Recent Publications

1. Szostak JW, Sparkuhl J, Goldstein ME. Sexual induction in Eudorina: effects of light, nutrients and conditioned medium. J Phycol. 1973; 9:215-218.

2. Szostak JW. Specific binding of a synthetic oligonucleotide to the yeast Iso-1 cytochrome c mRNA and gene. Thesis. Ithaca, New York: Cornell University, 1977.

3. Szostak JW, Stiles JI, Bahl CP, Wu R. Specific binding of a synthetic oligonucleotide to yeast cytochrome c mRNA. Nature 1977; 265:61-63.

4. Szostak JW, Stiles JI, Tye B-K, Chiu P, Sherman F, Wu R. Hybridization with synthetic oligonucleotides. In: Wu R, ed. Methods in Enzymology, 68:Chpt. 29. New York, NY: Academic Press; 1979.

5. Szostak JW, Wu R. Insertion of a genetic marker into the ribosomal DNA of yeast. Plasmid 1979; 2:536-554.

6. Szostak JW, Wu R. Unequal crossing over in the ribosomal DNA of Saccharomyces cerevisiae. Nature 1980; 284:426-430.

7. Stiles JI, Szostak JW, Young AT, Wu R, Consaul S, Sherman F. DNA Sequence of a mutation in the leader region of the yeast Iso-1 cytochrome c mRNA. Cell 1981; 25:277- 284.

8. Orr-Weaver TL, Szostak JW, Rothstein RJ. Yeast transformation: a model system for the study of recombination. Proc. Natl. Acad. Sci. USA 1981; 78:6354-6358.

9. Szostak JW, Blackburn EH. Cloning yeast telomeres on linear plasmid vectors. Cell 1982; 29:245-255.

10. Szostak JW. Evolutionary conservation of the structure of eucaryotic telomeres. Berkeley Workshop on Recent Advances in Yeast Molecular Biology, 1. 1982.

11. Rothstein RJ, Orr-Weaver TL, Szostak JW. Double strand breaks and genetic recombination. Berkeley Workshop on Recent Advances in Yeast Molecular Biology, 1. 1982.

12. Szostak JW. Structural requirements for telomere resolution. Cold Spring Harbor Symposium on DNA Structure. 1982; 43:1187-1194.

13. Ruby SW, Szostak JW, Murray AW. Cloning regulated yeast genes from a pool of LacZ fusions. Methods in Enzymology. 1982; 101:253-269.

14. Orr-Weaver TL, Szostak JW, Rothstein RJ. Genetic applications of yeast transformation with linear and gapped plasmids. Methods in Enzymology. 1982; 101:228-245.

15. Brown P, Szostak JW. Yeast vectors with negative selection. Methods in Enzymology. 1982; 101:278-290.

16. Sugawara NF, Szostak JW. The construction of specific chromosome rearrangements in yeast. Methods in Enzymology. 1982; 101:269-278.

17. Szostak JW. A rapid procedure for the construction of linear yeast plasmids. Methods in Enzymology. 1982; 101:245-252.

18. Walmsely R, Petes TD, Szostak JW. Is there left-handed DNA at the ends of yeast chromosomes? Nature 1983; 302:84-86.

19. Orr-Weaver TL, Szostak JW. Multiple, tandem plasmid integration in yeast. Mol. Cell. Biol. 1983; 3:747-749.

20. Orr-Weaver TL, Szostak JW. Yeast recombination: The association between double-strand- gap repair and crossing-over. Proc. Natl. Acad. Sci. USA. 1983; 80:4417-4421.

21. Szostak JW, Orr-Weaver TL, Rothstein RJ, Stahl F. The double-strand-break repair model for recombination. Cell 1983; 33:25-35.

22. Sugawara NF, Szostak JW. Recombination between sequences in non-homologous positions. Proc. Natl. Acad. Sci. USA. 1983; 80:5675-5679.

