Добірка наукової літератури з теми "Cross-species reactivity"
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Статті в журналах з теми "Cross-species reactivity":
ARLIAN, L., C. RAPP, and E. FERNANDEZCALDAS. "Allergenicity of and its cross-reactivity with species." Journal of Allergy and Clinical Immunology 91, no. 5 (May 1993): 1051–58. http://dx.doi.org/10.1016/0091-6749(93)90219-6.
RESTANI, GAIASCHI, PLEBANI, BERETTA, CAVAGNI, FIOCCHI, POIESI, VELONÀ, UGAZIO, and GALLI. "Cross-reactivity between milk proteins from different animal species." Clinical & Experimental Allergy 29, no. 7 (July 1999): 997–1004. http://dx.doi.org/10.1046/j.1365-2222.1999.00563.x.
SU, JUI-LAN, STEVE STIMPSON, CHRISTINE EDWARDS, JOHN VAN ARNOLD, SUSAN BURGESS, and PEIYUAN LIN. "Neutralizing IGF-1 Monoclonal Antibody With Cross-Species Reactivity." Hybridoma 16, no. 6 (December 1997): 513–18. http://dx.doi.org/10.1089/hyb.1997.16.513.
Christensen, L. H., C. Hejl, H. Henmar, N. Johansen, and H. Ipsen. "Extensive IgE Cross-reactivity towards Different US Ragweed Species." Journal of Allergy and Clinical Immunology 125, no. 2 (February 2010): AB17. http://dx.doi.org/10.1016/j.jaci.2009.12.098.
Losada, S., N. Chacón, C.Colmenares, H. Bermúdez, A. Lorenzo, J. P. Pointier, A. Theron, B. Alarcón de Noya, and O. Noya. "Schistosoma: Cross-reactivity and antigenic community among different species." Experimental Parasitology 111, no. 3 (November 2005): 182–90. http://dx.doi.org/10.1016/j.exppara.2005.07.007.
Gersten, Douglas M., and Vincent J. Hearing. "Antigens of Murine Melanoma and Their Cross-Species Reactivity." Pathobiology 60, no. 1 (1992): 49–56. http://dx.doi.org/10.1159/000163697.
Van den Bossche, D., A. De Bel, M. Hendrickx, A. De Becker, R. Jacobs, A. Naessens, and D. Pierard. "Galactomannan Enzymatic Immunoassay Cross-Reactivity Caused by Prototheca Species." Journal of Clinical Microbiology 50, no. 10 (July 25, 2012): 3371–73. http://dx.doi.org/10.1128/jcm.01028-12.
Gupta, R., B. P. Singh, S. Sridhara, S. N. Gaur, R. Kumar, V. K. Chaudhary, and N. Arora. "Allergenic cross-reactivity ofCurvularia lunatawith other airborne fungal species." Allergy 57, no. 7 (July 2002): 636–40. http://dx.doi.org/10.1034/j.1398-9995.2002.03331.x.
Conrad, Melanie L., William C. Davis, and Ben F. Koop. "TCR and CD3 antibody cross-reactivity in 44 species." Cytometry Part A 71A, no. 11 (2007): 925–33. http://dx.doi.org/10.1002/cyto.a.20435.
Emiliani, Yuliana, Andrés Sánchez, Marlon Munera, Jorge Sánchez, and Dilia Aparicio. "In silico analysis of cross reactivity among phospholipases from Hymenoptera species." F1000Research 10 (March 29, 2021): 2. http://dx.doi.org/10.12688/f1000research.27089.2.
Дисертації з теми "Cross-species reactivity":
Beale, Janine. "Molecular characterisation of parvalbumin and analysis of cross-reactivity in five fish species using sera from fish-allergic consumers and occupationally exposed workers." Master's thesis, University of Cape Town, 2008. http://hdl.handle.net/11427/3223.
Includes bibliographical references (leaves 101-108).
Parvalbumin, the fish major allergen, accounts for over 95% of clinical symptoms in allergic fish consumers. Importantly, this allergen displays lgE cross-reactivity thus allergic sufferers can exhibit clinical symptoms after the ingestion of non-sesitising fish species. In an occupational setting, fish products have also been shown to cause allergic disease in fish-processing factory workers. Whether parvalbumin is a causative allergen in this occupational environment is unknown. The aim of this study was to evaluate IgE reactivity to parvalbumin and other fish fillet proteins using sera from domestic consumers with ingestion-induced fish allergies and sera from occupationally exposed allergic workers. In addition, cross-reactivity among parvalbumins from five highly consumed fish species in South Africa were assessed by immunoblotting and the most cross-reactive species was characterised further. Pilchard parvalbumin was identified as the most cross-reactive allergen in fish-allergic consumers. The cDNA sequenceß form of pilchard parvalbumin was determined. This is the first time that parvalbumin from the fish order, Clupeiformes, has been characterised and represents a crucual primary step towards the generation of a recombinant form for potential diagnostic and therapeutic use in allergic individuals. Interestingly, sera IgE from fish-processing factory workers displayed no bing to parvalbumin, nor any other fish fillet proteins in immunoblotting. This result has raised several intriguing questions. Namely, does parvalbumin lack the intrinsic features required for eliciting allergic symptoms via inhalation and/or contact, as are primary routes of exposure in workers? Alternatively, could causative occupational allergens that appear to be absent in the fillet of fish occur in the enzyme-rich digestive tract or potentially the skin of fish species? Future studies aim to addess these questions amongst others, which will contribute to preventative and therapeutic strategies of occupational allergies in workers.
