Abdel-Rahman HM, Al-karamany GS, et al (2002) HIV protease inhibitors: pep-

tidomimetic drugs and future perspectives. Curr Med Chem 9:1905-22 Adams JA, Taylor SS (1992) Energetic limits of phosphotransfer in the catalytic subunit of cAMP-dependent protein kinase as measured by viscosity experiments. Biochemistry 31:8516-22

Alfaro-Lopez J, Yuan W, et al (1998) Discovery of a novel series of potent and selective substrate-based inhibitors of p60c-src protein tyrosine kinase: conformational and topographical constraints in peptide design. J Med Chem 41:2252-60 Ando S, Tsujimura K, et al (1993) Phosphorylation of synthetic vimentin peptides by cdc2 kinase. Biochem Biophys Res Commun 195:837-43 Ando S, Ikuhara T, et al (1997) Role of the pyrrolidine ring of proline in determining the substrate specificity of cdc2 kinase or cdk5. J Biochem [Tokyo] 122:409-14 Beaulieu PL, Cameron DR, et al (1999) Ligands for the tyrosine kinase p56lck SH2 domain: discovery of potent dipeptide derivatives with monocharged, nonhydrolyzable phosphate replacements. J Med Chem 42:1757-66 Bohacek RS, Dalgarno DC, et al (2001) X-Ray structure of citrate bound to Src SH2 leads to a high-affinity, bone-targeted Src SH2 inhibitor. J Med Chem 44:660-3 Burke TR Jr, Smyth MS, et al (1993) Preparation of fluoro-4-(phosphonomethyl)-D,L-phenylalanine and hydroxy-4-(phosphonomethyl)-D,L-phenylalanine suitably protected for solid phase synthesis of peptides containing hydrolytically stable analogues of O-phosphotyrosine. J Org Chem 58:1336-40

Burke TR Jr, Smyth MS, et al (1994) Nonhydrolyzable phosphotyrosyl mimetics for the preparation of phosphatase-resistant SH2 domain inhibitors. Biochemistry 33:6490-4 Burke TR Jr, Luo J, et al (1999) Monocarboxylic-based phosphotyrosyl mimetics in the design of GRB2 SH2 domain inhibitors. Bioorg Med Chem Lett 9:347-52 Burke TR Jr, Yao ZJ, et al (2001) Phosphoryltyrosyl mimetics in the design of peptide-

based signal transduction inhibitors. Biopolymers 60:32-44 Burke TR Jr, Lee K (2003) Phosphotyrosyl mimetics in the development of signal transduction inhibitors. Acc Chem Res 36:426-33 Burkoth TS, Fafarman AT, et al (2003) Incorporation of unprotected heterocyclic side chains into peptoid oligomers via solid-phase submonomer synthesis. J Am Chem Soc 125:8841-5

Case RD, Piccione E, et al (1994) SH-PTP2/Syp SH2 domain binding specificity is defined by direct interactions with platelet-derived growth factor beta-receptor, epidermal growth factor receptor, and insulin receptor substrate-1-derived phosphopeptides. J Biol Chem 269:10467-74 Cheng HC, Kemp BE, et al (1986) A potent synthetic peptide inhibitor of the cAMP-dependent protein kinase. J Biol Chem 261:989-92 Cole PA, Grace MR, et al (1995) The role of the catalytic base in the protein tyrosine kinase Csk. J Biol Chem 270:22105-8 Combs AP, Kapoor TM, et al (1996) Protein structure-based combinatorial chemistry: discovery of non-peptide binding elements to Src SH3 domain. J Am Chem Soc 118:287-8

Cowburn D, Zheng J, et al (1995) Enhanced affinities and specificities of consolidated lig-ands for the Src homology (SH) 3 and SH2 domains of Abelson protein-tyrosine ki-nase. J Biol Chem 270:26738-41 Csukai M, Mochly-Rosen D (1999) Pharmacologic modulation of protein kinase C isozymes: the role of RACKs and subcellular localisation. Pharmacol Res 39:253-9 Cussac D, Vidal M, et al (1999) A Sos-derived peptidimer blocks the Ras signaling pathway by binding both Grb2 SH3 domains and displays antiproliferative activity. FASEB J 13:31-8

