Bibliografie tematiche / Antibody affinity

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Letteratura scientifica selezionata sul tema "Antibody affinity"

Autore: Grafiati
Pubblicato: 4 giugno 2021
Ultima modifica: 14 febbraio 2022

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Articoli di riviste sul tema "Antibody affinity"

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Azimzadeh, A., and M. H. V. Van Regenmortel. "Antibody affinity measurements." Journal of Molecular Recognition 3, no. 3 (June 1990): 108–16. http://dx.doi.org/10.1002/jmr.300030304.

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van Regenmortel, Marc H. V., and Agnëgs Azimzadeh. "Determination of Antibody Affinity." Journal of Immunoassay 21, no. 2-3 (May 2000): 211–34. http://dx.doi.org/10.1080/01971520009349534.

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Wabl, Matthias, Marilia Cascalho, and Charles Steinberg. "Hypermutation in antibody affinity maturation." Current Opinion in Immunology 11, no. 2 (April 1999): 186–89. http://dx.doi.org/10.1016/s0952-7915(99)80031-4.

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Webster, D. M., S. Roberts, J. C. Cheetham, R. Griest, and A. R. Rees. "Engineering antibody affinity and specificity." International Journal of Cancer 41, S3 (1988): 13–16. http://dx.doi.org/10.1002/ijc.2910410804.

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Nervig, Christine S., and Shawn C. Owen. "Affinity-bound antibody–drug conjugates." Nature Biomedical Engineering 3, no. 11 (November 2019): 850–51. http://dx.doi.org/10.1038/s41551-019-0478-0.

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Griswold, William R. "A Quantitative Relationship Between Antibody Affinity and Antibody Avidity." Immunological Investigations 16, no. 2 (January 1987): 97–106. http://dx.doi.org/10.3109/08820138709030567.

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Yu, Guimei, Kunpeng Li, and Wen Jiang. "Antibody-based affinity cryo-EM grid." Methods 100 (May 2016): 16–24. http://dx.doi.org/10.1016/j.ymeth.2016.01.010.

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Steward, Michael W., Carolynne Stanley, and Maria D. Furlong. "Antibody affinity maturation in selectively bred high and low-affinity mice." European Journal of Immunology 16, no. 1 (1986): 59–63. http://dx.doi.org/10.1002/eji.1830160112.

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Makabe, Koki. "Molecular basis of flexible peptide recognition by an antibody." Journal of Biochemistry 167, no. 4 (February 6, 2020): 343–45. http://dx.doi.org/10.1093/jb/mvaa017.

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Abstract Antibodies can recognize various types of antigens with high specificity and affinity and peptide is one of their major targets. Understanding an antibody’s molecular recognition mechanism for peptide is important for developing clones with a higher specificity and affinity. Here, the author reviews recent progresses in flexible peptide recognition by an antibody using several biophysical techniques, including X-ray crystallography, molecular dynamics simulations and calorimetric measurements. A set of two reports highlight the importance of intramolecular hydrogen bonds that form in
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Fukunishi, Hiroaki, Jiro Shimada, and Kenji Shiraishi. "Antigen–Antibody Interactions and Structural Flexibility of a Femtomolar-Affinity Antibody." Biochemistry 51, no. 12 (March 13, 2012): 2597–605. http://dx.doi.org/10.1021/bi3000319.

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Tesi sul tema "Antibody affinity"

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Low, Nigel Murray. "Mimicking antibody affinity maturation." Thesis, University of Cambridge, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364567.

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Molari, Marco. "Modeling and Bayesian inference for antibody affinity maturation." Thesis, Université Paris sciences et lettres, 2020. http://www.theses.fr/2020UPSLE017.

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La Maturation d’Affinité (MA) est le processus biologique grâce auquel notre système immunitaire génère de puissants anticorps contre les nouveaux agents pathogènes rencontrés. Ce processus est également à la base de la vaccination, l’une des procédures médicales les plus efficaces jamais mises au point, qui permet de sauver des millions de vies chaque année. La MA présentent encore de nombreuses questions ouvertes, dont les réponses peuvent améliorer la manière dont nous vaccinons. Les mécanismes à la base de la MA sont extrêmement complexes, avec des interactions non linéaires entre nombreux
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Lang, Birthe Agnetha. "Nanofibrous affinity membranes containing non-antibody binding proteins." Thesis, University of Leeds, 2016. http://etheses.whiterose.ac.uk/15326/.

