Chemical Probes of Protein Prenylation

Enzymes

Volumn 30, Issue , 2011, Pages 91-127

  Placzek, Andrew T ^a,b   Krzysiak, Amanda J ^a,c   Gibbs, Richard A ^a  

^a PURDUE UNIVERSITY   (United States)

^b OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

^c BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

Farnesyltransferase inhibitors; Isoprenoid synthetic methods; Prenyl analogs; Prenyl proteomics studies; Protein prenylation; Substrate specificity studies

Indexed keywords

EID: 81255162429     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-415922-8.00005-7     Document Type: Chapter

References (149)

1. Caldwell G.A., Naider F., Becker J.M. Fungal lipopeptide mating pheromones: a model system for the study of protein prenylation. Microbiol Rev 1995, 59:406-422.
2. Casey P.J. Protein lipidation in cell signalling. Science 1995, 268:221-225.
3. Reid T.S., Terry K.L., Casey P.J., Beese L.S. Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J Mol Biol 2004, 343:417-433.
4. Lane K.T., Beese L.S. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. J Lipid Res 2006, 47:681-699.
5. Reiss Y., Goldstein J.L., Sebra M.C., Casey P.J., Brown M.S. Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides. Cell 1990, 62:81-88.
6. Reiss Y., Seabra M.C., Goldstein J.L., Brown M.S. Purification of ras farnesyl:protein transferase. Comp Methods Enzymol 1990, 1:241-245.
7. Schaber M.D., et al. Polyisoprenylation of Ras in vitro by a farnesyl-protein transferase. J Biol Chem 1990, 265:14701-14704.
8. ras farnesyltransferase, the counterpart of yeast DPR1/RAM1. Cell 1991, 66:327-334.
9. Kohl N.E., et al. Structural homology among mammalian and Saccharomyces cerevisiae isoprenyl-protein transferases. J Biol Chem 1991, 266:18884-18888.
10. Omer C.A., et al. Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. Biochemistry 1993, 32:5167-5176.
11. Goodman L.E., Perou C.M., Fujiyama A., Tamanoi F. Structure and expression of yeast DPR1, a gene essential for the processing and intracellular localization of ras proteins. Yeast 1988, 4:271-281.
12. Harris C.M., Poulter C.D. Recent studies of the mechanism of protein prenylation. Nat Prod Rep 2000, 17:137-144.
13. Casey P.J., Seabra M.C. Protein prenyltransferases. J Biol Chem 1996, 271:5289-5292.
14. Zhang F.L., et al. cDNA cloning and expression of Rat and human protein geranylgeranyltransferase type-I. J Biol Chem 1994, 269:3175-3180.
15. Moores S.L., et al. Sequence dependence of protein isoprenylation. J Biol Chem 1991, 266:14603-14610.
16. Armstrong S.A., Hannah V.C., Goldstein J.L., Brown M.S. CAAX geranylgeranyl transferase transfers farnesyl as efficiently as geranylgeranyl to RhoB. J Biol Chem 1995, 270:7864-7868.
17. Yokoyama K., McGeady P., Gelb M.H. Mammalian protein geranylgeranyltransferase i: substrate specificity, kinetic mechanism, metal requirements, and affinity labeling. Biochemistry 1995, 34:1344-1354.
18. Stirtan W.G., Poulter C.D. Yeast protein geranylgeranyltransferase type I: overproduction, purification, and characterization. Arch Biochem Biophys 1995, 321:182-190.
19. Pfeffer S.R., Dirac-Svejstrup A.B., Soldati T. Rab GDP dissociation inhibitor: putting Rab GTPases in the right placs. J Biol Chem 1995, 270:17057-17059.
20. Seabra M.C., Brown M.S., Goldstein J.L. Science 1993, 259:377-381.
21. Zhang H., Seabra M.C., Deisenhofer J. Crystal structure of Rab geranylgeranyltransferase at 2.0 å resolution. Structure 2000, 8:241-251.
22. Goldstein J.L., Brown M.S. Regulation of the mevalonate pathway. Nature 1990, 343:425-430.
23. Basso A.D., Kirschmeier P.T., Bishop W.R. Farnesyl transferase inhibitors. J Lipid Res 2006, 47:15-31.
24. Poulter C.D., Rilling H.C. The prenyl transfer reaction. Enzymatic and mechanistic studies of the 1'-4 coupling reaction in the terpene biosynthetic pathway. Acc Chem Res 1978, 11:307-313.