Dhanasekaran N, Premkumar Reddy E (1998) Signaling by dual specificity kinases. Oncogene 17:1447-55

Dostmann WR, Taylor MS, et al (2000) Highly specific, membrane-permeant peptide blockers of cGMP-dependent protein kinase Ialpha inhibit NO-induced cerebral dilation. Proc Natl Acad Sci U S A 97:14772-7 Figliozzi GM, Goldsmith R, et al (1996) Synthesis of N-substituted glycine peptoid libraries. Methods Enzymol 267:437-47 Frank R (2002) The SPOT-synthesis technique. Synthetic peptide arrays on membrane supports—principles and applications. J Immunol Methods 267:13-26 Fry DW, McMichael A, et al (1994) Design of a potent peptide inhibitor of the epidermal growth factor receptor tyrosine kinase utilizing sequences based on the natural phos-phorylation sites of phospholipase C-gamma 1. Peptides 15:951-7 Gao Y, Wu L, et al (2000) Examination of novel non-phosphorus-containing phosphotyrosyl mimetics against protein-tyrosine phosphatase-1B and demonstration of differential affinities toward Grb2 SH2 domains. Bioorg Med Chem Lett 10:923-7 Gilmer T, Rodriguez M, et al (1994) Peptide inhibitors of src SH3-SH2-phosphoprotein interactions. J Biol Chem 269:31711-9 Glass DB, Cheng HC, et al (1989) Primary structural determinants essential for potent inhibition of cAMP-dependent protein kinase by inhibitory peptides corresponding to the active portion of the heat-stable inhibitor protein. J Biol Chem 264:8802-10

Glass DB, Lundquist LJ, et al (1989) Protein kinase inhibitor-(6-22)-amide peptide analogs with standard and nonstandard amino acid substitutions for phenylalanine 10. Inhibition of cAMP-dependent protein kinase. J Biol Chem 264:14579-84 Granier C (2002) Special issue on methods of parallel peptide synthesis and their contributions to deciphering molecular interactions in the immune system. J Immunol Methods 267:1-2

Houghten RA, Blondelle SE, et al (1996) Libraries from libraries: generation and comparison of screening profiles. Mol Divers 2:41-5 Houseman BT, Huh JH, et al (2002) Peptide chips for the quantitative evaluation of protein kinase activity. Nat Biotechnol 20:270-4 Huse M, Kuriyan J (2002) The conformational plasticity of protein kinases. Cell 109:27582

Johnson LN, Lowe ED, et al (1998) The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases. FEBS Lett 430:1-11 Kaiser ET, Mihara H, et al (1989) Peptide and protein synthesis by segment synthesis-

condensation. Science 243:187-92 Kapoor TM, Andreotti AH, et al (1998) Exploring the specificity pockets of two homologous SH3 domains using structure-based, split-pool synthesis and affinity-based selection. J Am Chem Soc 120:23-9 Kim K, Cole PA (1998) Kinetic analysis of a protein tyrosine kinase reaction transition state in the forward and the reverse directions. J Am Chem Soc 120:6851-8 Kole HK, Akamatsu M, et al (1995) Protein-tyrosine phosphatase inhibition by a peptide containing the phosphotyrosyl mimetic, L-O-malonyltyrosine. Biochem Biophys Res Commun 209:817-22

Lam KS, Wu J, et al (1995) Identification and characterization of a novel synthetic pep-tide substrate specific for Src-family protein tyrosine kinases. Int J Pept Protein Res 45:587-92

Lam KS, Liu R, et al (2003) Applications of one-bead one-compound combinatorial libraries and chemical microarrays in signal transduction research. Acc Chem Res 36:370-7

Lashmet PR, Tang K-C, et al (1983) The synthesis of an ATP-gamma-peptidyl ester as a potential probe of c-AMP-dependent protein kinase. Tetrahedron Lett 24:1121-4 Lee TR, Lawrence DS (1999) Acquisition of high-affinity, SH2-targeted ligands via a spatially focused library. J Med Chem 42:784-7 Lee TR, Lawrence DS (2000) SH2-directed ligands of the Lck tyrosine kinase. J Med Chem 43:1173-9

