Auswahl der wissenschaftlichen Literatur zum Thema „Ligand/substrate identification“
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Zeitschriftenartikel zum Thema "Ligand/substrate identification"
Singh, Manvi, Priya Kempanna und Kavitha Bharatham. „Identification of Mtb GlmU Uridyltransferase Domain Inhibitors by Ligand-Based and Structure-Based Drug Design Approaches“. Molecules 27, Nr. 9 (28.04.2022): 2805. http://dx.doi.org/10.3390/molecules27092805.
Der volle Inhalt der QuelleRothweiler, Elisabeth M., Paul E. Brennan und Kilian V. M. Huber. „Covalent fragment-based ligand screening approaches for identification of novel ubiquitin proteasome system modulators“. Biological Chemistry 403, Nr. 4 (23.02.2022): 391–402. http://dx.doi.org/10.1515/hsz-2021-0396.
Der volle Inhalt der QuelleFernández, Rico-Jiménez, Ortega, Daddaoua, García García, Martín-Mora, Torres, Tajuelo, Matilla und Krell. „Determination of Ligand Profiles for Pseudomonas aeruginosa Solute Binding Proteins“. International Journal of Molecular Sciences 20, Nr. 20 (17.10.2019): 5156. http://dx.doi.org/10.3390/ijms20205156.
Der volle Inhalt der QuelleWang, Wenyuan, Junli Zhu, Qi Huang, Lei Zhu, Ding Wang, Weimin Li und Wenjie Yu. „DFT Exploration of Metal Ion–Ligand Binding: Toward Rational Design of Chelating Agent in Semiconductor Manufacturing“. Molecules 29, Nr. 2 (08.01.2024): 308. http://dx.doi.org/10.3390/molecules29020308.
Der volle Inhalt der QuelleWeng, Z., S. M. Thomas, R. J. Rickles, J. A. Taylor, A. W. Brauer, C. Seidel-Dugan, W. M. Michael, G. Dreyfuss und J. S. Brugge. „Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains“. Molecular and Cellular Biology 14, Nr. 7 (Juli 1994): 4509–21. http://dx.doi.org/10.1128/mcb.14.7.4509-4521.1994.
Der volle Inhalt der QuelleWeng, Z., S. M. Thomas, R. J. Rickles, J. A. Taylor, A. W. Brauer, C. Seidel-Dugan, W. M. Michael, G. Dreyfuss und J. S. Brugge. „Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains.“ Molecular and Cellular Biology 14, Nr. 7 (Juli 1994): 4509–21. http://dx.doi.org/10.1128/mcb.14.7.4509.
Der volle Inhalt der QuelleEvans, S. W., D. Rennick und W. L. Farrar. „Identification of a signal-transduction pathway shared by haematopoietic growth factors with diverse biological specificity“. Biochemical Journal 244, Nr. 3 (15.06.1987): 683–91. http://dx.doi.org/10.1042/bj2440683.
Der volle Inhalt der QuelleDuarte Filho, Luiz Antonio Miranda de Souza, Cintia Emi Yanaguibashi Leal, Pierre-Edouard Bodet, Edilson Beserra de Alencar Filho, Jackson Roberto Guedes da Silva Almeida, Manon Porta Zapata, Oussama Achour et al. „The Identification of Peptide Inhibitors of the Coronavirus 3CL Protease from a Fucus ceranoides L. Hydroalcoholic Extract Using a Ligand-Fishing Strategy“. Marine Drugs 22, Nr. 6 (27.05.2024): 244. http://dx.doi.org/10.3390/md22060244.
Der volle Inhalt der QuelleDrexler, Hannes C. A., Matthias Vockel, Christian Polaschegg, Maike Frye, Kevin Peters und Dietmar Vestweber. „Vascular Endothelial Receptor Tyrosine Phosphatase: Identification of Novel Substrates Related to Junctions and a Ternary Complex with EPHB4 and TIE2“. Molecular & Cellular Proteomics 18, Nr. 10 (19.08.2019): 2058–77. http://dx.doi.org/10.1074/mcp.ra119.001716.
Der volle Inhalt der QuelleLamaze, C., und S. L. Schmid. „Recruitment of epidermal growth factor receptors into coated pits requires their activated tyrosine kinase.“ Journal of Cell Biology 129, Nr. 1 (01.04.1995): 47–54. http://dx.doi.org/10.1083/jcb.129.1.47.
Der volle Inhalt der QuelleDissertationen zum Thema "Ligand/substrate identification"
Sylvestre-Gonon, Elodie. „Caractérisation biochimique et structurale de quelques glutathion transférases de la classe Tau d'arabette (Arabidopsis thaliana) et de peuplier (Populus trichocarpa)“. Electronic Thesis or Diss., Université de Lorraine, 2020. http://www.theses.fr/2020LORR0253.
