A curated list of targeted optimized promiscuous ketoreductases (TOP-K)

UCSF Chimera—A visualization system for exploratory research and analysis

Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 46,061

Highly accurate protein structure prediction with AlphaFold

Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764

Cd-hit: a fast program for clustering and comparing large sets of protein or nucleotide sequences

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Three-dimensional Epigenome Statistical Model: Genome-wide Chromatin Looping Prediction

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Complete set of ORF clones of Escherichia coli ASKA library (A Complete Set of E. coli K-12 ORF Archive): Unique Resources for Biological Research

Kitagawa, M., Ara, T., Arifuzzaman, M., Ioka-Nakamichi, T., Inamoto, E., Toyonaga, H., & Mori, H. (2006) · DNA Research · doi:10.1093/dnares/dsi012 · Cited by 1,388

Short-chain dehydrogenases/reductases (SDR)

Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzàlez‐Duarte, R., Jeffery, J., & Ghosh, D. (1995) · Biochemistry · doi:10.1021/bi00018a001 · Cited by 1,241

Catalytic promiscuity and the evolution of new enzymatic activities

O’Brien, P., & Herschlag, D. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(99)80033-7 · Cited by 731

ElemCor: accurate data analysis and enrichment calculation for high-resolution LC-MS stable isotope labeling experiments

Du, D., Tan, L., Wang, Y., Peng, B., Weinstein, J. N., Wondisford, F. E., Su, X., & Lorenzi, P. L. (2019) · BMC Bioinformatics · doi:10.1186/s12859-019-2669-9 · Cited by 554

Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins

Závodszky, P., Kardos, J., Svingor, Á., & Petsko, G. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7406 · Cited by 526

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative

Persson, B., Kallberg, Y., Bray, J. E., Bruford, E. A., Dellaporta, S. L., Favia, A. D., Duarte, R. G., Jörnvall, H., Kavanagh, K. L., Kedishvili, N. Y., et al. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.10.040 · Cited by 397

Update on the aldehyde dehydrogenase gene (ALDH) superfamily

Jackson, B. C., Brocker, C. N., Thompson, D. C., Black, W., Vasiliou, K., Nebert, D. W., & Vasiliou, V. (2011) · Human Genomics · doi:10.1186/1479-7364-5-4-283 · Cited by 357

Structural flexibility and protein adaptation to temperature: Molecular dynamics analysis of malate dehydrogenases of marine molluscs

Dong, Y., Liao, M., Meng, X., & Somero, G. N. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718910115 · Cited by 319

Relationship of protein flexibility to thermostability

Vihinen, M. (1987) · Protein Engineering Design and Selection · doi:10.1093/protein/1.6.477 · Cited by 302

iStable: off-the-shelf predictor integration for predicting protein stability changes

Chen, C.-W., Lin, J., & Chu, Y.-W. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-s2-s5 · Cited by 236

Round, round we go – strategies for enzymatic cofactor regeneration

Mordhorst, S., & Andexer, J. N. (2020) · Natural Product Reports · doi:10.1039/d0np00004c · Cited by 216

Deep Dive into Machine Learning Models for Protein Engineering

Xu, Y., Verma, D., Sheridan, R. P., Liaw, A. I., Ma, J., Marshall, N., McIntosh, J. A., Sherer, E. C., Svetnik, V., & Johnston, J. M. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00073 · Cited by 210

The refined three-dimensional structure of 3α, 20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases

Ghosh, D., Wawrzak, Z., Weeks, C. M., Duax, W. L., & Erman, M. (1994) · Structure · doi:10.1016/s0969-2126(00)00064-2 · Cited by 202

Classification of the short‐chain dehydrogenase/reductase superfamily using hidden Markov models

Kallberg, Y., Oppermann, U. C. T., & Persson, B. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07656.x · Cited by 181

ProteinNet: a standardized data set for machine learning of protein structure

AlQuraishi, M. (2019) · BMC Bioinformatics · doi:10.1186/s12859-019-2932-0 · Cited by 147

Highly efficient synthesis of chiral alcohols with a novel NADH-dependent reductase from Streptomyces coelicolor

Wang, L., Li, C., Ni, Y., Zhang, J., Liu, X., & Xu, J. (2011) · Bioresource Technology · doi:10.1016/j.biortech.2011.04.046 · Cited by 144

Recent trends and novel concepts in cofactor-dependent biotransformations

Kara, S., Schrittwieser, J. H., Hollmann, F., & Ansorge‐Schumacher, M. B. (2013) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-013-5441-5 · Cited by 141