25. Zhang D., Poulter C.D. Biosynthesis of non-head-to-tail isoprenoids. Synthesis of 1'-1 and 1'-3 structures by recombinant yeast squalene synthase. J Am Chem Soc 1995, 117:1641-1642.
26. Croteau R. Biosynthesis and catabolism of monoterpenoids. Chem Rev 1987, 87:929-954.
27. Cane D.E. Enzymatic formation of sesquiterpenes. Chem Rev 1990, 90:1089-1103.
28. Abe I., Tomesch J.C., Wattanasin S., Prestwich G.D. Inhibitors of squalene biosynthesis and metabolism. Nat Prod Rep 1994, 11:279-302.
29. Cainelli G., Cardillo G. Some aspects of the stereospecific synthesis of terpenoids by means of isoprene units. Acc Chem Res 1981, 14:89-94.
30. Oh-e T., Miyaura N., Suzuki A. Palladium-catalyzed cross-coupling reaction of organoboron compounds with organic triflates. J Org Chem 1993, 58:2201-2208.
31. Miyaura N., Suzuki A. Palladium-catalyzed cross-coupling reactions of organoboron compounds. Chem Rev 1995, 95:2457-2483.
32. Corey E.J., Shieh W.-C. A simple synthetic process for the elaboration of oligoprenols by stereospecific coupling of Di-, Tri-, or oligoisoprenoid units. Tetrahedron Lett 1992, 33:6435-6438.
33. Corey E.J., Noe M.C., Shieh W.-C. A short and convergent Enantioselective syntheis of (3S)-2,3-oxidosqualene. Tetrahedron Lett 1993, 34:5995-5998.
34. Sum F.W., Weiler L. Stereoselective synthesis of b-substituted a, b-unsaturated esters by dialkylcuprate coupling to the enol phosphate of b-ketoesters. Can J Chem 1979, 57:1431-1441.
35. Gibbs R.A., Krishnan U. A Pd(0)-catalyzed route to 13-methylidenefarnesyl diphosphate. Tetrahedron Lett 1994, 35:2509-2512.
36. Gibbs R.A., Krishnan U., Dolence J.M., Poulter C.D. A stereoselective palladium/copper-catalyzed route to isoprenoids: synthesis and biological evaluation of 13-methylidenefarnesyl diphosphate. J Org Chem 1995, 60:7821-7829.
37. Mu Y.Q., Gibbs R.A. Coupling of isoprenoid triflates with organoboron nucleophiles: synthesis of all-trans-geranylgeraniol. Tetrahedron Lett 1995, 36:5669-5672.
38. Xiao X.-y., Prestwich G.D. 24-Methylidene-2,3-oxidosqualene: a potent mechanism-based inactivator of oxidosqualene cyclase. J Am Chem Soc 1991, 113:9673-9674.
39. Cane D.E., Bryant C. Aristolochene synthase. Mechanism-based inhibition of a terpenoid cyclase. J Am Chem Soc 1994, 116:12063-12064.
40. Mu Y.Q., Gibbs R.A., Eubanks L., Poulter C.D. Cuprate-mediated synthesis and biological evaluation of tert-butyl and cyclopropyl farnesyl diphosphate analogs. J Org Chem 1996, 61:8010-8015.
41. Rawat D.S., Gibbs R.A. Synthesis of 7-substituted farnesyl diphosphate analogues. Org Lett 2002, 4:3027-3030.
42. Rawat D.S., Krzysiak A.J., Gibbs R.A. Synthesis and biochemical evaluation of 3,7-disubstituted farnesyl diphosphate analogs. J Org Chem 2008, 72:1881-1887.
43. Shao Y., Eummer J.T., Gibbs R.A. Stereospecific synthesis and biological evaluation of farnesyl diphosphate isomers. Org Lett 1999, 1:627-630.
44. Subramanian T., Wang Z., Troutman J.M., Andres D.A., Spielmann H.P. Directed library of anilinogeranyl analogues of farnesyl diphosphate via mixed solid- and solution-phase synthesis. Org Lett 2005, 7:2109-2112.
45. Mechelke M.F., Wiemer D.F. Synthesis of farnesol analogues through Cu(I)-mediated displacements of allylic THP ethers by grignard reagents. J Org Chem 1999, 64:4821-4829.
