Artigos de revistas sobre o tema "Serine hydrolases"
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Nishioka, Tuguhiro, Makoto Iwata, Takuya Imaoka, Maiko Mutoh, Yoshihiro Egashira, Takashi Nishiyama, Takashi Shin e Takao Fujii. "A Mono-2-Ethylhexyl Phthalate Hydrolase from a Gordonia sp. That Is Able To Dissimilate Di-2-Ethylhexyl Phthalate". Applied and Environmental Microbiology 72, n.º 4 (abril de 2006): 2394–99. http://dx.doi.org/10.1128/aem.72.4.2394-2399.2006.
Texto completo da fonteJeremy Johnson, R., Andrew Bartels, Rachel Erkilla, Nicole Green, Steven Han, Nathaniel Holt, Melissa Jones et al. "Proteopedia entry: Mammalian serine hydrolases". Biochemistry and Molecular Biology Education 43, n.º 1 (18 de novembro de 2014): 60–61. http://dx.doi.org/10.1002/bmb.20840.
Texto completo da fonteBotos, Istvan, e Alexander Wlodawer. "The expanding diversity of serine hydrolases". Current Opinion in Structural Biology 17, n.º 6 (dezembro de 2007): 683–90. http://dx.doi.org/10.1016/j.sbi.2007.08.003.
Texto completo da fonteTang, Shan, Adam T. Beattie, Lucie Kafkova, Gianluca Petris, Nicolas Huguenin-Dezot, Marc Fiedler, Matthew Freeman e Jason W. Chin. "Mechanism-based traps enable protease and hydrolase substrate discovery". Nature 602, n.º 7898 (16 de fevereiro de 2022): 701–7. http://dx.doi.org/10.1038/s41586-022-04414-9.
Texto completo da fonteLiu, Y., M. P. Patricelli e B. F. Cravatt. "Activity-based protein profiling: The serine hydrolases". Proceedings of the National Academy of Sciences 96, n.º 26 (21 de dezembro de 1999): 14694–99. http://dx.doi.org/10.1073/pnas.96.26.14694.
Texto completo da fonteRoss, Matthew K., e Ran Wang. "Expanding the Toolkit for the Serine Hydrolases". Chemistry & Biology 22, n.º 7 (julho de 2015): 808–9. http://dx.doi.org/10.1016/j.chembiol.2015.07.002.
Texto completo da fonteHernáez, M. J., E. Andújar, J. L. Ríos, S. R. Kaschabek, W. Reineke e E. Santero. "Identification of a Serine Hydrolase Which Cleaves the Alicyclic Ring of Tetralin". Journal of Bacteriology 182, n.º 19 (1 de outubro de 2000): 5448–53. http://dx.doi.org/10.1128/jb.182.19.5448-5453.2000.
Texto completo da fonteBernhardt, Peter, Karl Hult e Romas J. Kazlauskas. "Molecular Basis of Perhydrolase Activity in Serine Hydrolases". Angewandte Chemie International Edition 44, n.º 18 (29 de abril de 2005): 2742–46. http://dx.doi.org/10.1002/anie.200463006.
Texto completo da fonteBernhardt, Peter, Karl Hult e Romas J. Kazlauskas. "Molecular Basis of Perhydrolase Activity in Serine Hydrolases". Angewandte Chemie 117, n.º 18 (29 de abril de 2005): 2802–6. http://dx.doi.org/10.1002/ange.200463006.
Texto completo da fontePatočka, Jiří, Kamil Kuča e Daniel Jun. "Acetylcholinesterase and Butyrylcholinesterase – Important Enzymes of Human Body". Acta Medica (Hradec Kralove, Czech Republic) 47, n.º 4 (2004): 215–28. http://dx.doi.org/10.14712/18059694.2018.95.
Texto completo da fonteMartínez, Virginia, Fernando de la Peña, Javier García-Hidalgo, Isabel de la Mata, José Luis García e 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, n.º 17 (15 de junho de 2012): 6017–26. http://dx.doi.org/10.1128/aem.01099-12.
Texto completo da fonteChen, Biao, Sha-Sha Ge, Yuan-Chao Zhao, Chong Chen e Song Yang. "Activity-based protein profiling: an efficient approach to study serine hydrolases and their inhibitors in mammals and microbes". RSC Advances 6, n.º 114 (2016): 113327–43. http://dx.doi.org/10.1039/c6ra20006k.
