Littérature scientifique sur le sujet « Serine hydrolases »
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Articles de revues sur le sujet "Serine hydrolases"
Nishioka, Tuguhiro, Makoto Iwata, Takuya Imaoka, Maiko Mutoh, Yoshihiro Egashira, Takashi Nishiyama, Takashi Shin et 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, no 4 (avril 2006) : 2394–99. http://dx.doi.org/10.1128/aem.72.4.2394-2399.2006.
Texte intégralJeremy 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, no 1 (18 novembre 2014) : 60–61. http://dx.doi.org/10.1002/bmb.20840.
Texte intégralBotos, Istvan, et Alexander Wlodawer. « The expanding diversity of serine hydrolases ». Current Opinion in Structural Biology 17, no 6 (décembre 2007) : 683–90. http://dx.doi.org/10.1016/j.sbi.2007.08.003.
Texte intégralTang, Shan, Adam T. Beattie, Lucie Kafkova, Gianluca Petris, Nicolas Huguenin-Dezot, Marc Fiedler, Matthew Freeman et Jason W. Chin. « Mechanism-based traps enable protease and hydrolase substrate discovery ». Nature 602, no 7898 (16 février 2022) : 701–7. http://dx.doi.org/10.1038/s41586-022-04414-9.
Texte intégralLiu, Y., M. P. Patricelli et B. F. Cravatt. « Activity-based protein profiling : The serine hydrolases ». Proceedings of the National Academy of Sciences 96, no 26 (21 décembre 1999) : 14694–99. http://dx.doi.org/10.1073/pnas.96.26.14694.
Texte intégralRoss, Matthew K., et Ran Wang. « Expanding the Toolkit for the Serine Hydrolases ». Chemistry & ; Biology 22, no 7 (juillet 2015) : 808–9. http://dx.doi.org/10.1016/j.chembiol.2015.07.002.
Texte intégralHernáez, M. J., E. Andújar, J. L. Ríos, S. R. Kaschabek, W. Reineke et E. Santero. « Identification of a Serine Hydrolase Which Cleaves the Alicyclic Ring of Tetralin ». Journal of Bacteriology 182, no 19 (1 octobre 2000) : 5448–53. http://dx.doi.org/10.1128/jb.182.19.5448-5453.2000.
Texte intégralBernhardt, Peter, Karl Hult et Romas J. Kazlauskas. « Molecular Basis of Perhydrolase Activity in Serine Hydrolases ». Angewandte Chemie International Edition 44, no 18 (29 avril 2005) : 2742–46. http://dx.doi.org/10.1002/anie.200463006.
Texte intégralBernhardt, Peter, Karl Hult et Romas J. Kazlauskas. « Molecular Basis of Perhydrolase Activity in Serine Hydrolases ». Angewandte Chemie 117, no 18 (29 avril 2005) : 2802–6. http://dx.doi.org/10.1002/ange.200463006.
Texte intégralPatočka, Jiří, Kamil Kuča et 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.
Texte intégralThèses sur le sujet "Serine hydrolases"
Fransson, Linda. « Enzyme substrate solvent interactions : a case study on serine hydrolases ». Doctoral thesis, KTH, Biokemi, 2008. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-4867.
Texte intégralQC 20100722
Elahi, AEM Rubayet. « Proteome-wide Functional Profiling of Serine Hydrolases in the Human Malaria Parasite ». Diss., Virginia Tech, 2019. http://hdl.handle.net/10919/90181.
Texte intégralDoctor of Philosophy
Malaria contributed to nearly a half a million deaths in 2017. The vast majority of malaria-related deaths are due to the parasite Plasmodium falciparum. This parasite resides inside human red blood cells (erythrocytes) and grows rapidly during a 48 hour cycle. There are over 40 serine hydrolase (SH) superfamily proteins in the parasite. Biological functions of the majority of SHs in the parasite remains unknown. Study on these SHs will provide new insights into parasite biology, and possibly present new antimalarial drug targets. We used chemical biology techniques to identify and functionally characterize parasite SHs. In one study, we show the parasite intenalized a human erythrocyte SH, acylpeptide hydrolase (APEH). We used an APEH-specific inhibitor to investigate the biological significance of internalized APEH in parasite biology. Treatment of the parasite with the inhibitor resulted in parasite growth inhibition suggesting internalization of APEH is essential for parasite survival. Lipases are enzymes that aid in break down of lipids and have shown to be crucial for growth and pathogenicity in various organisms. Lipases and lipid catabolism remain understudied in the malaria parasite. We used mass spectrometry in our approach to identify 16 lipases in asexual parasites. We have also shown that screening with highly specific inhibitors can help in predicting biological function of a particular enzyme. In summary, in this body of work, we have presented an approach of studying SHs in the malaria parasite, which will provide new insights into parasite biology.
