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Journal articles on the topic 'Serine hydrolases'

Author: Grafiati

Published: 8 June 2024

Last updated: 31 July 2025

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1

Goss, Allison L., Renee E. Shudick, and R. Jeremy Johnson. "Shifting Mycobacterial Serine Hydrolase Activity Visualized Using Multi-Layer In-Gel Activity Assays." Molecules 29, no. 14 (2024): 3386. http://dx.doi.org/10.3390/molecules29143386.

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The ability of Mycobacterium tuberculosis to derive lipids from the host, store them intracellularly, and then break them down into energy requires a battery of serine hydrolases. Serine hydrolases are a large, diverse enzyme family with functional roles in dormant, active, and reactivating mycobacterial cultures. To rapidly measure substrate-dependent shifts in mycobacterial serine hydrolase activity, we combined a robust mycobacterial growth system of nitrogen limitation and variable carbon availability with nimble in-gel fluorogenic enzyme measurements. Using this methodology, we rapidly an

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2

Nishioka, Tuguhiro, Makoto Iwata, Takuya Imaoka, et al. "A Mono-2-Ethylhexyl Phthalate Hydrolase from a Gordonia sp. That Is Able To Dissimilate Di-2-Ethylhexyl Phthalate." Applied and Environmental Microbiology 72, no. 4 (2006): 2394–99. http://dx.doi.org/10.1128/aem.72.4.2394-2399.2006.

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ABSTRACT Gordonia sp. strain P8219, a strain able to decompose di-2-ethylhexyl phthalate, was isolated from machine oil-contaminated soil. Mono-2-ethylhexyl phthalate hydrolase was purified from cell extracts of this strain. This enzyme was a 32,164-Da homodimeric protein, and it effectively hydrolyzed monophthalate esters, such as monoethyl, monobutyl, monohexyl, and mono-2-ethylhexyl phthalate. The Km and V max values for mono-2-ethylhexyl phthalate were 26.9 ± 4.3 μM and 18.1 ± 0.9 μmol/min · mg protein, respectively. The deduced amino acid sequence of the enzyme exhibited less than 30% hom

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3

Jeremy Johnson, R., Andrew Bartels, Rachel Erkilla, et al. "Proteopedia entry: Mammalian serine hydrolases." Biochemistry and Molecular Biology Education 43, no. 1 (2014): 60–61. http://dx.doi.org/10.1002/bmb.20840.

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4

Botos, Istvan, and Alexander Wlodawer. "The expanding diversity of serine hydrolases." Current Opinion in Structural Biology 17, no. 6 (2007): 683–90. http://dx.doi.org/10.1016/j.sbi.2007.08.003.

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5

Tang, Shan, Adam T. Beattie, Lucie Kafkova, et al. "Mechanism-based traps enable protease and hydrolase substrate discovery." Nature 602, no. 7898 (2022): 701–7. http://dx.doi.org/10.1038/s41586-022-04414-9.

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AbstractHydrolase enzymes, including proteases, are encoded by 2–3% of the genes in the human genome and 14% of these enzymes are active drug targets1. However, the activities and substrate specificities of many proteases—especially those embedded in membranes—and other hydrolases remain unknown. Here we report a strategy for creating mechanism-based, light-activated protease and hydrolase substrate traps in complex mixtures and live mammalian cells. The traps capture substrates of hydrolases, which normally use a serine or cysteine nucleophile. Replacing the catalytic nucleophile with genetic

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6

Liu, Y., M. P. Patricelli, and B. F. Cravatt. "Activity-based protein profiling: The serine hydrolases." Proceedings of the National Academy of Sciences 96, no. 26 (1999): 14694–99. http://dx.doi.org/10.1073/pnas.96.26.14694.

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7

Ross, Matthew K., and Ran Wang. "Expanding the Toolkit for the Serine Hydrolases." Chemistry & Biology 22, no. 7 (2015): 808–9. http://dx.doi.org/10.1016/j.chembiol.2015.07.002.

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8

Hernáez, M. J., E. Andújar, J. L. Ríos, S. R. Kaschabek, W. Reineke, and E. Santero. "Identification of a Serine Hydrolase Which Cleaves the Alicyclic Ring of Tetralin." Journal of Bacteriology 182, no. 19 (2000): 5448–53. http://dx.doi.org/10.1128/jb.182.19.5448-5453.2000.