46. Bell I.M. Inhibitors of farnesyltransferase: a rational approach to cancer chemotherapy?. J Med Chem 2004, 47:1869-1878.
47. Gibbs J.B., et al. Selective inhibition of farnesyl-protein transferase blocks Ras processing in vivo. J Biol Chem 1993, 268:7617-7620.
48. Hohl R.J., Lewis K.A., Cermak D.M., Wiemer D.F. Stereochemistry dependent inhibition of RAS farnesylation by farnesyl phosphonic acids. Lipids 1998, 33:39-46.
49. Holstein S.A., Cermak D.M., Wiemer D.F., Lewis K., Hohl R.J. Phosphonate and bisphosphonate analogues of farnesyl pyrophosphate as potential inhibitors of farnesyl protein transferase. Bioorg Med Chem 1998, 6:687-694.
50. Stirtan W.G., Poulter C.D. Yeast protein geranylgeranyltransferase type-i: steady-state kinetics and substrate binding. Biochemistry 1997, 36:4552-4557.
51. Biller S.A., et al. The first potent inhibitor of squalene synthetase: a profound contribution of an ether oxygen to inhibitor-enzyme interaction. J Am Chem Soc 1991, 113:8522-8524.
52. Magnin D.R., et al. 1,1-Bisphosphonate squalene synthase inhibitors: interplay between the isoprenoid subuntit and the diphophate surrogate. J Med Chem 1995, 38:2596-2605.
53. Roelofs A.J., Thompson K., Gordon S., Rogers M.J. Molecular mechanisms of action of bisphosphonates: current status. Clin Cancer Res 2006, 12:6222s-6230s.
54. Varela I., et al. Combined treatment with statins and aminobisphosphonates extends longevity in a mouse model of human premature aging. Nat Med 2008, 14:767-772.
55. Oldfield E. Targeting isoprenoid biosynthesis for drug discovery: bench to bedside. Accounts Chem Res 2010, 43:1216-1226.
56. Zhang Y.H., et al. Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl diphosphate synthase inhibitors: an X-ray and NMR investigation. J Am Chem Soc 2009, 131:5153-5162.
57. Wiemer A.J., Tong H., Swanson K.M., Hohl R.J. Digeranyl bisphosphonate inhibits geranylgeranyl pyrophosphate synthase. Biochem Biophys Res Commun 2007, 353:921-925.
58. Wiemer A.J., et al. Pivaloyloxymethyl-modified isoprenoid bisphosphonates display enhanced inhibition of cellular geranylgeranylation. Bioorg Med Chem 2008, 16:3652-3660.
59. Barney R.J., Wasko B.M., Dudakovic A., Hohl R.J., Wiemer D.F. Synthesis and biological evaluation of a series of aromatic bisphosphonates. Bioorg Med Chem 2010, 18:7212-7220.
60. McKenna C.E., et al. Synthesis, chiral high performance liquid chromatographic resolution and enantiospecific activity of a potent New geranylgeranyl transferase inhibitor, 2-hydroxy-3-imidazo[1,2-a]pyridin-3-yl-2-phosphonopropionic acid. J Med Chem 2010, 53:3454-3464.
61. Manne V., et al. Ras farnesylation as a target for novel antitumor agents: potent and selective farnesyl diphosphate analog inhibitors of farnesyltransferase. Drug Dev Res 1995, 34:121-137.
62. Pickett J.S., et al. Kinetic studies of protein farnesyltransferase mutants establish active substrate conformation. Biochemistry 2003, 42:9741-9748.
63. Strickland C.L., et al. Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue. Biochemistry 1998, 37:16601-16611.
64. Long S.B., Casey P.J., Beese L.S. Reaction path of protein farnesyltransferase at atomic resolution. Nature 2002, 419:645-650.
65. Lamothe M., et al. Inhibition of farnesyl protein transferase by new farnesyl phosphonate derivatives of phenylalanine. Bioorg Med Chem Lett 1996, 6:1291-1296.
66. Overhand M., Pieterman E., Cohen L.H., Valentijn A.R.P.M., VanDerMarel G.A., vanBoom J.H. Synthesis of triphosphonate analogues of farnesyl pyrophosphate, inhibitors of squalene synthase and protein:farnesyl transferase. Bioorg Med Chem Lett 1997, 7:2435-2440.
