Relevant bibliographies by topics / EPITOPING

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'EPITOPING'

Author: Grafiati
Published: 11 September 2023

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Journal articles on the topic "EPITOPING"

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Kotani, Tomio, Masako Maeda, Kazumi Umeki, and Sachiya Ohtaki. "Epitopic difference among rat thyroglobulins." Immunology Letters 9, no. 2-3 (January 1985): 167–72. http://dx.doi.org/10.1016/0165-2478(85)90029-x.

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Leclerc, C., M. P. Schutze, E. Deriaud, and G. Przewlocki. "The in vivo elimination of CD4+ T cells prevents the induction but not the expression of carrier-induced epitopic suppression." Journal of Immunology 145, no. 5 (September 1, 1990): 1343–49. http://dx.doi.org/10.4049/jimmunol.145.5.1343.

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Abstract Injection of mice with an immunogenic dose of carrier (keyhole limpet hemocyanin (KLH)) followed by immunization with hapten-carrier conjugate (TNP-KLH) selectively suppresses anti-hapten antibody response. In this study, the cellular basis of this epitopic suppression and also of the suppression induced by a high dose of carrier were analyzed by in vivo depletion of CD4+ or CD8+ T cell subsets by using mAb. The mAb treatments were performed either at the time of carrier priming or at the time of hapten-carrier immunization. The elimination of CD8+ T cells has not modified the anti-carrier antibody response, whether this treatment was performed at the time of KLH-priming or during TNP-KLH immunization. Moreover, the in vivo treatment with the anti-CD8 mAb did not modify the carrier-induced epitopic suppression induced either by a low immunogenic dose of KLH or by a high dose of this Ag. The elimination of CD4+ T cells at the time of KLH immunization has prevented the induction of a memory response to KLH, clearly establishing that CD4+ T cells are essential in memory B cell development to T-dependent Ag. Moreover, this treatment has totally abrogated the epitopic suppression induced either by low or high dosages of KLH. In contrast, the in vivo elimination of CD4+ T cells after carrier immunization did not abolish the secondary anti-carrier antibody response and did not prevent the expression of epitopic suppression. These data indicate that primed CD4+ T cells are required neither for memory B cell expression nor for the expression of suppression. Finally, once induced, the suppression can be evidenced after in vivo depletion of both primed CD4+ and CD8+ T cells. These data support the view that epitopic suppression is induced through the expansion of carrier-specific B cells and resulted from intramolecular antigenic competition between hapten and carrier epitopes.
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Schutze, M. P., E. Deriaud, G. Przewlocki, and C. LeClerc. "Carrier-induced epitopic suppression is initiated through clonal dominance." Journal of Immunology 142, no. 8 (April 15, 1989): 2635–40. http://dx.doi.org/10.4049/jimmunol.142.8.2635.

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Abstract Injection of mice with an immunogenic dose of carrier followed by immunization with hapten-carrier conjugate selectively suppresses anti-hapten antibody response. Previous studies have proposed that this epitopic suppression is related to the induction of carrier-specific Ts cells which in turn could inhibit selectively anti-hapten response. In the present study, we propose that the epitopic suppression is in fact due to clonal dominance. Immunization with a carrier such as tetanus toxoid induces a clonal expansion of carrier-specific B cells, thus decreasing the probability of hapten-specific B cells to react with the Ag. Increasing the density of the TNP-hapten on the conjugate has totally prevented the induction of the epitopic suppression. Moreover, using low hapten-carrier concentrations to challenge carrier-primed mice has enhanced the induction of the suppression. Finally, priming hapten-specific B cells before carrier/hapten-carrier immunization has also abrogated the suppression. The results of these experiments support the view that epitopic suppression is induced through the expansion of the clones specific for the carrier epitopes and resulted from intra-molecular antigenic competition between hapten and carrier epitopes. Based on these findings a regulatory role is proposed for B cells, where through their capacity to process and present antigen, they would exercise a strong influence on the selection of immune responses.
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Mendz, G. L., W. J. Moore, S. Easterbrook-Smith, and D. S. Linthicum. "Proton-n.m.r. study of interaction of myelin basic protein with a monoclonal antibody." Biochemical Journal 228, no. 1 (May 15, 1985): 61–68. http://dx.doi.org/10.1042/bj2280061.

