytic mechanism for the dual-specific phosphatases. Proc Natl Acad Sci USA 1995; 92: 5910-4.
12. Maehama T, Taylor GS, Dixon JE. PTEN and myotubularin: Novel phosphoinositide phosphatases. Annu Rev Biochem 2001; 70: 247-79.
13. Andersen JN, Mortensen OH, Peters GH, Drake PG, Iversen LF, Olsen OH, et al. Structural and evolutionary relationships among protein tyrosine phosphatase domains. Mol Cell Biol 2001; 21: 7117-36.
14. Bordo DBP. The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations. EMBO Reports 2002: 3: 741-746.
15. Bennett MS, Guan Z, Laurberg M, Su XD. Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases. Proc Natl Acad Sci USA 2001; 98: 13577-82.
16. Wishart MJ, Dixon JE. Gathering STYX: Phosphatase-like form predicts functions for unique protein-interaction domains. Trends Biochem Sci 1998; 23: 301-6.
17. Changela AHC, Martins A, Shuman S, Mondragon A. Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme. EMBO Journal 2001; 20: 2575-2586.
18. Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995; 247: 536-40.
19. Huyer G, Liu S, Kelly J, Moffat J, Payette P, Kennedy B, et al. Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J Biol Chem 1997; 272: 843-51.
20. Rhee SG, Bae YS, Lee SR, Kwon J. Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation. Sci STKE 2000; 2000: PE1.
21. van Montfort RL, Congreve M, Tisi D, Carr R, Jhoti H. Oxidation state ofthe active-site cysteine in protein tyrosine phosphatase 1B. Nature 2003; 423: 773-7.
22. Salmeen A, Andersen JN, Myers MP, Tonks NK, Barford D. Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B. Mol Cell 2000; 6: 1401-12.
23. Fu H, Park J, Pei D. Peptidyl aldehydes as reversible covalent inhibitors of protein tyrosine phosphatases. Biochemistry 2002; 41: 10700-9.
24. Liljebris C, Martinsson J, Tedenborg L, Williams M, Barker E, Duffy JE, et al. Synthesis and biological activity of a novel class of pyridazine analogues as non-competitive reversible inhibitors of protein tyrosine phosphatase 1B (PTP1B). Bioorg Med Chem 2002; 10: 3197-212.
25. Meng TC, Fukada T, Tonks NK. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Molecular Cell 2002; 9: 387-399.
26. Liu G, Szczepankiewicz BG, Pei Z, Janowick DA, Xin Z, Hajduk PJ, et al. Discovery and structure-activity relationship of oxalylarylaminobenzoic acids as inhibitors of protein tyrosine phosphatase 1B. J Med Chem 2003; 46: 2093-103.
27. Larsen SD, Barf T, Liljebris C, May PD, Ogg D, O'Sullivan TJ, et al. Synthesis and biological activity of a novel class of small molecular weight peptidomimetic competitive inhibitors of protein tyrosine phosphatase 1B. J Med Chem 2002; 45: 598-622.
28. Bleasdale JE, Ogg D, Palazuk BJ, Jacob CS, Swanson ML, Wang XY, et al. Small molecule peptidomimetics containing a novel phosphotyrosine bioisostere inhibit protein tyrosine phosphatase 1B and augment insulin action. Biochemistry 2001; 40: 5642-54.
29. Jia Z, Barford D, Flint AJ,Tonks NK. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. Science 1995; 268: 1754-8.
30. Yuvaniyama J, Denu JM, Dixon, J.E.Saper, M.A. Crystal structure of the dual specificity protein phosphatase VHR. Science 1996; 272: 1328-31.
31. Wang, S., Tabernero, L., Zhang, M., Harms, E., Van Etten, R. L. Stauffacher, C.V. Crystal structures of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate. Biochemistry 2000; 39: 1903-14.
32. Pannifer AD, Flint AJ, Tonks NK, Barford D. Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by x-ray crystallography. J Biol Chem 1998; 273: 10454-62.
33. Groves MR, Yao ZJ, Roller PP, Burke TR, Jr Barford D. Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics. Biochemistry 1998; 37: 17773-83.
34. Sarmiento M, Wu L, Keng YF, Song L, Luo Z, Huang Z, et al. Structure-based discovery of small molecule inhibitors targeted to protein tyrosine phosphatase 1B. J Med Chem 2000; 43: 146-55.
35. Song H, Hanlon N, Brown NR, Noble ME, Johnson LN, Barford D. Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. Mol Cell 2001; 7: 615-26.
36. Stewart AF, Dowd S, Keyse SM, McDonald NQ. Crystal structure of the MAPK phosphatase Pystl catalytic domain and implications for regulated activation. Nat Struct Biol 1999; 6: 174-81.
37. Jia, Z, Ye Q, Dinaut AN, Wang Q, Waddleton D, Payette P, et al. Structure of protein tyrosine phosphatase 1B in complex with inhibitors bearing two phosphotyrosine minietics. J Med Chem 2001; 44: 4584-94.
38. Sarmiento M, Zhao Y, Gordon SJ, Zhang ZY. Molecular basis for substrate specificity of protein-tyrosine phosphatase 1B. J Biol Chem 1998; 273: 26368-74.
39. Asante-Appiah E, Patel S, Dufresne C, Roy P, Wang Q, Patel V, et al. The structure of PTP-1B in complex with a peptide inhibitor reveals an alternative binding mode for bisphosphonates. Biochemistry 2002; 41: 9043-51.
40. Iversen LF, Andersen HS, Branner S, Mortensen SB, Peters GH, Norris K, et al. Structure-based design of a low molecular weight, nonphosphorus, nonpeptide, and highly selective inhibitor of protein-tyrosine phosphatase 1B. J Biol Chem 2000: 275: 10300-7.
