Arnold, Frances

Combined from CaltechAUTHORS

• Alfonzo, Edwin and Hanley, Deirdre, et el. (2024) Biocatalytic Synthesis of α-Amino Esters via Nitrene C–H Insertion; Journal of the American Chemical Society; Vol. 146; No. 40; 27267–27273; 10.1021/jacs.4c09989
• Hanley, Deirdre and Li, Zi-Qi, et el. (2024) Stereospecific Enzymatic Conversion of Boronic Acids to Amines; Journal of the American Chemical Society; 10.1021/jacs.4c04190
• Almhjell, Patrick J. and Johnston, Kadina E., et el. (2024) The β-subunit of tryptophan synthase is a latent tyrosine synthase; Nature Chemical Biology; 10.1038/s41589-024-01619-z
• Mao, Runze and Gao, Shilong, et el. (2024) Biocatalytic, enantioenriched primary amination of tertiary C–H bonds; Nature Catalysis; Vol. 7; No. 5; 585-592; PMCID PMC11238567; 10.1038/s41929-024-01149-w
• Yang, Jason and Li, Francesca-Zhoufan, et el. (2024) Opportunities and Challenges for Machine Learning-Assisted Enzyme Engineering; ACS Central Science; Vol. 10; No. 2; 226-241; PMCID PMC10906252; 10.1021/acscentsci.3c01275
• Sarai, Nicholas S. and Fulton, Tyler J., et el. (2024) Directed evolution of enzymatic silicon-carbon bond cleavage in siloxanes; Science; Vol. 383; No. 6681; 438-443; 10.1126/science.adi5554
• Rogge, Torben and Zhou, Qingyang, et el. (2024) Iron Heme Enzyme-Catalyzed Cyclopropanations with Diazirines as Carbene Precursors: Computational Explorations of Diazirine Activation and Cyclopropanation Mechanism; Journal of the American Chemical Society; 10.1021/jacs.3c06030
• Yang, Jason and Ducharme, Julie, et el. (2024) Correction to "DeCOIL: Optimization of Degenerate Codon Libraries for Machine Learning-Assisted Protein Engineering"; ACS Synthetic Biology; Vol. 13; No. 2; 692; 10.1021/acssynbio.3c00751
• Wackelin, Daniel J. and Mao, Runze, et el. (2024) Enzymatic Assembly of Diverse Lactone Structures: An Intramolecular C–H Functionalization Strategy; Journal of the American Chemical Society; 10.1021/jacs.3c11722
• Qin, Zi-Yang and Gao, Shilong, et el. (2023) Biocatalytic Construction of Chiral Pyrrolidines and Indolines via Intramolecular C(sp³)–H Amination; ACS Central Science; Vol. 9; No. 12; 2333-2338; PMCID PMC10755850; 10.1021/acscentsci.3c00516
• Das, Anuvab and Long, Yueming, et el. (2023) Expanding Biocatalysis for Organosilane Functionalization: Enantioselective Nitrene Transfer to Benzylic Si–C–H Bonds; ACS Catalysis; Vol. 14; 148-152; 10.1021/acscatal.3c05370
• Mao, Runze and Taylor, Doris Mia, et el. (2023) Biocatalytic, stereoconvergent alkylation of (Z/E)-trisubstituted silyl enol ethers; Nature Synthesis; 10.1038/s44160-023-00431-2
• Gao, Shilong and Das, Anuvab, et el. (2023) Enzymatic Nitrogen Incorporation Using Hydroxylamine; Journal of the American Chemical Society; Vol. 145; No. 37; 20196-20201; PMCID PMC10560455; 10.1021/jacs.3c08053
• Mao, Runze and Wackelin, Daniel J., et el. (2023) Enantio- and Diastereoenriched Enzymatic Synthesis of 1,2,3-Polysubstituted Cyclopropanes from (Z/E)-Trisubstituted Enol Acetates; Journal of the American Chemical Society; Vol. 145; No. 29; 16176-16185; PMCID PMC10528827; 10.1021/jacs.3c04870
• Mao, Runze and Wackelin, Daniel J., et el. (2023) Enantio- and Diastereoenriched Enzymatic Synthesis of 1,2,3-Polysubstituted Cyclopropanes from (Z/E)-Trisubstituted Enol Acetates; PMCID PMC10120758; 10.21203/rs.3.rs-2802333/v1
• Danelius, Emma and Porter, Nicholas J., et el. (2023) MicroED Structure of a Protoglobin Reactive Carbene Intermediate; Journal of the American Chemical Society; Vol. 145; No. 13; 7159-7165; PMCID PMC10080679; 10.1021/jacs.2c12004
• Calvó-Tusell, Carla and Liu, Zhen, et el. (2023) Reversing the enantioselectivity of enzymatic carbene N–H insertion through mechanism-guided protein engineering; 10.26434/chemrxiv-2022-f02xh
• Athavale, Soumitra V. and Gao, Shilong, et el. (2023) Enzymatic Nitrogen Insertion into Unactivated C–H Bonds; 10.26434/chemrxiv-2022-w8sg3
• Danelius, Emma and Porter, Nicholas J., et el. (2023) MicroED structure of a protoglobin reactive carbene intermediate; 10.1101/2022.10.18.512604
• Zhang, Juner and Maggiolo, Ailiena O., et el. (2023) Chemodivergent C(sp³)–H and C(sp²)–H cyanomethylation using engineered carbene transferases; Nature Catalysis; Vol. 6; No. 2; 152-160; PMCID PMC9983643; 10.1038/s41929-022-00908-x
