Academic literature on the topic 'Domaine VH'

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Journal articles on the topic "Domaine VH"

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Riechmann, Lutz, and Serge Muyldermans. "Single domain antibodies: comparison of camel VH and camelised human VH domains." Journal of Immunological Methods 231, no. 1-2 (1999): 25–38. http://dx.doi.org/10.1016/s0022-1759(99)00138-6.

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Wang, Guanmeng, Xin Zhou, Giovanni Fucà, et al. "Fully human antibody VH domains to generate mono and bispecific CAR to target solid tumors." Journal for ImmunoTherapy of Cancer 9, no. 4 (2021): e002173. http://dx.doi.org/10.1136/jitc-2020-002173.

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BackgroundChimeric antigen receptor (CAR) T cells are effective in B-cell malignancies. However, heterogeneous antigen expression and antigen loss remain important limitations of targeted immunotherapy in solid tumors. Therefore, targeting multiple tumor-associated antigens simultaneously is expected to improve the outcome of CAR-T cell therapies. Due to the instability of single-chain variable fragments, it remains challenging to develop the simultaneous targeting of multiple antigens using traditional single-chain fragment variable (scFv)-based CARs.MethodsWe used Humabody VH domains derived
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Dewi, Kartika Sari, and Asrul Muhamad Fuad. "Comparison of Gene Expression Between Two Types of Anti-EGFRvIII ScFv Antibodies Having Different Variable Domain Orders in Escherichia coli." ANNALES BOGORIENSES 21, no. 1 (2017): 29. http://dx.doi.org/10.14203/ann.bogor.2017.v21.n1.29-37.

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Several studies reported that the expression of various kinds of Single-chain variable fragment (scFv) antibodies in Escherichia coli are significantly influenced by the order of their variable domains. To date, the effect of the order of variable domains in the expression of scFv antibodies against epidermal growth factor receptor variant III (EGFRvIII) has not been reported. This study aimed to compare the expression between VH-linker-VL and VL-linker-VH domain orders of the anti-EGFRvIII scFv antibodies in E. coli expression system. Recombinant plasmids inserted with DNA encoding scFv prote
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Feng, Ruonan, Ruixue Wang, Jessica Hong, Christopher M. Dower, Brad St Croix, and Mitchell Ho. "Isolation of rabbit single domain antibodies to B7-H3 via protein immunization and phage display." Antibody Therapeutics 3, no. 1 (2020): 10–17. http://dx.doi.org/10.1093/abt/tbaa002.

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Abstract Single domain antibodies have certain advantages including their small size, high stability and excellent tissue penetration, making them attractive drug candidates. Rabbit antibodies can recognize diverse epitopes, including those that are poorly immunogenic in mice and humans. In the present study, we established a method to isolate rabbit VH single domain antibodies for potential cancer therapy. We immunized rabbits with recombinant human B7-H3 (CD276) protein, made a phage-displayed rabbit VH single domain library with a diversity of 7 × 109, and isolated two binders (A1 and B1; a
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O'Connor, Kevin C., Khanh Nguyen, and B. David Stollar. "Recognition of DNA by VH and Fv domains of an IgG anti-poly(dC) antibody with a singly mutated VH domain." Journal of Molecular Recognition 14, no. 1 (2000): 18–28. http://dx.doi.org/10.1002/1099-1352(200101/02)14:1<18::aid-jmr515>3.0.co;2-2.

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Huber, Michael, Khoa M. Le, Katie J. Doores, et al. "Very Few Substitutions in a Germ Line Antibody Are Required To Initiate Significant Domain Exchange." Journal of Virology 84, no. 20 (2010): 10700–10707. http://dx.doi.org/10.1128/jvi.01111-10.

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ABSTRACT 2G12 is a broadly neutralizing anti-HIV-1 monoclonal human IgG1 antibody reactive with a high-mannose glycan cluster on the surface of glycoprotein gp120. A key feature of this very highly mutated antibody is domain exchange of the heavy-chain variable region (VH) with the VH of the adjacent Fab of the same immunoglobulin, which assembles a multivalent binding interface composed of two primary binding sites in close proximity. A non-germ line-encoded proline in the elbow between VH and CH1 and an extensive network of hydrophobic interactions in the VH/VH′ interface have been proposed
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Davies, Julian, and Lutz Riechmann. "Antibody VH Domains as Small Recognition Units." Nature Biotechnology 13, no. 5 (1995): 475–79. http://dx.doi.org/10.1038/nbt0595-475.

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Sepúlveda, Jorge, Hulin Jin, Daniele Sblattero, Andrew Bradbury, and Oscar R. Burrone. "Binders Based on Dimerised Immunoglobulin VH Domains." Journal of Molecular Biology 333, no. 2 (2003): 355–65. http://dx.doi.org/10.1016/j.jmb.2003.08.033.

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Nuttall, S., R. Iring, and P. Hudson. "Immunoglobulin VH Domains and Beyond Design and Selection of Single-Domain Binding and Targeting Reagents." Current Pharmaceutical Biotechnology 1, no. 3 (2000): 253–63. http://dx.doi.org/10.2174/1389201003378906.

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van den Brink, Edward N., Ellen A. M. Turenhout, Niels Bovenschen, et al. "Multiple VH genes are used to assemble human antibodies directed toward the A3-C1 domains of factor VIII." Blood 97, no. 4 (2001): 966–72. http://dx.doi.org/10.1182/blood.v97.4.966.

