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Статті в журналах з теми "Peptide toxin"
Karauzum, Hatice, and Sandip Datta. "Immunization with superantigen-derived oligopeptides protect against S. aureus bacteremia (VAC8P.1058)." Journal of Immunology 194, no. 1_Supplement (May 1, 2015): 144.14. http://dx.doi.org/10.4049/jimmunol.194.supp.144.14.
Повний текст джерелаStepensky, David. "Pharmacokinetics of Toxin-Derived Peptide Drugs." Toxins 10, no. 11 (November 20, 2018): 483. http://dx.doi.org/10.3390/toxins10110483.
Повний текст джерелаda Silva, Daiane Laise, Rodrigo Valladão, Emidio Beraldo-Neto, Guilherme Rabelo Coelho, Oscar Bento da Silva Neto, Hugo Vigerelli, Adriana Rios Lopes, et al. "Spatial Distribution and Biochemical Characterization of Serine Peptidase Inhibitors in the Venom of the Brazilian Sea Anemone Anthopleura cascaia Using Mass Spectrometry Imaging." Marine Drugs 21, no. 9 (August 30, 2023): 481. http://dx.doi.org/10.3390/md21090481.
Повний текст джерелаMaillère, B., J. Cotton, G. Mourier, M. Léonetti, S. Leroy, and A. Ménez. "Role of thiols in the presentation of a snake toxin to murine T cells." Journal of Immunology 150, no. 12 (June 15, 1993): 5270–80. http://dx.doi.org/10.4049/jimmunol.150.12.5270.
Повний текст джерелаBahraoui, E. M., C. Granier, J. Van Rietschoten, H. Rochat, and M. el Ayeb. "Specificity and neutralizing capacity of antibodies elicited by a synthetic peptide of scorpion toxin." Journal of Immunology 136, no. 9 (May 1, 1986): 3371–77. http://dx.doi.org/10.4049/jimmunol.136.9.3371.
Повний текст джерелаLiao, Qingyi, Xiangjin Kong, Guoqing Luo, Xiangyue Wu, Yinping Li, Qicai Liu, Cheng Tang, and Zhonghua Liu. "Molecular Diversity of Peptide Toxins in the Venom of Spider Heteropoda pingtungensis as Revealed by cDNA Library and Transcriptome Sequencing Analysis." Toxins 14, no. 2 (February 14, 2022): 140. http://dx.doi.org/10.3390/toxins14020140.
Повний текст джерелаHyland, Caroline, Laurent Vuillard, Colin Hughes, and Vassilis Koronakis. "Membrane Interaction of Escherichia coliHemolysin: Flotation and Insertion-Dependent Labeling by Phospholipid Vesicles." Journal of Bacteriology 183, no. 18 (September 15, 2001): 5364–70. http://dx.doi.org/10.1128/jb.183.18.5364-5370.2001.
Повний текст джерелаGREEN, Daniel, Suzi PACE, Suzanne M. CURTIS, Magdalena SAKOWSKA, Graham D. LAMB, Angela F. DULHUNTY, and Marco G. CASAROTTO. "The three-dimensional structural surface of two beta-sheet scorpion toxins mimics that of an alpha-helical dihydropyridine receptor segment." Biochemical Journal 370, no. 2 (March 1, 2003): 517–27. http://dx.doi.org/10.1042/bj20021488.
Повний текст джерелаMitpuangchon, Natrada, Kwan Nualcharoen, Singtoe Boonrotpong, and Patamarerk Engsontia. "Identification of Novel Toxin Genes from the Stinging Nettle Caterpillar Parasa lepida (Cramer, 1799): Insights into the Evolution of Lepidoptera Toxins." Insects 12, no. 5 (April 29, 2021): 396. http://dx.doi.org/10.3390/insects12050396.
Повний текст джерелаVan Baelen, Anne-Cécile, Xavier Iturrioz, Marion Chaigneau, Pascal Kessler, Catherine Llorens-Cortes, Denis Servent, Nicolas Gilles, and Philippe Robin. "Characterization of the First Animal Toxin Acting as an Antagonist on AT1 Receptor." International Journal of Molecular Sciences 24, no. 3 (January 24, 2023): 2330. http://dx.doi.org/10.3390/ijms24032330.