• Schaus, Lucas and Das, Anuvab, et el. (2023) Protoglobin-Catalyzed Formation of cis-Trifluoromethyl-Substituted Cyclopropanes by Carbene Transfer; Angewandte Chemie International Edition; Vol. 62; No. 4; Art. No. e202208936; PMCID PMC9894577; 10.1002/anie.202208936
• Alfonzo, Edwin and Das, Anuvab, et el. (2022) New additions to the arsenal of biocatalysts for noncanonical amino acid synthesis; Current Opinion in Green and Sustainable Chemistry; Vol. 38; Art. No. 100701; PMCID PMC9770695; 10.1016/j.cogsc.2022.100701
• Zhang, Juner and Maggiolo, Ailiena O., et el. (2022) Chemodivergent C(sp³)–H and C(sp²)–H Cyanomethylation Using Engineered Carbene Transferases; 10.26434/chemrxiv-2022-z6pkw
• Athavale, Soumitra V. and Gao, Shilong, et el. (2022) Enzymatic Nitrogen Insertion into Unactivated C-H Bonds; Journal of the American Chemical Society; Vol. 144; No. 41; 19097-19105; PMCID PMC9612832; 10.1021/jacs.2c08285
• Porter, Nicholas J. and Danelius, Emma, et el. (2022) Biocatalytic Carbene Transfer Using Diazirines; Journal of the American Chemical Society; Vol. 144; No. 20; 8892-8896; PMCID PMC9205183; 10.1021/jacs.2c02723
• Molina, Rosana S. and Rix, Gordon, et el. (2022) In vivo hypermutation and continuous evolution; Nature Reviews Methods Primers; Vol. 2; Art. No. 36; 10.1038/s43586-022-00119-5
• Miller, David C. and Lal, Ravi G., et el. (2022) Biocatalytic One-Carbon Ring Expansion of Aziridines to Azetidines via a Highly Enantioselective [1,2]-Stevens Rearrangement; Journal of the American Chemical Society; Vol. 144; No. 11; 4739-4745; PMCID PMC9022672; 10.1021/jacs.2c00251
• Wittmann, Bruce J. and Johnston, Kadina E., et el. (2022) evSeq: Cost-Effective Amplicon Sequencing of Every Variant in a Protein Library; ACS Synthetic Biology; Vol. 11; No. 3; 1313-1324; 10.1021/acssynbio.1c00592
• Arnold, Frances H. (2022) Innovation by evolution: bringing new chemistry to life; Biophysical Journal; Vol. 121; No. 3; 177a; 10.1016/j.bpj.2021.11.1846
• Liu, Zhen and Qin, Zi-Yang, et el. (2022) An Enzymatic Platform for Primary Amination of 1-Aryl-2-alkyl Alkynes; Journal of the American Chemical Society; Vol. 144; No. 1; 80-85; PMCID PMC8765727; 10.1021/jacs.1c11340
• Miller, David C. and Athavale, Soumitra V., et el. (2022) Combining chemistry and protein engineering for new-to-nature biocatalysis; Nature Synthesis; Vol. 1; No. 1; 18-23; PMCID PMC8995090; 10.1038/s44160-021-00008-x
• Athavale, Soumitra V. and Chen, Kai, et el. (2021) Engineering Enzymes for New‐to‐Nature Carbene Chemistry; ISBN 9783527347995; Transition Metal-Catalyzed Carbene Transformations; 95-138; 10.1002/9783527829170.ch4
• Liu, Zhen and Calvó-Tusell, Carla, et el. (2021) Dual-function enzyme catalysis for enantioselective carbon–nitrogen bond formation; Nature Chemistry; Vol. 13; No. 12; 1166-1172; 10.1038/s41557-021-00794-z
• Wu, Zachary and Johnston, Kadina E., et el. (2021) Protein sequence design with deep generative models; Current Opinion in Chemical Biology; Vol. 65; 18-27; 10.1016/j.cbpa.2021.04.004
• Wittmann, Bruce J. and Yue, Yisong, et el. (2021) Informed training set design enables efficient machine learning-assisted directed protein evolution; Cell Systems; Vol. 12; No. 11; 1026-1045; 10.1016/j.cels.2021.07.008
• Athavale, Soumitra V. and Gao, Shilong, et el. (2021) Biocatalytic, Intermolecular C−H Bond Functionalization for the Synthesis of Enantioenriched Amides; Angewandte Chemie International Edition; Vol. 60; No. 47; 24864-24869; PMCID PMC8578410; 10.1002/anie.202110873
• Watkins-Dulaney, Ella J. and Dunham, Noah P., et el. (2021) Asymmetric Alkylation of Ketones Catalyzed by Engineered TrpB; Angewandte Chemie International Edition; Vol. 60; No. 39; 21412-21417; PMCID PMC8440449; 10.1002/anie.202106938
• Wittmann, Bruce J. and Johnston, Kadina E, et el. (2021) Advances in machine learning for directed evolution; Current Opinion in Structural Biology; Vol. 69; 11-18; 10.1016/j.sbi.2021.01.008
• Arnold, Frances (2021) Innovation by evolution: bringing new chemistry to life; Acta Crystallographica Section A; Vol. A77; No. Supplement; Art. No. a70; 10.1107/S0108767321099293
• Sarai, Nicholas S. and Levin, Benjamin J., et el. (2021) Biocatalytic Transformations of Silicon—the Other Group 14 Element; ACS Central Science; Vol. 7; No. 6; 944-953; PMCID PMC8227617; 10.1021/acscentsci.1c00182
• Liu, Zhen and Arnold, Frances H. (2021) New-to-nature chemistry from old protein machinery: carbene and nitrene transferases; Current Opinion in Biotechnology; Vol. 69; 43-51; PMCID PMC8225731; 10.1016/j.copbio.2020.12.005