Texto completo da fonteBerger, Natascha, Hanna Allerkamp e Christian Wadsack. "Serine Hydrolases in Lipid Homeostasis of the Placenta-Targets for Placental Function?" International Journal of Molecular Sciences 23, n.º 12 (20 de junho de 2022): 6851. http://dx.doi.org/10.3390/ijms23126851.
Texto completo da fonteSchirmer, Andreas, Claudia Matz e 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, n.º 13 (15 de dezembro de 1995): 170–79. http://dx.doi.org/10.1139/m95-184.
Texto completo da fonteBachovchin, Daniel A., e Benjamin F. Cravatt. "The pharmacological landscape and therapeutic potential of serine hydrolases". Nature Reviews Drug Discovery 11, n.º 1 (janeiro de 2012): 52–68. http://dx.doi.org/10.1038/nrd3620.
Texto completo da fontevan Rantwijk, Fred, e Roger A. Sheldon. "Enantioselective acylation of chiral amines catalysed by serine hydrolases". Tetrahedron 60, n.º 3 (janeiro de 2004): 501–19. http://dx.doi.org/10.1016/j.tet.2003.10.018.
Texto completo da fonteCognetta, Armand B., Micah J. Niphakis, Hyeon-Cheol Lee, Michael L. Martini, Jonathan J. Hulce e Benjamin F. Cravatt. "Selective N-Hydroxyhydantoin Carbamate Inhibitors of Mammalian Serine Hydrolases". Chemistry & Biology 22, n.º 7 (julho de 2015): 928–37. http://dx.doi.org/10.1016/j.chembiol.2015.05.018.
Texto completo da fonteFischer, Frank, Stefan Künne e 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, n.º 18 (15 de setembro de 1999): 5725–33. http://dx.doi.org/10.1128/jb.181.18.5725-5733.1999.
Texto completo da fonteGLYNN, Paul. "Neuropathy target esterase". Biochemical Journal 344, n.º 3 (8 de dezembro de 1999): 625–31. http://dx.doi.org/10.1042/bj3440625.
Texto completo da fonteOtrubova, Katerina, Venkat Srinivasan e Dale L. Boger. "Discovery libraries targeting the major enzyme classes: The serine hydrolases". Bioorganic & Medicinal Chemistry Letters 24, n.º 16 (agosto de 2014): 3807–13. http://dx.doi.org/10.1016/j.bmcl.2014.06.063.
Texto completo da fonteCai, Yu-dong, Guo-Ping Zhou, Chin-Hung Jen, Shuo-Liang Lin e Kuo-Chen Chou. "Identify catalytic triads of serine hydrolases by support vector machines". Journal of Theoretical Biology 228, n.º 4 (junho de 2004): 551–57. http://dx.doi.org/10.1016/j.jtbi.2004.02.019.
Texto completo da fonteOtrubova, Katerina, Shreyosree Chatterjee, Srijana Ghimire, Benjamin F. Cravatt e Dale L. Boger. "N-Acyl pyrazoles: Effective and tunable inhibitors of serine hydrolases". Bioorganic & Medicinal Chemistry 27, n.º 8 (abril de 2019): 1693–703. http://dx.doi.org/10.1016/j.bmc.2019.03.020.
Texto completo da fonteField, S. Denise, Wankyu Lee, Jason K. Dutra, Finley Scott F. Serneo, Jon Oyer, Hua Xu, Douglas S. Johnson, Christopher W. am Ende e Uthpala Seneviratne. "Fluorophosphonate‐Based Degrader Identifies Degradable Serine Hydrolases by Quantitative Proteomics". ChemBioChem 21, n.º 20 (23 de julho de 2020): 2916–20. http://dx.doi.org/10.1002/cbic.202000253.
Texto completo da fonteJiang, Yun, Krista L. Morley, Joseph D. Schrag e Romas J. Kazlauskas. "Different Active-Site Loop Orientation in Serine Hydrolases versus Acyltransferases". ChemBioChem 12, n.º 5 (23 de fevereiro de 2011): 768–76. http://dx.doi.org/10.1002/cbic.201000693.
Texto completo da fonteXu, Hao, Hairat Sabit, Gordon L. Amidon e 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 (15 de janeiro de 2013): 89–96. http://dx.doi.org/10.3762/bjoc.9.12.
Texto completo da fonteArastu-Kapur, Shirin, Kevin Shenk, Francesco Parlati e Mark K. Bennett. "Non-Proteasomal Targets of Proteasome Inhibitors Bortezomib and Carfilzomib". Blood 112, n.º 11 (16 de novembro de 2008): 2657. http://dx.doi.org/10.1182/blood.v112.11.2657.2657.