Pruvost, Tiphanie. "Ingénierie moléculaire de la réactivité croisée inter-espèces d’anticorps thérapeutiques par Yeast Surface Display." Electronic Thesis or Diss., université Paris-Saclay, 2023. http://www.theses.fr/2023UPASQ074.
Success of the monoclonal antibodies as therapeutic tools is partly due to their high specificity for their targets. Because of this high specificity antibodies developed against a human target often fail to recognize this target in animals used as models in preclinical trials. Thus, the goal of this study is to develop a protein engineering method aiming at conferring an antibody the ability to recognize a same antigen belonging to different species. To do so, two antibodies recognizing the human LAMP1 protein but not the murine and simian LAMP1 are used as models. In this project an exhaustive mutagenesis (DMS) monitored by Yeast Surface Display (YSD) and flow cytometry. The first part describes how these technics are combined in order to identify the epitopes of two antibodies on human LAMP1. The amino acids of epitopes are compared to those of murine and simian LAMP1 to explain the lack of recongnition of this two proteins. The second part focuses on the engineering strategy developped on the two antibodies. The expression of the DMS libraries in YSD allowed to select single mutations improving the cross-reactivity on LMAP1 without affecting the functionality of the antibodies. These mutations have been combined in a second library that has been screened for promissing variants. The affinities of these variants for differents human et simian LAMP1 orthologs has been measured to confirm the succes of the strategy. For each antibody many cross-reactive variants have been obtained
Shepertycky, Martha Roma. "Humoral immune response in mice following immunization with Prevotella intermedia and cross-reactivity with species of Prevotella, Bacteroides and Porphyromonas." 1992. http://hdl.handle.net/1993/18652.
Частини книг з теми "Cross-species reactivity":
Fu, Linglin, Bobby J. Cherayil, Haining Shi, Yanbo Wang, and Yang Zhu. "Species and Structure of Food Allergens: Epitopes and Cross-Reactivity." In Food Allergy, 13–39. Singapore: Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-6928-5_2.
Mohr, H., J. Knüver-Hopf, J. Atzpodien, H. Kirchner, and U. Pohl. "Antibodies to Interleukin-2 (IL-2) in Patients: Cross Reactivity with Different IL-2 Species." In Cytokines in Hemopoiesis, Oncology, and AIDS, 751–56. Berlin, Heidelberg: Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-75510-1_95.
Chen, Ming, and Nian-hui Zhou. "IMMUNOLOGICAL CROSS REACTIVITY OF PARAMYOSINS OF THE STRIATED MUSCLE FROM VARIOUS SPECIES OF ANIMALS." In Retrospect and Prospect of Protein Research, 56–60. WORLD SCIENTIFIC, 1991. http://dx.doi.org/10.1142/9789814360425_0014.
Schmid-Hempel, Paul. "Specificity." In Evolutionary Parasitology, 159–82. Oxford University Press, 2021. http://dx.doi.org/10.1093/oso/9780198832140.003.0007.
Rodrigo-Garcia, Maria, Esther Rodriguez-de Haro, Salvador Priego-Poyato, Elena Lima-Cabello, Sonia Morales-Santana, and Jose C. Jimenez-Lopez. "Molecular and Functional Characterisation of Allergenic Non-specific Lipid Transfer Proteins of Sweet Lupin Seed Species." In Legumes Research - Volume 1 [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.102889.
Taber, Douglass. "Developments in Alkene and Alkyne Metathesis." In Organic Synthesis. Oxford University Press, 2011. http://dx.doi.org/10.1093/oso/9780199764549.003.0025.
O.M. Al-Dahmoshi, Hussein, and Hayder J. Al-Nayili. "Mitochondrial 16S rRNA Gene-Dependent Blood Typing as a Forensic Tool." In Forensic Analysis [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98248.
Osbourn, Jane K. "Selection of antibodies from phage libraries of immunoglobulin genes." In Monoclonal Antibodies, 67–89. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780199637232.003.0003.
Тези доповідей конференцій з теми "Cross-species reactivity":
Knaack, A., A. Offt, T. Mill, J. Walewski, and W. Schade. "Picosecond-LIF-Spectroscopy with NO in a High Pressure Cell." In Modern Spectroscopy of Solids, Liquids, and Gases. Washington, D.C.: Optica Publishing Group, 1995. http://dx.doi.org/10.1364/msslg.1995.sthb6.
Звіти організацій з теми "Cross-species reactivity":
Barefoot, Susan F., Bonita A. Glatz, Nathan Gollop, and Thomas A. Hughes. Bacteriocin Markers for Propionibacteria Gene Transfer Systems. United States Department of Agriculture, June 2000. http://dx.doi.org/10.32747/2000.7573993.bard.