41. Puius YA, Zhao Y, Sullivan M, Lawrence DS, Almo SC, Zhang ZY. Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: A paradigm for inhibitor design. Proc Natl Acad Sci USA 1997; 94: 13420-5.
42. Desmarais S, Friesen RW, Zamboni R, Ramachandran C. [Difluro(phosphono)methyl]phenylalanine-containing peptide inhibitors of protein tyrosine phosphatases. Biochem J 1999; 337 (Pt 2): 219-23.
43. Peters GH, Iversen LF, Branner S, Andersen HS, Mortensen SB, Olsen OH, et al. Residue 259 is a key determinant of substrate specificity of protein-tyrosine phosphatases 1B and alpha. J Biol Chem 2000; 275: 18201-9.
44. Iversen LF, Andersen HS, Moller KB, Olsen OH, Peters GH, Branner S, et al. Steric hindrance as a basis for structure-based design of selective inhibitors of protein-tyrosine phosphatases. Biochemistry 2001; 40: 14812-20.
45. Barford D, Flint AJ, Tonks NK. The crystal structure of kuman protein tyrosine phosphotase 1B. Science 1994; 263: 1397-1404.
46. Liu G, Trevillyan JM. Protein tyrosine phosphatase 1B as a target for the treatment of impaired glucose tolerance and type II diabetes. Curr Opin Investig Drugs 2002; 3: 1608-16.
47. Zhang ZY, Lee SY. PTP1B inhibitors as potential therapeutics in the treatment of type 2 diabetes and obesity. Expert Opin Investig Drugs 2003; 12: 223-33.
48. Johnson TO, Ermolieff J, Jirousek MR. Protein tyrosine phosphatase 1B inhibitors for diabetes. Nat Rev Drug Discov 2002; 1: 696-709.
49. Burke TR, Yao ZJ, Smyth MS, Ye B. Preparation of fluoro-4-(phosphonomethyl)-D,L-phenylalanine and hydroxy-4-(phosphonomethyl)-D,L-phenylalanine sduitably protected for solid-phase synthesis of peptides containing hydrolytically stable analogs of O-phosphotyrosine. J Org Chem 1993; 58: 1336-1340.
50. Burke TR, Smyth MS, Otaka A, Roller PP. Synthesis of 4-phosphono(difluoromethyl)-D,L-phenylalanine and N-Boc and N-Fmoc derivatives suitably protected for solid-phase synthesis of nonhydrolizable phosphoryl peptide analogues. Tetrahedron Lett. 1993; 34: 4125-4128.
51. Burke TR Jr, Kole HK, Roller PP. Potent inhibition of insulin receptor dephosphorylation by a hexamer peptide containing the phosphotyrosyl mimetic F2Pmp. Biochem Biophys Res Commun 1994; 204: 129-34.
52. Burke TR Jr, Ye B, Akamatsu M, Ford H Jr, Yan X, Kole HK, et al. 4′-O-[2-(2-fluoromalonyl)]-L-tyrosine: A phosphotyrosyl mimic for the preparation of signal transduction inhibitory peptides. J Med Chem 1996; 39: 1021-7.
53. Glover NR, Tracey AS. The phosphatase domains of LAR, CD45, and PTP1B: Structural correlations with peptide-based inhibitors. Biochem Cell Biol 2000; 78: 39-50.
54. Akamatsu M, Roller PP, Chen L, Zhang ZY, Ye B, Burke TR Jr. Potent inhibition of protein-tyrosine phosphatase by phosphotyrosine-mimic containing cyclic peptides. Bioorg Med Chem 1997; 5: 157-63.
55. Roller PP, Wu L, Zhang ZY, Burke TR Jr. Potent inhibition of protein-tyrosine phosphatase-1B using the phosphotyrosyl mimetic fluoro-O-malonyl tyrosine (FOMT). Bioorg Med Chem Lett 1998; 8: 2149-50.
56. Burke TR Jr, Zhang ZY. Protein-tyrosine phosphatases: structure, mechanism, and inhibitor discovery. Biopolymers 1998; 47: 225-41.
57. Ye B, Akamatsu M, Shoelson SE, Wolf G, Giorgetti-Peraldi S, Yan X, et al. L-O-(2-malonyl)tyrosine: A new phosphotyrosyl mimetic for the preparation of Src homology 2 domain inhibitory peptides. J Med Chem 1995; 38: 4270-5.
58. Pellegrini MC, Liang H, Mandiyan S, Wang K, Yuryev A, Vlattas I, et al. Mapping the subsite preferences of protein tyrosine phosphatase PTP-1B using combinatorial chemistry approaches. Biochemistry 1998; 37: 15598-606.
59. Kotoris, CC, Chen MJ,Taylor SD. Novel phosphate mimetics for the design of non-peptidyl inhibitors of protein tyrosine phosphatases. Bioorg Med Chem Lett 1998; 8: 3275-80.
60. Leung C, Grzyb J, Lee J, Meyer N, Hum G, Jia C, et al. The difluoromethylenesulfonic acid group as a monoanionic phosphate surrogate for obtaining PTP1B inhibitors. Bioorg Med Chem 2002; 10: 2309-23.
61. Rice RL, Rusnak JM, Yokokawa F, Yokokawa S, Messner DJ, Boynton AL, et al. A targeted library of small-molecule, tyrosine, and dual-specificity phosphatase inhibitors derived from a rational core design and random side chain variation. Biochemistry 1997; 36: 15965-74.