• Garcia-Borràs, Marc and Kan, S. B. Jennifer, et el. (2021) Origin and Control of Chemoselectivity in Cytochrome c Catalyzed Carbene Transfer into Si–H and N–H bonds; Journal of the American Chemical Society; Vol. 143; No. 18; 7114-7123; PMCID PMC9292473; 10.1021/jacs.1c02146
• Yang, Yang and Arnold, Frances H. (2021) Navigating the Unnatural Reaction Space: Directed Evolution of Heme Proteins for Selective Carbene and Nitrene Transfer; Accounts of Chemical Research; Vol. 54; No. 5; 1209-1225; PMCID PMC7931446; 10.1021/acs.accounts.0c00591
• Watkins-Dulaney, Ella and Straathof, Sabine, et el. (2021) Tryptophan Synthase: Biocatalyst Extraordinaire; ChemBioChem; Vol. 22; No. 1; 5-16; PMCID PMC7935429; 10.1002/cbic.202000379
• Pluchinsky, Adam J. and Wackelin, Daniel J., et el. (2020) High Throughput Screening with SAMDI Mass Spectrometry for Directed Evolution; Journal of the American Chemical Society; Vol. 142; No. 47; 19804-19808; 10.1021/jacs.0c07828
• Rix, Gordon and Watkins-Dulaney, Ella J., et el. (2020) Scalable continuous evolution for the generation of diverse enzyme variants encompassing promiscuous activities; Nature Communications; Vol. 11; Art. No. 5644; PMCID PMC7648111; 10.1038/s41467-020-19539-6
• Dunham, Noah P. and Arnold, Frances H. (2020) Nature's Machinery, Repurposed: Expanding the Repertoire of Iron-Dependent Oxygenases; ACS Catalysis; Vol. 10; No. 20; 12239-12255; PMCID PMC7710332; 10.1021/acscatal.0c03606
• Bähr, Susanne and Brinkmann-Chen, Sabine, et el. (2020) Selective Enzymatic Oxidation of Silanes to Silanols; Angewandte Chemie International Edition; Vol. 59; No. 36; 15507-15511; PMCID PMC7511438; 10.1002/anie.202002861
• Wu, Zachary and Yang, Kevin K., et el. (2020) Signal Peptides Generated by Attention-Based Neural Networks; ACS Synthetic Biology; Vol. 9; No. 8; 2154-2161; 10.1021/acssynbio.0c00219
• Wittmann, Bruce J. and Knight, Anders M., et el. (2020) Diversity-Oriented Enzymatic Synthesis of Cyclopropane Building Blocks; ACS Catalysis; Vol. 10; No. 13; 7112-7116; PMCID PMC7709968; 10.1021/acscatal.0c01888
• Jia, Zhi-Jun and Gao, Shilong, et el. (2020) Enzymatic Primary Amination of Benzylic and Allylic C(sp³)–H Bonds; Journal of the American Chemical Society; Vol. 142; No. 23; 10279-10283; 10.1021/jacs.0c03428
• Zhou, Andrew Z. and Chen, Kai, et el. (2020) Enzymatic Lactone-Carbene C‒H Insertion to Build Contiguous Chiral Centers; ACS Catalysis; Vol. 10; No. 10; 5393-5398; 10.1021/acscatal.0c01349
• Chen, Kai and Arnold, Frances H. (2020) Engineering cytochrome P450s for enantioselective cyclopropenation of internal alkynes; Journal of the American Chemical Society; Vol. 142; No. 15; 6891-6895; 10.1021/jacs.0c01313
• Chen, Kai and Arnold, Frances H. (2020) Engineering new catalytic activities in enzymes; Nature Catalysis; Vol. 3; No. 3; 203-213; 10.1038/s41929-019-0385-5
• Yang, Yang and Arnold, Frances Hamilton (2020) Enantioselective C-H amination via directed evolution of cytochrome P450 enzymes
• Goldberg, Nathaniel and Knight, Anders M., et el. (2020) Nitrene Transfer Catalyzed by a Non-Heme Iron Enzyme and Enhanced by Non-Native Small-Molecule Cofactors; 10.26434/chemrxiv.10062044.v1
• Watkins, Ella J. and Almhjell, Patrick J., et el. (2020) Direct enzymatic synthesis of a deep-blue fluorescent noncanonical amino acid from azulene and serine; ChemBioChem; Vol. 21; No. 1-2; 80-83; PMCID PMC6980211; 10.1002/cbic.201900497
• Dick, Markus and Sarai, Nicholas S., et el. (2019) Tailoring Tryptophan Synthase TrpB for Selective Quaternary Carbon Bond Formation; Journal of the American Chemical Society; Vol. 141; No. 50; 19817-19822; PMCID PMC6939453; 10.1021/jacs.9b09864
• Goldberg, Nathaniel W. and Knight, Anders M., et el. (2019) Nitrene Transfer Catalyzed by a Non-Heme Iron Enzyme and Enhanced by Non-Native Small-Molecule Ligands; Journal of the American Chemical Society; Vol. 141; No. 50; 19585-19588; PMCID PMC6924163; 10.1021/jacs.9b11608
• Bedbrook, Claire N. and Yang, Kevin K., et el. (2019) Machine learning-guided channelrhodopsin engineering enables minimally-invasive optogenetics; Nature Methods; Vol. 16; No. 11; 1176-1184; PMCID PMC6858556; 10.1038/s41592-019-0583-8
• Yang, Yang and Cho, Inha, et el. (2019) An enzymatic platform for the asymmetric amination of primary, secondary and tertiary C(sp³)–H bonds; Nature Chemistry; Vol. 11; No. 11; 987-993; PMCID PMC6998391; 10.1038/s41557-019-0343-5
