Almost all pubs indexed by and available from PubMed: (type "Forster AC")
Citations per paper are available from Google Scholar: (type "Forster AC")

Bao, L, Karpenko, V V, Forster, A C. Rate-limiting hydrolysis in ribosomal release reactions revealed by ester activation. J. Biol. Chem., in press, 2022.

Forster, A C. Tales of the unexpected in Sidney Altman's lab. RNA, in press, 2022.

Liljeruhm, J, Leppik, M, Bao, L, Truu, T, Calvo-Noriega, M, Freyer, N S, Liiv, A, Wang, J, Crespo Blanco, R, Ero, R, Remme, J, Forster, A C. Plasticity and conditional essentiality of modification enzymes for domain V of Escherichia coli 23S ribosomal RNA. RNA, 28, 796-807, 2022. doi:10.1261/rna.079096.121

Forster, A C. Revisiting the extinction of the RNA world. Biochemistry, 61, 749-751, 2022.

Doerr, A, Foschepoth, D, Forster, A C, Danelon, C. In vitro synthesis of 32 translation-factor proteins from a single template reveals impaired ribosomal processivity. Sci. Rep. 11:1898, 1-12, 2021.
Open access at

Bao, L, Menon, P N K, Liljeruhm, J, Forster, A C. Overcoming chromoprotein limitations by engineering a red fluorescent protein. Anal. Biochem. 611:113936, 1-8, 2020
Open access at

Vogel, C, Gynnå, A, Yuan, J, Bao, L, Liljeruhm, J, Forster, A C. Rationally-designed Spot 42 RNAs with an inhibition/toxicity profile advantageous for engineering E. coli. Engineering Reports, 2:3, e12126, 1-10, 2020
Our front cover and open access reprint:

Liljeruhm, J, Wang, J, Kwiatkowski, M, Sabari, S, Forster, A C. Kinetics of D-amino acid incorporation in translation. ACS Chem. Biol., DOI: 10.1021/acschembio.8b00952, 2019
Open access reprint:

Wang, J, Forster A C. Ribosomal incorporation of unnatural amino acids: lessons and improvements from fast kinetics studies. Curr. Opin. Chem. Biol. 46:180-187, 2018.
Open access reprint:

Liljeruhm, J, Funk, S K, Tietscher, S, Edlund, A D, Jamal, S, Wistrand-Yuen, P, Dyrhage, K, Gynnå, A, Ivermark, K, Lövgren, J, Törnblom, V, Virtanen, A, Lundin, E R, Wistrand-Yuen, E, Forster, A C. Engineering a palette of eukaryotic chromoproteins for bacterial synthetic biology. J. Biol. Eng. 12:8, 1-10, 2018.

Shepherd, T R, Du, L, Liljeruhm, J, Samudyata, Wang, J, Sjödin, M O D, Wetterhall, M, Yomo, T, Forster A C. De novo design and synthesis of a 30-cistron translation-factor module. Nucleic Acids Res 45, 10895-10905, 2017.

Wang, J, Forster A C. Translational roles of the C75 2'OH in an in vitro tRNA transcript at the ribosomal A, P and E sites. Scientific Reports 7, 6709, 1-8, 2017. 

Wang, J, Kwiatkowski, M, Forster A C. Ribosomal peptide syntheses from activated substrates reveal rate limitation by an unexpected step at the peptidyl site. J Am Chem Soc 138, 15587-15595, 2016.

Wang, J, Kwiatkowski, M, Forster A C. Kinetics of tRNAPyl-mediated amber suppression in E. coli translation reveals unexpected limiting steps and competing reactions. Biotechnol Bioeng 113, 1552-1559, 2016.

Wang, J, Kwiatkowski, M, Forster A C. Kinetics of ribosome-catalyzed polymerization using artificial aminoacyl-tRNA substrates clarifies inefficiencies and improvements. ACS Chem. Biol. 10, 2187-2192, 2015.

Kwiatkowski, M, Wang, J, Forster, A C. Facile synthesis of N-acyl-aminoacyl-pCpA for preparation of mischarged fully ribo tRNA. Bioconjugate Chem. 25, 2086-2091, 2014.