A critical review of five machine learning-based algorithms for predicting protein stability changes upon mutation

Fang, J. (2019) · Briefings in Bioinformatics · doi:10.1093/bib/bbz071 · Cited by 140

The Plant Short-Chain Dehydrogenase (SDR) superfamily: genome-wide inventory and diversification patterns

Moummou, H., Kallberg, Y., Tonfack, L. B., Persson, B., & van der Rest, B. (2012) · BMC Plant Biology · doi:10.1186/1471-2229-12-219 · Cited by 134

The Crystal Structure of 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase from Comamonas testosteroni Shows a Novel Oligomerization Pattern within the Short Chain Dehydrogenase/Reductase Family

Grimm, C., Maser, E., Möbus, E., Klebe, G., Reuter, K., & Ficner, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m007559200 · Cited by 107

PredyFlexy: flexibility and local structure prediction from sequence

de Brevern, A. G., Bornot, A., Craveur, P., Etchebest, C., & Gelly, J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks482 · Cited by 102

Stereoselective Enzymatic Synthesis of Chiral Alcohols with the Use of a Carbonyl Reductase from Candida m agnoliae with Anti-Prelog Enantioselectivity

Zhu, D., Yang, Y., & Hua, L. (2006) · The Journal of Organic Chemistry · doi:10.1021/jo0603328 · Cited by 102

Co-expression of 3-ketoacyl-ACP reductase and polyhydroxyalkanoate synthase genes induces PHA production in Escherichia coli HB101 strain

Taguchi, K., Aoyagi, Y., Matsusaki, H., Fukui, T., & Doi, Y. (1999) · FEMS Microbiology Letters · doi:10.1016/s0378-1097(99)00215-3 · Cited by 98

Supervised machine learning algorithms for protein structure classification

Jain, P., Garibaldi, J. M., & Hirst, J. D. (2009) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2009.04.004 · Cited by 95

Structural and Functional Analysis of A-Type Ketoreductases from the Amphotericin Modular Polyketide Synthase

Zheng, J., Taylor, C. A., Piasecki, S. K., & Keatinge‐Clay, A. T. (2010) · Structure · doi:10.1016/j.str.2010.04.015 · Cited by 93

Current knowledge of the multifunctional 17β-hydroxysteroid dehydrogenase type 1 (HSD17B1)

He, W., Misra, G., Li, T., Wang, R., & Lin, S. (2016) · Gene · doi:10.1016/j.gene.2016.04.031 · Cited by 78

Increased Flexibility as a Strategy for Cold Adaptation

Olufsen, M., Smalås, A. O., Moe, E., & Brandsdal, B. O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500948200 · Cited by 78

Discovery of a Switch Between Prelog and Anti-Prelog Reduction toward Halogen-Substituted Acetophenones in Short-Chain Dehydrogenase/Reductases

Qin, F., Qin, B. Y., Zhang, W., Liu, Y., Su, X., Zhu, T., Ouyang, J., Guo, J., Li, Y., Zhang, F., et al. (2018) · ACS Catalysis · doi:10.1021/acscatal.8b00807 · Cited by 77

How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation

Glasner, M. E., Truong, D. P., & Morse, B. C. (2019) · FEBS Journal · doi:10.1111/febs.15185 · Cited by 76

Impact and relevance of alcohol dehydrogenase enantioselectivities on biotechnological applications

Koesoema, A. A., Standley, D. M., Senda, T., & Matsuda, T. (2020) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-020-10440-2 · Cited by 75

MEDUSA: Prediction of Protein Flexibility from Sequence

Meersche, Y. V., Cretin, G., de Brevern, A. G., Gelly, J., & Galochkina, T. V. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166882 · Cited by 72

Fundamentals of Molecular Evolution

Choudhuri, S. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-410471-6.00002-5 · Cited by 63

Approaching boiling point stability of an alcohol dehydrogenase through computationally-guided enzyme engineering

Aalbers, F. S., Fürst, M. J. L. J., Rovida, S., Trajković, M., Castellanos, J. R. G., Bartsch, S., Vogel, A., Mattevi, A., & Fraaije, M. W. (2020) · eLife · doi:10.7554/elife.54639 · Cited by 60

Structural and Stereochemical Analysis of a Modular Polyketide Synthase Ketoreductase Domain Required for the Generation of a cis-Alkene

Bonnett, S. A., Whicher, J. R., Kancharla, P., Florova, G., Smith, J. L., & Reynolds, K. A. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.04.014 · Cited by 59