• Arnold, Frances H. (2019) Innovation by Evolution: Bringing New Chemistry to Life (Nobel Lecture); Angewandte Chemie International Edition; Vol. 58; No. 41; 14420-14426; 10.1002/anie.201907729
• Brandenberg, Oliver F. and Miller, David C., et el. (2019) Engineering Chemoselectivity in Hemoprotein-Catalyzed Indole Amidation; ACS Catalysis; Vol. 9; No. 9; 8271-8275; PMCID PMC6959474; 10.1021/acscatal.9b02508
• Romney, David K. and Sarai, Nicholas S., et el. (2019) Nitroalkanes as Versatile Nucleophiles for Enzymatic Synthesis of Noncanonical Amino Acids; ACS Catalysis; Vol. 9; No. 9; 8726-8730; PMCID PMC7709965; 10.1021/acscatal.9b02089
• Yang, Kevin K. and Wu, Zachary, et el. (2019) Machine-learning-guided directed evolution for protein engineering; Nature Methods; Vol. 16; No. 8; 687-694; 10.1038/s41592-019-0496-6
• Zhang, Juner and Huang, Xiongyi, et el. (2019) Enantiodivergent α-Amino C–H Fluoroalkylation Catalyzed by Engineered Cytochrome P450s; Journal of the American Chemical Society; Vol. 141; No. 25; 9798-9802; PMCID PMC6666315; 10.1021/jacs.9b04344
• Brandenberg, Oliver F. and Chen, Kai, et el. (2019) Directed Evolution of a Cytochrome P450 Carbene Transferase for Selective Functionalization of Cyclic Compounds; Journal of the American Chemical Society; Vol. 141; No. 22; 8989-8995; 10.1021/jacs.9b02931
• Wu, Zachary and Kan, S. B. Jennifer, et el. (2019) Machine learning-assisted directed protein evolution with combinatorial libraries; Proceedings of the National Academy of Sciences of the United States of America; Vol. 116; No. 18; 8852-8858; PMCID PMC6500146; 10.1073/pnas.1901979116
• Arnold, Frances Hamilton (2019) Newest advances in enzymatic carbene- and nitrene-transfer catalysis
• Arnold, Frances Hamilton (2019) Advances in directed protein evolution
• Zhang, Ruijie K. and Huang, Xiongyi, et el. (2019) Selective C-H bond functionalization with engineered heme proteins: new tools to generate complexity; Current Opinion in Chemical Biology; Vol. 49; 67-75; PMCID PMC6461521; 10.1016/j.cbpa.2018.10.004
• Cho, Inha and Jia, Zhi-Jun, et el. (2019) Genetically Tunable Enzymatic C‒H Amidation for Lactam Synthesis
• Cho, Inha and Prier, Christopher K., et el. (2019) Enantioselective Aminohydroxylation of Styrenyl Olefins Catalyzed by an Engineered Hemoprotein; Angewandte Chemie International Edition; Vol. 58; No. 10; 3138-3142; 10.1002/anie.201812968
• Chen, Kai and Huang, Xiongyi, et el. (2019) Engineered Cytochrome c-Catalyzed Lactone-Carbene B–H Insertion; Synlett; Vol. 30; No. 4; 378-382; PMCID PMC6436545; 10.1055/s-0037-1611662
• Huang, Xiongyi and Garcia-Borràs, Marc, et el. (2019) A Biocatalytic Platform for Synthesis of Chiral α-Trifluoromethylated Organoborons; ACS Central Science; Vol. 5; No. 2; 270-276; PMCID PMC6396380; 10.1021/acscentsci.8b00679
• Zhang, Ruijie K. and Chen, Kai, et el. (2019) Enzymatic assembly of carbon–carbon bonds via iron-catalysed sp³ C–H functionalization; Nature; Vol. 565; No. 7737; 67-72; PMCID PMC6440214; 10.1038/s41586-018-0808-5
• Arnold, Frances H. and Strickland, Donna H. (2019) Nobel Prizes 2018; Deutsche Lebensmittel-Rundschau; Vol. 115; No. 1; 40-41
• Almhjell, Patrick J. and Boville, Christina E., et el. (2018) Engineering enzymes for noncanonical amino acid synthesis; Chemical Society Reviews; Vol. 47; No. 24; 8980-8997; PMCID PMC6434697; 10.1039/c8cs00665b
• Chen, Kai and Zhang, Shuo-Qing, et el. (2018) Alternate heme ligation steers activity and selectivity in engineered cytochrome P450-catalyzed carbene transfer reactions; Journal of the American Chemical Society; Vol. 140; No. 48; 16402-16407; 10.1021/jacs.8b09613
• Boville, Christina E. and Scheele, Remkes A., et el. (2018) Engineered biosynthesis of β‐alkyl tryptophan analogs; Angewandte Chemie International Edition; Vol. 57; No. 45; 14764-14768; 10.1002/anie.201807998
• Yang, Kevin K. and Wu, Zachary, et el. (2018) Learned Protein Embeddings for Machine Learning; Bioinformatics; Vol. 34; No. 15; 2642-2648; PMCID PMC6061698; 10.1093/bioinformatics/bty178
• Boville, Christina E. and Romney, David K., et el. (2018) Improved synthesis of 4-cyanotryptophan and other tryptophan analogs in aqueous solvent using variants of TrpB from Thermotoga maritima; Journal of Organic Chemistry; Vol. 83; No. 14; 7447-7452; PMCID PMC6054569; 10.1021/acs.joc.8b00517