67. Overhand M., et al. Inhibitors of protein:farnesyltransferase and protein:geranylgeranyl transferase I: Synthesis of homologous diphosphonate analogues of isoprenylated pyrophosphate. Bioorg Chem 1998, 26:269-282.
68. Cohen L.H., et al. Inhibition of human smooth muscle cell proliferation by farnesyl pyrophosphate analogues, inhibitors of in vitro protein:farnesyl transferase. Biochem Pharmacol 1999, 57:365-373.
69. Barber A.M., Hardcastle I.R., Rowlands M.G., Nutley B.P., Marriott J.H., Jarman M. Solid-phase synthesis of novel inhibitors of farnesyl transferase. Bioorg Med Chem Lett 1999, 9:623-626.
70. Schlitzer M., Sattler I. Aromatic carboxylic acids as farnesyl surrogates in farnesylpyrophosphate-based farnesyltransferase inhibitors. Bioorg Med Chem 1999, 7:2391-2395.
71. Clark M.K., et al. Synthesis, biochemical, and cellular evaluation of farnesyl monophosphate prodrugs as farnesyltransferase inhibitors. J Med Chem 2007, 50:3274-3282.
72. Wojtkowiak J., et al. Induction of apoptosis in Neurofibromatosis Type 1 malignant peripheral nerve sheath tumor cell lines by a combination of novel farnesyl transferase inhibitors and lovastatin. J Pharm Exp Ther 2008, 326:1-11.
73. Sane K.M., et al. A novel geranylgeranyl transferase inhibitor in combination with lovastatin inhibits proliferation and induces autophagy in STS-26T MPNST cells. J Pharm Exp Ther 2010, 333:23-33.
74. Troutman J.M., Chehade K.A.H., Kiegiel K., Andres D.A., Spielmann H.P. Synthesis of acyloxymethyl ester prodrugs of the transferable protein farnesyl transferase substrate farnesyl methylenediphosphonate. Bioorg Med Chem Lett 2004, 14:4979-4982.
75. Dolence J.M., Poulter C.D. A mechanism for posttranslational modifications of proteins by yeast protein farnesyltransferase. Proc Natl Acad Sci USA 1995, 92:5008-5011.
76. Gibbs R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. Comprehensive Biological Catalysis 1998, Vol. 1:31-118. Academic Press, London.
77. Poulter C.D., Wiggins P.L., Le A.T. Farnesylpyrophosphate synthetase. A stepwise mechanism for the 1'-4 condensation reaction. J Am Chem Soc 1981, 103:3926-3927.
78. Huang C.C., Hightower K.E., Fierke C.A. Mechanistic studies of Rat protein farnesyltransferase indicate an associative transition state. Biochemistry 2000, 39:2593-2602.
79. Mu Y., Omer C.A., Gibbs R.A. On the stereochemical course of human protein-farnesyl transferase. J Am Chem Soc 1996, 118:1817-1823.
80. Edelstein R.L., Weller V.A., Distefano M.D., Tung J.S. Stereochemical analysis of the reaction catalyzed by yeast protein farnesyltransferase. J Org Chem 1998, 63:5298-5299.
81. Weller V.A., Distefano M.D. Measurement of the a-secondary kinetic isotope effect for a prenyltransferase by MALDI mass spectrometry. J Am Chem Soc 1998, 120:7975-7976.
82. Pais J.E., Bowers K.E., Stoddard A.K., Fierke C.A. A continuous fluorescent assay for protein prenyltransferases measuring diphosphate release. Anal Biochem 2005, 345:302-311.
83. Lenevich S., Xu J., Hoeokawa A., Cramer C.J., Distefano M.D. Transition state analysis of model and enzymatic prenylation reactions. J Am Chem Soc 2007, 129:5796-5797.
84. Long S.B., Casey P.J., Beese L.S. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry 1998, 37:9612-9618.
85. Zahn T.J., Ksebati M., Gibbs R.A. Synthesis and conformational analysis of Bis-carbon-13 labeled farnesyl diphosphate analogs. Tetrahedron Lett 1998, 39:3991-3994.
86. Zahn T.J., et al. Evaluation of isoprenoid conformation in solution and in the active site of protein-farnesyl transferase using carbon-13 labeling in conjunction with solution and solid state NMR. J Am Chem Soc 2000, 122:7153-7164.