23. Murray AW, Szostak JW. Pedigree analysis of plasmid segregation in yeast. Cell 1983; 34:961-970.

24. Murray AW, Szostak JW. The construction and properties of artificial chromosomes in yeast. Nature 1983; 305:189-193.

25. Blackburn EH, Szostak JW. The molecular structure of centromeres and telomeres. Ann Rev Biochem. 1984; 53:163-194.

26. Shampay J, Szostak JW, Blackburn EH. DNA sequences of telomeres maintained in yeast. Nature 1984; 310:154-157.

27. Dunn BL, Szauter P, Pardue M-L, Szostak JW. Transfer of telomere-adjacent sequences to linear plasmids by recombination. Cell 1984; 39:191-201.

28. Szostak JW, Rothstein RJ. Theory and practice of genetic engineering. In: Kosuge T, Nester EW, eds. Plant microbe interactions, 1. 1984:125-146.

29. Szostak JW, Murray AW, Claus TE, Dunn BL. Telomeres and artificial chromosomes in yeast. In: Bennet MD, Gropp A, Wolf U., eds. Chromosomes today, 8. 1984

30. Ruby SW, Szostak JW. Specific Saccharomyces cerevisiae genes are expressed in response to DNA-damaging agents. Mol. Cell. Biol. 1985; 5:75-84.

31. Orr-Weaver TL, Szostak JW. Fungal recombination. Microbiol. Reviews. 1985; 49:33-58.

32. Whiteway MS, Szostak JW. The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways. Cell 1985; 43:483-492.

33. Murray AW, Szostak JW. Chromosome segregation in mitosis and meiosis. Annual Review of Cell Biology. 1985; 1:289-315.

34. Murray AW, Schultes NP, Szostak JW. Length is a major determinant of chromosome stability. Cell 1986; 45:529-536.

35. Szostak JW. Enzymatic activity of the conserved core of a group I self-splicing intron. Nature 1986; 322:83-86.

36. Murray AW, Szostak JW. Construction and behavior of circularly permuted and telocentric chromosomes in yeast. Mol. Cell. Biol. 1986; 6:3166-3172.

37. Dawson D, Murray AW, Szostak JW. An alternate pathway for meiotic chromosome segregation in yeast. Science 1986; 234:713-717

38. Murray AW, Szostak JW. Artificial Chromosomes. Scientific American. November, 1987; pp. 62-68.

39. Reynolds A, Murray AW, Szostak JW. Role of the 2um gene products in stable maintenance of the 2um plasmid of Saccharomyces cerevisiae. Mol. Cell. Biol. 1987; 7:3566-3573.

40. Whiteway MS, Freedman R, Van Arsdell S, Szostak JW, Thorner J. Yeast ARD1 gene product is required for repression of cryptic mating type information at the HML locus. Mol. Cell. Biol. 1987; 7:3713-3722.

41. Burke JM, Belfort M, Cech TR, Davies RW, Schweyen JR, Shub DA, Szostak JW, Tabak HF. Structural conventions for group I introns. Nucleic Acids Research 1987; 15:7217-7221.

42. Matsumoto T, Fukui K, Niwa O, Sugawara N, Szostak JW, Yanagida M. Identification of Healed Terminal DNA Fragments in Linear Minichromosomes of Schizosaccharomyces pombe. Mol. Cell. Biol. 1987; 7:4424-4430.

43. Doudna J, Gerber AS, Cherry JM, Szostak JW. Genetic Dissection of an RNA Enzyme - Cold Spring Harbor Symposia, Vol. LII. 1987.

44. Szostak, JW. Structure and Activity of Ribozymes. 1988, in 'Redesigning Life', A symposium of the Swiss Association of Chemists, ed. S.A. Benner.

45. Allshire R, Gosden JR, Cross SH, Cranston G, Rout D, Sugawara N, Szostak JW, Fantes, P, Hastie ND. The telomeric repeat from Tetrahymena thermophila cross hybridizes with Human telomeres. Nature 1988; 332: 656-659.

46. Orr-Weaver TL, Nicolas AG, Szostak JW. Gene conversion adjacent to regions of double- strand break repair. Mol. Cell. Biol. 1988; 8: 5292- 5298.

47. Murray AW, Claus T, Szostak JW. Characterization of two telomeric DNA processing reactions in S. cerevisiae. Mol. Cell. Biol., 1988; 8: 4642-4650.