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Proton n.m.r. at 400 MHz has been applied to study the interactions of bovine or porcine myelin basic protein (b- or p-MBP) with a monoclonal antibody to human (h-) MBP. The antibody, an IgG immunoglobulin that contains a sequential epitopic region, cross-reacts with b-MBP but not with p-MBP, the presumed epitope being identical in h- and b-MBP. N.m.r. spectra were recorded from the Fab fragment of the antibody and for mixtures of Fab and MBP at various molar ratios. The n.m.r. spectrum of MBP in the mixture consists mostly of well resolved peaks against a broad background due to the Fab. With b-MBP, but not p-MBP, specific interactions are observed at the residue tyrosine-135, which is part of the epitopic sequence. Other interactions occur between the Fab and both b- and p-MBP at residues distant from the epitopic region. Standard radioassay techniques were employed to calculate the binding constants of both basic proteins with the immunoglobulin. The binding constant, Kb, for IgG to column-immobilized b-MBP at 298K is (0.95 +/- 0.07) X 10(7) dm3/mol. The value of Kb decreases with the ionic strength of the medium, suggesting a coulombic interaction between antigen and antibody. N.m.r. spectra were also measured for mixtures of the Fab fragment and peptides containing the epitopic site, with results in agreement with those for the whole protein.
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Barre, Annick, Hélène Sénéchal, Christophe Nguyen, Claude Granier, Pascal Poncet, and Pierre Rougé. "Structural Basis for the IgE-Binding Cross-Reacting Epitopic Peptides of Cup s 3, a PR-5 Thaumatin-like Protein Allergen from Common Cypress (Cupressus sempervirens) Pollen." Allergies 3, no. 1 (January 10, 2023): 11–24. http://dx.doi.org/10.3390/allergies3010002.

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The present work was aimed at identifying the IgE-binding epitopic regions on the surface of the Cup s 3 allergen from the common cypress Cupressus sempervirens, that are possibly involved in the IgE-binding cross-reactivity reported between Cupressaceae species. Three main IgE-binding epitopic regions were mapped on the molecular surface of Cup s 3, the PR-5 thaumatin-like allergen of common cypress Cupressus sempervirens. They correspond to exposed areas containing either electropositive (R, K) or electronegative (D, E) residues. A coalescence occurs between epitopes #1 and #2, that creates an extended IgE-binding regions on the surface of the allergen. Epitope #3 contains a putative N-glycosylation site which is actually glycosylated and could therefore comprise a glycotope. However, most of the allergenic potency of Cup s 3 depends on non-glycosylated epitopic peptides. The corresponding regions of thaumatin-like allergens from other closely related Cupressaceae (Cryptomeria, Juniperus, Thuja) exhibit a very similar conformation that should account for the IgE-binding cross-reactivity observed among the Cupressaceae allergens.
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Barre, Annick, Christophe Nguyen, Claude Granier, Hervé Benoist, and Pierre Rougé. "IgE-Binding Epitopes of Pis v 1, Pis v 2 and Pis v 3, the Pistachio (Pistacia vera) Seed Allergens." Allergies 1, no. 1 (March 23, 2021): 63–91. http://dx.doi.org/10.3390/allergies1010006.

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Sequential IgE-binding epitopes were identified on the molecular surface of the Pis v 1 (2S albumin), Pis v 2 (11S globulin/legumin) and Pis v 3 (7S globulin/vicilin)—major allergens from pistachio (Pistacia vera) seeds—using the Spot technique. They essentially consist of hydrophilic and electropositively charged residues well exposed on the surface of the allergens. Most of the epitopic regions identified on Pis v 1 and Pis v 3 do not coincide with the putative N-glycosylation sites and thus are not considered as glycotopes. Surface analysis of these epitopic regions indicates a high degree of conformational similarity with the previously identified epitopic regions of the corresponding allergens Ana o 1 (vicilin), Ana o 2 (legumin) and Ana o 3 (2S albumin) from the cashew (Anacardium occidentale) nut. These results offer a molecular basis for the IgE-binding cross-reactivity often observed between pistachio and cashew nut. They support the recommendation for prescribing pistachio avoidance in cashew allergic patients. Other conformational similarities were identified with the corresponding allergens Ses i 1 (2S albumin), Ses i 3 (vicilin) and Ses i 6 (legumin) from sesame (Sesamum indicum), and Jug r 1 (2S albumin), Jug r 2 (vicilin) and Jug r 4 (legumin) from walnut (Juglans regia). Conversely, conformation of most of the epitopic regions of the pistachio allergens often differs from that of epitopes occurring on the molecular surface of the corresponding Ara h 1 (vicilin), Ara h 2 (2S albumin) and Ara h 3 (legumin) allergens from peanut (Arachis hypogaea).
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Mañes, S., L. Kremer, B. Vangbo, A. López, C. Gómez-Mouton, E. Peiró, J. P. Albar, I. B. Mendel-Hartvig, R. Llopis, and C. Martínez-A. "Physical mapping of human insulin-like growth factor-I using specific monoclonal antibodies." Journal of Endocrinology 154, no. 2 (August 1997): 293–302. http://dx.doi.org/10.1677/joe.0.1540293.