Повний текст джерелаДисертації з теми "Peptide toxin"
Thompson, Christopher Hal. "Identification and characterization of a peptide toxin inhibitor of ClC-2 chloride channels." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/26604.
Повний текст джерелаCommittee Chair: McCarty, Nael; Committee Co-Chair: Harvey, Stephen; Committee Member: Hartzell, Criss; Committee Member: Kubanek, Julia; Committee Member: Lee, Robert. Part of the SMARTech Electronic Thesis and Dissertation Collection.
Ekberg, Jenny. "Novel peptide toxin and protein modulators of voltage-gated ion channels /." [St. Lucia, Qld.], 2005. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe20102.pdf.
Повний текст джерелаDroctove, Laura. "Premières toxines Kunitz antagonistes du récepteur de type 2 à la vasopressine : étude pharmacodynamique et relations structure-activité." Thesis, Université Paris-Saclay (ComUE), 2018. http://www.theses.fr/2018SACLS009/document.
Повний текст джерелаMambaquaretin-1 (MQ-1), a green mamba toxin, is the very first Kunitz peptide to selectively hinder the vasopressin type 2 receptor (V2R) activation. This receptor controls the final concentration of urine in kidneys. Involved in a number of pathologies, its inhibition is currently considered as the best therapeutic strategy in the treatment of polycystic kidney disease, a hereditary genetic disease. Pharmacodynamic study of MQ-1 carried out on healthy rats confirmed its in vivo activity which consists in inducing a dose-dependent aquaretic effect. Maximum effect is reached 2 hours after an intraperitoneal injection and disappears in a biological half-life ranging from 1 to 4 hours according to the dose. The daily injection of small quantities pointed to a cumulative effect over the first three days, leading to a plateau, which suggests a residual activity exceeding 24 hours. The screening of the three other mamba venoms along with a comparative analysis of the closest peptide sequences reported in databases revealed the existence of a phylogenetic group of eleven V2R antagonist Kunitz toxins. An innovative approach combining binding assays on MQ-1 variants and the modelling of the MQ-1-V2R complex has led to a partial deciphering of the pharmacophore of the toxin. The two partners share a significant ionic complementarity involving a number of extracellular loops of the receptor, and a hydrophobic region of MQ-1 interacts within V2R in the vicinity of its supposed orthosteric site. Lastly, a collaboration initiated with a pharmaceutical company brought out the need for the closer scrutiny of some crucial points to succeed in a therapeutic development of MQ-1
Blagojevic, Mariana. "Epithelial cell death induced by Candidalysin, a cytolytic peptide toxin of Candida albicans." Thesis, King's College London (University of London), 2018. https://kclpure.kcl.ac.uk/portal/en/theses/epithelial-cell-death-induced-by-candidalysin-a-cytolytic-peptide-toxin-of-candida-albicans(7a2a83b3-dd43-472f-87b3-1d157687b440).html.
Повний текст джерелаJohnson, Stephen Roy. "A Biochemical And Pharmacological Characterization Of A Novel Neuroactive Peptide From The Neotropical Hunting Ant Dinoponera Australis." Available to subscribers only, 2009. http://proquest.umi.com/pqdweb?did=1879010761&sid=3&Fmt=2&clientId=1509&RQT=309&VName=PQD.
Повний текст джерела"Department of Pharmacology." Keywords: Peptides, Toxins, Venom, Neuroactive peptide, Neurotoxins. Includes bibliographical references (p. 200-210). Also available online.
Perez, Morales Tiara G. "Production of and Response to the Cannibalism Peptide SDP in Bacillus subtilis." Diss., University of Iowa, 2013. https://ir.uiowa.edu/etd/4895.