• Romney, David K. and Arnold, Frances H., et el. (2018) Chemistry Takes a Bath: Reactions in Aqueous Media; Journal of Organic Chemistry; Vol. 83; No. 14; 7319-7322; 10.1021/acs.joc.8b01412
• Lewis, Russell D. and Garcia-Borràs, Marc, et el. (2018) Catalytic iron-carbene intermediate revealed in a cytochrome c carbene transferase; Proceedings of the National Academy of Sciences of the United States of America; Vol. 115; No. 28; 7308-7313; PMCID PMC6048479; 10.1073/pnas.1807027115
• Buller, Andrew R. and van Roye, Paul, et el. (2018) Directed evolution mimics allosteric activation by stepwise tuning of the conformational ensemble; Journal of the American Chemical Society; Vol. 140; No. 23; 7256-7266; PMCID PMC5999571; 10.1021/jacs.8b03490
• Arnold, Frances H. (2018) Directed Evolution: Bringing New Chemistry to Life; Angewandte Chemie International Edition; Vol. 57; No. 16; 4143-4148; PMCID PMC5901037; 10.1002/anie.201708408
• Brandenberg, Oliver F. and Prier, Christopher K., et el. (2018) Stereoselective Enzymatic Synthesis of Heteroatom-Substituted Cyclopropanes; ACS Catalysis; Vol. 8; No. 4; 2629-2634; 10.1021/acscatal.7b04423
• Chen, Kai and Huang, Xiongyi, et el. (2018) Enzymatic construction of highly strained carbocycles; Science; Vol. 360; No. 6384; 71-75; PMCID PMC6104391; 10.1126/science.aar4239
• Knight, Anders M. and Kan, S. B. Jennifer, et el. (2018) Diverse engineered heme proteins enable stereodivergent cyclopropanation of unactivated alkenes; ACS Central Science; Vol. 4; No. 3; 372-377; PMCID PMC5879470; 10.1021/acscentsci.7b00548
• Zhang, Ruijie K. and Romney, David K., et el. (2018) Directed Evolution of Artificial Metalloenzymes: Bridging Synthetic Chemistry and Biology; ISBN 9783527341788; Artificial Metalloenzymes and MetalloDNAzymes in Catalysis; 137-170; 10.1002/9783527804085.ch5
• Kan, S. B. Jennifer and Huang, Xiongyi, et el. (2017) Genetically programmed chiral organoborane synthesis; Nature; Vol. 552; No. 7683; 132-136; PMCID PMC5819735; 10.1038/nature24996
• Cahn, Jackson K. B. and Brinkmann-Chen, Sabine, et el. (2017) Enzyme Nicotinamide Cofactor Specificity Reversal Guided by Automated Structural Analysis and Library Design; ISBN 978-1-4939-7294-4; Synthetic Metabolic Pathways; 15-26; 10.1007/978-1-4939-7295-1_2
• Bedbrook, Claire N. and Yang, Kevin K., et el. (2017) Machine learning to design integral membrane channelrhodopsins for efficient eukaryotic expression and plasma membrane localization; PLOS Computational Biology; Vol. 13; No. 10; Art. No. e1005786; PMCID PMC5695628; 10.1371/journal.pcbi.1005786
• Hammer, Stephan C. and Kubik, Grzegorz, et el. (2017) Anti-Markovnikov alkene oxidation by metal-oxo–mediated enzyme catalysis; Science; Vol. 358; No. 6360; 215-218; 10.1126/science.aao1482
• Brandenberg, Oliver F. and Fasan, Rudi, et el. (2017) Exploiting and engineering hemoproteins for abiological carbene and nitrene transfer reactions; Current Opinion in Biotechnology; Vol. 47; 102-111; PMCID PMC5617781; 10.1016/j.copbio.2017.06.005
• Hammer, Stephan C. and Knight, Anders M., et el. (2017) Design and Evolution of Enzymes for Non-natural Chemistry; Current Opinion in Green and Sustainable Chemistry; Vol. 7; 23-30; 10.1016/j.cogsc.2017.06.002
• Romney, David K. and Murciano-Calles, Javier, et el. (2017) Unlocking Reactivity of TrpB: A General Biocatalytic Platform for Synthesis of Tryptophan Analogues; Journal of the American Chemical Society; Vol. 139; No. 31; 10769-10776; PMCID PMC5589443; 10.1021/jacs.7b05007
• Romney, David K. and Murciano-Calles, Javier, et el. (2017) Unlocking reactivity of TrpB: a general biocatalytic platform for synthesis of tryptophan analogs; Journal of the American Chemical Society; Vol. 131; No. 39; 10769-10776; PMCID PMC5589443; 10.1021/jacs.7b05007
• Loskot, Steven A. and Romney, David K., et el. (2017) Enantioselective Total Synthesis of Nigelladine A via Late-Stage C–H Oxidation Enabled by an Engineered P450 Enzyme; Journal of the American Chemical Society; Vol. 139; No. 30; 10196-10199; PMCID PMC5679227; 10.1021/jacs.7b05196
• Prier, Christopher K. and Zhang, Ruijie K., et el. (2017) Enantioselective, intermolecular benzylic C–H amination catalysed by an engineered iron-haem enzyme; Nature Chemistry; Vol. 9; No. 7; 629-634; PMCID PMC5555633; 10.1038/nchem.2783
• Romney, David K. and Murciano-Calles, Javier, et el. (2017) Engineered TrpB biocatalysts for the synthesis of tryptophan analogs
• Arnold, Frances H. (2017) New enzymes for green chemistry