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ABSTRACT A gene designated thnD, which is required for biodegradation of the organic solvent tetralin by Sphingomonas macrogoltabidus strain TFA, has been identified. Sequence comparison analysis indicated that thnD codes for a carbon-carbon bond serine hydrolase showing highest similarity to hydrolases involved in biodegradation of biphenyl. An insertion mutant defective in ThnD accumulates the ring fission product which results from the extradiol cleavage of the aromatic ring of dihydroxytetralin. The gene product has been purified and characterized. ThnD is an octameric thermostable enzyme

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9

Bernhardt, Peter, Karl Hult, and Romas J. Kazlauskas. "Molecular Basis of Perhydrolase Activity in Serine Hydrolases." Angewandte Chemie International Edition 44, no. 18 (2005): 2742–46. http://dx.doi.org/10.1002/anie.200463006.

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10

Bernhardt, Peter, Karl Hult, and Romas J. Kazlauskas. "Molecular Basis of Perhydrolase Activity in Serine Hydrolases." Angewandte Chemie 117, no. 18 (2005): 2802–6. http://dx.doi.org/10.1002/ange.200463006.

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11

Patočka, Jiří, Kamil Kuča, and Daniel Jun. "Acetylcholinesterase and Butyrylcholinesterase – Important Enzymes of Human Body." Acta Medica (Hradec Kralove, Czech Republic) 47, no. 4 (2004): 215–28. http://dx.doi.org/10.14712/18059694.2018.95.

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The serine hydrolases and proteases are a ubiquitous group of enzymes that is fundamental to many critical lifefunctions. Human tissues have two distinct cholinesterase activities: acetylcholinesterase and butyrylcholinesterase. Acetylcholinesterase functions in the transmission of nerve impulses, whereas the physiological function of butyrylcholinesterase remains unknown. Acetylcholinesterase is one of the crucial enzymes in the central and peripheral nerve system. Organophosphates and carbamates are potent inhibitors of serine hydrolases and well suited probes for investigating the chemical

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12

Chen, Biao, Sha-Sha Ge, Yuan-Chao Zhao, Chong Chen, and Song Yang. "Activity-based protein profiling: an efficient approach to study serine hydrolases and their inhibitors in mammals and microbes." RSC Advances 6, no. 114 (2016): 113327–43. http://dx.doi.org/10.1039/c6ra20006k.

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13

Berger, Natascha, Hanna Allerkamp, and Christian Wadsack. "Serine Hydrolases in Lipid Homeostasis of the Placenta-Targets for Placental Function?" International Journal of Molecular Sciences 23, no. 12 (2022): 6851. http://dx.doi.org/10.3390/ijms23126851.

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The metabolic state of pregnant women and their unborn children changes throughout pregnancy and adapts to the specific needs of each gestational week. These adaptions are accomplished by the actions of enzymes, which regulate the occurrence of their endogenous substrates and products in all three compartments: mother, placenta and the unborn. These enzymes determine bioactive lipid signaling, supply, and storage through the generation or degradation of lipids and fatty acids, respectively. This review focuses on the role of lipid-metabolizing serine hydrolases during normal pregnancy and in p

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14

Martínez, Virginia, Fernando de la Peña, Javier García-Hidalgo, Isabel de la Mata, José Luis García, and María Auxiliadora Prieto. "Identification and Biochemical Evidence of a Medium-Chain-Length Polyhydroxyalkanoate Depolymerase in the Bdellovibrio bacteriovorus Predatory Hydrolytic Arsenal." Applied and Environmental Microbiology 78, no. 17 (2012): 6017–26. http://dx.doi.org/10.1128/aem.01099-12.

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ABSTRACTThe obligate predatorBdellovibrio bacteriovorusHD100 shows a large set of proteases and other hydrolases as part of its hydrolytic arsenal needed for its predatory life cycle. We present genetic and biochemical evidence that open reading frame (ORF) Bd3709 ofB. bacteriovorusHD100 encodes a novel medium-chain-length polyhydroxyalkanoate (mcl-PHA) depolymerase (PhaZBd). The primary structure of PhaZBdsuggests that this enzyme belongs to the α/β-hydrolase fold family and has a typical serine hydrolase catalytic triad (serine-histidine-aspartic acid) in agreement with other PHA depolymeras

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15

Schirmer, Andreas, Claudia Matz, and Dieter Jendrossek. "Substrate specificities of poly(hydroxyalkanoate)-degrading bacteria and active site studies on the extracellular poly(3-hydroxyoctanoic acid) depolymerase of Pseudomonas fluorescens GK13." Canadian Journal of Microbiology 41, no. 13 (1995): 170–79. http://dx.doi.org/10.1139/m95-184.