Повний текст джерелаVoegele, Alexis. "Study of the translocation mechanism of the cyaa toxin from bordetella pertussis." Thesis, Université de Paris (2019-....), 2019. https://theses.md.univ-paris-diderot.fr/VOEGELE_Alexis_va.pdf.
Повний текст джерелаThe adenylate cyclase toxin (CyaA) is one of the major virulence factor produced by Bordetella pertussis, the causative agent of whopping cough. CyaA has the unique capacity to translocate its catalytic domain directly across the plasma membrane. Then, the catalytic domain binds to calmodulin (CaM) to produce high levels of cAMP, leading to cell intoxication. Although several models have been proposed, the molecular mechanism and the forces involved in the translocation of CyaA remain elusive. The calcium gradient, the membrane potential across the plasma membrane and post-translational acylation are required for an efficient CyaA translocation. During my PhD, I mainly investigated the translocation process. It has been previously shown that deletion of the translocation region abolishes the delivery of the catalytic domain into the cytosol of target cells. In this region, the peptide P454 (residues 454 to 484 of CyaA) was identified and exhibits membrane-active properties related to antimicrobial peptides, i.e membrane interaction, α-helical folding upon membrane insertion and membrane permeabilization. We have investigated the role of P454 on the translocation process. We observed that negatively charged and fluidic membrane favor P454 membrane insertion. The peptide contains two arginine residues that are critically involved in its membrane-active properties. We further identified that P454 exhibits the intrinsic propensity to translocate across lipid bilayers and forms a stable complex with CaM. We identified several residues from P454 involved in both membrane interaction and CaM binding. We showed in the context of the full-length CyaA toxin that these residues are essential for the efficient translocation of the catalytic domain into the cell and production of cAMP. We propose a translocation model in which the membrane-active P454 segment from the translocation region destabilizes the membrane, favoring its translocation. In the cytosol, the P454 segment is trapped by CaM and the formation of the complex may act as a driving force pulling the catalytic domain across the plasma membrane. We further showed that CaM binding to the main CaM-binding site in the catalytic domain induces local and long-range allosteric effects that stabilize the enzymatic site, allowing fast ATP catalysis to cAMP, leading to host subversion. The relevance of these results for the translocation and activation of CyaA are discussed
Wernecke, Julia [Verfasser]. "Biophysical characterisation of the fungal peptide toxin Ece1-III and its interaction with lipid membranes / Julia Wernecke." Lübeck : Zentrale Hochschulbibliothek Lübeck, 2016. http://d-nb.info/1121535852/34.
Повний текст джерелаTisseyre, Céline. "La maurocalcine : substance naturelle d'intérêt thérapeutique." Thesis, Grenoble, 2014. http://www.theses.fr/2014GRENV047/document.
Повний текст джерелаMaurocalcine (MCa) is a 33-mer toxin originally isolated from the venom of the scorpioScorpio maurus palmatus, and has been considered as a cell-penetrating peptide (CPP) for severalyears. MCa presents a therapeutic interest for the intracellular delivery of cargoes, andthis thesis aims to characterise the cell penetration properties of the native molecule as well assome of its variants’.After quantifying several truncated (linear) variants’ internalisation, I have been able tohighlight the fact that all of those analogs possess a higher internalization ability than those ofstandard CPP (especially Tat and penetratin). Among those variants, the analog MCaUF1−9 hasa relatively high rentention time within cells, as well as a slightly increased accumulation whenin an acidic environment (which occurs during solid tumours formation). This new CPP showsa certain therapeutic potential but the study of nativeMCa, remarkably stable in vivo, remainsa priority
Höfs, Sarah [Verfasser], Bernhard Gutachter] Hube, Joachim [Gutachter] Ernst, and Kerstin [Gutachter] [Voigt. "Identification of Candidalysin : a Candida albicans peptide toxin involved in epithelial damage / Sarah Höfs ; Gutachter: Bernhard Hube, Joachim Ernst, Kerstin Voigt." Jena : Friedrich-Schiller-Universität Jena, 2016. http://d-nb.info/1177608758/34.