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Abstract A well-known complication of factor VIII replacement therapy in patients with hemophilia A is the development of inhibitory antibodies. Several studies have demonstrated the presence of a binding site for factor VIII inhibitors in the A3 domain. Six different human monoclonal single-chain variable domain antibody fragments (scFv) directed toward the A3-C1 domains of factor VIII have been isolated, using phage display technology. Sequence analysis revealed that the VH domains of 2 scFv were encoded by germline gene segments from the VH1 gene family and 4 by germline gene segments belon
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Dissertations / Theses on the topic "Domaine VH"

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Kim, Yong Joo. "Application des expressions en phage à l'étude du virus de la fièvre aphteuse : expression et caractérisation de fragments d'anticorps bovins dirigés contre le virus de la fièvre aphteuse et expression d'un épitope immunodominant du virus de la fièvre aphteuse sur un bactériophage." Paris 7, 2003. http://www.theses.fr/2003PA077221.

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Davies, Julian. "Antibody VH domains as small recognition units." Thesis, University of Cambridge, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.263483.

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John, Christine [Verfasser], Johannes [Akademischer Betreuer] Buchner, Matthias [Gutachter] Feige, and Johannes [Gutachter] Buchner. "Analysis of different antibody domain mutations affecting the VH/VL interface, CH1 folding and CH2 stability / Christine John ; Gutachter: Matthias Feige, Johannes Buchner ; Betreuer: Johannes Buchner." München : Universitätsbibliothek der TU München, 2016. http://d-nb.info/1173322620/34.

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John, Christine Verfasser], Johannes [Akademischer Betreuer] [Buchner, Matthias [Gutachter] Feige, and Johannes [Gutachter] Buchner. "Analysis of different antibody domain mutations affecting the VH/VL interface, CH1 folding and CH2 stability / Christine John ; Gutachter: Matthias Feige, Johannes Buchner ; Betreuer: Johannes Buchner." München : Universitätsbibliothek der TU München, 2016. http://nbn-resolving.de/urn:nbn:de:bvb:91-diss-20161213-1335389-1-3.

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Kandalaft, Hiba. "Isolation and Characterization of Anti-SLP Single Domain Antibodies for the Therapy of C. difficile Infection." Thesis, Université d'Ottawa / University of Ottawa, 2012. http://hdl.handle.net/10393/20624.

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Clostridium difficile is the leading cause of death from gastrointestinal infections in Canada. Current antiobiotic treatment is non-ideal due to the high incidence of relapse and the rise in hyper-virulent antibiotic-resistant strains. Surface layer proteins (SLPs) cover the entire bacterial surface and mediate adherence to host cells. Passive and active immunization against SLPs greatly enhances survival in hamsters, suggesting that antibody-mediated bacterial neutralization may be an effective alternative therapeutic strategy. Using a recombinant-antibody phage display library, and SLPs fr
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Book chapters on the topic "Domaine VH"

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Kim, Dae Young, Wen Ding, and Jamshid Tanha. "Solubility and Stability Engineering of Human VH Domains." In Single Domain Antibodies. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-968-6_21.

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Tonikian, Raffi, and Sachdev S. Sidhu. "Selecting and Purifying Autonomous Human Variable Heavy (VH) Domains." In Single Domain Antibodies. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-968-6_20.

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Dudgeon, Kip, Romain Rouet, Kristoffer Famm, and Daniel Christ. "Selection of Human VH Single Domains with Improved Biophysical Properties by Phage Display." In Single Domain Antibodies. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-968-6_23.

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Chen, Weizao, Zhongyu Zhu, Xiaodong Xiao, and Dimiter S. Dimitrov. "Construction of a Human Antibody Domain (VH) Library." In Therapeutic Antibodies. Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-554-1_4.

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Arbabi-Ghahroudi, Mehdi, Roger MacKenzie, and Jamshid Tanha. "Site-Directed Mutagenesis for Improving Biophysical Properties of VH Domains." In Methods in Molecular Biology. Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60761-652-8_22.

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Gong, Rui, Weizao Chen, and Dimiter S. Dimitrov. "Expression, Purification, and Characterization of Engineered Antibody CH2 and VH Domains." In Methods in Molecular Biology. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-921-1_6.

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Abdelatti, Mahmoud, Peter Schofield, and Daniel Christ. "Expression of Human VH Single Domains as Fc Fusions in Mammalian Cells." In Target Identification and Validation in Drug Discovery. Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9145-7_8.

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Ward, E. S., D. H. Gussow, A. Griffiths, P. T. Jones, and G. P. Winter. "Expression and Secretion of Repertoires of VH Domains in Escherichia Coli: Isolation of Antigen Binding Activities." In Progress in Immunology. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-83755-5_153.

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Ignatovich, Olga, Laurent Jespers, Ian M. Tomlinson, and Ruud M. T. de Wildt. "Creation of the Large and Highly Functional Synthetic Repertoire of Human VH and Vκ Domain Antibodies." In Methods in Molecular Biology. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-968-6_4.

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Henry, Kevin A. "Next-Generation DNA Sequencing of VH/VL Repertoires: A Primer and Guide to Applications in Single-Domain Antibody Discovery." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7447-4_24.

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Conference papers on the topic "Domaine VH"

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Gelfand, Israel, Alexander Kister, Casimir Kulikowski, and Ognyan Stoyanov. "Algorithmic determination of core positions in the VL and VH domains of immunoglobulin molecules." In the second annual international conference. ACM Press, 1998. http://dx.doi.org/10.1145/279069.279095.

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Mcguinness, Brian, James Legg, Phil Bland-Ward, and Peter Pack. "Abstract 5766: Multifunctional biologics for targeted T-cell therapy based onin vivomatured fully human VH domains." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-5766.

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