Subdivision of the MDR superfamily of medium-chain dehydrogenases/reductases through iterative hidden Markov model refinement

Hedlund, J., Jörnvall, H., & Persson, B. (2010) · BMC Bioinformatics · doi:10.1186/1471-2105-11-534 · Cited by 56

Establishment of a yeast-based VLP platform for antigen presentation

Wetzel, D., Rolf, T., Suckow, M., Kranz, A., Barbian, A., Chan, J.-A., Leitsch, J., Weniger, M., Jenzelewski, V., Kouskousis, B. P., et al. (2018) · Microbial Cell Factories · doi:10.1186/s12934-018-0868-0 · Cited by 56

Redesigning alcohol dehydrogenases/reductases for more efficient biosynthesis of enantiopure isomers

Zhang, R., Xu, Y., & Xiao, R. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.08.002 · Cited by 51

The Short‐chain Dehydrogenase/Reductase Engineering Database (SDRED): A classification and analysis system for a highly diverse enzyme family

Gräff, M., Buchholz, P. C. F., Stockinger, P., Bommarius, B., Bommarius, A. S., & Pleiss, J. (2019) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.25666 · Cited by 50

Gene Duplications Are At Least 50 Times Less Frequent than Gene Transfers in Prokaryotic Genomes

Tria, F. D. K., & Martin, W. F. (2021) · Genome Biology and Evolution · doi:10.1093/gbe/evab224 · Cited by 48

Use of the anti-Prelog stereospecific alcohol dehydrogenase from Leifsonia and Pseudomonas for producing chiral alcohols

Itoh, N. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5619-5 · Cited by 48

Mechanisms of Gene Duplication and Translocation and Progress towards Understanding Their Relative Contributions to Animal Genome Evolution

Ramos, O. M., & Ferrier, D. E. K. (2012) · International Journal of Evolutionary Biology · doi:10.1155/2012/846421 · Cited by 42

A Method for Prediction of Thermophilic Protein Based on Reduced Amino Acids and Mixed Features

Feng, C., Ma, Z., Yang, D., Li, X., Zhang, J., & Li, Y. (2020) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2020.00285 · Cited by 42

Identification, Cloning, and Characterization of a Novel Ketoreductase from the Cyanobacterium Synechococcus sp. Strain PCC 7942

Hölsch, K., Havel, J., Haslbeck, M., & Weuster‐Botz, D. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.00925-08 · Cited by 40

Vehicles, Replicators, and Intercellular Movement of Genetic Information: Evolutionary Dissection of a Bacterial Cell

Jalasvuori, M. (2012) · International Journal of Evolutionary Biology · doi:10.1155/2012/874153 · Cited by 38

Enzyme promiscuity prediction using hierarchy-informed multi-label classification

Visani, G. M., Hughes, M. C., & Hassoun, S. (2021) · Bioinformatics · doi:10.1093/bioinformatics/btab054 · Cited by 36

Genome-Wide Identification and Characterization of Short-Chain Dehydrogenase/Reductase (SDR) Gene Family in Medicago truncatula

Yu, S., Sun, Q., Wu, J., Zhao, P., Sun, Y., & Guo, Z. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179498 · Cited by 33

Purification, characterization, cDNA cloning and expression of a novel ketoreductase from Zygosaccharomyces rouxii

Costello, C. A., Payson, R., Menke, M. A., Larson, J. L., Brown, K. A., Tanner, J. E., KAISER, R. E., Hershberger, C. L., & Zmijewski, M. J. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01608.x · Cited by 31

Diversity and Evolutionary Analysis of Iron-Containing (Type-III) Alcohol Dehydrogenases in Eukaryotes

Gaona‐López, C., Julián‐Sánchez, A., & Riveros‐Rosas, H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166851 · Cited by 30

Molecular Modeling and Site-Directed Mutagenesis Reveal the Benzylisoquinoline Binding Site of the Short-Chain Dehydrogenase/Reductase Salutaridine Reductase

Geißler, R., Brandt, W., & Ziegler, J. (2007) · PLANT PHYSIOLOGY · doi:10.1104/pp.106.095166 · Cited by 29

A flexible lid controls access to the active site in 1,3,8‐trihydroxynaphthalene reductase

Andersson, A., Jordan, D. B., Schneider, G., & Lindqvist, Y. (1997) · FEBS Letters · doi:10.1016/s0014-5793(96)01382-8 · Cited by 29