Повний текст джерелаКниги з теми "Peptide toxin"
Binnington-Boyd, Beth A. Studies to determine the vaccine potential of the B-subunit of Shiga-like toxin 1 and its peptide fragments. Ottawa: National Library of Canada = Bibliothèque nationale du Canada, 1992.
Знайти повний текст джерелаF, Watanabe Mariyo, ed. Toxic microcystis. Boca Raton, FL: CRC Press, 1996.
Знайти повний текст джерелаInternational Agency for Research on Cancer and World Health Organization, eds. Ingested nitrate and nitrite, and cyanobacterial peptide toxins. Lyon, France: International Agency for Research on Cancer, 2010.
Знайти повний текст джерелаGianfranco, Menestrina, and Dalla Serra Mauro, eds. Pore-forming peptides and protein toxins. London: Taylor and Francis, 2003.
Знайти повний текст джерелаMeriluoto, Jussi. Liquid chromatographic analysis of cyanobacterial peptide hepatotoxins. Åbo: Åbo Akademis förlag, 1990.
Знайти повний текст джерелаWalton, Jonathan. The Cyclic Peptide Toxins of Amanita and Other Poisonous Mushrooms. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-76822-9.
Повний текст джерелаStocklin, Reto. A Handbook of Animal Toxins: Peptides and Proteins. John Wiley & Sons, 2004.
Знайти повний текст джерелаMenestrina, Gianfranco, and M. Dalla Sera. Pore-Forming Peptides and Protein Toxins. Taylor & Francis Group, 2003.
Знайти повний текст джерелаMenestrina, Gianfranco, and M. Dalla Sera. Pore-Forming Peptides and Protein Toxins. Taylor & Francis Group, 2003.
Знайти повний текст джерелаMenestrina, Gianfranco, and M. Dalla Sera. Pore-Forming Peptides and Protein Toxins. Taylor & Francis Group, 2003.
Знайти повний текст джерелаЧастини книг з теми "Peptide toxin"
Norton, Raymond S. "Peptide Toxin Structure and Function by NMR." In Modern Magnetic Resonance, 1–18. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-28275-6_120-1.
Повний текст джерелаNorton, Raymond S. "Peptide Toxin Structure and Function by NMR." In Modern Magnetic Resonance, 2081–97. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-28388-3_120.
Повний текст джерелаMcDonough, Stefan I. "Peptide Toxin Inhibition of Voltage Gated Calcium Channels." In Calcium Channel Pharmacology, 95–142. Boston, MA: Springer US, 2004. http://dx.doi.org/10.1007/978-1-4419-9254-3_4.
Повний текст джерелаMurphy, John R., Diane P. Williams, Tetsuyuki Kiyokawa, Paige L. Anderson, and Terry B. Strom. "Diphtheria Toxin-Related Peptide Hormone Fusion Proteins: New Toxins with Therapeutic Potential." In Cytotoxic Anticancer Drugs: Models and Concepts for Drug Discovery and Development, 281–301. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3492-1_17.
Повний текст джерелаLee, Sejeong, Nessim Kichik, Olivia W. Hepworth, Jonathan P. Richardson, and Julian R. Naglik. "In Vitro Biophysical Characterization of Candidalysin: A Fungal Peptide Toxin." In Methods in Molecular Biology, 163–76. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2549-1_12.
Повний текст джерелаBanerjee, Aishiki, and Saurav Saha. "Antimicrobial Peptide and Toxin-Based Mutualism: Obligate Symbiotic Entomopathogenic Nematode—Bacterium Associations." In Microbes in Microbial Communities, 91–114. Singapore: Springer Singapore, 2021. http://dx.doi.org/10.1007/978-981-16-5617-0_4.
Повний текст джерелаRussell, Michael W., Hong-Yin Wu, Pamela L. White, Ichiro Takahashi, Nobuo Okahashi, and Toshihiko Koga. "Peroral Immunization with a Cholera Toxin-Linked Bacterial Protein Antigen and Synthetic Peptide." In Genetically Engineered Vaccines, 199–207. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3410-5_22.