Der volle Inhalt der QuelleGlutathione transferases (GSTs) constitute a ubiquitous multigene superfamily of enzymes involved in xenobiotic detoxification and secondary metabolism. Canonical GSTs consist of an N-terminal thioredoxin domain and a α-helical C-terminal domain. In terrestrial plants, GSTs can be grouped in 14 classes but also according to the conserved residue found in their catalytic site either cysteine (Cys-GSTs) or serine (Ser-GSTs) GSTs. Ser-GSTs exhibit reduction of peroxides and/or glutathione (GSH) conjugation activities while Cys-GSTs rather exhibit deglutathionylation and dehydroascorbate reductase activities. Some of them also appear to have non-catalytic ligandin properties for the transport or storage of various molecules. The plant-specific Tau GST (GSTU) class is usually the most expanded one. The GSTUs are often over-expressed during biotic and abiotic stresses contributing notably to herbicide detoxification. However, the physiological role of most GSTUs is still poorly documented in planta. By combining phylogenetic, biochemical and structural approaches, this work led to the characterisation of nine GSTUs from Arabidopsis thaliana (AtGSTUs) and six GSTUs from Populus trichocarpa (PtGSTUs). Phylogenetic analysis of the Ser-GSTs present in photosynthetic organisms revealed that the expansion of GSTUs occurred concomitantly with the appearance of vasculature in plants, although some mosses and bryophytes possess GSTUs. Within an organism, GSTUs can be classified into distinct groups according to their catalytic motif. Enzymatic tests using recombinant proteins showed that almost all studied GSTUs exhibit GSH conjugation and peroxide reduction activities against different model substrates (CDNB, isothiocyanate derivatives, hydroperoxides). The three-dimensional structures of two GSTUs have been resolved and these adopt the classical canonical GST fold with some notable difference between them. The biochemical and structural analyses of these AtGSTUs and PtGSTUs further showed that some of them bind bacterial porphyrins while others bind polyphenolic compounds. Among the enzyme-ligand complexes identified, the structure of a bacalein-GSTU has been solved. The use of metabolites enriched samples extracted from A. thaliana and P. trichocarpa is the next step to decipher the role of GSTUs in planta
Williams, Jamie John Lewis. „Identification of substrates for the EPAC1-inducible E3 ubiquitin ligase component SOCS3“. Thesis, University of Glasgow, 2012. http://theses.gla.ac.uk/4013/.
Der volle Inhalt der QuelleBurande, Clara. „Identification des substracts d'ASB2alpha, la sous-unité de spécificité d'une E3 ubiquitine ligase impliquée dans la différenciation hématopoïétique“. Toulouse 3, 2010. http://thesesups.ups-tlse.fr/1639/.
Der volle Inhalt der QuelleThe ubiquitin-proteasome system is a central mechanism for controlled proteolysis that regulates numerous cellular processes in eukaryotes. E3 ubiquitin ligases are responsible for the specificity of this system. They provide platforms for binding specific substrates thereby coordinating their ubiquitination and subsequent degradation by the proteasome. We have developed a global proteomic strategy to identified E3 ubiquitin ligase substrates targeted to proteasomal degradation. The proof of principle of this strategy is provided by our results highlighting FLNa and FLNb as substrates of the ASB2alpha E3 ubiquitin ligase that is involved in hematopoiesis. Furthermore, we have shown that FLNc, the third member of the filamin family, is also a target of ASB2alpha. This study provides a new strategy for the identification of E3 ubiquitin ligase substrates that have to be degraded in physiologically relevant settings. We have also demonstrated that ASB2alpha, through degradation of FLNs, can regulate integrin-dependent cell motility. Moreover, structural and cell biology studies have unraveled the domain of ASB2α that is involved in the recruitment of its substrate, FLNa. This study has provided an original strategy to identify E3 ubiquitin ligase substrates targeted to degradation. Furthermore, our work has contributed to the understanding of the function and mechanisms of action of ASB2α in hematopoietic cells
Buchteile zum Thema "Ligand/substrate identification"
Cox, Eric, Ijeoma Uzoma, Catherine Guzzo, Jun Seop Jeong, Michael Matunis, Seth Blackshaw und Heng Zhu. „Identification of SUMO E3 Ligase-Specific Substrates Using the HuProt Human Proteome Microarray“. In Methods in Molecular Biology, 455–63. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2550-6_32.
Der volle Inhalt der QuelleJing, Lei, Xin Huo, Yufeng Li, Yuyin Li und Aipo Diao. „Identification of the Binding Domains of Nedd4 E3 Ubiquitin Ligase with Its Substrate Protein TMEPAI“. In Lecture Notes in Electrical Engineering, 47–53. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-45657-6_6.
Der volle Inhalt der QuelleAyad, Nagi G., Susannah Rankin, Danny Ooi, Michael Rape und Marc W. Kirschner. „Identification of Ubiquitin Ligase Substrates by In Vitro Expression Cloning“. In Methods in Enzymology, 404–14. Elsevier, 2005. http://dx.doi.org/10.1016/s0076-6879(05)99028-9.
Der volle Inhalt der QuelleKonferenzberichte zum Thema "Ligand/substrate identification"
Geddes, V. A., G. V. Louie, G. D. Brayer und R. T. A. MacGillivray. „MOLECULAR BASIS OF HEMOPHILIA B: IDENTIFICATION OF THE DEFECT IN FACTOR IX VANCOUVER“. In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643872.
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