62. Moran EJ, Sarshar S, Cargill JF, Shahbaz MM, Lio A, Mjalli AMM, et al. Radio frequencybtag encoded combinatorial library method for the discovery of tripeptide-substituted cinnamic acid inhibitors of the protein tyrosine phosphatase PTP1B. J Am Chem Soc 1995; 117: 10787-10788.
63. Liu G, Xin Z, Liang H, Abad-Zapatero C, Hajduk PJ, Janowick DA, et al. Selective protein tyrosine phosphatase 1B inhibitors: targeting the second phosphotyrosine binding site with non-carboxylic acid-containing ligands. J Med Chem 2003; 46: 3437-40.
64. Szczepankiewicz BG, Liu G, Hajduk PJ, Abad-Zapatero C, Pei Z, Xin Z, et al. Discovery of a potent, selective protein tyrosine phosphatase 1B inhibitor using a linked-fragment strategy. J Am Chem Soc 2003; 125: 4087-96.
65. Andersen HS, Iversen LF, Jeppesen CB, Branner S, Norris K, Rasmussen HB, et al. 2-(oxalylamino)-benzoic acid is a general. competitive inhibitor of protein-tyrosine phosphatases. J Biol Chem 2000; 275: 7101-8.
66. Burke TR Jr, Ye B, Yan X, Wang S, Jia Z, Chen L, et al. Small molecule interactions with protein-tyrosine phosphatase PTP1B and their use in inhibitor design. Biochemistry 1996; 35: 15989-96.
67. Yao ZJ, Ye B, Wu XW, Wang S, Wu L, Zhang ZY, et al. Structure-based design and synthesis of small molecule protein-tyrosine phosphatase 1B inhibitors. Bioorg Med Chem 1998; 6: 1799-810.
68. Taylor, S.D., Kotoris, C.C., Dinaut, A.N., Wang, Q., Ramachandran, C.Huang, Z. Potent non-peptidyl inhibitors of protein tyrosine phosphatase 1B. Bioorg Med Chem 1998; 6: 1457-68.
69. Yokomatsu T, Murano T, Umesue I, Soeda S, Shimeno H, Shibuya S. Synthesis and biological evaluation of alpha,alpha-difluorobenzylphosphonic acid derivatives as small molecular inhibitors of protein-tyrosine phosphatase 1B. Bioorg Med Chem Lett 1999; 9: 529-32.
70. Ibrahimi OA, Wu L, Zhao K, Zhang ZY. Synthesis and characterization of a novel class of protein tyrosine phosphatase inhibitors. Bioorg Med Chem Lett 2000: 10: 457-60.
71. Beers SA, Malloy, EA, Wu W, Wachter MP, Gunnia U, Cavender D, et al. Nitroarylhydroxymethylphosphonic acids as inhibitors of CD45. Bioorg Med Chem 1997; 5: 2203-11.
72. Huang P, Ramphal J, Wei J, Liang C, Jallal B, McMahon G, et al. Structure-Based design and discovery of novel inhibitors of protein tyrosine phosphatases. Bioorg Med Chem 2003; 11: 1835-49.
73. Burke TR Jr, Lee K. Phosphotyrosyl mimetics in the development of signal transduction inhibitors. Acc Chem Res 2003; 36: 426-33.
74. Chatterjee S, Goldstein BJ, Csermley P, Shoelson SE. Design and synthesis of potent substrates and inhibitors of PTPases., in Peptides: Chemistry and biology., J.E. Rivier and J.A. Smith, Editors. 1992, ESCOM Science Publishers: Leiden, Netherlands. p. 553-555.
75. Montserat J, Chen L, Lawrence DS, Zhang ZY. Potent low molecular weight substrates for protein-tyrosine phosphatase. J Biol Chem 1996; 271: 7868-72.
76. Doman TN, McGovern SL, Witherbee BJ, Kasten TP, Kurumbail R, Stallings WC, et al. Molecular docking and high-throughput screening for novel inhibitors of protein tyrosine phosphatase-1B. J Med Chem 2002; 45: 2213-21.
77. Wrobel J, Sredy J, Moxham C, Dietrich A, Li Z, Sawicki DR, et al. PTP1B inhibition and antihyperglycemic activity in the ob/ob mouse model of novel 11-arylbenzo[b]naphtho[2,3-d]furans and 11-arylbenzo[b]naphtho[2,3-d]thiophenes. J Med Chem 1999; 42: 3199-202.
78. Burkey BF, Dong M, Wennogle L, Babb R, Dressman M, Islam A, et al. Pharmacogenomic evaluation of a putative orally active PTP-1B inhibitor using ob/ob mice reveals an alternative mechanism of action., in The 62nd American Diabetes Association Annual Meeting. 2002: San Francisco, CA, USA.
79. You-Ten KE, Muise ES, Itie A, Michaliszyn E, Wagner J, Jothy S, et al. Impaired bone marrow microenvironment and immune function in T cell protein tyrosine phosphatase-deficient mice. J Exp Med 1997; 186: 683-93.
80. Galic S, Klingler-Hoffmann M, Fodero-Tavoletti MT, Puryer MA, Meng TC, Tonks NK, et al. Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP. Mol Cell Biol 2003; 23: 2096-108.
81. Shen K, Keng YF, Wu L, Guo XL, Lawrence DS, Zhang ZY. Acquisition of a specific and potent PTP1B inhibitor from a novel combinatorial library and screening procedure. J Biol Chem 2001; 276: 47311-9.
82. Guo XL, Shen K, Wang F, Lawrence DS, Zhang ZY. Probing the molecular basis for potent and selective protein-tyrosine phosphatase 1B inhibition. J Biol Chem 2002; 277: 41014-22.
83. Sun JP, Fedorov AA, Lee SY, Guo XL, Shen K, Lawrence DS, et al. Crystal structure of PTP1B complexed with a potent and selective bidentate inhibitor. J Biol Chem 2003; 278: 12406-14.