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Abstract The primary structure of recombinant human (h) insulin-like growth factor-I (IGF-I) epitopes recognized by a panel of 28 monoclonal antibodies (mAbs) is characterized. Pairwise mAb epitope mapping defines eight 'epitopic clusters' (I–VIII) which cover nearly the entire solvent-exposed IGF-I surface. Monoclonal antibody reactivity with 32 overlapping synthetic peptides and with IGF-I mutants is used to associate these epitopic clusters with the probable primary IGF-I sequences recognized. Epitopic cluster I involves residues in the C-domain and the first α-helix of the A-domain; clusters II, V and VII involve principally the B-domain; clusters III and IV map to amino acid sequences (55–70) and (1–13) respectively; cluster VI includes the A- and B-domains; and cluster VIII involves mainly the C-terminal part of the B-domain. Data indicate that this mAb panel defines 14 distinct IGF-I epitopes. The specific inhibition of HEL 92.1.7 IGF-I-promoted proliferation by these mAbs was explored. Direct correlation between mAb affinity and inhibitory activity was observed except in the case of clusters III- and VII-specific mAbs. Finally, the combination of epitopic cluster I and II mAbs detect 0·5–10 ng/ml hIGF-I in a sandwich immunoassay, with no IGF-II crossreactivity. These anti-IGF-I mAbs are, therefore, useful for both the inhibition of IGF-I mitogenic activity and for the quantification of this growth factor. The potential use of this mAb panel in tumor cell growth control is discussed. Journal of Endocrinology (1997) 154, 293–302
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Nakada, H., M. Inoue, A. Mellors, and I. Yamashina. "S12.15 Epitopic structure of tn antigen." Glycoconjugate Journal 10, no. 4 (August 1993): 299–300. http://dx.doi.org/10.1007/bf01210049.

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Piechaczyk, M., M. Bouanani, S. L. Salhi, J. M. Bastide, M. Bastide, and B. Pau. "Epitopic specificities of anti-thyroglobulin autoantibodies." International Journal of Radiation Applications and Instrumentation. Part B. Nuclear Medicine and Biology 17, no. 7 (January 1990): 719–22. http://dx.doi.org/10.1016/0883-2897(90)90095-i.

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Casina, Veronica C., Wenbing Hu, Jian-Hua Mao, Rui-Nan Lu, Hayley A. Hanby, Brandy Pickens, Zhong-Yuan Kan, et al. "High-resolution epitope mapping by HX MS reveals the pathogenic mechanism and a possible therapy for autoimmune TTP syndrome." Proceedings of the National Academy of Sciences 112, no. 31 (July 22, 2015): 9620–25. http://dx.doi.org/10.1073/pnas.1512561112.

