Academic literature on the topic 'Unnatural amino acid mutagenesis'

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Journal articles on the topic "Unnatural amino acid mutagenesis"

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Ravikumar, Yuvaraj, Saravanan Prabhu Nadarajan, Tae Hyeon Yoo, Chong-soon Lee, and Hyungdon Yun. "Unnatural amino acid mutagenesis-based enzyme engineering." Trends in Biotechnology 33, no. 8 (2015): 462–70. http://dx.doi.org/10.1016/j.tibtech.2015.05.002.

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Wang, Feng, Wei Niu, Jiantao Guo, and Peter G. Schultz. "Unnatural Amino Acid Mutagenesis of Fluorescent Proteins." Angewandte Chemie International Edition 51, no. 40 (2012): 10132–35. http://dx.doi.org/10.1002/anie.201204668.

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Wang, Feng, Wei Niu, Jiantao Guo, and Peter G. Schultz. "Unnatural Amino Acid Mutagenesis of Fluorescent Proteins." Angewandte Chemie 124, no. 40 (2012): 10279–82. http://dx.doi.org/10.1002/ange.201204668.

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Chin, Jason W., and Peter G. Schultz. "In Vivo Photocrosslinking with Unnatural Amino Acid Mutagenesis." ChemBioChem 3, no. 11 (2002): 1135–37. http://dx.doi.org/10.1002/1439-7633(20021104)3:11<1135::aid-cbic1135>3.0.co;2-m.

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Wang, Lei, Jianming Xie, Ashok A. Deniz, and Peter G. Schultz. "Unnatural Amino Acid Mutagenesis of Green Fluorescent Protein." Journal of Organic Chemistry 68, no. 1 (2003): 174–76. http://dx.doi.org/10.1021/jo026570u.

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Beene, Darren L., Dennis A. Dougherty, and Henry A. Lester. "Unnatural amino acid mutagenesis in mapping ion channel function." Current Opinion in Neurobiology 13, no. 3 (2003): 264–70. http://dx.doi.org/10.1016/s0959-4388(03)00068-0.

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Daggett, Kelly A., Mark Layer, and T. Ashton Cropp. "A General Method for Scanning Unnatural Amino Acid Mutagenesis." ACS Chemical Biology 4, no. 2 (2009): 109–13. http://dx.doi.org/10.1021/cb800271f.

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Anthony-Cahill, Spencer J., Michael C. Griffith, Christopher J. Noren, Daniel J. Suich, and Peter G. Schultz. "Site-specific mutagenesis with unnatural amino acids." Trends in Biochemical Sciences 14, no. 10 (1989): 400–403. http://dx.doi.org/10.1016/0968-0004(89)90287-9.

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Mendel, David, Jonathan A. Ellman, and Peter G. Schultz. "Construction of a light-activated protein by unnatural amino acid mutagenesis." Journal of the American Chemical Society 113, no. 7 (1991): 2758–60. http://dx.doi.org/10.1021/ja00007a063.

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Rust, Heather L., Venkataraman Subramanian, Graham M. West, Douglas D. Young, Peter G. Schultz, and Paul R. Thompson. "Using Unnatural Amino Acid Mutagenesis To Probe the Regulation of PRMT1." ACS Chemical Biology 9, no. 3 (2014): 649–55. http://dx.doi.org/10.1021/cb400859z.

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Dissertations / Theses on the topic "Unnatural amino acid mutagenesis"

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Mendes, Kimberly Rose Marie. "Catalysis and Regulation of the Allosteric Enzyme Aspartate Transcarbamoylase." Thesis, Boston College, 2010. http://hdl.handle.net/2345/2975.

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Thesis advisor: Evan R. Kantrowitz<br>The understanding of how cells regulate and control all aspects of their function is vital for our ability to intervene when these control mechanisms break down. Almost all modes of cellular regulation can be related in some manner to protein conformational changes such as the quaternary conformational changes of allosteric enzymes that alter enzyme activity to regulate metabolism. The control of metabolic pathways by allosteric enzymes is analogous to a molecular valve with "on" and "off" positions. In the "off" position, flow through the pathway is sever
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Poshtiban, Anahita [Verfasser]. "Gating modules of the AMPA receptor pore domain revealed by unnatural amino acid mutagenesis / Anahita Poshtiban." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2020. http://d-nb.info/1218075902/34.

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Crane, Peter. "Protein based molecular probes by unnatural amino acid incorporation." Thesis, University of Oxford, 2018. http://ora.ox.ac.uk/objects/uuid:772076fc-00f2-4ca7-bfa9-3da1ce7093cb.