Galmés, Ordinas Miquel Àngel. « Molecular insights into the promiscuity of serine hydrolases. Towards a computationally guided protocol for the redesign of enzymes ». Doctoral thesis, Universitat Jaume I, 2022. http://dx.doi.org/10.6035/14122.2022.725777.
Texte intégralPrograma de Doctorat en Química Teòrica i Modelització Computacional
Kreuzer, Johannes Verfasser], Stephan A. [Akademischer Betreuer] Sieber et Aymelt [Akademischer Betreuer] [Itzen. « The Natural Product Acivicin as a Tool for ABPP and the Activity of Serine Hydrolases in Uterine Fibroids / Johannes Kreuzer. Gutachter : Aymelt Itzen ; Stephan A. Sieber. Betreuer : Stephan A. Sieber ». München : Universitätsbibliothek der TU München, 2015. http://d-nb.info/1071651544/34.
Texte intégralYedji, Rodrigue. « Perturbateurs endocriniens de type phtalate et poisson zèbre Danio rerio : approche chémoprotéomique pour l'identification des cibles et recherche de signatures d'exposition ». Electronic Thesis or Diss., Université de Lorraine, 2022. http://www.theses.fr/2022LORR0106.
Texte intégralPhthalate esters are a family of synthetic compounds widely used as plasticisers. They are used in a number of plastic products such as packaging, toys, cosmetics, plastic roofing system and furniture decoration materials. Phthalates are not covalently bonded to the polymer matrix and are therefore easily released into the environment, resulting in animal and human exposure. In the absence of non-toxic substitutes, phthalate compounds are still widely used in industry, despite the classification of some of them by the European Chemicals Agency (ECHA) as suspected toxic substances and as endocrine disruptors. In addition, they are carcinogenic and teratogenic. The deleterious effect of phthalate esters on organisms is established, but the multiple nature of the effects observed shows that the mechanisms of action of phthalates are only partially elucidated. We used two targeted proteomics approaches to shed light on the mechanisms of action of phthalate esters. Dibutyl phthalate (DBP) was used as a model phthalate and zebrafish (D. rerio) as a model organism. Using the first targeted proteomics approach, affinity-based protein profiling (AfBPP), the functional disruption of proteins by DBP with photoaffinity probes from aryl azide synthesis was demonstrated. Optimisation of the binding conditions for diazirine probes (Diazirine 2) should provide us with a probe that can be used to identify DBP protein targets in the zebrafish proteome. The second approach, activity-based protein profiling (ABPP), used a reactive probe specific for serine hydrolases (SHs) to map active SHs in the zebrafish proteome for the first time. The identification of deregulated SHs in the presence of DBP in zebrafish larvae was also reported in this study. Overall, our results indicate that targeted proteomics approaches such as ABPP or AfBPP can be an asset for understanding xenobiotic-related mechanisms of action in ecotoxicology
Hamberg, Anders. « Serine Hydrolase Selectivity : Kinetics and applications in organic and analytical chemistry ». Doctoral thesis, KTH, Biokemi, 2010. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-12831.
Texte intégralQC20100629
Hamon, Nadège. « Synthese de nucleosides en serie carbocyclique à visée antivirale ». Thesis, Montpellier 2, 2010. http://www.theses.fr/2010MON20087/document.