87. Kim M., Kleckley T.S., Wiemer A.J., Holstein S.A., Hohl R.J., Wiemer D.F. Synthesis and activity of fluorescent isoprenoid pyrophosphate analogues. J Org Chem 2004, 69:8186-8193.
88. Dursina B., et al. Identification and specificity profiling of protein prenyltransferase inhibitors using New fluorescent phosphoisoprenoids. J Am Chem Soc 2006, 128:2822-2835.
89. Liu X., Prestwich G.D. Didehydrogeranylgeranyl (DDGG): a fluorescent probe for protein prenylation. J Am Chem Soc 2002, 124:20-21.
90. Park H.W., Boduluri S.R., Moomaw J.F., Casey P.J., Beese L.S. Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution. Science 1997, 275:1800-1804.
91. Bukhtiyarov Y.E., Omer C.A., Allen C.M. Photoreactive analogs of prenyl diphosphates as inhibitors and probes of human farnesyltransferase and geranylgeranyltransferase type I. J Biol Chem 1995, 270:19035-19040.
92. Edelstein R.L., Distefano M.D. Photoaffinity labeling of yeast farnesyl protein transferase and enzymatic synthesis of a Ras protein incorporating a photoactive isoprenoid. Biochem Biophys Res Commun 1997, 235:377-382.
93. Gaon I., Turek T.C., Weller V.A., Edelstein R.L., Singh S.K., Distefano M.D. Photoactive analogs of farnesyl pyrophosphate containing benzoylbenzoate esters: synthesis and application to photoaffinity labeling of yeast protein farnesyltransferase. J Org Chem 1996, 61:7738-7745.
94. Dorman G., Prestwich G.D. Benzophenone photophores in biochemistry. Biochemistry 1994, 33:5661-5673.
95. Kale T.A., Raab C., Yu N., Dean D.C., Distefano M.D. A photoactivatable prenylated cysteine designed to study isoprenoid recognition. J Am Chem Soc 2001, 123:4373-4381.
96. Turek T.C., Gaon I., Distefano M.D., Strickland C.L. Synthesis of farnesyl diphosphate analogues containing ether-linked photoactive benzophenones and their application in studies of protein prenyltransferases. J Org Chem 2001, 66:3253-3264.
97. Turek-Etienne T.C., Strickland C.L., Distefano M.D. Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase. Biochemistry 2003, 42:3716-3724.
98. Volkert M., et al. Synthesis and biological activity of photoactivatable N-Ras peptides and proteins. J Am Chem Soc 2003, 125:12749-12758.
99. DeGraw A.J., et al. A photoactive isoprenoid diphosphate analogue containing a stable phosphonate linkage: synthesis and biochemical studies with prenyltransferases. J Org Chem 2007, 72:4587-4595.
100. Henry O., et al. A versatile photoactivatable probe designed to label the diphosphate binding site of farnesyl diphosphate utilizing enzymes. Bioorg Med Chem 2009, 17:4797-4805.
101. Chehade K.A.H., et al. Photoaffinity analogues of farnesyl pyrophosphate transferable by protein farnesyl transferase. J Am Chem Soc 2002, 124:8206-8219.
102. Pompliano D.L., Schaber M.D., Mosser S.D., Omer C.A., Shafer J.A., Gibbs J.B. Isoprenoid diphosphate utilization by recombinant human farnesyl:protein transferase: interactive binding between substrates and a preferred kinetic pathway. Biochemistry 1993, 32:8341-8347.
103. Reiss Y., Brown M.S., Goldstein J.L. Divalent cation and prenyl pyrophosphate specificities of the protein farnesyltransferase from Rat brain, a zinc metalloenzyme. J Biol Chem 1992, 267:6403-6408.
104. Rowell C.A., Kowalczyk J.J., Lewis M.D., Garcia A.M. Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo. J Biol Chem 1997, 272:14093-14097.
105. Whyte D.B., et al. K- and N-Ras are geranylgeranylated in cells trated with farnesyl protein transferase inhibitors. J Biol Chem 1997, 272:14459-14464.
106. Kloog Y., Cox A.D. Prenyl-binding domains: potential targets for Ras inhibitors and anti-cancer drugs. Semin Cancer Biol 2004, 14:253-261.
107. McGeady P., Kuroda S., Shimizu K., Takai Y., Gelb M.H. The farnesyl group of H-Ras facilitates the activation of a soluble upstream activator of mitogen-activated protein kinase. J Biol Chem 1995, 270:26347-26351.