84. Xin Z, Oost TK, Abad-Zapatero C, Hajduk PJ, Pei Z, Szczepankiewicz BG, et al. Potent, selective inhibitors of protein tyrosine phosphatase 1B. Bioorg Med Chem Lett 2003; 13: 1887-90.
85. Mooney RA, LeVea CM. The leukocyte common antigen-related protein LAR: Candidate PTP for inhibitory targeting. Curr Top Med Chem 2003; 3: 809-19.
86. Schaapveld RQ, Schepens JT, Robinson GW, Attema J, Oerlemans FT, Fransen JA, et al. Impaired mammary gland development and function in mice lacking LAR receptor-like tyrosine phosphatase activity. Dev Biol 1997; 188: 134-46.
87. HamaguchiT, Takahashi A, KagamizonoT,Manaka A,Sato M, Osada H. Synthesis and characterization of a potent and selective protein tyrosine phosphatase inhibitor, 2. Bioorg Med Chem Lett 2000; 10: 2657-60.
88. Ahn JH, Cho SY, Ha JD, Chu SY, Jung SH, Jung YS, et al. Synthesis and PTP1B inhibition of 1,2-naphthoquinone derivatives as potent anti-diabetic agents. Bioorg Med Chem Lett 2002; 12: 1941-6.
89. Andersen HS, Olsen OH, Iversen LF, Sorensen AL, Mortensen SB, Christensen MS, et al. Discovery and SAR of a novel selective and orally bioavailable nonpeptide classical competitive inhibitor class of protein-tyrosine phosphatase 1B. J Med Chem 2002; 45: 4443-59.
90. Chen YT, Seto CT. Divalent and trivalent alpha-ketocarboxylic acids as inhibitors of protein tyrosine phosphatases. J Med Chem 2002; 45: 3946-52.
91. Taing M, Keng YF, Shen K, Wu L, Lawrence DS, Zhang, ZY. Potent and highly selective inhibitors of the protein tyrosine phosphatase 1B. Biochemistry 1999; 38: 3793-803.
92. Malamas MS, Sredy J, Moxham C, Katz A, Xu W, McDevitt R, et al. Novel benzofuran and benzothiophene biphenyls as inhibitors of protein tyrosine phosphatase 1B with antihyperglycemic properties. J Med Chem 2000; 43: 1293-310.
93. Ponniah S, Wang DZ, Lim KL, Pallen CJ. Targeted disruption of the tyrosine phosphatase PTPalpha leads to constitutive downregulation of the kinases Src and Fyn. Curr Biol 1999; 9: 535-8.
94. Gil-Henn H, Elson A. Tyrosine phosphatase-epsilon activates Src and supports the transformed phenotype of Neu-induced mammary tumor cells. J Biol Chem 2003; 278: 15579-86.
95. Schmidt A, Rutledge SJ, Endo N, Opas EE, Tanaka H, Wesolowski G, et al. Protein-tyrosine phosphatase activity regulates osteoclast formation and function: Inhibition by alendronate. Proc Natl Acad Sci USA 1996; 93: 3068-73.
96. Koretzky, G.A., Picus, J., Thomas, M.L.Weiss, A. Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway. Nature 1990; 346: 66-8.
97. Stone JD, Conroy LA, Byth KF, Hederer RA, Howlett S, Takemoto Y, et al. Aberrant TCR-mediated signaling in CD45-null thymocytes involves dysfunctional regulation of Lck, Fyn, TCR-zeta, and ZAP-70. J Immunol 1997; 158: 5773-82.
98. Kishihara K, Penninger J, Wallace VA, Kundig TM, Kawai K, Wakeham A, et al. Normal B lymphocyte development but impaired T cell maturation in CD45-exon6 protein tyrosine phosphatase-deficient mice. Cell 1993; 74: 143-56.
99. Byth KF, Conroy LA, Howlett S, Smith AJ, May, J, Alexander DR, et al. CD45-null transgenic mice reveal a positive regulatory role for CD45 in early thymocyte development, in the selection of CD4+CD8+ thymocytes, and B cell maturation. J Exp Med 1996; 183: 1707-18.
100. Kung C, Pingel JT, Heikinheimo M, Klemola T, Varkila K, Yoo, LI, et al. Mutations in the tyrosine phosphatase CD45 gene in a child with severe combined immunodeficiency disease. Nat Med 2000; 6: 343-5.
101. Ratei R, Sperling C, Karawajew L, Schott G, Schrappe M, Harbott J, et al. Immunophenotype and clinical characteristics of CD45-negative and CD45-positive childhood acute lymphoblastic leukemia. Ann Hematol 1998; 77: 107-14.
102. Ozdemirli, M., Mankin, H.J., Aisenberg, A.C.Harris, N.L. Hodgkin's disease presenting as a solitary bone tumor. A report of four cases and review of the literature. Cancer 1996; 77: 79-88.
103. Irie-Sasaki J, Sasaki T, Matsumoto W, Opavsky A, Cheng M, Welstead G, et al. CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling. Nature 2001; 409: 349-54.
104. Tan J, Town T, Mori T, Wu Y, Saxe M, Crawford F, et al. CD45 opposes beta-amyloid peptide-induced microglial activation via inhibition of p44/42 mitogen-activated protein kinase. J Neurosci 2000; 20: 7587-94.
105. Urbanek RA, Suchard SJ, Steelman GB, Knappenberger KS, Sygowski LA, Veale CA, et al. Potent reversible inhibitors of the protein tyrosine phosphatase CD45. J Med Chem 2001; 44: 1777-93.