48. Nicolas A, Treco D, Schultes N, Szostak JW. An initiation site for meiotic gene conversion in the yeast Saccharomyces cerevisiae. Nature 1989; 338: 35-39.

49. Sun H, Treco D, Schultes N, Szostak JW. Double-strand breaks at an initiation site for meiotic gene conversion. Nature 1989; 338: 87- 90.

50. Szostak JW. Telomerase: The beginning of the ends. Nature 1989; 337: 303-304.

51. Lundblad V, Szostak JW. A mutant with a defect in telomere maintenance leads to senescence in yeast. Cell 1989; 57: 633-643.

52. Doudna JA, Cormack BP, Szostak JW. RNA structure, not sequence, determines the 5' splice-site specificity of a group I intron. Proc. Natl. Acad. S ci. USA 1989; 86: 7402-7406.

53. Rajagopal J, Doudna JA, Szostak JW. Stereochemical Course of Catalysis by the Tetrahymena Ribozyme. Science 1989; 244: 692-694

54. Doudna JA, Szostak JW. RNA catalyzed synthesis of complementary strand RNA. Nature 1989; 339: 519-522

55. Doudna JA, Szostak JW. Miniribozymes, Small Derivatives of the sunY Intron, Are Catalytically Active. Mol. Cell. Biol. 1989; 9: 5480-5483.

56. Michel F, Hanna M, Green R, Bartel DB, Szostak JW. The guanosine binding site of the Tetrahymena ribozyme. Nature 1989; 342: 391-395

57. Ellington AE, Szostak JW. In vitro Selection of RNA Molecules that Bind Specific Ligands. Nature 1990; 346: 818-822.

58. Lichten M, Goyon C, Schultes NP, Treco D, Szostak JW, Haber JE, Nicolas A. Detection of heteroduplex DNA molecules among the products of Saccharomyces cerevisiae meiosis. Proc. Natl. Acad. Sci. USA 1990; 87:7653-7657.

59. Green R, Ellington AE, Szostak JW. In vitro Genetic Analysis of the Tetrahymena Self- splicing Intron. Nature 1990; 347: 406-408.

60. Park E.-C., Szostak JW. Point mutations in the yeast histone H4 gene prevent silencing of the silent mating type locus HML. Mol. Cell. Biol. 1990; 10: 4932-4934.

61. Michel F, Ellington AE, Couture, S, Szostak JW. Phylogenetic and genetic evidence for base-triples in the catalytic domain of group I introns. Nature 1990; 347: 578-580.

62. Schultes NP, Szostak JW. Decreasing Gradients of Gene Conversion on Both Sides of the Initiation Site for Meiotic Recombination at the ARG4 Locus in Yeast. Genetics 1990; 126: 813-822.

63. Schultes NP, Ellington AD, Cherry JM, Szostak JW. Saccharomyces cerevisiae Homoserine Kinase is Homologous to Prokaryotic Homoserine Kinases. Gene 1990; 96: 177-180.

64. Couture S, Ellington AD, Gerber AS, Cherry JM, Doudna JA, Green R, Hanna M, Pace U, Rajogopal J, Szostak JW. Mutational analysis of conserved nucleotides in a self-splicing group I intron. J. Mol. Biol. 1990; 215: 345-358.

65. Doudna JA, Szostak JW, Rich A, Usman N. Chemical Synthesis of Oligoribonucleotides Containing 2-Aminopurine: Substrates for the Investigation of Ribozyme Function. J. Org. Chem. 1990; 55: 5547-5549.

66. Schultes NP, Szostak JW. A Poly dA.dT Tract Is a Component of the Recombination Initiation Site at the ARG4 Locus in Saccharomyces cerevisiae. Mol. Cell. Biol. 1991; 11: 322-328.

67. Sun H, Treco D, Szostak JW. Extensive 3'-overhanging, single-stranded DNA tails are associated with the meiosis-specific double-strand breaks at the ARG4 recombination initiation site. Cell 1991; 64: 1155-1161.