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The "tag & modify" strategy for protein modification relies upon the genetic incorporation of an uncommon or unnatural amino acid into a protein backbone, followed by a chemo-selective modification to yield differentially modified proteins. This thesis describes the creation of a protein-based glycoconjugate tool for interrogating biological function. In Chapter 2, the unnatural amino acid, azidohomoalanine was genetically incorporated into a library of distance defined Np276 proteins via a selective pressure incorporation. Methods to prevent the common post translational modification N-termin
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Zheng, Yunan. "Expanding the Scope of Multisite Noncanonical Amino Acid Mutagenesis." Thesis, Boston College, 2018. http://hdl.handle.net/2345/bc-ir:108150.

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Thesis advisor: Abhishek Chatterjee<br>Noncanonical amino acid (ncAA) mutagenesis provides powerful new ways to probe and manipulate protein function both in vitro and in living cells. Increasing the number of ncAAs that can be site-specifically encoded can greatly expand the scope of this promising technology. We aimed to address the challenges that limit the multisite ncAA incorporation technology in both Escherichia coli and mammalian cells. Our work has significantly expanded the scope of this technology through the development of mutually compatible suppression systems and the optimizatio
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Al, Saleem Evan. "Improving unnatural amino acid mutagensis efficiency and selectivity in mammalian cell." Thesis, KTH, Skolan för bioteknologi (BIO), 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-190765.

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Genetically encoded, site-specific incorporation of unnatural amino acids (UAA)into proteins through selective recoding of an amber stop codon provides apowerful route for expressing synthetic proteins in living cells. Recoding of theamber stop codon is achieved by introducing an amber suppressortRNA/synthetase pair orthogonal to the endogenous tRNA complement intocells. Methanosarcina is a methane producing archaea with the unusualcapability of suppressing the stop codon (specifically the amber codon). Bysuppressing the amber codon Methanosarcina facilitate the incorporation of thenon-canonic
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Nguyen, Duy Phuoc. "Unnatural amino acid incorporation via the orthogonal pyrrolysyl-tRNA synthetase/tRNACUA pair." Thesis, University of Cambridge, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.610160.

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Erickson, Sarah. "Using Unnatural Amino Acid Incorporation to Modify and Manipulate Adeno-Associated Virus:." Thesis, Boston College, 2020. http://hdl.handle.net/2345/bc-ir:108955.

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Thesis advisor: Eranthie Weerapana<br>Adeno-Associated Virus (AAV) has been developed into a powerful therapeutic tool - in the last ten years it has acted as a gene-delivery vehicle in several approved therapeutics and many more therapeutics on trial. Despite extensive research, gaps in our understanding of AAV’s infectious cycle still exist, and further development is needed for the creation of improved gene therapy vectors. Technology to incorporate Unnatural Amino Acids (UAAs) into the AAV capsid has recently been developed, and could aid in both furthering our understanding of AAV’s biolo
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Qi, Xin Dervan Peter B. "Unnatural amino acid incorporation to rewrite the genetic code and RNA-peptide interactions /." Diss., Pasadena, Calif. : California Institute of Technology, 2005. http://resolver.caltech.edu/CaltechETD:etd-05272005-133323.

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Liu, Zhihua. "THE DESIGN AND SYNTHESIS OF NOVEL UNNATURAL AMINO ACIDS AND THE DESIGN AND SYNTHESIS OF PEPTIDES & PEPTIDOMIMETICS CONTAINING UNNATURAL AMINO ACIDS FOR THE STUDY OF G-PROTEIN COUPLED RECEPTORS." Diss., The University of Arizona, 2010. http://hdl.handle.net/10150/204274.

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Nature has gifted peptides as important modulators in the human body, but these types of molecules often have not been favored when we were looking for therapeutic agents. The poor bioavailability, fast degradation and until recent high manufacturing costs of some bioactive peptides lowered their potential usage in the health industry. Under these circumstances, unnatural amino acids were developed as indispensible tools providing enormous support to peptide science. By incorporating proper unnatural amino acids into a peptide or protein, we now can significantly improve peptide's or protein's
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Lee, Meng Huee. "Studies on ketoacid-dependent dioxygenases involved in amino acid metabolism." Thesis, University of Oxford, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.362049.

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Book chapters on the topic "Unnatural amino acid mutagenesis"

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Liu, Jia, and T. Ashton Cropp. "Experimental Methods for Scanning Unnatural Amino Acid Mutagenesis." In Methods in Molecular Biology. Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-331-8_11.

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Kim, Robin Y., and Harley T. Kurata. "Site-Directed Unnatural Amino Acid Mutagenesis to Investigate Potassium Channel Pharmacology in Xenopus laevis Oocytes." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7362-0_19.