106. Wang Q, Huang Z, Ramachandran C, Dinaut ANTaylor SD. Naphthalenebis[alpha,alpha-difluoromethylenephosphonates] as potent inhibitors of protein tyrosine phosphatases. Bioorg Med Chem Lett 1998; 8: 345-50.
107. Wang H, Lim KL, Yeo SL, Xu X, Sim MM, Ting AE, et al. Isolation of a novel protein tyrosine phosphatase inhibitor, 2-methyl-fervenulone, and its precursors from Streptomyces. J Nat Prod 2000; 63: 1641-6.
108. Alvi KA, Casey A, Nair BG. Pulchellalactam: A CD45 protein tyrosine phosphatase inhibitor from the marine fungus Corollospora pulchella. J Antibiot (Tokyo) 1998; 51: 515-7.
109. Lee KBurke, TR Jr. CD45 protein-tyrosine phosphatase inhibitor development. Curr Top Med Chem 2003; 3: 797-807.
110. Mustelin T, Brockdorff J, Gjorloff-Wingren A, Tailor P, Han S, Wang X, et al. Lymphocyte activation: The coming of the protein tyrosine phosphatases. Front Biosci 1998; 3: D1060-96.
111. Pathak MK, Dhawan D, Lindner DJ, Borden EC, Farver C, Yi T. Pentamidine is an inhibitor of PRT phosphatases with anticancer activity. Mol CancerTher 2002; 1: 1255-64.
112. Yi T, Pathak MK, Lindner DJ, Ketterer ME, Farver C, Borden EC. Anticancer activity of sodium stibogluconate in synergy with IFNs. J Immunol 2002; 169: 5979-85.
113. Higashi H, Tsutsumi R, Muto S, Sugiyama T, Azuma T, Asaka M, et al. SHP-2 tyrosine phosphatase as an intracellular target of Helicobacter pylori CagA protein. Science 2002; 295: 683-6.
114. Covacci A, Telford JL, Del Giudice G, Parsonnet J, Rappuoli R. Helicobacter pylori virulence and genetic geography. Science 1999; 284: 1328-33.
115. Tartaglia M, Mehler EL, Goldberg R, Zampino G, Brunner HG, Kremer H, et al. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nat Genet 2001; 29: 465-8.
116. Park J, Fu H, Pei D. Peptidyl aldehydes as reversible covalent inhibitors of SRC homology 2 domains. Biochemistry 2003; 42: 5159-67.
117. McLean J, Batt J, Doering LC, Rotin D, Bain JR. Enhanced rate of nerve regeneration and directional errors after sciatic nerve injury in receptor protein tyrosine phosphatase sigma knock-out mice. J Neurosci 2002; 22: 5481-91.
118. Suhr SM, Pamula S, Baylink DJ, Lau KH. Antisense oligodeoxynucleotide evidence that a unique osteoclastic protein-tyrosine phosphatase is essential for osteoclastic resorption. J Bone Miner Res 2001; 16: 1795-803.
119. Seo Y, Matozaki T, Tsuda M, Hayashi Y, Itoh H, Kasuga M. Overexpression of SAP-1, a transmembrane-type protein tyrosine phosphatase, in human colorectal cancers. Biochem Biophys Res Commun 1997; 231: 705-11.
120. Shiota M, Tanihiro T, Nakagawa Y, Aoki N, Ishida N, Miyazaki K, el al. Protein Tyrosine Phosphatase PTP20 Induces Actin Cytoskeleton Reorganization by Dephosphorylating p190 RhoGAP in Rat Ovarian Granulosa Cells Stimulated with Follicle-Stimulating Hormone. Mol Endocrinol 2003; 17: 534-49.
121. Harroch S, Furtado GC, Brueck W, Rosenbluth J, Lafaille J, Chao M, et al. A critical role for the protein tyrosine phosphatase receptor type Z in functional recovery from demyelinating lesions. Nat Genet 2002; 32: 411-4.
122. Lin SL, Le TX, Cowen DS. SptP, a Salmonella typhimurium type III-secreted protein, inhibits the mitogen-activated protein kinase pathway by inhibiting Raf activation. Cell Microbiol 2003; 5: 267-75.
123. Sun JP, Wu L, Fedorov AA, Almo SC, Zhang ZY. Crystal structure of the yersinia protein-tyrosine Phosphatase YopH complexed with a specific small molecule inhibitor. J Biol Chem 2003.
124. Liang F, Huang Z, Lee SY, Liang J, Ivanov MI, Alonso A, et al. Aurintricarboxylic acid blocks in vitro and in vivo activity of YopH, an essential virulent factor of Yersinia pestis, the agent of plague. J Biol Chem 2003.
125. Todd JL, Rigas JD, Rafty LA, Denu JM. Dual-specificity protein tyrosine phosphatase VHR down-regulates c-Jun N-terminal kinase (JNK). Oncogene 2002; 21: 2573-83.
126. Alonso, A, Rahmouni S, Williams S, van Stipdonk M, Jaroszewski L, Godzik A, et al. Tyrosine phosphorylation of VHR phosphatase by ZAP-70. Nat Immunol 2003; 4: 44-8.
127. Usui T, Kojima S, Kidokoro S, Ueda K, Osada H, Sodeoka M. Design and synthesis of a dimeric derivative of RK-682 with increased inhibitory activity against VHR, a dual-specificity ERK phosphatase: implications for the molecular mechanism of the inhibition. Chem Biol 2001; 8: 1209-20.
128. Sodeoka, M, Sampe R, Kojima S, Baba Y, Usui T, Ueda K, et al. Synthesis of a tetronic acid library focused on inhibitors of tyrosine and dual-specificity protein phosphatases and its evaluation regarding VHR and cdc25B inhibition. J Med Chem 2001; 44: 3216-22.