68. Doudna JA, Couture S, Szostak JW. A multi-subunit ribozyme that is a catalyst of and a template for complementary strand RNA synthesis. Science 1991; 251: 1605-1608.

69. Pace U, Szostak JW. Mutations in a semi-conserved region of the Tetrahymena intron.FEBS Lett. 1991; 280: 171-174.

70. Bartel DP, Szostak JW. Template-Directed Primer Extension Catalyzed by the Tetrahymena Ribozyme. Mol. Cell. Biol. 1991; 11: 3390-3394.

71. Green R, Ellington AD, Bartel DP, Szostak JW. In Vitro Genetic Analysis: Selection and Amplification of Rare Functional Nucleic Acids. Methods: A Companion to Methods in Enzymol. 1991; 2: 75-86.

72. Bartel DP, Zapp M, Green M, Szostak JW. HIV-1 Rev Regulation Involves Recognition of Non-Watson-Crick Base-pairs in Viral RNA. Cell 1991; 67: 529-536.

73. Green R, Szostak JW, Benner SA, Rich A, Usman N. Synthesis of RNA containing inosine: analysis of the sequence requirements for the 5' splice-site of the Tetrahymena group I intron. Nuc. Acids Res. 1991; 19: 4161-4166.

74. Sun H, Dawson D, Szostak JW. Genetic and Physical Analyses of Sister-Chromatid Exchange in Yeast Meiosis. Mol. Cell. Biol. 1991; 11: 6328-6336.

75. Park E.-C., Finley D. and Szostak JW. A novel strategy for the generation of conditional mutations by protein destabilization. Proc. Natl. Acad. Sci. USA 1992; 89:1249-1252.

76. Ellington AE, Szostak JW. Selection in vitro of single-stranded DNA molecules that fold into specific ligand binding structures. Nature 1992; 355:850-852.

77. Szostak JW. In Vitro Genetics. Trends in Biochem. Sci. 1992; 17: 89-93.

78. Park E.-C., Szostak JW. ARD1 and NAT1 proteins form a complex that has N-terminal acetyltransferase activity. EMBO J. 1992; 11:2087-2094.

79. Famulok M, Szostak JW. Stereospecific Recognition of Tryptophan Agarose by in Vitro Selected RNA. J. Am. Chem. Soc. 1992; 114: 3990-3991.

80. Famulok M, Szostak JW. In Vitro Selection of Specific Ligand Binding Nucleic Acids. Angew. Chem. Int. Ed. Engl. 1992; 31: 979-988.

81. Ross LO, Treco D, Nicolas A, Szostak JW, Dawson D. Meiotic Recombination on Artificial Chromosomes in Yeast. Genetics 1992; 131: 541-550.

82. Wilson CL, Szostak JW. Ribozyme Catalysis. Curr. Opin. in Struct. Biol. 1992; 2:749-756.

83. Green R and Szostak JW. Selection of a Ribozyme that Functions as a Superior Template in a Self-Copying Reaction. Science 1992; 258:1910-1915.

84. Doudna JA, Szostak JW. Triplet extension: a novel strategy for RNA catalyzed RNA replication. Biochemistry 1993; 32:2111-2115.

85. Szostak JW. Evolution ex vivo. Nature 1993; 361: 119-120.

86. Szostak, J.W. and Ellington, A.E. In Vitro Selection of Functional RNA Sequences. pp. 511-533 in "The RNA World", ed. R. Gesteland and J. Atkins; Cold Spring Harbor Press, 1993.

87. Famulok M, Szostak JW. Selection of Functional RNA and DNA Molecules from Randomized Sequences. pp. 271-284, in Nucleic Acids and Molecular Biology, ed. F. Eckstein and D.M.J. Lilley, Springer-Verlag, 1993.

88. Sassanfar M, Szostak JW. An RNA motif that binds ATP. Nature 1993; 364: 550-553.

89. Bartel DP, Szostak JW. Isolation of new ribozymes from a large pool of random sequences. Science 1993; 261:1411-1418.

90. Szostak, JW. Prospects for the Construction of an RNA Replicase. Chpt. 13, pp. 183-197, in "Proceedings of The Robert A. Welch Foundation 37th Conference on Chemical Research". Houston, Texas, 1993.