Lee TR, Niu J, et al (1994) Phenol kinase activity of the serine/threonine-specific cAMP-

dependent protein kinase: steric and electronic effects. Biochemistry 33:4245-4250 Lee TR, Niu J, et al (1995a) The extraordinary active site substrate specificity of pp60c-

src. A multiple specificity protein kinase. J Biol Chem 270:5375-80 Lee TR, Till JH, et al (1995b) Precision substrate targeting of protein kinases v-Abl and c-Src. J Biol Chem 270:27022-6 Lee JH, Nandy SK, et al (2004) A highly potent and selective PKCalpha inhibitor generated via combinatorial modification of a peptide scaffold. J Am Chem Soc 126:3394-5 Loog M, Uri A, et al (1999) Adenosine-5'-carboxylic acid peptidyl derivatives as inhibitors of protein kinases. Bioorg Med Chem Lett 9:1447-52 Loog M, Uri A, et al (2000) Bi-substrate analogue ligands for affinity chromatography of protein kinases. FEBS Lett 480:244-8 Lou Q, Leftwich ME, et al (1997) Potent pseudosubstrate-based peptide inhibitors for p60(c-src) protein tyrosine kinase. Cancer Res 57:1877-81

Lukas TJ, Mirzoeva S, et al (1999) Identification of novel classes of protein kinase inhibitors using combinatorial peptide chemistry based on functional genomics knowledge. J Med Chem 42:910-9 Marin O, Meggio F, et al (1999) Tyrosine versus serine/threonine phosphorylation by protein kinase casein kinase-2. A study with peptide substrates derived from im-munophilin Fpr3. J Biol Chem 274:29260-5 McMurray JS, Budde RJ, et al (1998) Cyclic peptides as probes of the substrate binding site of the cytosolic tyrosine kinase, pp60c-src. Arch Biochem Biophys 355:124-30 Medzihradszky D, Chen SL, et al (1994) Solid-phase synthesis of adenosine phosphopep-tides as potential bisubstrate inhibitors of protein kinases. J Am Chem Soc 116:94139

Mitchell RD, Glass DB, et al (1995) Heat-stable inhibitor protein derived peptide substrate analogs: phosphorylation by cAMP-dependent and cGMP-dependent protein kinases. Biochemistry 34:528-34 Morken JP, Kapoor TM, et al (1998) Exploring the leucine-proline binding pocket of the Src SH3 domain using structure-based, split-pool synthesis and affinity selection. J Am Chem Soc 120:30-6 Nguyen JT, Turck CW, et al (1998) Exploiting the basis of proline recognition by SH3 and

WW domains: design of N-substituted inhibitors. Science 282:2088-92 Nguyen JT, Porter M, et al (2000) Improving SH3 domain ligand selectivity using a non-

natural scaffold. Chem Biol 7:463-73 Niu J, Lawrence DS (1997a) L-dopa: a potent nonphosphorylatable tyrosine mimetic for pp60c-src. J Am Chem Soc 119:3844-5 Niu J, Lawrence DS (1997b) Nonphosphorylatable tyrosine surrogates. Implications for protein kinase inhibitor design. J Biol Chem 272:1493-9 O'Brian CA, Ward NE, et al (1990) N-myristyl-Lys-Arg-Thr-Leu-Arg: a novel protein ki-

nase C inhibitor. Biochem Pharmacol 39:49-57 O'Brian CA, Ward NE, et al (1991) A novel N-myristylated synthetic octapeptide inhibits protein kinase C activity and partially reverses murine fibrosarcoma cell resistance to adriamycin. Invest New Drugs 9:169-79 Olivos HJ, Alluri PG, et al (2002) Microwave-assisted solid-phase synthesis of peptoids. Org Lett 4:4057-9

Parang K, Till JH, et al (2001) Mechanism-based design of a protein kinase inhibitor. Nat Struct Biol 8:37-41