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Acquired thrombotic thrombocytopenic purpura (TTP), a thrombotic disorder that is fatal in almost all cases if not treated promptly, is primarily caused by IgG-type autoantibodies that inhibit the ability of the ADAMTS13 (a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13) metalloprotease to cleave von Willebrand factor (VWF). Because the mechanism of autoantibody-mediated inhibition of ADAMTS13 activity is not known, the only effective therapy so far is repeated whole-body plasma exchange. We used hydrogen–deuterium exchange mass spectrometry (HX MS) to determine the ADAMTS13 binding epitope for three representative human monoclonal autoantibodies, isolated from TTP patients by phage display as tethered single-chain fragments of the variable regions (scFvs). All three scFvs bind the same conformationally discontinuous epitopic region on five small solvent-exposed loops in the spacer domain of ADAMTS13. The same epitopic region is also bound by most polyclonal IgG autoantibodies in 23 TTP patients that we tested. The ability of ADAMTS13 to proteolyze VWF is impaired by the binding of autoantibodies at the epitopic loops in the spacer domain, by the deletion of individual epitopic loops, and by some local mutations. Structural considerations and HX MS results rule out any disruptive structure change effect in the distant ADAMTS13 metalloprotease domain. Instead, it appears that the same ADAMTS13 loop segments that bind the autoantibodies are also responsible for correct binding to the VWF substrate. If so, the autoantibodies must prevent VWF proteolysis simply by physically blocking normal ADAMTS13 to VWF interaction. These results point to the mechanism for autoantibody action and an avenue for therapeutic intervention.
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Dissertations / Theses on the topic "EPITOPING"

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Obst, Stefan. "Exponierung von Epitopen bakterieller Lipopolysaccharide und ihrer Aggregate." [S.l.] : [s.n.], 1997. http://darwin.inf.fu-berlin.de/1998/5/index.html.

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Hoff, Merle [Verfasser]. "Kombinatorische Analyse von Nanobody-markierten Epitopen zur Proteinbestimmung / Merle Hoff." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2021. http://d-nb.info/122862383X/34.

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Schöne, Dominik [Verfasser], and Ulf [Akademischer Betreuer] Dittmer. "Identifikation von CD8+ T-Zell Epitopen in adenoviralen Kapsid-Proteinen und Analyse von Immundominanz-Hierarchien adenoviraler Epitope gegenüber Transgen-Epitopen bei Immunisierung mit adenoviralen Vektoren / Dominik Schöne ; Betreuer: Ulf Dittmer." Duisburg, 2019. http://d-nb.info/1191692299/34.

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Armengol, Bara Elisenda. "Identifizierung von B- und T-Zell-Epitopen des klassischen Schweinepestvirus mittels synthetischer Peptide." [S.l.] : [s.n.], 2001. http://deposit.ddb.de/cgi-bin/dokserv?idn=963259482.

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Lounsbach, Gillian Ruth. "Expression and epitopic analysis of the respiratory syncytial virus fusion protein in Escherichia coli." Thesis, University of Newcastle Upon Tyne, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.384807.

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Pisch, Thorsten. "Präklinische Evaluation einer Vakzinierungsstrategie gegen HIV-1 basierend auf konformationellen Epitopen des Env-Glykoproteins." [S.l. : s.n.], 2005.

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Zhang, Jerry Gongdu. "Enhancement of the epitopic activity of anti-thrombotic peptidomimetics by conjucation to a macromolecular carrier." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/5536.

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Background: Novel peptides with epitopic activity can be discovered by a combination of peptide arrays and computational interpolation. These peptides can mimic the activity of cellular receptors or their ligands, and are thus called peptidomimetics. The activity of peptidomimetics evidently varies in accordance with the attributes of the peptide. The fibrin-mimetic, Arginine-Glycine-Aspartate (RGD), is a well known anti-thrombotic peptide which inhibits the interaction between the platelet integrin GPITbIIIa and fibrinogenlfibrin. Short peptides often suffer from high inhibitory concentrations in vitro and short clearance times in vivo. To increase vascular residence times of such antithrombotic peptides, they were coupled to macromolecular carriers. Hyperbranched polyglycerols (I{PG), macromolecules designed as a dendritic carrier species, at a range of HPG molecular weights (MW) were tested as the carriers for antithrombotic peptidomimetics. Methods: HPG of MW 3 to 500 kDa were conjugated with RGD at a range of substitution ratios. The optimum molecular weight and substitution ratio were then applied to the peptide SHAYIGLKDR, a vWf mimic peptide discovered through the use of bioinformatics. For peptidomimetics (RGD and SHAYIGLKDR), enzymatic proteolysis was employed to distinguish the specificity of the inhibitory activity among HPG, peptide, and the HPG-peptide conjugate. Flow cytometry, UV spectroscopy, compound light microscopy, and lummiaggregometry were used to characterize the function of the conjugates in vitro. Results: Conjugation of RGD to HPG resulted in a decrease of the inhibitory concentration required to interrupt platelet-fibrinogen interactions by up to three orders of magnitude. Inhibitory activity was directly related to the number of peptides attached per HPG. Similar results were found when high molecular weight HPG, selected from the RGD-related experiments, was used to carry the peptide SHAYIGLKDR. None of HPG, RGD, SHAYIGLKDR, or their conjugates caused spontaneous platelet activation, or inhibited thrombin-mediated platelet activation, showing that the peptides’ activity is directed specifically toward their targets: GPllblllalfibrinogen (RGD) and GPIb/vWf (SHAYIGLKDR) interactions. Tryptic digestion of conjugates confirmed that the inhibitory activity of HPG conjugates was dependent on the presence of the intact peptides. Conclusions: Conjugation of peptidomimetics or other molecules to macromolecular platforms such as HPG is a viable method to enhance the peptidomimetics’ activity. The degree of enhancement is dependent upon the level of peptide substitution as well as the size of the carrier.
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PALMIERI, GRAZIANA. "Induzione di una risposta anticorpale e cellulare verso epitopi di HIV in modelli animali." Doctoral thesis, Università degli Studi di Roma "Tor Vergata", 2009. http://hdl.handle.net/2108/803.