91. Green R, Szostak JW. In vitro genetic analysis of the hinge region between helical elements P5-P4-P6 and P7-P3-P8 in the sunY group I self-splicing intron. J. Mol. Biol. 1994; 235:140-155.

92. Lin, C-W, Szostak JW. Evidence That the Guanosine Substrate of the Tetrahymena Ribozyme is Bound in the Anti Conformation and That N7 Contributes to Binding. Biochemistry 1994; 33:2703-2707.

93. Lorsch J, Szostak, JW. In Vitro Selection of RNA Aptamers Specific for Cyanocobalamin. Biochemistry 1994; 33:973-982.

94. Peterson RD, Bartel DP, Szostak JW, Horvath SJ, Feigon J. 1H NMR Studies of the High- Affinity Rev Binding Site of the Rev Responsive Element of HIV-1 mRNA: Base Pairing in the Core Binding Element. Biochemistry 1994; 33: 5357-5366.

95. Green R, Szostak JW. Template-directed oligonucleotide assembly reactions catalyzed by a minimally structured ribozyme derived from a group I intron. pp. 277-283 in, Structural Biology: The State of the Art, Proceedings of the Eighth Conversation, State University of New York, Albany, NY 1993 Eds. Ramaswamy H. Sarma and Mukti H. Sarma, Adenine Press 1994

96. Chapman KB, Szostak JW. In Vitro Selection of Catalytic RNAs. Current Opinions in Structural Biology 1994; 4:618-622.

97. Lorsch JR, Szostak JW. In vitro evolution of new ribozymes with polynucleotide kinase activity. Nature 1994; 371:31-36.

98. Hanna M, Szostak JW. Suppression of mutations in the core of the Tetrahymena
ribozyme by spermidine, ethanol and by substrate stabilization. Nuc. Acids Res. 1994; 22: 5326-5331.

99. Bartel DP, Szostak JW. Study of RNA-protein recognition by in vitro selection. in RNA- Protein Interactions, eds. K. Nagai and I.W. Mattaj, Oxford University Press 1994.

100. Huizenga DE, Szostak JW. A DNA Aptamer that Binds Adenosine and ATP. Biochemistry 1995; 34: 656-665.

101. Lauhon CT, Szostak JW. RNA Aptamers that bind Flavin and Nicotinamide Redox Cofactors. J. Am. Chem. Soc. 1995; 117: 1246-1257.

102. Whoriskey S, Usman N, Szostak JW. Total chemical synthesis of a ribozyme derived from a group I intron. Proc. Natl. Acad. Sci. U.S.A. 1995; 92: 2465-2469.

103. Wilson CW, Szostak JW. In vitro evolution of a self-alkylating ribozyme. Nature 1995; 374: 777-782.

104. Chapman KB, Szostak JW. Isolation of a ribozyme with 5'-5' ligase activity. Chemistry and Biology 1995; 2: 325-333.

105. Cuenoud B, Szostak JW. A DNA metalloenzyme with DNA ligase activity. Nature 1995;
375: 611-614.

106. Ekland EH, Szostak JW, Bartel DP. Structurally complex and highly active RNA ligases derived from random RNA sequences. Science 1995; 269: 364-370.

107. Lorsch JR, Bartel DP, Szostak JW. Reverse transcriptase reads through a 2'-5' linkage and a 2'-thiophosphate in a template. Nuc. Acids Res. 1995; 23: 2811-2814.

108. Lorsch JR, Szostak JW. Kinetic and Thermodynamic Characterization of the Reaction Catalyzed by a Polynucleotide Kinase Ribozyme. Biochemistry 1995; 34: 15315-15327.

109. Lorsch JR, Szostak JW. In Vitro Selection of Nucleic Acid Sequences that Bind Small Molecules. 1996. Chpt. 4 in Combinatorial Libraries: Synthesis, Screening and Application Potential. Ed. R. Cortese. Publ. Walter de Gruyter, Berlin, New York.

110. Lorsch JR, Szostak JW. Chance and Necessity in the Selection of Nucleic Acid Catalysts. Accounts Chem. Res. 1996; 29: 103-110.