129. Ducruet AP, Rice RL, Tamura K, Yokokawa F, Yokokawa S, Wipf P, et al. Identification of new Cdc25 dual specificity phosphatase inhibitors in a targeted small molecule array. Bioorg Med Chem 2000; 8: 1451-66.
130. Bhalla US, Ram PT, Iyengar R. MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network. Science 2002; 297: 1018-23.
131. Camps M, Nichols A, Gillieron C, Antonsson B, Muda M, Chabert C, et al. Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase. Science 1998; 280: 1262-5.
132. Farooq A, Plotnikova O, Chaturvedi G, Yan S, Zeng L, Zhang Q, et al. Solution Structure of the MAPK Phosphatase PAC-1 Catalytic Domain. Insights into Substrate-Induced Enzymatic Activation of MKP. Structure (Camb) 2003; 11: 155-64.
133. Furukawa T, Sunamura M, Motoi F, Matsuno S, Horii A. Potential tumor suppressive pathway involving DUSP6/MKP-3 in pancreatic cancer. Am J Pathol 2003; 162: 1807-15.
134. Wang Z, Southwick EC, Wang M, Kar S, Rosi KS, Wilcox CS, et al. Involvement of Cdc25A phosphatase in Hep3B hepatoma cell growth inhibition induced by novel K vitamin analogs. Cancer Res 2001; 61: 7211-6.
135. Bang YJ, Kwon JH, Kang SH, Kim JW, Yang YC. Increased MAPK activity and MKP-1 overexpression in human gastric adenocarcinoma. Biochem Biophys Res Commun 1998; 250: 43-7.
136. Yokoyama A, Karasaki H, Urushibara N, Nomoto K, Imai Y, Nakamura K, et al. The characteristic gene expressions of MAPK phosphatases 1 and 2 in hepatocarcinogenesis, rat ascites hepatoma cells, and regenerating rat liver. Biochem Biophys Res Commun 1997; 239: 746-51.
137. Laderoute KR, Mendonca HL, Calaoagan JM, Knapp AM, Giaccia AJ, Stork PJ. Mitogen-activated protein kinase phosphatase-1 (MKP-1) expression is induced by low oxygen conditions found in solid tumor microenvironments. A candidate MKP for the inactivation of hypoxia-inducible stress-activated protein kinase/c-Jun N-terminal protein kinase activity. J Biol Chem 1999; 274: 12890-7.
138. Goo YL, Kang B, Williamson JR. Inhibition of the expression of mitogen-activated protein phosphatase-1 potentiates apoptosis induced by tumor necrosis factor-alpha in rat mesangial cells. J Biol Chem 1998; 273: 10362-6.
139. Kawanaka H, Tomikawa M, Baatar D, Jones MK, Pai R, Szabo IL, et al. Despite activation of EGF-receptor-ERK signaling pathway, epithelial proliferation is impaired in portal hypertensive gastric mucosa: Relevance of MKP-1, c-fos, c-myc, and cyclin D1 expression. Life Sci 2001; 69: 3019-33.
140. Dorfman, K, Carrasco D, Gruda M, Ryan C, Lira SA, Bravo R. Disruption of the erp/mkp-1 gene does not affect mouse development: normal MAP kinase activity in ERP/MKP-1-deficient fibroblasts. Oncogene 1996; 13: 925-31.
141. Hutter D, Chen P, Li J, Barnes J, Liu Y. The carboxyl-terminal domains of MKP-1 and MKP-2 have inhibitory effects on their phosphatase activity. Mol Cell Biochem 2002; 233: 107-17.
142. Chu Y, Solski, PA, Khosravi-Far R, Der CJ, Kelly K. The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation. J Biol Chem 1996; 271: 6497-501.
143. Dwivedi Y, Rizavi HS, Roberts RC, Conley RC, Tamminga CA. Pandey GN. Reduced activation and expression of ERK 1/2 MAP kinase in the post-mortem brain of depressed suicide subjects. J Neurochem 2001; 77: 916-28.
144. Xu H, Dembski M, Yang Q, Yang D, Moriarty A, Tayber O, et al. Dual specificity mitogen-activated protein (MAP) kinase phosphatase-4 plays a potential role in insulin resistance. J Biol Chem 2003; 278: 30187-92.
145. Xu LG, Wu M, Hu J, Zhai Z, Shu HB. Identification of downstream genes up-regulated by the tumor necrosis factor family member TALL-1. J Leukoc Biol 2002; 72: 410-6.
146. Lee SW, Reimer CL, Fang L, Iruela-Arispe ML, Aaronson SA. Overexpression of kinase-associated phosphatase (KAP) in breast and prostate cancer and inhibition of the transformed phenotype by antisense KAP expression. Mol Cell Biol 2000; 20: 1723-32.
147. Shen Y, Luche R, Wei B, Gordon ML, Diltz CD, Tonks NK. Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1. Proc Natl Acad Sci USA 2001; 98: 13613-8.
148. Najarro P, Traktman P, Lewis JA. Vaccinia virus blocks gamma interferon signal transduction: Viral VH1 phosphatase reverses Stat1 activation. J Virol 2001; 75: 3185-96.
149. Liu K, Lemon B, Traktman P. The dual-specificity phosphatase encoded by vaccinia virus, VH1 is essential for viral transcription in vivo and in vitro. J Virol 1995; 69: 7823-34.
150. Hakes DJ, Martell KJ, Zhao WG, Massung RF, Esposito JJ, Dixon JE. A protein phosphatase related to the vaccinia virus VH1 is encoded in the genomes of several orthopoxviruses and a baculovirus. Proc Natl Acad Sci USA 1993; 90: 4017-21.