• Bedbrook, Claire N. and Rice, Austin J., et el. (2017) Structure-guided SCHEMA recombination generates diverse chimeric channelrhodopsins; Proceedings of the National Academy of Sciences of the United States of America; Vol. 114; No. 13; E2624-E2633; PMCID PMC5380088; 10.1073/pnas.1700269114
• Herwig, Lukas and Rice, Austin J., et el. (2017) Directed Evolution of a Bright Near-Infrared Fluorescent Rhodopsin Using a Synthetic Chromophore; Cell Chemical Biology; Vol. 24; No. 3; 415-425; PMCID PMC5357175; 10.1016/j.chembiol.2017.02.008
• Cahn, Jackson K. B. and Werlang, Caroline A., et el. (2017) A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases; ACS Synthetic Biology; Vol. 6; No. 2; 326-333; PMCID PMC8611728; 10.1021/acssynbio.6b00188
• Murciano-Calles, Javier and Buller, Andrew R., et el. (2017) Directed Evolution of an Allosteric Tryptophan Synthase to Create a Platform for Synthesis of Noncanonical Amino Acids; ISBN 978-3-319-50411-7; Directed Enzyme Evolution: Advances and Applications; 1-16; 10.1007/978-3-319-50413-1_1
• Buller, Andrew R. and van Roye, Paul, et el. (2016) Tryptophan synthase uses an atypical mechanism to achieve substrate specificity; Biochemistry; Vol. 55; No. 51; 7043-7046; PMCID PMC5207025; 10.1021/acs.biochem.6b01127
• Kan, S. B. Jennifer and Lewis, Russell D., et el. (2016) Directed evolution of cytochrome c for carbon–silicon bond formation: Bringing silicon to life; Science; Vol. 354; No. 6315; 1048-1051; PMCID PMC5243118; 10.1126/science.aah6219
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• Shao, Zhixin and Zhao, Huimin, et el. (1998) Random-priming in vitro recombination: an effective tool for directed evolution; Nucleic Acids Research; Vol. 26; No. 2; 681-683; PMCID PMC147287; 10.1093/nar/26.2.681
• Kuchner, Olga and Arnold, Frances H. (1997) Directed evolution of enzyme catalysts; Trends in Biotechnology; Vol. 15; No. 12; 523-530; 10.1016/S0167-7799(97)01138-4
• Moore, Jeffrey C. and Jin, Hua-Ming, et el. (1997) Strategies for the in vitro evolution of protein function: enzyme evolution by random recombination of improved sequences; Journal of Molecular Biology; Vol. 272; No. 3; 336-347; 10.1006/jmbi.1997.1252
• Zhao, Huimin and Arnold, Frances H. (1997) Combinatorial protein design: strategies for screening protein libraries; Current Opinion in Structural Biology; Vol. 7; No. 4; 480-485; 10.1016/S0959-440X(97)80110-8
• Zhao, Huimin and Arnold, Frances H. (1997) Functional and nonfunctional mutations distinguished by random recombination of homologous genes; Proceedings of the National Academy of Sciences of the United States of America; Vol. 94; No. 15; 7997-8000; PMCID PMC21544
• Pack, Daniel W. and Arnold, Frances H. (1997) Langmuir monolayer characterization of metal chelating lipids for protein targeting to membranes; Chemistry and Physics of Lipids; Vol. 86; No. 2; 135-152; 10.1016/s0009-3084(97)02662-5
• Chen, G. and Guan, Z., et el. (1997) A glucose sensing polymer; Abstracts of Papers of the American Chemical Society; Vol. 213; 176-ANYL
• Chen, G. and Guan, Z., et el. (1997) A glucose-sensing polymer; Abstracts of Papers of the American Chemical Society; Vol. 213; 234-PMSE
• Chen, Guohua and Guan, Zhibin, et el. (1997) A glucose-sensing polymer; Nature Biotechnology; Vol. 15; No. 4; 354-357; 10.1038/nbt0497-354
• Zhao, Huimin and Arnold, Frances H. (1997) Optimization of DNA shuffling for high fidelity recombination; Nucleic Acids Research; Vol. 25; No. 6; 1307-1308; PMCID PMC146579; 10.1093/nar/25.6.1307
• Pack, Daniel W. and Chen, Guohua, et el. (1997) A Metal-Chelating Lipid for 2D Protein Crystallization via Coordination of Surface Histidines; Journal of the American Chemical Society; Vol. 119; No. 10; 2479-2487; 10.1021/ja964099e
• Zhao, Huimin and Li, You, et el. (1996) Strategy for the Directed Evolution of a Peptide Ligase; Annals of the New York Academy of Sciences; Vol. 799; No. 1; 1-5; 10.1111/j.1749-6632.1996.tb33169.x
• Shao, Zhixin and Arnold, Frances H. (1996) Engineering new functions and altering existing functions; Current Opinion in Structural Biology; Vol. 6; No. 4; 513-518; 10.1016/S0959-440X(96)80117-5
• Frey, Wolfgang and Schief, William R., Jr., et el. (1996) Two-dimensional protein crystallization via metal-ion coordination by naturally occurring surface histidines; Proceedings of the National Academy of Sciences of the United States of America; Vol. 93; No. 10; 4937-4941; PMCID PMC39383