Texte intégralNucleosides analogues constitute an important family of therapeutic agents in the treatment of viral diseases. Among these compounds, carbocyclic nucleosides have interesting biological properties. The first chapter of this thesis is dedicated to a family of natural carbonucleosides, the neplanocins. We have presented their mode of action against S-adenosylhomocysteine hydrolase, as well as various syntheses of natural neplanocins and their enantiomers before reviewing their biological activities. In the second chapter, we described the first enantioselective synthesis of (¨D)-neplanocine B. The third chapter is devoted to the development of the synthesis of 3 '-halo-5¡¯-norcarbonucleosides phosphonates as well as the evaluation of their antiviral activities
Ambrose, Timothy James William. « Serine hydrolase activity and roles for monoacylglycerol lipase in innate immunity and intestinal inflammation ». Thesis, University of Oxford, 2018. http://ora.ox.ac.uk/objects/uuid:f7a12796-ae8f-4121-ab1a-26778261ac78.
Texte intégralHo, Cherry Pei-Yee. « Evaluation of a Serine Hydrolase Inhibitor JZL184 as an Immunomodulator against Avian Pathogenic Escherichia Coli O78 in Chickens ». Thesis, Mississippi State University, 2018. http://pqdtopen.proquest.com/#viewpdf?dispub=10788360.
Texte intégralStudies with the serine hydrolase inhibitor JZL184 have suggested that enhanced 2-arachidonoylglycerol signaling could be strategized to stimulate innate immune cells to combat invading pathogens and improve host defense by prompting the systemic release of proinflammatory cytokines. Although the neurochemical effects of JZL184 were found to cultivate within 30 min in mice, its immune-regulating effects have been studied much later and its effects on chickens have not been clear. To explore the modulations in the chickens’ immune responses, we studied the effects of intraperitoneal injections of JZL184 in APEC O78-infected chickens on pathogenicity, histopathology, and IL-1β levels. The pathogenicity of the strain was assessed by isolating bacteria from livers, blood, air sacs, and hearts at 8, 28, and 56 h post-infection (p.i.). Air sacs, livers, and hearts were examined for histopathological changes at 8, 28, and 56 h p.i. Serum samples were collected at 8, 28, and 56 h p.i. and analyzed with a chicken IL-1β ELISA kit. Liver and spleen samples were homogenized for detection of serine hydrolases and carboxylesterases. Our work showed that 10 mg/kg and 40 mg/kg of JZL184 did not reduce the severity and progression of lesions produced in chickens challenged with 108 CFU of E. coli O78. The JZL184 treatments made colibacillosis lesions in the E. coli O78-challenged chickens worse and we did not find evidence of the injections increasing the serum cytokine levels of IL-1β at our sampling times.
Kornahrens, Anne. « Methodology development and synthesis of a biologically relevant natural product and targeted scaffold discovery for serine hydrolase inhibition ». Thesis, University of Oxford, 2016. https://ora.ox.ac.uk/objects/uuid:4cf5026f-e421-4b0b-9f62-707622f780b7.
Texte intégralLivres sur le sujet "Serine hydrolases"
Barrett, Alan J., John N. Abelson et Melvin I. Simon. Proteolytic Enzymes : Serine and Cysteine Peptidases. Elsevier Science & Technology Books, 1994.
Trouver le texte intégralProteolytic Enzymes : Serine and Cysteine Peptidases, Volume 244 (Methods in Enzymology). Academic Press, 1994.
Trouver le texte intégral(Editor), John N. Abelson, Melvin I. Simon (Editor) et Alan J. Barrett (Editor), dir. Proteolytic Enzymes : Serine and Cysteine Peptidases, Volume 244 (Methods in Enzymology). Academic Press, 1994.
Trouver le texte intégralBarrett, Alan J., John N. Abelson et Melvin I. Simon. Proteolytic Enzymes : Aspartic and Metallo Peptidases. Elsevier Science & Technology Books, 1995.
Trouver le texte intégralTiezzi, Antonio, Elisa Ovidi et Tomasz M. Karpiński, dir. New Findings from Natural Substances. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/97898150514211220101.
Texte intégralChapitres de livres sur le sujet "Serine hydrolases"
Schomburg, Dietmar, et Ida Schomburg. « L-serine-phosphatidylethanolamine phosphatidyltransferase 2.7.8.29 ». Dans Class 2–3.2 Transferases, Hydrolases, 447. Berlin, Heidelberg : Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36240-8_99.
Texte intégralSchomburg, Dietmar, et Ida Schomburg. « D-alanine-d-serine ligase 6.3.2.35 ». Dans Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases, 687–89. Berlin, Heidelberg : Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36260-6_93.