151. Cheng S, Clancy CJ, Checkley MA, Handfield M, Hillman JD, Progulske-Fox, A, et al. Identification of Candida albicans genes induced during thrush offers insight into pathogenesis. Mol Microbiol 2003; 48: 1275-88.
152. Csank C, Makris C, Meloche S, Schroppel K, Rollinghoff M, Dignard D, et al. Derepressed hyphal growth and reduced virulence in a VH1 family-related protein phosphatase mutant of the human pathogen Candida albicans. Mol Biol Cell 1997; 8: 2539-51.
153. Lyon MA, Ducruet AP, Wipf P, Lazo JS. Dual-specificity phosphatases as targets for antineoplastic agents. Nat Rev Drug Discov 2002; 1: 961-76.
154. Fauman EB, Cogswell JP, Lovejoy B, Rocque WJ, Holmes W, Montana VG, et al. Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A. Cell 1998; 93: 617-25.
155. Rudolph J. Catalytic mechanism of Cdc25. Biochemistry 2002; 41: 14613-23.
156. Zou X, Tsutsui T, Ray D, Blomquist JF, Ichijo H, Ucker DS, et al. The cell cycle-regulatory CDC25A phosphatase inhibits apoptosis signal-regulating kinase 1. Mol Cell Biol 2001; 21: 4818-28.
157. Horiguchi T, Nishi K, Hakoda S, Tanida S, Nagata A, Okayama H. Dnacin A1 and dnacin B1 are antitumor antibiotics that inhibit cdc25B phosphatase activity. Biochem Pharmacol 1994; 48: 2139-41.
158. Bergnes G, Gilliam CL, Boisclair MD, Blanchard JL, Blake KV, Epstein DM, et al. Generation of an Ugi library of phosphate mimic-containing compounds and identification of novel dual specific phosphatase inhibitors. Bioorg Med Chem Lett 1999; 9: 2849-54.
159. Lazo JS, Aslan DC, Southwick EC, Cooley KA, Ducruet AP, Joo B, et al. Discovery and biological evaluation of a new family of potent inhibitors of the dual specificity protein phosphatase Cdc25. J Med Chem 2001; 44: 4042-9.
160. Pu L, Amoscato AA, Bier ME, Lazo JS. Dual G1 and G2 phase inhibition by a novel, selective Cdc25 inhibitor 6-chloro-7-[corrected](2-morpholin-4-ylethylamino)-quinoline-5,8-dione. J Biol Chem 2002; 277: 46877-85.
161. Sohn J, Kiburz B, Li Z, Deng L., Safi A, Pirrung MC, et al. Inhibition of Cdc25 phosphatases by indolyldihydroxyquinones. J Med Chem 2003; 46: 2580-8.
162. Ham SW, Park J, Lee SJ, Kim W, Kang K, Choi KH. Naphthoquinone analogs as inactivators of cdc25 phosphatase. Bioorg Med Chem Lett 1998; 8: 2507-10.
163. Tamura K, Southwick EC, Kerns J, Rosi K, Carr BI, Wilcox C, et al. Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue. Cancer Res 2000; 60: 1317-25.
164. Myers MP, Tonks NK. PTEN: Sometimes taking it off can be better than putting it on. Am J Hum Genet 1997; 61: 1234-8.
165. Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, et al. Crystal structure of the PTEN tumor suppressor: Implications for its phosphoinositide phosphatase activity and membrane association. Cell 1999; 99: 323-34.
166. Li J, Yen C, Liaw D, Podsypanina K, Bose S, Wang SI, et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 1997; 275: 1943-7.
167. Liaw D, Marsh DJ, Li J, Dahia PL, Wang SI, Zheng Z, et al. Germline mutations of the PTEN gene in Cowden disease, an inherited breast and thyroid cancer syndrome. Nat Genet 1997; 16: 64-7.
168. Nelen MR, van Staveren WC, Peeters EA, Hassel MB, Gorlin RJ, Hamm H, et al. Germline mutations in the PTEN/MMAC1 gene in patients with Cowden disease. Hum Mol Genet 1997; 6: 1383-7.
169. Furnari FB, Huang HJ, Cavenee WK. The phosphoinositol phosphatase activity of PTEN mediates a serum-sensitive G1 growth arrest in glioma cells. Cancer Res 1998; 58: 5002-8.
170. Jiang G, Zhang BB. Pi 3-kinase and its up- and down-stream modulators as potential targets for the treatment of type II diabetes. Front Biosci 2002; 7: D903-7.
171. Butler M, McKay RA, Popoff, IJ, Gaarde WA, Witchell D, Murray SF, et al. Specific inhibition of PTEN expression reverses hyperglycemia in diabetic mice. Diabetes 2002; 51: 1028-34.
172. Walker SM, Downes CP, Leslie NR. TPIP: A novel phosphoinositide 3-phosphatase. Biochem J 2001: 360: 277-83.
173. Taylor V, Wong M, Brandts C, Reilly L, Dean NM, Cowsert LM, et al. 5′ phospholipid phosphatase SHIP-2 causes protein kinase B inactivation and cell cycle arrest in glioblastoma cells. Mol Cell Biol 2000; 20: 6860-71.
174. Blondeau F, Laporte J, Bodin S, Superti-Furga G, Payrastre B, Mandel JL. Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway. Hum Mol Genet 2000; 9: 2223-9.
175. Zhao R, Qi Y, Chen J, Zhao ZJ. FYVE-DSP2, a FYVE domain-containing dual specificity protein phosphatase that dephosphorylates phosphotidylinositol 3-phosphate. Exp Cell Res 2001; 265: 329-38.