Повний текст джерелаLee, Jane, Phil Kennedy, and Jacob M. Waugh. "Experiences with CPP-Based Self Assembling Peptide Systems for Topical Delivery of Botulinum Toxin." In Methods in Molecular Biology, 397–415. New York, NY: Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2806-4_27.
Повний текст джерелаMurphy, John R. "Diphtheria-related peptide hormone gene fusions: A molecular genetic approach to chimeric toxin development." In Immunotoxins, 123–40. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4613-1083-9_9.
Повний текст джерелаSuryanarayana, Nagendra, Vanlalhmuaka, Kulanthaivel Thavachelvam, and Urmil Tuteja. "Humoral Responses of In Silico Designed Immunodominant Antigenic Peptide Cocktails from Anthrax Lethal Toxin Components." In Recent advances in Applied Microbiology, 249–58. Singapore: Springer Singapore, 2017. http://dx.doi.org/10.1007/978-981-10-5275-0_12.
Повний текст джерелаТези доповідей конференцій з теми "Peptide toxin"
Bozsó, Zsolt, Ferenc Bogár, János Szolomájer, Zoltán Kele, Ágota Csóti, Tibor G. Szántó, György Panyi, and Gábor K. Tóth. "Design and Synthesis of Selective Ion Channel Blocker Peptide Toxin Analogs." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.093.
Повний текст джерелаBozsó, Zsolt, Ferenc Bogár, Janos Szolomájer, Zoltán Kele, Ágota Csóti, Tibor G. Szántó, György Panyi, and Gábor K. Tóth. "Design and Synthesis of Selective Ion Channel Blocker Peptide Toxin Analogs." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps.2022.093.
Повний текст джерелаIglesias-García, Lucía C., Jesica A. Rodríguez, Gabriela R. Barredo-Vacchelli, Juan M. Minoia, Silvia A. Camperi, Gerardo Acosta, and Fernando Albericio. "Identification and Synthesis of Epitopes from a Phoneutria Nigriventer Toxin to Produce Immunogens." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps.2022.045.
Повний текст джерелаIglesias-García, Lucía C., Jésica A. Rodríguez, Gabriela R. Barredo-Vacchelli, Juan M. Minoia, Gerardo Acosta, Fernando Albericio, and Silvia A. Camperi. "Identification and Synthesis of Epitopes from a Phoneutria Nigriventer Toxin to Produce Immunogens." In 36th European Peptide Symposium. The European Peptide Society, 2022. http://dx.doi.org/10.17952/36eps/36eps.2022.045.
Повний текст джерелаEstrada, Rosendo, Redwan Huq, Rajeev Tajhya, Satendra Chauhan, Christine Beeton, and Michael W. Pennington. "Kv1.3 Selective Peptides Based Upon N-Terminal Extension and Internal Substitutions of ShK Toxin." In The 24th American Peptide Symposium. Prompt Scientific Publishing, 2015. http://dx.doi.org/10.17952/24aps.2015.238.
Повний текст джерелаOjha, Sumedha, Kanika Kundu, and Subir Kundu. "Antimicrobial peptide Microcin C7 as an alternative drug candidate against Diphtheria toxin." In 2016 International Conference on Bioinformatics and Systems Biology (BSB). IEEE, 2016. http://dx.doi.org/10.1109/bsb.2016.7552140.
Повний текст джерелаMikheeva, N. A., E. P. Drozhdina, and N. A. Kurnosova. "Morphofunctional features of proliferating cells exposed to PSMA peptide." In VIII Vserossijskaja konferencija s mezhdunarodnym uchastiem «Mediko-fiziologicheskie problemy jekologii cheloveka». Publishing center of Ulyanovsk State University, 2021. http://dx.doi.org/10.34014/mpphe.2021-142-144.
Повний текст джерелаRigby, Mike, Paul Beswick, Gemma Mudd, Katerine Van Rietschoten, Liuhong Chen, Sophie M. Watcham, Heather Allen, et al. "Abstract 4479: BT8009: A bicyclic peptide toxin conjugate targeting Nectin-4 (PVRL4) displays efficacy in preclinical tumor models." In 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.sabcs18-4479.