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La costruzione di un vaccino protettivo basato su peptidi sintetici di HIV è limitata dalla loro scarsa immunogenicità. Sfruttando le note proprietà immunomodulatorie del BCG e a seguito dell’identificazione in una sub-popolazione africana (Burkina Faso, Costa d’Avorio, West-Camerun) di epitopi virali in grado di suscitare una risposta immunitaria, abbiamo effettuato uno studio per verificare l’induzione di una risposta anticorpale e cellulare verso tali epitopi. Per prima cosa abbiamo valutato l’eventuale tossicità dei prodotti utilizzati e ci siamo chiesti se la presenza di peptidi di HIV nella cosomministrazione o nel costrutto ricombinante potessero influenzare la risposta verso lo stesso BCG. Le capacità adiuvanti del BCG wild-type e ricombinante sono state valutate sia nel modello murino che in primati non umani con il fine ultimo di formulare un vaccino pediatrico contro la trasmissione verticale dalla madre al figlio del virus di HIV attraverso il latte materno.
The formulation of a protective anti-HIV vaccine based on the used of sintetic HIV peptides is limited by their poor immunogenicity. Taking advantage of known immunomodulatory properties of BCG and identified immunogenic viral epitopes in an African sub-population (Burkina Faso, Ivory Coast and West-Camerun), we verified the induction of humoral and cellular response towards these epitopes. First of all we evaluated the potential toxicity of the product used by checking if the contemporary administration of these peptides with BCG or the administration of an HIV-peptide recombinant BCG could interfere with immunological response to BCG. We evaluated the adjuvant capabilities of wild-type BCG and of recombinant BCG both in a mouse and in non-human primate models to generate a pediatric vaccine against mother to child transmission (MTCT) of HIV virus through breast feeding.
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Auth, Verna [Verfasser], and Jens [Akademischer Betreuer] Verheyen. "Einfluss der flankierenden Sequenzen von Hepatitis-C-Virus-Epitopen auf die Antigenpräsentation / Verena Auth ; Betreuer: Jens Verheyen." Duisburg, 2020. http://d-nb.info/1223849473/34.

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Pisch, Thorsten [Verfasser], and Valerie [Akademischer Betreuer] Bosch. "Präklinische Evaluation einer Vakzinierungsstrategie gegen HIV-1 basierend auf konformationellen Epitopen des Env-Glykoproteins / Thorsten Pisch ; Betreuer: Valerie, Bosch." Heidelberg : Universitätsbibliothek Heidelberg, 2005. http://d-nb.info/1178676714/34.

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Books on the topic "EPITOPING"

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M. G. (Manōlēs G.) Varvounēs. Symvolē stē methodologia tēs epitopias laographikēs ereunas. Athēnas: Ekdoseis Odysseas, 1994.

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Papamichaēl-Koutroumpa, Anna I. Laographikes apostoles: Porismata, provlēmatismoi, kai thematikē tēs epitopias ereunas. Athēna: Akadēmia Athēnōn, 1990.