111. Rohatgi R, Bartel D, Szostak JW. Kinetic and Mechanistic Analysis of Nonenzymatic, Template-Directed Oligonucleotide Ligation. J. Am. Chem. Soc. 1996; 118: 3332-3339.

112. Rohatgi R, Bartel D, Szostak JW. Non-enzymatic, Template-Directed Ligation of Oligoribonucleotides is Highly Regioselective for the Formation of 3'-5' Phosphodiester Bonds. J. Am. Chem. Soc. 1996; 118: 3340-3334.

113. Lohse P, Szostak JW. Ribozyme-catalysed amino acid transfer reactions. Nature 1996; 381: 442-444.

114. Huang Z, Szostak JW. 3' End-Labeling of RNA with DNA Polymerase. Nuc. Acids Res. 1996; 24: 4360-4361.

115. Hager AJ, Pollard JD, Szostak JW. Ribozymes: aiming at RNA replication and translation. Chem. Biol. 1996; 3:717-725.

116. Szostak JW. Introduction: Combinatorial Chemistry. Chem. Rev. 1997; 97 (2): 347-348, in: Chemical Reviews: Combinatorial Chemistry, a Thematic Issue, Guest Editor Jack W. Szostak.

117. Dieckmann T, Butcher SE, Sassanfar M, Szostak JW and Feigon J. Mutant ATP-Binding RNA aptamers reveal the structural basis for ligand binding. J. Mol. Biol. 1997; 273: 467- 478.

118. Hager AJ, Szostak JW. Isolation of Novel Ribozymes that Ligate AMP-Activated RNA Substrates. Chem. Biol. 1997; 4:607-617.

119. Roberts RW, Szostak JW. RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. USA 1997; 94: 12297-12302.

120. Suga H, Lohse P, Szostak JW. Structural and Kinetic Characterization of an Acyl Transferase Ribozyme. J. Am. Chem. Soc. 1998; 120: 1151-1156.

121. Suga H, Cowan JA, Szostak JW. Unusual metal ion catalysis in an acyl transferase ribozyme. Biochemistry 1998; 37:10118-10125.

122. Wilson C, Nix J, Szostak JW. Functional requirements for specific ligand recognition by a biotin-binding RNA pseudoknot. Biochemistry 1998; 37:14410-9.

123. Wilson C, Szostak JW. Isolation of a fluorophore-specific DNA aptamer with weak redox activity. Chem. Biol., 1998; 5: 609-617.

124. Holeman LA, Robinson SL, Szostak JW and Wilson C. Isolation and characterization of fluorophore-binding RNA aptamers. Folding & Design, 1998; 3:423-431.

125. Szostak JW. In Vitro Selection and Directed Evolution. Harvey Lect. 1997-98; 93:95-118.

126. Wilson DS, Szostak JW. In vitro Selection of Functional Nucleic Acids. Ann. Rev. Biochem., 1999; 68:611-648.

127. Liu R, Barrick JE, Szostak JW, Roberts RW. Optimized synthesis of RNA-protein fusions for in vitro protein selection. Methods in Enzymol. 2000; 318: 268-293.

128. Szostak JW. Constraints on the sizes of the earliest cells. In, 'Size Limits of Very Small Microorganisms', Proceedings of a Workshop of the Space Studies Board, National Research Council. 1999, National Academy Press.

129. Lee N, Bessho Y, Wei K, Szostak JW, Suga H. Ribozyme-catalyzed tRNA aminoacylation. Nature Struct. Biol., 2000; 7: 28-33.

130. Cho, G, Keefe, AD, Wilson, DS, Liu, R and Szostak, JW. Constructing high complexity synthetic libraries of long ORFs using in vitro selection. J. Mol. Biol., 2000; 297:309-319.

131. Vaish NK, Fraley AW, Szostak JW and McLaughlin LW. Expanding the Structural and Functional Diversity of RNA: Analogue Uridine Triphosphates as Candidates for In Vitro Selection of Nucleic Acids. Nuc. Acids Res., 2000; 28:3316-20.