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The isolation of poly(3-hydroxyoctanoic acid)- and poly(6-hydroxyhexanoic acid)-degrading bacteria yielded 28 strains with abilities to degrade various polymers. The most versatile strains hydrolyzed five different polyesters comprising short chain length and medium chain length poly(hydroxyalkanoates). The new isolates together with previously isolated poly(hydroxyalkanoate)-degrading bacteria were classified into 11 groups with respect to their polymer-degrading specificities. All PHA depolymerases studied so far have been characterized by the lipase consensus sequence Gly-X-Ser-X-Gly in the

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16

Bachovchin, Daniel A., and Benjamin F. Cravatt. "The pharmacological landscape and therapeutic potential of serine hydrolases." Nature Reviews Drug Discovery 11, no. 1 (2012): 52–68. http://dx.doi.org/10.1038/nrd3620.

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17

van Rantwijk, Fred, and Roger A. Sheldon. "Enantioselective acylation of chiral amines catalysed by serine hydrolases." Tetrahedron 60, no. 3 (2004): 501–19. http://dx.doi.org/10.1016/j.tet.2003.10.018.

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18

Cognetta, Armand B., Micah J. Niphakis, Hyeon-Cheol Lee, Michael L. Martini, Jonathan J. Hulce, and Benjamin F. Cravatt. "Selective N-Hydroxyhydantoin Carbamate Inhibitors of Mammalian Serine Hydrolases." Chemistry & Biology 22, no. 7 (2015): 928–37. http://dx.doi.org/10.1016/j.chembiol.2015.05.018.

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19

Fischer, Frank, Stefan Künne та Susanne Fetzner. "Bacterial 2,4-Dioxygenases: New Members of the α/β Hydrolase-Fold Superfamily of Enzymes Functionally Related to Serine Hydrolases". Journal of Bacteriology 181, № 18 (1999): 5725–33. http://dx.doi.org/10.1128/jb.181.18.5725-5733.1999.

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ABSTRACT 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (Qdo) fromPseudomonas putida 33/1 and 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (Hod) fromArthrobacter ilicis Rü61a catalyze an N-heterocyclic-ring cleavage reaction, generatingN-formylanthranilate and N-acetylanthranilate, respectively, and carbon monoxide. Amino acid sequence comparisons between Qdo, Hod, and a number of proteins belonging to the α/β hydrolase-fold superfamily of enzymes and analysis of the similarity between the predicted secondary structures of the 2,4-dioxygenases and the known secondary structure of haloalkane deha

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20

GLYNN, Paul. "Neuropathy target esterase." Biochemical Journal 344, no. 3 (1999): 625–31. http://dx.doi.org/10.1042/bj3440625.

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Neuropathy target esterase (NTE) is an integral membrane protein present in all neurons and in some non-neural-cell types of vertebrates. Recent data indicate that NTE is involved in a cell-signalling pathway controlling interactions between neurons and accessory glial cells in the developing nervous system. NTE has serine esterase activity and efficiently catalyses the hydrolysis of phenyl valerate (PV) in vitro, but its physiological substrate is unknown. By sequence analysis NTE has been found to be related neither to the major serine esterase family, which includes acetylcholinesterase, no

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21

Xu, Hao, Hairat Sabit, Gordon L. Amidon, and H. D. Hollis Showalter. "An improved synthesis of a fluorophosphonate–polyethylene glycol–biotin probe and its use against competitive substrates." Beilstein Journal of Organic Chemistry 9 (January 15, 2013): 89–96. http://dx.doi.org/10.3762/bjoc.9.12.

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The fluorophosphonate (FP) moiety attached to a biotin tag is a prototype chemical probe used to quantitatively analyze and enrich active serine hydrolases in complex proteomes in an approach called activity-based protein profiling (ABPP). In this study we have designed a novel synthetic route to a known FP probe linked by polyethylene glycol to a biotin tag (FP–PEG–biotin). Our route markedly increases the efficiency of the probe synthesis and overcomes several problems of a prior synthesis. As a proof of principle, FP–PEG–biotin was evaluated against isolated protein mixtures and different r

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22

Otrubova, Katerina, Venkat Srinivasan, and Dale L. Boger. "Discovery libraries targeting the major enzyme classes: The serine hydrolases." Bioorganic & Medicinal Chemistry Letters 24, no. 16 (2014): 3807–13. http://dx.doi.org/10.1016/j.bmcl.2014.06.063.

