Littérature scientifique sur le sujet « Cross-species reactivity »
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Articles de revues sur le sujet "Cross-species reactivity"
ARLIAN, L., C. RAPP et E. FERNANDEZCALDAS. « Allergenicity of and its cross-reactivity with species ». Journal of Allergy and Clinical Immunology 91, no 5 (mai 1993) : 1051–58. http://dx.doi.org/10.1016/0091-6749(93)90219-6.
Texte intégralRESTANI, GAIASCHI, PLEBANI, BERETTA, CAVAGNI, FIOCCHI, POIESI, VELONÀ, UGAZIO et GALLI. « Cross-reactivity between milk proteins from different animal species ». Clinical & ; Experimental Allergy 29, no 7 (juillet 1999) : 997–1004. http://dx.doi.org/10.1046/j.1365-2222.1999.00563.x.
Texte intégralSU, JUI-LAN, STEVE STIMPSON, CHRISTINE EDWARDS, JOHN VAN ARNOLD, SUSAN BURGESS et PEIYUAN LIN. « Neutralizing IGF-1 Monoclonal Antibody With Cross-Species Reactivity ». Hybridoma 16, no 6 (décembre 1997) : 513–18. http://dx.doi.org/10.1089/hyb.1997.16.513.
Texte intégralChristensen, L. H., C. Hejl, H. Henmar, N. Johansen et H. Ipsen. « Extensive IgE Cross-reactivity towards Different US Ragweed Species ». Journal of Allergy and Clinical Immunology 125, no 2 (février 2010) : AB17. http://dx.doi.org/10.1016/j.jaci.2009.12.098.
Texte intégralLosada, S., N. Chacón, C.Colmenares, H. Bermúdez, A. Lorenzo, J. P. Pointier, A. Theron, B. Alarcón de Noya et O. Noya. « Schistosoma : Cross-reactivity and antigenic community among different species ». Experimental Parasitology 111, no 3 (novembre 2005) : 182–90. http://dx.doi.org/10.1016/j.exppara.2005.07.007.
Texte intégralGersten, Douglas M., et 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.
Texte intégralVan den Bossche, D., A. De Bel, M. Hendrickx, A. De Becker, R. Jacobs, A. Naessens et D. Pierard. « Galactomannan Enzymatic Immunoassay Cross-Reactivity Caused by Prototheca Species ». Journal of Clinical Microbiology 50, no 10 (25 juillet 2012) : 3371–73. http://dx.doi.org/10.1128/jcm.01028-12.
Texte intégralGupta, R., B. P. Singh, S. Sridhara, S. N. Gaur, R. Kumar, V. K. Chaudhary et N. Arora. « Allergenic cross-reactivity ofCurvularia lunatawith other airborne fungal species ». Allergy 57, no 7 (juillet 2002) : 636–40. http://dx.doi.org/10.1034/j.1398-9995.2002.03331.x.
Texte intégralConrad, Melanie L., William C. Davis et 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.
Texte intégralEmiliani, Yuliana, Andrés Sánchez, Marlon Munera, Jorge Sánchez et Dilia Aparicio. « In silico analysis of cross reactivity among phospholipases from Hymenoptera species ». F1000Research 10 (29 mars 2021) : 2. http://dx.doi.org/10.12688/f1000research.27089.2.
Texte intégralThèses sur le sujet "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.
Texte intégralIncludes 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.
Texte intégralSuccess 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.
Texte intégralChapitres de livres sur le sujet "Cross-species reactivity"
Fu, Linglin, Bobby J. Cherayil, Haining Shi, Yanbo Wang et Yang Zhu. « Species and Structure of Food Allergens : Epitopes and Cross-Reactivity ». Dans Food Allergy, 13–39. Singapore : Springer Singapore, 2019. http://dx.doi.org/10.1007/978-981-13-6928-5_2.
Texte intégralMohr, H., J. Knüver-Hopf, J. Atzpodien, H. Kirchner et U. Pohl. « Antibodies to Interleukin-2 (IL-2) in Patients : Cross Reactivity with Different IL-2 Species ». Dans 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.
Texte intégralChen, Ming, et Nian-hui Zhou. « IMMUNOLOGICAL CROSS REACTIVITY OF PARAMYOSINS OF THE STRIATED MUSCLE FROM VARIOUS SPECIES OF ANIMALS ». Dans Retrospect and Prospect of Protein Research, 56–60. WORLD SCIENTIFIC, 1991. http://dx.doi.org/10.1142/9789814360425_0014.
Texte intégralSchmid-Hempel, Paul. « Specificity ». Dans Evolutionary Parasitology, 159–82. Oxford University Press, 2021. http://dx.doi.org/10.1093/oso/9780198832140.003.0007.
Texte intégralRodrigo-Garcia, Maria, Esther Rodriguez-de Haro, Salvador Priego-Poyato, Elena Lima-Cabello, Sonia Morales-Santana et Jose C. Jimenez-Lopez. « Molecular and Functional Characterisation of Allergenic Non-specific Lipid Transfer Proteins of Sweet Lupin Seed Species ». Dans Legumes Research - Volume 1 [Working Title]. IntechOpen, 2022. http://dx.doi.org/10.5772/intechopen.102889.
Texte intégralTaber, Douglass. « Developments in Alkene and Alkyne Metathesis ». Dans Organic Synthesis. Oxford University Press, 2011. http://dx.doi.org/10.1093/oso/9780199764549.003.0025.
Texte intégralO.M. Al-Dahmoshi, Hussein, et Hayder J. Al-Nayili. « Mitochondrial 16S rRNA Gene-Dependent Blood Typing as a Forensic Tool ». Dans Forensic Analysis [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.98248.
Texte intégralOsbourn, Jane K. « Selection of antibodies from phage libraries of immunoglobulin genes ». Dans Monoclonal Antibodies, 67–89. Oxford University PressOxford, 2000. http://dx.doi.org/10.1093/oso/9780199637232.003.0003.
Texte intégralActes de conférences sur le sujet "Cross-species reactivity"
Knaack, A., A. Offt, T. Mill, J. Walewski et W. Schade. « Picosecond-LIF-Spectroscopy with NO in a High Pressure Cell ». Dans Modern Spectroscopy of Solids, Liquids, and Gases. Washington, D.C. : Optica Publishing Group, 1995. http://dx.doi.org/10.1364/msslg.1995.sthb6.
Texte intégralRapports d'organisations sur le sujet "Cross-species reactivity"
Barefoot, Susan F., Bonita A. Glatz, Nathan Gollop et Thomas A. Hughes. Bacteriocin Markers for Propionibacteria Gene Transfer Systems. United States Department of Agriculture, juin 2000. http://dx.doi.org/10.32747/2000.7573993.bard.
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