• Moore, Jeffrey C. and Arnold, Frances H. (1996) Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents; Nature Biotechnology; Vol. 14; No. 4; 458-467; 10.1038/nbt0496-458
• Johnson, R. D. and Wang, Z.-G., et el. (1996) Surface Site Heterogeneity and Lateral Interactions in Multipoint Protein Adsorption; Journal of Physical Chemistry; Vol. 100; No. 12; 5134-5139; 10.1021/jp9523682
• Johnson, Robert D. and Todd, Robert J., et el. (1996) Multipoint binding in metal-affinity chromatography: II. Effect of pH and imidazole on chromatographic retention of engineered histidine-containing cytochromes c; Journal of Chromatography A; Vol. 725; No. 2; 225-235; 10.1016/0021-9673(95)00992-2
• You, L. and Arnold, F. H. (1996) Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide; Protein Engineering; Vol. 9; No. 1; 77-83; 10.1093/protein/9.1.77
• Vidyasankar, Sundaresan and Dhal, Pradeep K., et el. (1995) Review: Selective ligand-exchange adsorbents prepared by template polymerization; Biotechnology and Bioengineering; Vol. 48; No. 5; 431-436; 10.1002/bit.260480504
• Johnson, Robert D. and Arnold, Frances H. (1995) Review: Multipoint binding and heterogeneity in immobilized metal affinity chromatography; Biotechnology and Bioengineering; Vol. 48; No. 5; 437-443; 10.1002/bit.260480505
• Ng, Kingman and Pack, Daniel W., et el. (1995) Engineering Protein-Lipid Interactions: Targeting of Histidine-Tagged Proteins to Metal-Chelating Lipid Monolayers; Langmuir; Vol. 11; No. 10; 4048-4055; 10.1021/la00010a069
• Plunkett, Sean D. and Arnold, Frances H. (1995) Molecularly imprinted polymers on silica: selective supports for high-performance ligand-exchange chromatography; Journal of Chromatography A; Vol. 708; No. 1; 19-29; 10.1016/0021-9673(95)00378-Z
• Sasaki, Darryl Y. and Shnek, Deborah R., et el. (1995) Metal-Induced Dispersion of Lipid Aggregates: A Simple, Selective, and Sensitive Fluorescent Metal Ion Sensor; Angewandte Chemie International Edition; Vol. 34; No. 8; 905-907; 10.1002/anie.199509051
• Johnson, Robert D. and Arnold, Frances H. (1995) The temkin isotherm describes heterogeneous protein adsorption; Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology; Vol. 1247; No. 2; 293-297; 10.1016/0167-4838(95)00006-G
• Shnek, D. R. and Pack, D. W., et el. (1994) Specific Protein Attachment to Artificial Membranes via Coordination to Lipid-Bound Copper(II); Langmuir; Vol. 10; No. 7; 2382-2388; 10.1021/la00019a058
• Arnold, Frances H. and Zhang, Ji-Hu (1994) Metal-mediated protein stabilization; Trends in Biotechnology; Vol. 12; No. 5; 189-192; 10.1016/0167-7799(94)90081-7
• Todd, Robert J. and Johnson, Robert D., et el. (1994) Multiple-site binding interactions in metal-affinity chromatography: I. Equilibrium binding of engineered histidine-containing cytochromes c; Journal of Chromatography A; Vol. 662; No. 1; 13-26; 10.1016/0021-9673(94)85291-x
• Chung, Bong H. and Bailey, Darwin, et el. (1994) Metal affinity partitioning; ISBN 9780121821296; Aqueous Two-Phase Systems; 167-179; 10.1016/0076-6879(94)28017-7
• Arnold, Frances H. and Chen, Keqin, et el. (1993) Engineering Nonaqueous Solvent-Compatible Enzymes; ISBN 9780841225183; Biocatalyst Design for Stability and Specificity; 109-113; 10.1021/bk-1993-0516.ch008
• Umaña, Pablo and Kellis, James T., et el. (1993) Recombinant Protein Stabilization through Engineered Metal-Chelating Sites; ISBN 9780841225183; Biocatalyst Design for Stability and Specificity; 102-108; 10.1021/bk-1993-0516.ch007
• Arnold, Frances H. (1993) Protein engineering for unusual environments; Current Opinion in Biotechnology; Vol. 4; No. 4; 450-455; 10.1016/0958-1669(93)90011-k
• Arnold, F. H. (1993) Engineering proteins for nonnatural environments; FASEB Journal; Vol. 7; No. 9; 744-749; 10.1096/fasebj.7.9.8330682
• Chen, Keqin and Arnold, Frances H. (1993) Tuning the Activity of an Enzyme for Unusual Environments: Sequential Random Mutagenesis of Subtilisin E for Catalysis in Dimethylformamide; Proceedings of the National Academy of Sciences of the United States of America; Vol. 90; No. 6; 5618-5622; PMCID PMC46772
• Mallik, Sanku and Johnson, Robert D., et el. (1993) Selective recognition of bis-imidazoles by complementary bis-metal ion complexes; Journal of the American Chemical Society; Vol. 115; No. 6; 2518-2520; 10.1021/ja00059a063