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23

Cai, Yu-dong, Guo-Ping Zhou, Chin-Hung Jen, Shuo-Liang Lin, and Kuo-Chen Chou. "Identify catalytic triads of serine hydrolases by support vector machines." Journal of Theoretical Biology 228, no. 4 (2004): 551–57. http://dx.doi.org/10.1016/j.jtbi.2004.02.019.

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24

Otrubova, Katerina, Shreyosree Chatterjee, Srijana Ghimire, Benjamin F. Cravatt, and Dale L. Boger. "N-Acyl pyrazoles: Effective and tunable inhibitors of serine hydrolases." Bioorganic & Medicinal Chemistry 27, no. 8 (2019): 1693–703. http://dx.doi.org/10.1016/j.bmc.2019.03.020.

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25

Field, S. Denise, Wankyu Lee, Jason K. Dutra, et al. "Fluorophosphonate‐Based Degrader Identifies Degradable Serine Hydrolases by Quantitative Proteomics." ChemBioChem 21, no. 20 (2020): 2916–20. http://dx.doi.org/10.1002/cbic.202000253.

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26

Jiang, Yun, Krista L. Morley, Joseph D. Schrag, and Romas J. Kazlauskas. "Different Active-Site Loop Orientation in Serine Hydrolases versus Acyltransferases." ChemBioChem 12, no. 5 (2011): 768–76. http://dx.doi.org/10.1002/cbic.201000693.

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27

Denesyuk, Alexander I., Konstantin Denessiouk, Mark S. Johnson, and Vladimir N. Uversky. "Structural Catalytic Core in Subtilisin-like Proteins and Its Comparison to Trypsin-like Serine Proteases and Alpha/Beta-Hydrolases." International Journal of Molecular Sciences 25, no. 22 (2024): 11858. http://dx.doi.org/10.3390/ijms252211858.

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Subtilisin-like proteins are serine proteases that use two types of catalytic triads: Ser-His-Asp and Ser-Glu-Asp. Here, we investigate the two known families of subtilisin-like proteins, the subtilases (Ser-His-Asp triad) and the serine-carboxyl proteinases (Ser-Glu-Asp triad), and describe the local structural arrangements (cores) that govern the catalytic residues in these proteins. We show the separation of the cores into conserved structural zones, which can be repeatedly found in different structures, and compare the structural cores in subtilisin-like proteins with those in trypsin-like

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28

Arastu-Kapur, Shirin, Kevin Shenk, Francesco Parlati, and Mark K. Bennett. "Non-Proteasomal Targets of Proteasome Inhibitors Bortezomib and Carfilzomib." Blood 112, no. 11 (2008): 2657. http://dx.doi.org/10.1182/blood.v112.11.2657.2657.

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Abstract The proteasome is a multicatalytic protease complex that has been validated as a therapeutic target in oncology with the approval of bortezomib for the treatment of multiple myeloma and mantle cell lymphoma. Carfilzomib is a next generation proteasome inhibitor that is structurally and mechanistically distinct from bortezomib and has entered clinical development in oncology. Both inhibitors target the chymotrypsin-like activity of the proteasome, but their mechanism of action differs due to their unique chemical pharmacores (or “warheads”): bortezomib is a boronate while carfilzomib i

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29

RIDDER, Ivo S., and Bauke W. DIJKSTRA. "Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY." Biochemical Journal 339, no. 2 (1999): 223–26. http://dx.doi.org/10.1042/bj3390223.

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The large HAD (haloacid dehalogenase) superfamily of hydrolases comprises P-type ATPases, phosphatases, epoxide hydrolases and l-2-haloacid dehalogenases. A comparison of the three-dimensional structure of l-2-haloacid dehalogenase with that of the response regulator protein CheY allowed the assignment of a conserved pair of aspartate residues as the Mg2+-binding site in the P-type ATPase and phosphatase members of the superfamily. From the resulting model of the active site, a conserved serine/threonine residue is suggested to be involved in phosphate binding, and a mechanism comprising a pho

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30

Willing, Stephanie, Emma Dyer, Olaf Schneewind, and Dominique Missiakas. "FmhA and FmhC of Staphylococcus aureus incorporate serine residues into peptidoglycan cross-bridges." Journal of Biological Chemistry 295, no. 39 (2020): 13664–76. http://dx.doi.org/10.1074/jbc.ra120.014371.