Pellicena P, Stowell KR, et al (1998) Enhanced phosphorylation of Src family kinase substrates containing SH2 domain binding sites. J Biol Chem 273:15325-8 Pinna LA, Ruzzene M (1996) How do protein kinases recognize their substrates? Biochim

Biophys Acta 1314:191-225 Pluskey S, Wandless TJ, et al (1995) Potent stimulation of SH-PTP2 phosphatase activity by simultaneous occupancy of both SH2 domains. J Biol Chem 270:2897-900 Profit AA, Lee TR, et al (1999) Bivalent inhibitors of protein tyrosine kinases. J Am Chem Soc 121:280-3

Profit AA, Lee TR, et al (2001) Molecular rulers: an assessment of distance and spatial relationships of Src tyrosine kinase Sh2 and active site regions. J Biol Chem 276:9446-51

Puius YA, Zhao Y, et al (1997) Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design. Proc Natl Acad Sci USA 94:13420-5

Ramdas L, Obeyesekere NU, et al (1999) N-myristoylation of a peptide substrate for Src converts it into an apparent slow-binding bisubstrate-type inhibitor. J Pept Res 53:569-77

Ricouart A, Gesquiere JC, et al (1991) Design of potent protein kinase inhibitors using the bisubstrate approach. J Med Chem 34:73-8 Ross H, Armstrong CG, et al (2002) A non-radioactive method for the assay of many ser-

ine/threonine-specific protein kinases. Biochem J 366:977-81 Sasaki S, Hashimoto T, et al (1998) Design of new inhibitors for cdc2 kinase based on a multiple pseudosubstrate structure. Bioorg Med Chem Lett 8:1019-22 Scott JD, Fischer EH, et al (1985a) Identification of an inhibitory region of the heat-stable protein inhibitor of the cAMP-dependent protein kinase. Proc Natl Acad Sci USA 82:4379-83

Scott JD, Fischer EH, et al (1985b) Amino acid sequence of the heat-stable inhibitor of the cAMP-dependent protein kinase from rabbit skeletal muscle. Proc Natl Acad Sci USA 82:5732-6

Scott JD, Glaccum MB, et al (1986) Primary-structure requirements for inhibition by the heat-stable inhibitor of the cAMP-dependent protein kinase. Proc Natl Acad Sci USA 83:1613-6

Scott JK, Smith GP (1990) Searching for peptide ligands with an epitope library. Science 249:386-90

Shen K, Keng YF, et al (2001) Acquisition of a specific and potent PTP1B inhibitor from a novel combinatorial library and screening procedure. J Biol Chem 276:47311-47319 Shoelson SE, White MF, et al (1989) Nonphosphorylatable substrate analogs selectively block autophosphorylation and activation of the insulin receptor, epidermal growth factor receptor, and pp60v-src kinases. J Biol Chem 264:7831-6 Smith GP, Scott JK (1993) Libraries of peptides and proteins displayed on filamentous phage. Methods Enzymol 217:228-57 Smothers JF, Henikoff S, et al (2002) Tech.Sight. Phage display. Affinity selection from biological libraries. Science 298:621-2 Smyth MS, Ford H, et al (1992) A general method for the preparation of benzylic alpha, alpha-difluorophosphonic acids; non-hydrolyzable mimetics of phosphotyrosine. Tetrahedron Lett 33:4137-40 Songyang Z, Shoelson SE, et al (1993) SH2 domains recognize specific phosphopeptide sequences. Cell 72:767-78 Songyang Z, Blechner S, et al (1994) Use of an oriented peptide library to determine the optimal substrates of protein kinases. Curr Biol 4:973-82 Songyang Z, Cantley LC (1998) The use of peptide library for the determination of kinase peptide substrates. Methods Mol Biol 87:87-98 Stankovic CJ, Surendranc N, et al (1997) The role of 4-phosphonodifluoromethyl- and 4-phosphonon-phenylalanine in the selectivity and cellular uptake of SH2 domain ligands. Bioorg Med Chem Lett 7:1909-14 Stanyon CA, Bernard O (1999) LIM-kinase1. Int J Biochem Cell Biol 31:389-94 Sugimoto S, Wandless TJ, et al (1994) Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1. J Biol Chem 269:13614-22 Tong L, Warren TC, et al (1996) Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution. J Mol Biol 256:601-10