108. Dolence J.M., Cassidy P.B., Mathis J.R. Yeast protein farnesyltransferase: steady-state kinetic studies of substrate binding. Biochemistry 1995, 34:16687-16694.
109. Yokoyama K., Zimmerman K., Scholten J., Gelb M.H. Differential prenyl pyrophosphate binding to mammalian protein geranylgeranyltransferase I and protein farnesyltransferase and its consequence on the specificity of protein prenylation. J Biol Chem 1997, 272:3944-3952.
110. Gibbs B.S., Zahn T.J., Mu Y.Q., Sebolt-Leopold J., Gibbs R.A. Novel farnesol and geranylgeraniol analogues: a potential new class of anticancer agents directed against protein prenylation. J Med Chem 1999, 42:3800-3808.
111. Zahn T.J., Weinbaum C., Gibbs R.A. Grignard-mediated synthesis and preliminary biological evaluation of novel 3-substituted farnesyl diphosphate analogues. Bioorg Med Chem Lett 2000, 10:1763-1766.
112. Krzysiak A.J., et al. Combinatorial modulation of protein prenylation. ACS Chem Biol 2007, 2:385-389.
113. Placzek A.T., Gibbs R.A. New synthetic methodology for the construction of 7-substituted farnesyl diphosphate analogs. Org Lett 2011, 13:3576-3579.
114. Dunten P., Kammlott U., Crowther R., Weber D., Palermo R., Birktoft J. Protein farnesyltransferase: structure and implications for substrate binding. Biochemistry 1998, 37:7907-7912.
115. Micali E., Chehade K.A.H., Isaacs R.J., Andres D.A., Spielmann H.P. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. Biochemistry 2001, 40:12254-12265.
116. Zhou C., Shao Y., Gibbs R.A. Aromatic farnesyl diphosphate analogues: vinyl triflate-mediated synthesis and preliminary evaluation. Bioorg Med Chem Lett 2002, 12:1417-1420.
117. Chehade K.A.H., Andres D.A., Morimoto H., Spielmann H.P. Design and synthesis of a transferable farnesyl pyrophosphate analogue to Ras by protein farnesyltransferase. J Org Chem 2000, 65:3027-3033.
118. Troutman J.M., Roberts M.J., Andres D.A., Spielmann H.P. Tools to analyze protein farnesylation in cells. Bioconjug Chem 2005, 16:1209-1217.
119. Dechat T., et al. Alterations in mitosis and cell cycle progression caused by a mutant lamin A known to accelerate human aging. Proc Natl Acad Sci USA 2007, 104:4955-4960.
120. Davies B.S., et al. Increasing the length of progerin's isoprenyl anchor does not worsen bone disease or survival in mice with Hutchinson-Gilford progeria syndrome. J Lipid Res 2009, 50:126-134.
121. Onono F.K., et al. A tagging-via-substrate approach to detect the farnesylated proteome using Two-dimensional electrophoresis coupled with western blotting. Mol Cell Proteom 2010, 9:742-751.
122. Roberts M.J., et al. Hydrophilic anilinogeranyl diphosphate prenyl analogues Are Ras function inhibitors. Biochemistry 2006, 45:15862-15872.
123. Troutman J.M., Subramanian T., Andres D.A., Spielmann H.P. Selective modification of CaaX peptides with ortho-substituted anilinogeranyl lipids by protein farnesyl transferase: competitive substrates and potent inhibitors from a library of farnesyl diphosphate analogues. Biochemistry 2007, 46:11310-11321.
124. Troutman J.M., Andres D.A., Spielmann H.P. Protein farnesyl transferase target selectivity is dependent upon peptide stimulated product release. Biochemistry 2007, 46:11299-11309.
125. Subramanian T., Liu S., Troutman J.M., Andres D.A., Spielmann H.P. Protein farnesyltransferase-catalyzed isoprenoid transfer to peptide depends on lipid size and shape, not hydrophobicity. Chembiochem 2008, 9:2872-2882.
126. Gibbs J.B. Ras C-terminal processing enzymes-New drug targets?. Cell 1991, 65:1-4.
127. Mu Y.Q., Eubanks L.M., Poulter C.D., Gibbs R.A. Coupling of isoprenoid triflates with organoboron nucleophiles: synthesis and biological evaluation of geranylgeranyl diphosphate analogues. Bioorg Med Chem 2002, 10:1207-1219.