176. Walker DM, Urbe S, Dove SK, Tenza D, Raposo G, Clague MJ. Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity. Curr Biol 2001; 11: 1600-5.
177. Berger P, Bonneick S, Willi S, Wymann M, Suter U. Loss of phosphatase activity in myotubularin-related protein 2 is associated with Charcot-Marie-Tooth disease type 4B1. Hum Mol Genet 2002; 11: 1569-79.
178. Laporte J, Hu LJ, Kretz C, Mandel JL, Kioschis P, Coy JF, et al. A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast. Nat Genet 1996; 13: 175-82.
179. Laporte J, Biancalana V, Tanner SM, Kress W, Schneider V, Wallgren-Pettersson C, et al. MTM1 mutations in X-linked myotubular myopathy. Hum Mutat 2000; 15: 393-409.
180. Bolino A, Muglia M, Conforti FL, LeGuern E, Salih MA, Georgiou DM, et al. Charcot-Marie-Tooth type 4B is caused by mutations in the gene encoding myotubularin-related protein-2. Nat Genet 2000; 25: 17-9.
181. Houlden H, King RH, Wood NW, Thomas PK, Reilly MM. Mutations in the 5′ region of the myotubularin-related protein 2 (MTMR2) gene in autosomal recessive hereditary neuropathy with focally folded myelin. Brain 2001; 124: 907-15.
182. Gray CH, Good VM, Tonks NK, Barford D. The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase. EMBO Journal 2003; 22: 3524-35.
183. Li L, Ernsting BR, Wishart MJ, Lohse DL, Dixon JE. A family of Putative tumor suppressors is structurally and functionally conserved in humans and yeast. J Biol Chem 1997; 272: 29403-29406.
184. Mailand N, Lukas C, Kaiser BK, Jackson PK, Bartek J, Lukas J. Deregulated human Cdc14A phosphatase disrupts centrosome separation and chromosome segregation. Nat Cell Biol 2002; 4: 317-322.
185. Bembenek J, Yu H. Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a. J Biol Chem 2001; 276: 48237-48242.
186. Kaiser BK, Zimmerman ZA, Charbonneau H, Jackson PK. Disruption of centrosome structure, chromosome segregation, and cytokinesis by misexpression of human Cdc14A phosphatase. Mol Biol Cell 2002; 13: 2289-2300.
187. Li L, Ljungman M, Dixon JE. The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53. J Biol Chem 2000; 275: 2410-4.
188. Stern BM. FEARless in meiosis. Mol Cell 2003; 11: 1123-1125.
189. Zeng Q, Dong JM, Goo K, Li J, Tan HX, Koh V, et al. PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. Cancer Res 2003; 63: 2716-22.
190. Zeng Q, Si X, Horstmann H, Xu Y, Hong W, Pallen CJ. Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. J Biol Chem 2000; 275: 21444-52.
191. Zhou, H., Gallina, M., Mao, H., Nietlispach, D., Betz, S.F., Fetrow, J.S., et al. Letter to the Editor: 1H, 13C and 15N resonance assignments and secondary structure of the human protein tyrosine phosphatase, PRL-2. Journal of Biomolecular NMR 2003; forthcoming.
192. Kozlov G, Cheng J, Lievre C, Banville D, Gehring K, Ekiel I. 1H, 13C and 15N resonance assignments of the human phosphatase PRL-3. J Biomol NMR 2002; 24: 169-70.
193. Cates CA, Michael RL, Stayrook KR, Harvey KA, Burke YD, Randall SK, et al. Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases. Cancer Lett 1996; 110: 49-55.
194. Saha S, Bardelli A, Buckhaults P, Velculescu VE, Rago C, St Croix B, et al. A phosphatase associated with metastasis of colorectal cancer. Science 2001; 294: 1343-6.
195. Fuchs KR, Shekels LL, Bernlohr DA. Analysis of the ACP1 gene product: Classification as an FMN phosphatase. Biochem Biophys Res Commun 1992; 189: 1598-605.
196. Greene LS, Bottini N, Borgiani P, Gloria-Bottini F. Acid phosphatase locus 1 (ACP1): Possible relationship of allelic variation to body size and human population adaptation to thermal stress-A theoretical perspective. Am J Human Biol 2000; 12: 688-701.
197. Mansfield, E.Sensabaugh, G.F. Red cell acid phosphatase: modulation of activity by purines. Prog Clin Biol Res 1978; 21: 233-49.
198. McGovern, S.L.Shoichet, B.K. Kinase inhibitors: Not just for kinases anymore. J Med Chem 2003; 46: 1478-83.
199. Ryan AJ, Gray NM, Lowe PN, Chung CW. Effect of detergent on "pRomiIcuous" inhibitors. J Med Chem 2003; 46: 3448-51.
200. Goldstein BM, Colby TD. IMP dehydrogenase: Structural aspects of inhibitor binding. Curr Med Chem 1999; 6: 519-36.
201. Velazquez-Campoy A, Freire E. Incorporating target heterogeneity in drug design. J Cell Biochem Suppl 2001; Suppl 37: 82-8.
202. Monfardini C, Canziani G, Plugariui C, Kieber-Emmons T, Godillot AP, Kwah J, et al. Structure-based design of mimetics for granulocyte-macrophage colony stimulating factor (GM-CSF). Curr Pharm Design 2002; 8(24): 2185-99.
203. Wagman AS, Nuss JM. Current therapies and emerging targets for the treatment of diabetes. Curr Pharm Design 2001; 7(6): 417-50.
204. Woolfrey JR, Weston GS. The use of computational methods in the discovery and design of kinase inhibitors. Curr Pharm Design 2002; 8(17): 1527-45.