Повний текст джерелаRigby, Mike, Paul Beswick, Gemma Mudd, Katerine Van Rietschoten, Liuhong Chen, Sophie M. Watcham, Heather Allen, et al. "Abstract 4479: BT8009: A bicyclic peptide toxin conjugate targeting Nectin-4 (PVRL4) displays efficacy in preclinical tumor models." In 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.am2019-4479.
Повний текст джерелаSarigiannis, Yiannis, Constantinos Avraamides, Spiridoula Diavoli, Ariana Robertson, Manos Vlasiou, Elena Mourelatou, and Christos Petrou. "Linear Scorpion Peptides: An unexplored pool for peptide hydrogels." In 1st International Electronic Conference on Toxins. Basel, Switzerland: MDPI, 2021. http://dx.doi.org/10.3390/iect2021-09124.
Повний текст джерелаЗвіти організацій з теми "Peptide toxin"
Gurevitz, Michael, Michael E. Adams, Boaz Shaanan, Oren Froy, Dalia Gordon, Daewoo Lee, and Yong Zhao. Interacting Domains of Anti-Insect Scorpion Toxins and their Sodium Channel Binding Sites: Structure, Cooperative Interactions with Agrochemicals, and Application. United States Department of Agriculture, December 2001. http://dx.doi.org/10.32747/2001.7585190.bard.
Повний текст джерелаGurevitz, Michael, William A. Catterall, and Dalia Gordon. face of interaction of anti-insect selective toxins with receptor site-3 on voltage-gated sodium channels as a platform for design of novel selective insecticides. United States Department of Agriculture, December 2013. http://dx.doi.org/10.32747/2013.7699857.bard.
Повний текст джерелаCamarero, J. Developing New Tools for the in vivo Generation/Screening of Cyclic Peptide Libraries. A New Combinatorial Approach for the Detection of Bacterial Toxin Inhibitors. Office of Scientific and Technical Information (OSTI), November 2006. http://dx.doi.org/10.2172/902307.
Повний текст джерелаMevarech, Moshe, Jeremy Bruenn, and Yigal Koltin. Virus Encoded Toxin of the Corn Smut Ustilago Maydis - Isolation of Receptors and Mapping Functional Domains. United States Department of Agriculture, September 1995. http://dx.doi.org/10.32747/1995.7613022.bard.
Повний текст джерелаShai, Yechiel, Arthur Aronson, Aviah Zilberstein, and Baruch Sneh. Study of the Basis for Toxicity and Specificity of Bacillus thuringiensis d-Endotoxins. United States Department of Agriculture, January 1996. http://dx.doi.org/10.32747/1996.7573995.bard.
Повний текст джерелаKrishnamurthy, Thaiya. Investigation on Toxins and Venoms by Novel MS Techniques. Mass Spectral Investigations on Blue-Green Algal Toxic Peptides and Other Toxins. Fort Belvoir, VA: Defense Technical Information Center, August 1990. http://dx.doi.org/10.21236/ada246914.
Повний текст джерелаHorwitz, Benjamin A., and Barbara Gillian Turgeon. Fungal Iron Acquisition, Oxidative Stress and Virulence in the Cochliobolus-maize Interaction. United States Department of Agriculture, March 2012. http://dx.doi.org/10.32747/2012.7709885.bard.
Повний текст джерелаSela, Shlomo, and Michael McClelland. Investigation of a new mechanism of desiccation-stress tolerance in Salmonella. United States Department of Agriculture, January 2013. http://dx.doi.org/10.32747/2013.7598155.bard.
Повний текст джерелаNaim, Michael, Andrew Spielman, Shlomo Nir, and Ann Noble. Bitter Taste Transduction: Cellular Pathways, Inhibition and Implications for Human Acceptance of Agricultural Food Products. United States Department of Agriculture, February 2000. http://dx.doi.org/10.32747/2000.7695839.bard.
Повний текст джерела