Promiscuous Ligands from Experimentally Determined Structures, Binding Conformations, and Protein Family-Dependent Interaction Hotspots

Gilberg, E., Gütschow, M., & Bajorath, J. (2019) · ACS Omega · doi:10.1021/acsomega.8b03481 · Cited by 26

Directed evolution of a carbonyl reductase LsCR for the enantioselective synthesis of (1S)-2-chloro-1-(3,4-difluorophenyl) ethanol

Liu, H., Weng, C., Xu, S., Li, S., Wang, Y., & Zheng, Y. (2022) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2022.105991 · Cited by 24

Prediction of Different Classes of Promiscuous and Nonpromiscuous Compounds Using Machine Learning and Nearest Neighbor Analysis

Blaschke, T., Miljković, F. N., & Bajorath, J. (2019) · ACS Omega · doi:10.1021/acsomega.9b00492 · Cited by 22

A strategy to identify a ketoreductase that preferentially synthesizes pharmaceutically relevant (S)-alcohols using whole-cell biotransformation

Haq, S. F., Shanbhag, A. P., Karthikeyan, S., Hassan, I., Thanukrishnan, K., Ashok, A., Sukumaran, S., Ramaswamy, S., Bharatham, N., Datta, S., et al. (2018) · Microbial Cell Factories · doi:10.1186/s12934-018-1036-2 · Cited by 21

Asymmetric synthesis of a fluoxetine precursor with an artificial fusion protein of a ketoreductase and a formate dehydrogenase

Sührer, I., Haslbeck, M., & Castiglione, K. (2014) · Process Biochemistry · doi:10.1016/j.procbio.2014.06.001 · Cited by 21

FabG: from a core to circumstantial catalyst

Shanbhag, A. P. (2019) · Biotechnology Letters · doi:10.1007/s10529-019-02678-2 · Cited by 20

Dimerization and enzymatic activity of fungal 17β-hydroxysteroid dehydrogenase from the short-chain dehydrogenase/reductase superfamily

Kristan, K., Deluca, D., Adamski, J., Stojan, J., & Rižner, T. L. (2005) · BMC Biochemistry · doi:10.1186/1471-2091-6-28 · Cited by 19

The rarity of gene shuffling in conserved genes

Conant, G. C., & Wagner, A. (2005) · Genome biology · doi:10.1186/gb-2005-6-6-r50 · Cited by 19

Elucidating Substrate Promiscuity within the FabI Enzyme Family

Freund, G. S., O’Brien, T. E., Vinson, L., Carlin, D. A., Yao, A. I., Mak, W. S., Tagkopoulos, I., Facciotti, M. T., Tantillo, D. J., & Siegel, J. B. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00400 · Cited by 19

Structure-guided design of Serratia marcescens short-chain dehydrogenase/reductase for stereoselective synthesis of (R)-phenylephrine

Liu, J.-S., Kuan, Y.-C., Tsou, Y., Lin, T.-Y., Hsu, W.-H., Yang, M., Lin, J., & Wang, W. (2018) · Scientific Reports · doi:10.1038/s41598-018-19235-y · Cited by 16

Binding of NADP+ triggers an open-to-closed transition in a mycobacterial FabG β-ketoacyl-ACP reductase

Blaise, M., van Wyk, N., Roquet, F., Guérardel, Y., & Kremer, L. (2017) · Biochemical Journal · doi:10.1042/bcj20161052 · Cited by 16

Pseudosterase activity-based specific detection of human serum albumin on gel

Kumar, D., Bhattacharyya, R., & Banerjee, D. (2020) · Talanta · doi:10.1016/j.talanta.2020.121906 · Cited by 14

Thermostability of Proteins Revisited Through Machine Learning Methodologies: From Nucleotide Sequence to Structure

Chakravorty, D., Khan, M. F., & Patra, S. (2015) · Current Biotechnology · doi:10.2174/2211550105666151222183232 · Cited by 12

Keratin protein property based classification of mammals and non-mammals using machine learning techniques

Banerjee, A. K., Ravi, V., Murty, U. S., Shanbhag, A. P., & Prasanna, V. L. (2013) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2013.04.007 · Cited by 11

Industrial light at the end of the iron‐containing (group III) alcohol dehydrogenase tunnel

Shanbhag, A. P., Ghatak, A., & Rajagopal, S. (2022) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2376 · Cited by 10

Delineating Substrate Diversity of Disparate Short-Chain Dehydrogenase Reductase from Debaryomyces hansenii