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The specific removal of molecules from various media is an area receiving increasing attention. Affnity membranes, i.e. membranes containing ligands, which can specifically capture target molecules, can meet this demand. One important area, in which the use of affinity membranes will be beneficial, is blood filtration, specifically haemodialysis treatments. The specific removal of toxins can reduce treatment time and/or frequency and therefore increase patients' quality of life as well as reduce costs for the health care sector. The presented research investigates the feasibility of combining
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Attiya, Said. "Antibody labeling methods for automated affinity electrophoresis on microchips." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0010/NQ59926.pdf.

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Hey, Carolyn McKenzie. "Antibody Purification from Tobacco by Protein A Affinity Chromatography." Thesis, Virginia Tech, 2010. http://hdl.handle.net/10919/42645.

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Antibodies represent the largest group of biopharmaceuticals. Due to the nature of their clinical applications, they often need to be produced in large quantities. Plants have distinct advantages of producing large quantities of recombinant proteins, and tobacco is arguably the most promising plant for plant-made-pharmaceuticals (PMP) due to its high biomass yields and robust transformation technology. However, to produce proteins using transgenic tobacco for human applications, purification of the proteins is challenging. On the other hand, Protein A, a bacterial cell wall protein isolated fr
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Sundberg, Mårten. "Protein microarrays for validation of affinity binders." Licentiate thesis, KTH, Proteomik, 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-48256.

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Is specificity an important issue regarding affinity reagents? What about the validation of affinity reagents today, is it good enough? This depends on the application and the producer of the reagent. Validation should be the most important marketing argument that can be found.Today there is a continuous growth of both the number of affinity reagents that are produced and the different types of affinity reagents that are developed. In proteomics they become more and more important in exploring the human proteome. Therefore, validated affinity reagents should be on top of every proteomic resear
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Qundos, Ulrika. "Antibody based plasma protein profiling." Doctoral thesis, KTH, Proteomik och nanobioteknologi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-126270.

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This thesis is about protein profiling in serum and plasma using antibody suspension bead arrays for the analysis of biobanked samples and in the context of prostate cancer biomarker discovery. The influence of sample preparation methods on antibody based protein profiles were investigated (Papers I-III) and a prostate cancer candidate biomarker identified and verified (Papers III-V). Furthermore, a perspective on the research area affinity proteomics and its’ employment in biomarker discovery, for improved understanding and potentially improved disease diagnosis, is provided. Paper I presents
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Ye, Jianmin. "The relationship between antibody redox structure and affinity in rainbow trout." W&M ScholarWorks, 2008. https://scholarworks.wm.edu/etd/1539616918.

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Teleost immunoglobulin M (IgM), an 800 kDa tetramer, possesses considerable structural diversity due to the non-uniform disulfide polymerization of its halfmeric or monomeric subunits. However, to date, no plausible functional role for this diversity has been demonstrated or proposed. This research was, therefore, designed to investigate the possible functional role(s) for this diversity using the trout model. The possible relationship between this structural diversity and affinity was specifically addressed. The relationship between high levels of disulfide polymerization and high affinity wa
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Midelfort, Katarina Senn. "Biophysical characterization of high affinity engineered single chain Fv antibody fragments." Thesis, Massachusetts Institute of Technology, 2004. http://hdl.handle.net/1721.1/30051.

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Thesis (Ph. D. in Molecular Systems Toxicology and Pharmacology)--Massachusetts Institute of Technology, Biological Engineering Division, 2004.<br>Vita.<br>Includes bibliographical references.<br>High affinity antibody binding interactions are important for both pharmaceutical and biotechnological uses. However, designing higher affinity interactions has remained difficult. Both high affinity interactions from nature and the results from directed evolution affinity maturation processes may yield clues about the important structural and energetic contributions to attain these tight associations
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Fernandes, Telma Godinho Barroso Maciel. "Functional monolithic platforms for antibody purification." Doctoral thesis, Faculdade de Ciências e Tecnologia, 2014. http://hdl.handle.net/10362/11550.