Tong L, Warren TC, et al (1998) Carboxymethyl-phenylalanine as a replacement for phos-photyrosine in SH2 domain binding. J Biol Chem 273:20238-42

Uri A, Raidaru G, et al (2002) Identification of the ability of highly charged nanomolar inhibitors of protein kinases to cross plasma membranes and carry a protein into cells. Bioorg Med Chem Lett 12:2117-20 Van Patten SM, Fletcher WH, et al (1986) The inhibitor protein of the cAMP-dependent protein kinase-catalytic subunit interaction. Parameters of complex formation. J Biol Chem 261:5514-23

Viht K, Padari K, et al (2003) Liquid-phase synthesis of a pegylated adenosine-oligoargi-nine conjugate, cell-permeable inhibitor of cAMP-dependent protein kinase. Bioorg Med Chem Lett 13:3035-9 Wang W, Ramdas L, et al (2000) Cyclic peptides incorporating 4-carboxyphenylalanine and phosphotyrosine are potent inhibitors of pp60(c-)(src). Biochemistry 39:5221-8 Ward NE, O'Brian AA (1993) Inhibition of protein kinase C by N-myristoylated peptide substrate analogs. Biochemistry 32:11903-9 Whitehouse S, Walsh DA (1983) Mg X ATP2-dependent interaction of the inhibitor protein of the cAMP-dependent protein kinase with the catalytic subunit. J Biol Chem 258:3682-92

Whitehouse S, Feramisco JR, et al (1983) Studies on the kinetic mechanism of the catalytic subunit of the cAMP-dependent protein kinase. J Biol Chem 258:3693-701 Wong TW, Goldberg AR (1984) Kinetics and mechanism of angiotensin phosphorylation by the transforming gene product of Rous sarcoma virus. J Biol Chem 259:3127-31 Wood J, Koszelak M, et al (1998) A caged protein kinase inhibitor. J Am Chem Soc 120:7145-7146

Wood JS, Yan X, et al (1996) Precision substrate targeting of protein kinases. The cGMP-

and cAMP-dependent protein kinases. J Biol Chem 271:174-9 Wu J, Ma QN, et al (1994) Identifying substrate motifs of protein kinases by a random library approach. Biochemistry 33:14825-33 Wu J, Phan H, et al (1996) Development of a selective pseudosubstrate-based peptide inhibitor of p60c-src. Lett Pept Sci 3:309-16 Xu Q, Zheng J, et al (1999) Flexibility of interdomain contacts revealed by topological isomers of bivalent consolidated ligands to the dual Src homology domain SH(32) of abelson. Biochemistry 38:3491-7 Yan X, Curley K, et al (2000) The specificity of the protein kinase C alpha, betaII and gamma isoforms as assessed by an unnatural alcohol-appended peptide library. Bio-chem J 349 Pt 3:709-15 Ye B, Akamatsu M, et al (1995) L-O-(2-malonyl)tyrosine: a new phosphotyrosyl mimetic for the preparation of Src homology 2 domain inhibitory peptides. J Med Chem 38:4270-5

Yeh RH, Lee TR, et al (2001) From consensus sequence peptide to high affinity ligand, a library scan strategy. J Biol Chem 276:12235-40 Yuan CJ, Jakes S, et al (1990) A rationale for the design of an inhibitor of tyrosyl kinase.

J Biol Chem 265:16205-9 Zaliani A, Pinori M, et al (1998) The interaction of myristylated peptides with the catalytic domain of protein kinase C revealed by their sequence palindromy and the identification of a myristyl binding site. Protein Eng 11:803-10 Zhu H, Klemic JF, et al (2000) Analysis of yeast protein kinases using protein chips. Nat Genet 26:283-9

Part II

Pharmacological Potential and Inhibitors of Individual Classes of Protein Kinases

HEP (2005) 167:47-64 © Springer-Verlag 2005

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