Ghatak, A., Bharatham, N., Shanbhag, A. P., Datta, S., & Venkatraman, J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0170202 · Cited by 10

1-Naphthyl acetate: A chromogenic substrate for the detection of erythrocyte acetylcholinesterase activity

Chowdhary, S., Bhattacharyya, R., & Banerjee, D. (2018) · Biochimie · doi:10.1016/j.biochi.2018.09.002 · Cited by 8

The Structural Flexibility of Cold- and Warm-Adapted Enzymes (Endonucleases I) by Molecular Dynamics Simulation

Benrezkallah, D., Sediki, H., & Krallafa, A. M. (2020) · International Electronic Conference on Synthetic Organic Chemistry (ECSOC) · doi:10.3390/ecsoc-24-08387 · Cited by 5

Structure of a short-chain dehydrogenase/reductase fromBacillus anthracis

Hou, J., Wojciechowska, K., Zheng, H., Chruszcz, M., Cooper, D. R., Cymborowski, M., Skarina, T., Gordon, E., Luo, H., Savchenko, A. V., et al. (2012) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309112017939 · Cited by 5

Domain swapping between FabGs deciphers the structural determinant for in-solution oligomerization and substrate binding

Biswas, R., Singh, B. K., Dutta, D., Basak, A., & Das, A. K. (2018) · Biophysical Chemistry · doi:10.1016/j.bpc.2018.03.003 · Cited by 2

Supervised learning of protein thermal stability using sequence mining and distribution statistics of network centralityPreprint

Sharma, A., Bagler, G., & Bera, D. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/777177 · Cited by 1

Enzymatic degradation of mycotoxin patulin by a short-chain dehydrogenase/reductase from Bacillus subtilis and its application in apple juice

Niu, J., Ma, B., Shen, J., Zhu, H., Lu, Z., Lu, Z., Lü, F., & Ping, Z. (2024) · Food Microbiology · doi:10.1016/j.fm.2024.104676 · Cited by 15

Identification and Application of Novel Patulin-Degrading Enzymes from Bacillus subtilis 168

Niu, J., Zhu, H., Shen, J., Ma, B., Chi, H., Lu, Z., Lü, F., & Ping, Z. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.4c06999 · Cited by 9

Cancer to Cataracts: The Mechanistic Impact of Aldo-Keto Reductases in Chronic Diseases

Shanbhag, A. P., & Bhowmik, P. (2024) · The Yale Journal of Biology and Medicine · doi:10.59249/vtbv6559 · Cited by 4

Identification and functional characterization of a novel CaSrpA enzyme for selenite reduction and selenium nanoparticle formation

Hou, X., Gu, J., Chen, J., Ullah, H., Mamtimin, T., Wang, X., Li, X., Jiang, Y., Fan, J., Han, H., et al. (2025) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2025.138486 · Cited by 3

Exploring the catalytic diversity of two short-chain dehydrogenases/reductases from Stachybotrys chartarum

Wang, Y.-X., Cai, X.-Y., Liu, J., Han, Y.-T., Sui, S., Chen, D., Xie, K.-B., Chen, R.-D., & Dai, J.-G. (2023) · Figshare · doi:10.6084/m9.figshare.24885560

Multi‐faceted Set‐up of a Diverse Ketoreductase Library Enables the Synthesis of Pharmaceutically‐relevant Secondary Alcohols

Voß, M., Küng, R., Hayashi, T., Jonczyk, M. S., Niklaus, M., Iding, H., Wetzl, D., & Buller, R. (2020) · ChemCatChem · doi:10.1002/cctc.202001871 · Cited by 22

Induction of NAD+-dependent alcohol dehydrogenase with activity towards long-chain aliphatic alcohols in thermophilic organisms

Alarcón, L. A., Acevedo, F., & Frontaura, A. I. (2009) · New Biotechnology · doi:10.1016/j.nbt.2009.06.255

Delineating Substrate Diversity of Disparate Short-Chain Dehydrogenase Reductase from Debaryomyces hansenii

Ghatak, A., Bharatham, N., Shanbhag, A. P., Datta, S., & Venkatraman, J. (2017) · PLoS ONE · doi:10.1371/journal.pone.0170202 · Cited by 10

Fluorogenic kinetic assay for high-throughput discovery of stereoselective ketoreductases relevant to pharmaceutical synthesis

Thai, Y.-C., Szekrényi, A., Qi, Y., Black, G. W., Charnock, S. J., & Fessner, W. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.05.024 · Cited by 13