Liljeruhm, J, Gullberg, E, Forster A C. Synthetic biology: A lab manual. World Scientific Press, 204 pp, 2014.

Wang, J, Kwiatkowski, M, Pavlov, M Y, Ehrenberg, M, Forster, A C. Peptide formation by N-methyl amino acids in translation is hastened by higher pH and tRNAPro. ACS Chem. Biol. 9, 1303-1311 and front cover, 2014.

Ieong, K-W, Pavlov, M Y, Kwiatkowski, M, Ehrenberg, M., Forster, A C. A tRNA body with high affinity for EF-Tu hastens ribosomal incorporation of unnatural amino acids. RNA 20, 632-643, 2014.

Punekar, A, Liljeruhm, J, Shepherd, T R, Forster, A C, Selmer, M. Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ. Nucleic Acids Res 41, 9537-9548, 2013.

Quax, T E F, Wolf, Y I, Koehorst, J J, Wurtzel, O, van der Oost, R, Ran, W, Blombach, F, Makarova, K S, Brouns, S J J, Forster, A C, Wagner, E G H, Sorek, R, Koonin, E V, van der Oost, J. Differential translation tunes uneven production of operon-encoded proteins. Cell Reports 4, 938-944, 2013.

Ieong, K-W, Pavlov, M Y, Kwiatkowski, M, Forster, A C(corresponding), Ehrenberg, M. Inefficient delivery but fast peptide bond formation of unnatural L-aminoacyl-tRNAs in translation, J Am Chem Soc 134, 17955-17962, 2012.

Punekar, A, Shepherd, T R, Liljeruhm, J, Forster, A C, Selmer, M. Crystal structure of RlmM, the 2'O-ribose methyltransferase for C2498 of E. coli 23S rRNA. Nucleic Acids Res, 40, 10507-10520, 2012.

Forster, A C. Synthetic biology challenges long-held hypotheses in translation, codon bias and transcription. Biotech J, 7, 835-845, 2012.

Forster, A C, Lee, S Y. Editorial: NextGen SynBio has arrived... Biotech J, 7, 827, 2012.

Du, L, Villarreal, S, Forster, A C. Multigene expression in vivo: supremacy of large versus small terminators for T7 RNA polymerase. Biotechnol Bioeng, 109, 1043-1050, 2012.

Wang, H H, Huang P-Y, Xu G, Haas W, Marblestone A, Li J, Gygi S P, Forster A C, Jewett M C, Church G M. Multiplexed in vivo His-tagging of enzyme pathways for in vitro single-pot multienzyme catalysis. ACS Synthetic Biology, 1, 43-52, 2012

Watts, R E, Forster A C. Update on pure translation display with unnatural amino acid incorporation. Methods in Molecular Biology, 805, 349-365, 2012

Gao, R, Forster, A C. Changeability of individual domains of an aminoacyl-tRNA in polymerization by the ribosome. FEBS Lett, 584(1), 99-105, 2010

Jewett, M C, Forster, A C. Update on designing and building minimal cells. Current Opinion in Biotechnology, 21, 697-703, 2010

Watts, R E, Forster, A C. Chemical models of peptide formation in translation. Biochemistry, 49, 2177-2185, 2010

Du, L, Gao, R, Forster, A C. Engineering multigene expression in vitro and in vivo with small terminators for T7 RNA polymerase. Biotechnol Bioeng, 104, 1189-1196, 2009

Forster, A C. Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome. Nucleic Acids Res, 37, 3747-3755, 2009

Pavlov, M Y, Watts, R E, Tan, Z, Cornish, V W, Ehrenberg, M, Forster, A C. Slow peptide bond formation by proline and other N-alkylamino acids in translation. Proc Natl Acad Sci U S A, 106(1), 50-4, 2009

Forster, A C, Church, G M. Synthetic biology projects in vitro. Genome Res, 17(1), 1-6 and front cover, 2007

Zhang, B, Tan, Z, Gartenmann Dickson, L, Nalam, M N L, Cornish, V W, Forster, A C. Specificity of Translation for N-Alkyl Amino Acids. J Am Chem Soc, 129(37), 11316-11317, 2007