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Chakraborty, Anirban, Abhishek Mazumder, Miaoxin Lin, et al. "Site-Specific Incorporation of Probes into RNA Polymerase by Unnatural-Amino-Acid Mutagenesis and Staudinger–Bertozzi Ligation." In Methods in Molecular Biology. Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2392-2_6.

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Maitre, L., P. R. Hedwall, and P. C. Waldmeier. "α-Methyldopa, An Unnatural Aromatic Amino Acid." In Novartis Foundation Symposia. John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720059.ch19.

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Minchev, S., H. Nedev, N. Stoyanov, N. Sofroniev, and D. Efremova. "Synthesis of enkephalins containing unnatural amino acid residues." In Peptides 1990. Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3034-9_261.

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Bahera, Basanta Kumara, Ram Prasad, and Shyambhavee Behera. "Unnatural Amino Acid and its Incorporation in Protein." In Life Sciences Industry. Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-2051-5_4.

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Radel, Peggy A., and Stephen B. Kahl. "Enantioselective Synthesis of an Unnatural Amino Acid, L-Carboranylalanine." In Advances in Neutron Capture Therapy. Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2978-1_57.

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Smider, Vaughn. "Unnatural Amino Acid Antibody Conjugates as Next Generation Biologics." In Resistance to Targeted Anti-Cancer Therapeutics. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-7654-2_9.

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Furuta, Takumi. "Biaryl Amino Acids and Their Surrogates: A Unique Class of Unnatural Amino Acid." In Designed Molecular Space in Material Science and Catalysis. Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-1256-4_6.

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Watts, R. Edward, and Anthony C. Forster. "Update on Pure Translation Display with Unnatural Amino Acid Incorporation." In Ribosome Display and Related Technologies. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-61779-379-0_20.

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Conference papers on the topic "Unnatural amino acid mutagenesis"

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Vrabel, Milan, Emine Kaya, and Thomas Carell. "Incorporation of unnatural amino acids into proteins for click chemistry." In XVth Symposium on Chemistry of Nucleic Acid Components. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2011. http://dx.doi.org/10.1135/css201112487.

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Silva, Maísa de Carvalho, Lariza Laura De Oliveira, and Renato Tinós. "Optimization of Expanded Genetic Codes via Genetic Algorithms." In XV Encontro Nacional de Inteligência Artificial e Computacional. Sociedade Brasileira de Computação - SBC, 2018. http://dx.doi.org/10.5753/eniac.2018.4440.

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In the last decades, researchers have proposed the use of genetically modified organisms that utilize unnatural amino acids, i.e., amino acids other than the 20 amino acids encoded in the standard genetic code. Unnatural amino acids have been incorporated into genetically engineered organisms for the development of new drugs, fuels and chemicals. When new amino acids are incorporated, it is necessary to modify the standard genetic code. Expanded genetic codes have been created without considering the robustness of the code. The objective of this work is the use of genetic algorithms (GAs) for
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Katti, Kalpana S., Dinesh R. Katti, and Avinash H. Ambre. "Unnatural Amino Acids Modified Clays for Design of Scaffolds for Bone Tissue Engineering." In ASME 2010 First Global Congress on NanoEngineering for Medicine and Biology. ASMEDC, 2010. http://dx.doi.org/10.1115/nemb2010-13242.

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Here, we incorporate the results of our new “altered phase theory” (Sikdar et al. 2008a) into design of new polymer clay nanocomposites (PCNs) for bone biomaterials applications. Montmorillonite (MMT) clay was modified using unnatural amino acids as potentially new biocompatible modifiers. The longer carbon chain structures of the unnatural amino acids are expected to enhance non bonded interactions with clay as well as maintaining the usefulness of functional groups of natural amino acids. The specific choice of amino acids is based on both the antibacterial activity reported in literature an
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Kimoto, Michiko, Tsuneo Mitsui, Yoko Harada, Akira Sato, Shigeyuki Yokoyama, and Ichiro Hirao. "Site-specific incorporation of fluorescent 2-amino-6-(2-thienyl)purine into RNA by transcription using an unnatural base pair system." In XIVth Symposium on Chemistry of Nucleic Acid Components. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2008. http://dx.doi.org/10.1135/css200810355.

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Gitsov, Ivan. "“Synthesis of unnatural poly(amino acid)s and their dendritic derivatives by polymer-enhanced laccase complexes”." In 2015 41st Annual Northeast Biomedical Engineering Conference (NEBEC). IEEE, 2015. http://dx.doi.org/10.1109/nebec.2015.7117036.