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Staphylococcal peptidoglycan is characterized by pentaglycine cross-bridges that are cross-linked between adjacent wall peptides by penicillin-binding proteins to confer robustness and flexibility. In Staphylococcus aureus, pentaglycine cross-bridges are synthesized by three proteins: FemX adds the first glycine, and the homodimers FemA and FemB sequentially add two Gly-Gly dipeptides. Occasionally, serine residues are also incorporated into the cross-bridges by enzymes that have heretofore not been identified. Here, we show that the FemA/FemB homologues FmhA and FmhC pair with FemA and FemB t

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31

Derewenda, Zygmunt S., and Urszula Derewenda. "Relationships among serine hydrolases: evidence for a common structural motif in triacylglyceride lipases and esterases." Biochemistry and Cell Biology 69, no. 12 (1991): 842–51. http://dx.doi.org/10.1139/o91-125.

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A detailed analysis of the highly refined (1.9 Å resolution) molecular model of the fungal (Rhizomucor miehei) triglyceride lipase reveals a unique conformation of the oligopeptide containing the active serine (Ser 144) residue. It consists of a six-residue β-strand (strand 4 of the central sheet), a four-residue turn of type II′ with serine in the ε conformation, and a buried α-helix packed in a parallel way against strands 4 and 5 of the central β-pleated sheet. It is shown that the invariant glycines in positions (1) and (5) of the so-called lipase consensus sequence (G-X-S-X-G) are in exte

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32

Kumar, Kundan, Amol Mhetre, Girish S. Ratnaparkhi, and Siddhesh S. Kamat. "A Superfamily-wide Activity Atlas of Serine Hydrolases in Drosophila melanogaster." Biochemistry 60, no. 16 (2021): 1312–24. http://dx.doi.org/10.1021/acs.biochem.1c00171.

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33

Roda, Sergi, Laura Fernandez-Lopez, Rubén Cañadas, Gerard Santiago, Manuel Ferrer, and Victor Guallar. "Computationally Driven Rational Design of Substrate Promiscuity on Serine Ester Hydrolases." ACS Catalysis 11, no. 6 (2021): 3590–601. http://dx.doi.org/10.1021/acscatal.0c05015.

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34

Yin, Hequn, Jeffrey P. Jones, and M. W. Anders. "Slow-binding inhibition of carboxylesterase and other serine hydrolases by chlorodifluoroacetaldehyde." Chemical Research in Toxicology 6, no. 5 (1993): 630–34. http://dx.doi.org/10.1021/tx00035a007.

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35

Barton, Jennifer Marie, and R. Jeremy Johnson. "Role of conserved serine hydrolases in controlling acetaldehyde toxicity in yeast." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04367.

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36

Gonzales, C. R., Sahai Srivastava, and J. E. Fitzpatrick. "Diisopropylfluorophosphate Binding Proteins (Serine Hydrolases) from Normal and Leukemic Hematopoietic Cells." Acta Haematologica 84, no. 1 (1990): 5–13. http://dx.doi.org/10.1159/000205019.

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37

Nickel, Sabrina, Farnusch Kaschani, Tom Colby, Renier A. L. van der Hoorn, and Markus Kaiser. "A para-nitrophenol phosphonate probe labels distinct serine hydrolases of Arabidopsis." Bioorganic & Medicinal Chemistry 20, no. 2 (2012): 601–6. http://dx.doi.org/10.1016/j.bmc.2011.06.041.

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38

Dijkstra, Harmen P., Hein Sprong, Bas N. H. Aerts, Cornelis A. Kruithof, Maarten R. Egmond, and Robertus J. M. Klein Gebbink. "Selective and diagnostic labelling of serine hydrolases with reactive phosphonate inhibitors." Org. Biomol. Chem. 6, no. 3 (2008): 523–31. http://dx.doi.org/10.1039/b717345h.