Texto completo da fonteWilling, Stephanie, Emma Dyer, Olaf Schneewind e Dominique Missiakas. "FmhA and FmhC of Staphylococcus aureus incorporate serine residues into peptidoglycan cross-bridges". Journal of Biological Chemistry 295, n.º 39 (5 de agosto de 2020): 13664–76. http://dx.doi.org/10.1074/jbc.ra120.014371.
Texto completo da fonteRIDDER, Ivo S., e 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, n.º 2 (8 de abril de 1999): 223–26. http://dx.doi.org/10.1042/bj3390223.
Texto completo da fonteDerewenda, Zygmunt S., e Urszula Derewenda. "Relationships among serine hydrolases: evidence for a common structural motif in triacylglyceride lipases and esterases". Biochemistry and Cell Biology 69, n.º 12 (1 de dezembro de 1991): 842–51. http://dx.doi.org/10.1139/o91-125.
Texto completo da fonteKumar, Kundan, Amol Mhetre, Girish S. Ratnaparkhi e Siddhesh S. Kamat. "A Superfamily-wide Activity Atlas of Serine Hydrolases in Drosophila melanogaster". Biochemistry 60, n.º 16 (7 de abril de 2021): 1312–24. http://dx.doi.org/10.1021/acs.biochem.1c00171.
Texto completo da fonteRoda, Sergi, Laura Fernandez-Lopez, Rubén Cañadas, Gerard Santiago, Manuel Ferrer e Victor Guallar. "Computationally Driven Rational Design of Substrate Promiscuity on Serine Ester Hydrolases". ACS Catalysis 11, n.º 6 (5 de março de 2021): 3590–601. http://dx.doi.org/10.1021/acscatal.0c05015.
Texto completo da fonteYin, Hequn, Jeffrey P. Jones e M. W. Anders. "Slow-binding inhibition of carboxylesterase and other serine hydrolases by chlorodifluoroacetaldehyde". Chemical Research in Toxicology 6, n.º 5 (setembro de 1993): 630–34. http://dx.doi.org/10.1021/tx00035a007.
Texto completo da fonteBarton, Jennifer Marie, e R. Jeremy Johnson. "Role of conserved serine hydrolases in controlling acetaldehyde toxicity in yeast". FASEB Journal 34, S1 (abril de 2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04367.
Texto completo da fonteGonzales, C. R., Sahai Srivastava e J. E. Fitzpatrick. "Diisopropylfluorophosphate Binding Proteins (Serine Hydrolases) from Normal and Leukemic Hematopoietic Cells". Acta Haematologica 84, n.º 1 (1990): 5–13. http://dx.doi.org/10.1159/000205019.
Texto completo da fonteNickel, Sabrina, Farnusch Kaschani, Tom Colby, Renier A. L. van der Hoorn e Markus Kaiser. "A para-nitrophenol phosphonate probe labels distinct serine hydrolases of Arabidopsis". Bioorganic & Medicinal Chemistry 20, n.º 2 (janeiro de 2012): 601–6. http://dx.doi.org/10.1016/j.bmc.2011.06.041.
Texto completo da fonteDijkstra, Harmen P., Hein Sprong, Bas N. H. Aerts, Cornelis A. Kruithof, Maarten R. Egmond e Robertus J. M. Klein Gebbink. "Selective and diagnostic labelling of serine hydrolases with reactive phosphonate inhibitors". Org. Biomol. Chem. 6, n.º 3 (2008): 523–31. http://dx.doi.org/10.1039/b717345h.
Texto completo da fonteWang, Chao, Daniel Abegg, Brendan G. Dwyer e Alexander Adibekian. "Discovery and Evaluation of New Activity‐Based Probes for Serine Hydrolases". ChemBioChem 20, n.º 17 (29 de julho de 2019): 2212–16. http://dx.doi.org/10.1002/cbic.201900126.
Texto completo da fonteRudolf, Bogna, Michèle Salmain, Pierre Haquette, Marcin Stachowicz e Krzysztof Woźniak. "Novel ferrocenyl phosphonate derivatives. Inhibition of serine hydrolases by ferrocene azaphosphonates". Applied Organometallic Chemistry 24, n.º 10 (16 de setembro de 2010): 721–26. http://dx.doi.org/10.1002/aoc.1673.