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Pittman, Debra D., Louise C. Wasley, Beth L. Murray, Jack H. Wang, and Randal J. Kaufman. "ANALYSIS OF STRUCTURAL REQUIREMENTS FOR FACTOR VIII FUNCTION USING SITE-DIRECTED MUTAGENESIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644044.

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Factor VIII (fVIII) functions in the intrinsic pathway of coagulation as the cofactor for Factor IXa proteolytic activation of Factor X. fVIII contains multiple sites which are susceptible to cleavage by thrombin, Factor Xa, and activate) protein C. Proteolytic cleavage is required for cofactor activity and may be responsible for inactivation of cofactor activity. In order to identify the role ofthe individual cleavages of fVIII in its activation and inactivation, site-directed DNA mediated mutagenesis of fVIII was performed and the altered forms of fVIII produced and characterized. Conversion
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VOVIS, G. F., J. MAO, R. BROEZE, et al. "AMINO ACID CHANGES AT LYS-158 THAT ALTER THE SENSITIVITY OF SCUPA TO CLEAVAGE BY PLASMIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644417.

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Plasmin converts Scu-PA to two-chain urokinase by hydrolyzing the lys-158/ile-159 peptide bond. Using site directed mutagenesis, the codon at amino acid position 158 was changed from one that codes for lysine to one that codes for either alanine, glutamic acid, or methionine. These DNA constructions were expressed and amplified in Chinese hamster ovary cells. The resulting protein products were isolated and characterized ip vitro. Under conditions where Scu-PA is completely converted by plasmin to two chain urokinase, none of these derivatives were cleaved by plasmin. However, all of these mol
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Lord, S. T. "DIRECTED MUTAGENESIS OF HUMAN FIBRINOGEN: Aα CHAIN SUBSTITUTIONS THAT ALTER THROMBIN CLEAVAGE AND ANTIBODY RECOGNITION". У XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642887.

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The initial event in fibrin clot formation is the thrombin catalized cleavage of the Aa chain of fibrinogen between Argl6 and Glyl7, releasing fibrinopeptide A. Previous data indicate that most of the information required for thrombin recognition and cleavage of the Aa chain lies within the amino terminal 51 residue CNBr fragment. In order to use protein engineering techniques to study the interaction of thrombin with the Aa chain, we have constructed a plasmid expression vector which encodes a tripartite protein consisting of amino acids 1-50 of the Aa chain of human fibrinogen followed by 60
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Ashok Kumar, A., Margaret Insley, Jay Gambee, Sharon J. Busby, and Kathleen L. Berkner. "SITE SPECIFIC MUTAGENESIS WITHIN THE GLA-DOMAIN OF HUMAN FACTOR IX." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644079.

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Factor IX, a plasma protein, plays a critical role in blood coagulation. The biological activity of factor IX as well as several other plasma proteins depends on the presence of gamma-carboxy glutamic acid (Gla) residues in their amino terminal region. In vitro mutagenesis has been used to selectively replace Gla residues of factor IX with aspartic acid (Asp) residues in order to establish the contribution of individual as well as paired Gla residues to the normal functioning of the protein. These substitutions were made at positions 7, 15, 20 and 26 in human factor IX. In addition, residue nu
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Kaufman, Randal J., Debra D. Pittman, Louise C. Wasley, W. Barry Foster, Godfrey W. Amphlett, and Alan R. Giles. "DIRECTED MUTAGENESIS IN THE STUDY OF THE REQUIREMENTS FOR FACTOR VIII ACTIVITY IN VITRO AND IN VIVO." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644769.

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Factor VIII is a high molecular weight plasma glycoprotein that functions in the blood clotting cascade as the cofactor for factor DCa proteolytic activation of factor X. Factor VIII does not function proteolytically in this reaction hut itself can be proteolytically activated by other coagulation enzymes such as factor Xa and thrombin. In the plasma, factor VIII exists as a 200 kDa amino-terminal fragment in a metal ion stabilized complex with a 76 kDa carboxy-terminal fragment. The isolation of the cENA for human factor VIII provided the deduced primary amino acid sequence of factor VIIT and
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Reports on the topic "Unnatural amino acid mutagenesis"

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Jones, Anne K. Engineering Oxidoreductases: Utilization of an Unnatural Amino Acid to Create Artificial Hydrogenases. Defense Technical Information Center, 2011. http://dx.doi.org/10.21236/ada557996.

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Lester, Henry A. Nicotinic Receptor Binding Site Probed with Unnatural Amino Acid Incorporation in Intact Cells. Defense Technical Information Center, 1995. http://dx.doi.org/10.21236/ada299991.

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