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Maurogiannēs, Dionysēs. Hoi Sarakatsanoi tēs Thrakēs, tēs Kentrekēs kai Anatolikēs Makedonias: Epitopia koinōniologikē ereuna apo Evro heos Thessalonikē. Athēna: Ekdoseis "Dōdōnē", 1998.

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Book chapters on the topic "EPITOPING"

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Boumsell, Laurence, Martine Amiot, Brigitte Raynal, Véronique Gay-Bellile, Bernard Caillou, and Alain Bernard. "Epitopic Groups of CD1 Molecules." In Leukocyte Typing II, 289–302. New York, NY: Springer New York, 1986. http://dx.doi.org/10.1007/978-1-4613-8587-5_23.

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Biedermann, T. "Typ-I-Allergien gegenüber Epitopen auf Oligosacchariden." In Allergologie, 413–22. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-642-37203-2_38.

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Peterson, Jerry A., David Larocca, Gary Walkup, Richard Amiya, and Roberto L. Ceriani. "Molecular Analysis of Epitopic Heterogeneity of the Breast Mucin." In Breast Epithelial Antigens, 55–68. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3740-3_6.

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Holly, Sándor, Ilona Laczkó, Zsuzsa Majer, Gábor Tóth, and Miklós Hollósi. "FT-IR Studies on T-cell Epitopic Deletion Peptides of Influenza Virus Hemagglutinin." In Progress in Fourier Transform Spectroscopy, 445–47. Vienna: Springer Vienna, 1997. http://dx.doi.org/10.1007/978-3-7091-6840-0_105.

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Toth, Istvan, Peter M. Moyle, Pavla Simerska, Yoshio Fujita, Colleen Olive, and Michael F. Good. "Vaccine Delivery: Synthesis and Investigation of a Highly Pure, Multi-Epitopic Lipopeptide Vaccine Candidate." In Advances in Experimental Medicine and Biology, 347–49. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_154.

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Nardin, Elizabeth H. "Epitopic Malaria Vaccines Comprised of Minimal T- and B-Cell Epitopes of the P. falciparum CS Protein." In Malaria, 171–94. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-45210-4_9.

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Morris, Gary L., and J. H. Wang. "Effects on Ca2+ Uptake of Monoclonal Antibodies Raised Against Canine Cardiac Phospholamban and Their Correlation with Epitopic Location." In Excitation-Contraction Coupling in Skeletal, Cardiac, and Smooth Muscle, 417. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3362-7_61.

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Bernard, Alain, Philippe Brottier, Eric Georget, Virginia Lepage, and Laurence Boumsell. "The Epitopic Dissection of the CD2 Defined Molecule: Relationship of the Second Workshop Antibodies in Terms of Reactivities with Leukocytes, Rosette Blocking Properties, Induction of Positive Modulation of the Molecule, and Triggering T Cell Activation." In Leukocyte Typing II, 53–66. New York, NY: Springer New York, 1986. http://dx.doi.org/10.1007/978-1-4613-8587-5_4.

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Smith, Jean S. "Rabies Virus Epitopic Variation: Use in Ecologic Studies." In Advances in Virus Research, 215–53. Elsevier, 1989. http://dx.doi.org/10.1016/s0065-3527(08)60586-2.

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Renaudet, Olivier, Isabelle Bossu, and Pascal Dumy. "SYNTHESIS OF MULTI-EPITOPIC GLYCOPEPTIDE-BASED CANCER VACCINES." In Biologically-Responsive Hybrid Biomaterials, 147–70. WORLD SCIENTIFIC, 2010. http://dx.doi.org/10.1142/9789814295680_0007.

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Conference papers on the topic "EPITOPING"

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Huang, Jian, and Zili You. "Differential Performance Between Structural and Functional B-Cell Epitopic Residue Prediction." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.29.

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Simbrunner, B., T. Afonyushkin, B. Hofer, P. Königshofer, G. Semmler, L. Balcar, S. Taqi, et al. "Extrazelluläre Vesikel mit Oxidations-spezifischen Epitopen als Effektoren bei akuter hepatischer Dekompensation und akut-auf-chronischem Leberversagen." In 56. Jahrestagung & 33. Fortbildungskurs der Österreichischen Gesellschaft für Gastroenterologie & Hepatologie – ÖGGH & ˶Pre˵ Symposium der young ÖGGH. Georg Thieme Verlag, 2023. http://dx.doi.org/10.1055/s-0043-1769058.

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