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39

Wang, Chao, Daniel Abegg, Brendan G. Dwyer, and Alexander Adibekian. "Discovery and Evaluation of New Activity‐Based Probes for Serine Hydrolases." ChemBioChem 20, no. 17 (2019): 2212–16. http://dx.doi.org/10.1002/cbic.201900126.

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40

Rudolf, Bogna, Michèle Salmain, Pierre Haquette, Marcin Stachowicz, and Krzysztof Woźniak. "Novel ferrocenyl phosphonate derivatives. Inhibition of serine hydrolases by ferrocene azaphosphonates." Applied Organometallic Chemistry 24, no. 10 (2010): 721–26. http://dx.doi.org/10.1002/aoc.1673.

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41

LUSH, Michael J., Yong LI, David J. READ, Anthony C. WILLIS, and Paul GLYNN. "Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man." Biochemical Journal 332, no. 1 (1998): 1–4. http://dx.doi.org/10.1042/bj3320001.

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The N-terminal amino acid sequences of proteolytic fragments of neuropathy target esterase (NTE), covalently labelled on its active-site serine by a biotinylated organophosphorus ester, were determined and used to deduce the location of this serine residue and to initiate cloning of its cDNA. A putative NTE clone, isolated from a human foetal brain cDNA library, encoded a 1327 residue polypeptide with no homology to any known serine esterases or proteases. The active-site serine of NTE (Ser-966) lay in the centre of a predicted hydrophobic helix within a 200-amino-acid C-terminal domain with m

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42

Liu, Hui, Huimin Zhou, Huaqiao Du, Qiaoling Xiao, and Marco Pistolozzi. "Kinetically-controlled mechanism-based isolation of metabolic serine hydrolases in active form from complex proteomes: butyrylcholinesterase as a case study." RSC Advances 9, no. 66 (2019): 38505–19. http://dx.doi.org/10.1039/c9ra07583f.

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43

Long, Jonathan Z., and Benjamin F. Cravatt. "The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease." Chemical Reviews 111, no. 10 (2011): 6022–63. http://dx.doi.org/10.1021/cr200075y.

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44

Shamshurin, Dmitry, Oleg V. Krokhin, David Levin, Richard Sparling, and John A. Wilkins. "In situ activity-based protein profiling of serine hydrolases in E. coli." EuPA Open Proteomics 4 (September 2014): 18–24. http://dx.doi.org/10.1016/j.euprot.2014.04.007.

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45

Kaschani, Farnusch, Sabrina Nickel, Bikram Pandey, Benjamin F. Cravatt, Markus Kaiser, and Renier A. L. van der Hoorn. "Selective inhibition of plant serine hydrolases by agrochemicals revealed by competitive ABPP." Bioorganic & Medicinal Chemistry 20, no. 2 (2012): 597–600. http://dx.doi.org/10.1016/j.bmc.2011.06.040.

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46

Makhaeva, G. F., V. V. Malygin, A. Yu Aksinenko та ін. "Fluorinated α-aminophosphonates—a new type of irreversible inhibitors of serine hydrolases". Doklady Biochemistry and Biophysics 400, № 1-6 (2005): 92–95. http://dx.doi.org/10.1007/s10628-005-0041-7.

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47

Simon, Gabriel M., and Benjamin F. Cravatt. "Activity-based Proteomics of Enzyme Superfamilies: Serine Hydrolases as a Case Study." Journal of Biological Chemistry 285, no. 15 (2010): 11051–55. http://dx.doi.org/10.1074/jbc.r109.097600.

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48

Faucher, Franco, John M. Bennett, Matthew Bogyo, and Scott Lovell. "Strategies for Tuning the Selectivity of Chemical Probes that Target Serine Hydrolases." Cell Chemical Biology 27, no. 8 (2020): 937–52. http://dx.doi.org/10.1016/j.chembiol.2020.07.008.

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49

Otte, Nikolaj, Marco Bocola, and Walter Thiel. "Force-field parameters for the simulation of tetrahedral intermediates of serine hydrolases." Journal of Computational Chemistry 30, no. 1 (2009): 154–62. http://dx.doi.org/10.1002/jcc.21037.

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50

Ganci, W., U. Ringeisen, and P. Ruedi. "ChemInform Abstract: Synthesis of Rigid Acetylcholine Mimics as Inhibitors of Serine Hydrolases." ChemInform 32, no. 23 (2010): no. http://dx.doi.org/10.1002/chin.200123272.

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