132. Szostak JW, Bartel DP, Luisi PL. Synthesizing life. Nature, 2001; 409:387-390.

133. Wilson DS, Keefe AD, Szostak JW. The use of mRNA display to select high-affinity protein-binding peptides. Proc. Natl. Acad. Sci., 2001; 98:3750-3755.

134. Keefe AD, Szostak JW. Functional proteins from a random sequence library. Nature, 2001; 410:715-718.

135. Salehi-Ashtiani K, Szostak JW. In vitro evolution suggests multiple origins for the hammerhead ribozyme. Nature, 2001; 414:82-84.

136. Keefe AD, Wilson DS, Seelig B, Szostak JW. One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-tag. Protein Expression and Purification, 2001; 23:440-446.

137. Baggio R, Burgstaller P, Hale S, Putney A, Lane M, Lipovsek D, Wright M, Roberts RW, Liu R, Szostak JW, Wagner RW. Identification of epitope-like consensus motifs using mRNA display. J. Mol. Recog., 2002; 15:126-134.

138. Davis JH, Szostak JW, Isolation of high-affinity GTP aptamers from partially structured RNA libraries. Proc. Natl. Acad. Sci. USA, 2002; 99:11616-11621.

139. Szostak JW. RNA gets a grip on translation (News and Views). Nature, 2002; 419:890-891.

140. Chaput J, Ichida J, Szostak JW, DNA Polymerase-mediated DNA Synthesis on a TNA Template. J. Am. Chem. Soc., 2003; 125: 856-857 (web publication 12/28/02).

141. Huang Z and Szostak JW. Selective labeling and detection of specific RNAs in an RNA mixture. Anal. Biochem., 2003; 315: 129-133.

142. Vaish NK, Larralde R, Fraley AW, Szostak JW, McLaughlin LW. A novel, modification-dependent ATP-binding aptamer selected from an RNA library incorporating a cationic functionality. Biochemistry, 2003; 42:8842-8851. Published on web 07/03.

143. Szostak JW. Functional information: molecular messages. Nature, 2003; 423:689.

144. Chaput JC and Szostak JW. TNA Synthesis by DNA polymerases. J. Am. Chem. Soc., 2003; 125:856-857. (web publication 07/03).

145. Hanczyc MM, Fujikawa SM, Szostak JW. Experimental Models of Primitive Cellular Compartments: Encapsulation, Growth and Division. Science, 2003; 302:618-622.

146. Huang Z and Szostak JW. Evolution of Aptamers with a New Specificity and New Secondary Structures from an ATP Aptamer. RNA, 2003; 9:1456-1463.

147. Carothers JC, Oestreich S, Davis JH and Szostak JW. Informational complexity and functional activity of RNA structures. J. Am. Chem. Soc. 2004, in press.

148. Monnard, P.-A., Szostak JW. Eutectic Phases In Water Ice: A Microenvironment Conducive To Non-Enzymatic Biopolymer Formation. In press.

149. Chaput JC, Szostak JW. Directed evolution of improved protein stability. Chemistry and Biology, in press.

150. Chen IA and Szostak JW. Generation of pH gradients during fatty acid vesicle growth. submitted.

151. Nilsson MTI, Short GF, Szostak JW, Widersten M. Functional selection of a helix-turn-helix DNA-binding protein by mRNA-display. submitted.

152. Chen IA and Szostak JW. A kinetic study of fatty acid vesicle growth. submitted.

153. Sazani P, Szostak JW. A small RNA aptamer that interacts strongly and specifically with the triphosphate of ATP. submitted.

154. Oestreich S, Carothers JC, Szostak JW. Affinity and specificity in a diverse set of GTP aptamers. In preparation.

155. Larralde R, Szostak JW. Functional optimization of an ATP-binding RNA aptamer by the accretion a second domain. In preparation.

156. Chen IA, Szostak JW. Systems-level properties of model protocells and the emergence of Darwinian evolution. In preparation.

157. Plummer KA, Carothers JM, Yoshimura M, Szostak JW and Verdine GL. Creation of a Cell-Orthogonal RNA-Targeting System through Chemical Synthesis, Protein Design and In Vitro Selection. In preparation.