128. Zahn T.J., Whitney J., Weinbaum C., Gibbs R.A. Synthesis and evaluation of GGPP geometric isomers: divergent substrate specificities of FTase and GGTase I. Bioorg Med Chem Lett 2001, 11:1605-1608.
129. Maynor M., Scott S.A., Rickert E.A., Gibbs R.A. Synthesis and evaluation of 3- and 7-substituted geranylgeranyl pyrophosphate analogs. Bioorg Med Chem Lett 2008, 18:1889-1892.
130. Hang H.C., Bertozzi C.R. Chemoselective approaches to glycoprotein assembly. Acc Chem Res 2001, 34:727-736.
131. Agard N.J., Baskin J.M., Prescher J.A., Lo A., Bertozzi C.R. A comparative study of bioorthogonal reactions with azides. ACS Chem Biol 2006, 1:644-648.
132. Duckworth B.P., Zhang Z., Hosokawa A., Distefano M.D. Selective labeling of proteins by using protein farnesyltransferase. Chembiochem 2007, 8:98-105.
133. Chan L.N., et al. A novel approach to tag and identify geranylgeranylated proteins. Electrophoresis 2009, 30:3598-3606.
134. Kolb H.C., Finn M.G., Sharpless K.B. Click chemistry: diverse chemical function from a few good reactions. Angew Chem Int Ed 2001, 40:2004-2021.
135. Rostovtsev V.V., Green L.G., Fokin V.V., Sharpless K.B. A stepwise huisgen cycloaddition process: copper(I)-catalyzed regioselective " ligation" of azides and terminal alkynes. Angew Chem Int Ed 2002, 33:45.
136. Labadie G.R., Wiswanathan R., Poulter C.D. Farnesyl diphosphate analogues with ö-bioorthogonal azide and alkyne functional groups for protein farnesyl transferase-catalyzed ligation reactions. J Org Chem 2007, 72:9291-9297.
137. Gauchet C., Labadie G.R., Poulter C.D. Regio- and chemoselective covalent immobilization of proteins through unnatural amino acids. J Am Chem Soc 2006, 128:9274-9275.
138. Wollack J.W., Silverman J.M., Petzold C.J., Mougous J.D., Distefano M.D. A minimalist substrate for enzymatic peptide and protein conjugation. Chembiochem 2009, 10:2934-2943.
139. Rashidian M., Dozler J.K., Lenevich S., Distefano M.D. Selective labeling of polypeptides using protein farnesyltransferase via rapid oxime ligation. Chem Commun 2010, 46:8998-9000.
140. Charron G., Tsou L.K., Maguire W., Yount J.S., Hang H.C. Alkynyl-farnesol reporters for detection of protein S-prenylation in cells. Mol Biosyst 2011, 7:67-73.
141. Song J., et al. A Novel and Efficient Alkyne-Prenyl Diphosphate Tag for Proteomic Characterization of the Prenylome. To be submitted for publication 2011.
142. Nguyen U.T.T., et al. Exploiting the substrate tolerance of farnesyltransferase for site-selective protein derivatization. Chembiochem 2007, 8:408-423.
143. Chen Y.X., Triola G., Waldmann H. Bioorthogonal chemistry for site-specific labeling and surface immobilization of proteins. Acc Chem Res 2011, 44:762-773.
144. Nguyen U.T.T., et al. Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. Nat Chem Biol 2009, 5:227-235.
145. Naider F.R., Becker J.M. Synthesis of prenylated peptides and peptide esters. Biopolymers 1997, 43:3-14.
146. Dawe A.L., et al. Novel modifications to the farnesyl moiety of the a-factor lipopeptide pheromone from Saccharomyces cerevisiae-a role for isoprene modifications in ligand presentation. Biochemistry 1997, 36:12036-12044.
147. Xie H., Shao Y., Becker J.M., Naider F., Gibbs R.A. Synthesis and biological evaluation of the geometric farnesylated analogues of the a-factor mating peptide of Saccharomyces cerevisiae. J Org Chem 2000, 65:8552-8563.
148. Wollack J.W., et al. Multifunctional prenylated peptides for live cell analysis. J Am Chem Soc 2009, 131:7293-7303.
149. Weise K., et al. Membrane-mediated induction and sorting of K-Ras microdomain signaling platforms. J Am Chem Soc 2011, 1333:880-887.