Forster, A C, Church, G M. Towards synthesis of a minimal cell. Mol Syst Biol, 2(45), 1-10, 2006

Forster, A C. Engineering translation: A nano-review. Methods, 36(3), 225-6, 2005

Tan, Z, Blacklow, S C, Cornish, V W, Forster, A C. De novo genetic codes and pure translation display. Methods, 36(3), 279-90, 2005

Forster, A C, Cornish, V W, Blacklow, S C. Pure translation display. Anal Biochem, 333(2), 358-64, 2004

Tan, Z, Forster, A C, Blacklow, S C, Cornish, V W. Amino acid backbone specificity of the Escherichia coli translation machinery. J Am Chem Soc, 126(40), 12752-3, 2004

Forster, A C, Tan, Z, Nalam, M N L, Lin, H, Qu, H, Cornish, V W, Blacklow, S C. Programming peptidomimetic syntheses by translating genetic codes designed de novo. Proc Natl Acad Sci U S A, 100(11), 6353-7, 2003

Forster, A C, Weissbach, H, Blacklow, S C. A simplified reconstitution of mRNA-directed peptide synthesis: activity of the epsilon enhancer and an unnatural amino acid. Anal Biochem, 297(1), 60-70, 2001

Li, E, Beard, C, Forster, A C, Bestor, T H, Jaenisch, R. DNA methylation, genomic imprinting, and mammalian development. Cold Spring Harb Symp Quant Biol, 58, 297-305, 1993

Forster, A C, Altman, S. External guide sequences for an RNA enzyme. Science, 249(4970), 783-6, 1990

Forster, A C, Altman, S. Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes. Cell, 62(3), 407-9, 1990

Forster, A C, Davies, C, Hutchins, C J, Symons, R H. Characterization of self-cleavage of viroid and virusoid RNAs. Methods Enzymol, 181, 583-607, 1990

McInnes, J L, Forster, A C, Skingle, D C, Symons, R H. Preparation and uses of photobiotin. Methods Enzymol, 184, 588-600, 1990

Forster, A C, Davies, C, Sheldon, C C, Jeffries, A C, Symons, R H. Self-cleaving viroid and newt RNAs may only be active as dimers. Nature, 334(6179), 265-7, 1988

McInnes, J L, Forster, A C, Symons, R H. Photobiotin-labelled DNA and RNA hybridization probes. Methods in Molecular Biology, 4, 401-414, 1988

Forster, A C, Jeffries, A C, Sheldon, C C, Symons, R H. Structural and ionic requirements for self-cleavage of virusoid RNAs and trans self-cleavage of viroid RNA. Cold Spring Harb Symp Quant Biol, 52, 249-59, 1987

Forster, A C, Symons, R H. Self-cleavage of virusoid RNA is performed by the proposed 55-nucleotide active site. Cell, 50(1), 9-16, 1987

Forster, A C, Symons, R H. Self-cleavage of plus and minus RNAs of a virusoid and a structural model for the active sites. Cell, 49(2), 211-20, 1987

Symons, R H, Hutchins, C J, Forster, A C, Rathjen, P D, Keese, P, Visvader, J E. Self-cleavage of RNA in the replication of viroids and virusoids. J Cell Sci Suppl, 7, 303-18, 1987

Hutchins, C J, Rathjen, P D, Forster, A C, Symons, R H. Self-cleavage of plus and minus RNA transcripts of avocado sunblotch viroid. Nucleic Acids Res, 14(9), 3627-40, 1986

Forster, A C, McInnes, J L, Skingle, D C, Symons, R H. Non-radioactive hybridization probes prepared by the chemical labelling of DNA and RNA with a novel reagent, photobiotin. Nucleic Acids Res, 13(3), 745-61, 1985

Visvader, J E, Forster, A C, Symons, R H. Infectivity and in vitro mutagenesis of monomeric cDNA clones of citrus exocortis viroid indicates the site of processing of viroid precursors. Nucleic Acids Res, 13(16), 5843-56, 1985

Last modified: 2022-09-13