Texte intégralSchomburg, Dietmar, et Ida Schomburg. « O-phospho-l-serine-tRNA ligase 6.1.1.27 ». Dans Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases, 651–60. Berlin, Heidelberg : Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36260-6_84.
Texte intégralBaggelaar, Marc P., et Mario Van der Stelt. « Competitive ABPP of Serine Hydrolases : A Case Study on DAGL-Alpha ». Dans Methods in Molecular Biology, 161–69. New York, NY : Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-6439-0_12.
Texte intégralDeng, Shiping, et Inna Popova. « Carbohydrate Hydrolases ». Dans SSSA Book Series, 185–209. Madison, WI, USA : American Society of Agronomy, Crop Science Society of America, and Soil Science Society of America, 2015. http://dx.doi.org/10.2136/sssabookser9.c9.
Texte intégralDing, Shi-You, William S. Adney, Todd B. Vinzant, Stephen R. Decker, John O. Baker, Steven R. Thomas et Michael E. Himmel. « Glycoside Hydrolase Gene Cluster ofAcidothermus cellulolyticus ». Dans ACS Symposium Series, 332–60. Washington, DC : American Chemical Society, 2003. http://dx.doi.org/10.1021/bk-2003-0855.ch020.
Texte intégralHong, Tram Ngoc, et Renier A. L. van der Hoorn. « DIGE-ABPP by Click Chemistry : Pairwise Comparison of Serine Hydrolase Activities from the Apoplast of Infected Plants ». Dans Methods in Molecular Biology, 183–94. Totowa, NJ : Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-986-4_15.
Texte intégralMoris-Varas, Francisco, Laura Hartman, Amit Shah et David C. Demirjian. « Screening of Hydrolase Libraries Using pH-Shift Reagents : Rapid Evaluation of Enantioselectivity ». Dans ACS Symposium Series, 41–54. Washington, DC : American Chemical Society, 2001. http://dx.doi.org/10.1021/bk-2001-0776.ch003.
Texte intégralChou, Yat-Chen, William S. Adney, Stephen R. Decker, John O. Baker, Glenna Kunkel, David W. Templeton et Michael E. Himmel. « Cloning and Heterologous Expression of the Gene Encoding a Family 7 Glycosyl Hydrolase fromPenicillium funiculosum ». Dans ACS Symposium Series, 170–93. Washington, DC : American Chemical Society, 2004. http://dx.doi.org/10.1021/bk-2004-0889.ch010.
Texte intégralMcCleary, Barry V. « Comparison of Endolytic Hydrolases That Depolymerize 1,4-β-D-Mannan, 1,5-α-L-Arabinan, and 1,4-β-D-Galactan ». Dans ACS Symposium Series, 437–49. Washington, DC : American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0460.ch034.
Texte intégralActes de conférences sur le sujet "Serine hydrolases"
Rüedi, P., W. Ganci et U. Ringeisen. « Synthesis of Rigid Acetylcholine Mimics as Inhibitors of Serine Hydrolases ». Dans The 1st International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland : MDPI, 1997. http://dx.doi.org/10.3390/ecsoc-1-02032.
Texte intégralRüedi, P., S. Furegati, A. Linden, G. Przibille et D. Rentsch. « Synthesis, ee-Determination and Absolute Configuration of Chiral Organophosphorus Inhibitors of Serine Hydrolases ». Dans The 1st International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland : MDPI, 1997. http://dx.doi.org/10.3390/ecsoc-1-02031.
Texte intégralSajic, Tatjana, Stephan Arni, Walter Weder, Rudolf Aebersold et Sven Hillinger. « Abstract 4934 : Modified SWATH MS analysis of serine hydrolase activity in lung adenocarcinoma ». Dans Proceedings : AACR Annual Meeting 2019 ; March 29-April 3, 2019 ; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4934.
Texte intégralSajic, Tatjana, Stephan Arni, Walter Weder, Rudolf Aebersold et Sven Hillinger. « Abstract 4934 : Modified SWATH MS analysis of serine hydrolase activity in lung adenocarcinoma ». Dans Proceedings : AACR Annual Meeting 2019 ; March 29-April 3, 2019 ; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4934.
Texte intégral