Texto completo da fonteLUSH, Michael J., Yong LI, David J. READ, Anthony C. WILLIS e 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, n.º 1 (15 de maio de 1998): 1–4. http://dx.doi.org/10.1042/bj3320001.
Texto completo da fonteLong, Jonathan Z., e Benjamin F. Cravatt. "The Metabolic Serine Hydrolases and Their Functions in Mammalian Physiology and Disease". Chemical Reviews 111, n.º 10 (12 de outubro de 2011): 6022–63. http://dx.doi.org/10.1021/cr200075y.
Texto completo da fonteShamshurin, Dmitry, Oleg V. Krokhin, David Levin, Richard Sparling e John A. Wilkins. "In situ activity-based protein profiling of serine hydrolases in E. coli". EuPA Open Proteomics 4 (setembro de 2014): 18–24. http://dx.doi.org/10.1016/j.euprot.2014.04.007.
Texto completo da fonteKaschani, Farnusch, Sabrina Nickel, Bikram Pandey, Benjamin F. Cravatt, Markus Kaiser e Renier A. L. van der Hoorn. "Selective inhibition of plant serine hydrolases by agrochemicals revealed by competitive ABPP". Bioorganic & Medicinal Chemistry 20, n.º 2 (janeiro de 2012): 597–600. http://dx.doi.org/10.1016/j.bmc.2011.06.040.
Texto completo da fonteMakhaeva, G. F., V. V. Malygin, A. Yu Aksinenko, V. B. Sokolov, N. N. Strakhova, A. N. Rasdolsky, R. J. Richardson e I. V. Martynov. "Fluorinated α-aminophosphonates—a new type of irreversible inhibitors of serine hydrolases". Doklady Biochemistry and Biophysics 400, n.º 1-6 (janeiro de 2005): 92–95. http://dx.doi.org/10.1007/s10628-005-0041-7.
Texto completo da fonteSimon, Gabriel M., e Benjamin F. Cravatt. "Activity-based Proteomics of Enzyme Superfamilies: Serine Hydrolases as a Case Study". Journal of Biological Chemistry 285, n.º 15 (10 de fevereiro de 2010): 11051–55. http://dx.doi.org/10.1074/jbc.r109.097600.
Texto completo da fonteFaucher, Franco, John M. Bennett, Matthew Bogyo e Scott Lovell. "Strategies for Tuning the Selectivity of Chemical Probes that Target Serine Hydrolases". Cell Chemical Biology 27, n.º 8 (agosto de 2020): 937–52. http://dx.doi.org/10.1016/j.chembiol.2020.07.008.
Texto completo da fonteOtte, Nikolaj, Marco Bocola e Walter Thiel. "Force-field parameters for the simulation of tetrahedral intermediates of serine hydrolases". Journal of Computational Chemistry 30, n.º 1 (15 de janeiro de 2009): 154–62. http://dx.doi.org/10.1002/jcc.21037.
Texto completo da fonteGanci, W., U. Ringeisen e P. Ruedi. "ChemInform Abstract: Synthesis of Rigid Acetylcholine Mimics as Inhibitors of Serine Hydrolases". ChemInform 32, n.º 23 (26 de maio de 2010): no. http://dx.doi.org/10.1002/chin.200123272.
Texto completo da fonteLiu, Hui, Huimin Zhou, Huaqiao Du, Qiaoling Xiao e 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, n.º 66 (2019): 38505–19. http://dx.doi.org/10.1039/c9ra07583f.
Texto completo da fonteHwang, Jisub, Hackwon Do, Youn-Soo Shim e Jun Hyuck Lee. "Crystal Structure and Functional Characterization of an S-Formylglutathione Hydrolase (BuSFGH) from Burkholderiaceae sp." Crystals 13, n.º 4 (4 de abril de 2023): 621. http://dx.doi.org/10.3390/cryst13040621.
Texto completo da fontePolderman-Tijmes, Jolanda J., Peter A. Jekel, Erik J. de Vries, Annet E. J. van Merode, René Floris, Jan-Metske van der Laan, Theo Sonke e Dick B. Janssen. "Cloning, Sequence Analysis, and Expression in Escherichia coli of the Gene Encoding an α-Amino Acid Ester Hydrolase from Acetobacter turbidans". Applied and Environmental Microbiology 68, n.º 1 (janeiro de 2002): 211–18. http://dx.doi.org/10.1128/aem.68.1.211-218.2002.
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