• Dhal, Pradeep K. and Arnold, Frances H. (1992) Metal-coordination interactions in the template-mediated synthesis of substrate-selective polymers: recognition of bis(imidazole) substrates by copper(II) iminodiacetate containing polymers; Macromolecules; Vol. 25; No. 25; 7051-7059; 10.1021/ma00051a050
• Economou, Chariklia and Chen, Keqin, et el. (1992) Random mutagenesis to enhance the activity of subtilisin in organic solvents: Characterization of Q103R subtilisin E; Biotechnology and Bioengineering; Vol. 39; No. 6; 658-662; 10.1002/bit.260390610
• Martinez, Pascal and Van Dam, Mariana E., et el. (1992) Stabilization of substilisin E in organic solvents by site‐directed mutagenesis; Biotechnology and Bioengineering; Vol. 39; No. 2; 141-147; 10.1002/bit.260390204
• Martinez, Pascal and Van Dam, Mariana E., et el. (1992) Stabilization of substilisin E in organic solvents by site-directed mutagenesis; Biotechnology and Bioengineering; Vol. 39; No. 2; 141-147; 10.1002/bit.260390204
• Chung, Bong Hyun and Arnold, Frances H. (1992) Metal Affinity Partitioning of Phosphoproteins in Aqueous Two-Phase Systems; ISBN 9784431681823; Biochemical Engineering for 2001; 557-559; 10.1007/978-4-431-68180-9_148
• Chen, Keqin and Arnold, Frances H. (1991) Enzyme Engineering for Nonaqueous Solvents: Random Mutagenesis to Enhance Activity of Subtilisin E in Polar Organic Media; Bio/Technology; Vol. 9; No. 11; 1073-1077; 10.1038/nbt1191-1073
• Kellis, James T., Jr. and Todd, Robert J., et el. (1991) Protein Stabilization by Engineered Metal Chelation; Bio/Technology; Vol. 9; No. 10; 994-995; 10.1038/nbt1091-994
• Dhal, Pradeep K. and Arnold, Frances H. (1991) Template-mediated synthesis of metal-complexing polymers for molecular recognition; Journal of the American Chemical Society; Vol. 113; No. 19; 7417-7418; 10.1021/ja00019a046
• Arnold, Frances H. and Haymore, Barry L. (1991) Engineered metal-binding proteins: purification to protein folding; Science; Vol. 252; No. 5014; 1796-1797; 10.1126/science.1648261
• Chen, Keqin and Robinson, Amy C., et el. (1991) Enzyme engineering for nonaqueous solvents. II. Additive effects of mutations on the stability and activity of subtilisin E in polar organic media; Biotechnology Progress; Vol. 7; No. 2; 125-129; 10.1021/bp00008a007
• Suh, Sung-Sup and Haymore, Barry L., et el. (1991) Characterization of His-X_3-His sites in α-helices of synthetic metal-binding bovine somatotropin; Protein Engineering, Design and Selection; Vol. 4; No. 3; 301-305; 10.1093/protein/4.3.301
• Todd, Robert J. and Van Dam, Mariana E., et el. (1991) Cu(II)-Binding properties of a cytochrome c with a synthetic metal-binding site: His-X_3-His in an α-helix; Proteins; Vol. 10; No. 2; 156-161; 10.1002/prot.340100209
• Arnold, Frances H. (1991) Metal-Affinity Separations: A New Dimension in Protein Processing; Bio/Technology; Vol. 9; No. 2; 151-156; 10.1038/nbt0291-151
• Wuenschell, G. E. and Wen, E., et el. (1991) Chiral copper—chelate complexes alter selectivities in metal affinity protein partitioning; Journal of Chromatography A; Vol. 543; 345-354; 10.1016/S0021-9673(01)95786-3
• Arnold, Frances H. (1990) Engineering enzymes for non-aqueous solvents; Trends in Biotechnology; Vol. 8; No. 9; 244-249; 10.1016/0167-7799(90)90186-2
• Suh, S.-S. and Van Dam, M. E., et el. (1990) Novel Metal-Affinity Protein Separations; 10.1021/bk-1990-0427.ch010
• Suh, Sung-Sup and Arnold, Frances H. (1990) A mathematical model for metal affinity protein partitioning; Biotechnology and Bioengineering; Vol. 35; No. 7; 682-690; 10.1002/bit.260350705
• Claeys, Ivan L. and Arnold, Frances H. (1989) Nuclear magnetic relaxation study of hindered rotational diffusion in gels; AIChE Journal; Vol. 35; No. 2; 335-338; 10.1002/aic.690350223
• Arnold, Frances H. and Wolk, Steven, et el. (1987) Structure, dynamics, and thermodynamics of mismatched DNA oligonucleotide duplexes d(CCCAGGG)_2 and d(CCCTGGG)_2; Biochemistry; Vol. 26; No. 13; 4068-4075; 10.1021/bi00387a049
• Arnold, F. H. and Schofield, S. A., et el. (1986) Analytical affinity chromatography: I. Local equilibrium theory and the measurement of association and inhibition constants; Journal of Chromatography A; Vol. 355; 1-12; 10.1016/s0021-9673(01)97299-1
• Arnold, F. H. and Blanch, H. W. (1986) Analytical affinity chromatography: II. Rate theory and the measurement of biological binding kinetics; Journal of Chromatography A; Vol. 355; 13-27; 10.1016/S0021-9673(01)97300-5