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Dissertação para obtenção do Grau de Doutor em Química Sustentável<br>Fundação para a Ciência e Tecnologia - contracts PEst-C/EQB/LA0006/2011, MIT-Pt/BS-CTRM/0051/2008, PTDC/EBB-BIO/102163/2008, PTDC/EBBBIO/ 098961/2008, PTDC/EBB-BIO/118317/2010 and doctoral grant SFRH/ BD/62475/2009, and Fundação Calouste Gulbenkian
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Libri sul tema "Antibody affinity"

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1933-, Voss Edward W., ed. Anti-DNA antibodies in SLE. Boca Raton, Fla: CRC Press, 1988.

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Capitoli di libri sul tema "Antibody affinity"

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Frenzel, André, Lorin Roskos, Scott Klakamp, Meina Liang, Rosalin Arends, and Larry Green. "Antibody Affinity." In Handbook of Therapeutic Antibodies, 115–40. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2014. http://dx.doi.org/10.1002/9783527682423.ch6.

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Martineau, Pierre. "Affinity Measurements by Competition ELISA." In Antibody Engineering, 657–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_41.

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Boschert, Verena, and Peter Scheurich. "Affinity Measurements with Radiolabeled Antibodies." In Antibody Engineering, 695–704. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_44.

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Kuroda, Daisuke, and Kouhei Tsumoto. "Antibody Affinity Maturation by Computational Design." In Antibody Engineering, 15–34. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8648-4_2.

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Barderas, Rodrigo, Johan Desmet, Philippe Alard, and J. Ignacio Casal. "Affinity Maturation by Semi-rational Approaches." In Antibody Engineering, 463–86. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-974-7_27.

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Johansson, Thomas. "Affinity Measurements Using Quartz Crystal Microbalance (QCM)." In Antibody Engineering, 683–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_43.

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Takkinen, Kristiina, Ari Hemminki, and Hans Söderlund. "Affinity and Specificity Maturation by CDR Walking." In Antibody Engineering, 540–45. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-04605-0_38.

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Thie, Holger. "Affinity Maturation by Random Mutagenesis and Phage Display." In Antibody Engineering, 397–409. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_26.

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Bumke, Maja A., and Dario Neri. "Affinity Measurements by Band Shift and Competition ELISA." In Antibody Engineering, 385–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/978-3-662-04605-0_28.

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Even-Desrumeaux, Klervi, and Patrick Chames. "Affinity Determination of Biotinylated Antibodies by Flow Cytometry." In Antibody Engineering, 443–49. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-974-7_25.

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Atti di convegni sul tema "Antibody affinity"

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Berkner, J. A., G. Mitra, and J. W. Bloom. "MONOCLONAL ANTIBODY BINDING TO FACTOR VIII:C." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644063.

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The interactions of monoclonal antibodies with highly purified Factor VIII:c have been studied utilizing the ELISA technique. ELISA plates were coated with Factor VIII:c, protein A purified monoclonal IgG was then added and bound antibody detected with peroxidase labeled antimouse IgG. A Scatchard-Sips plot approach to data analysis was used to calculate binding constants. The binding constants for four antibodies designated BD10, AD7, C7F7 and 39MH8 were as follows: BD10, KO = 7.1 x 108 M-1, n = 1.1 (moles antibody/moles ligand); AD7, KO = 3.1 x 108 M-1, n = 2.7; C7F7, KO = 3.6 x 1011M-1, n =
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Ryu, Tomiko, Akiko Nakayama, Atsushi Oguchi, Tadatoshi Kinoshita, Mutsuyoshi Kazama, and Takeshi Abe. "MONOCLONAL ANTIBODY WITH PREFERENTIAL AFFINITY FOR LARGE MULTIMERS OF VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644081.

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von Willebrand factor (vWF) consists of a series of multimers of 270,000 mol. wt. subunits. Ristocetin cofactor activity (vWF:RCo) and capacity of binding to platelets of vWF are associated with large multimers, and Type IIA von Willebrand's disease (vWD) is characterized by lack of the large multimers. The significance of multimeric structure in relation to vWF function remains unclear. We obtained a monoclonal antibody (MAb) to human vWF which inhibited ristocetin-induced platelet aggregation. This antibody proved to bind preferentially to larger multimers by the finding that the MAb-conjuga
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Zhou, Zhenhao. "Abstract 340: Development of high affinity anti-CLDN18.2 antibody to treat gastric cancers." 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.am2019-340.

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Haber, Edgar, Marchall T. Runge, Christoph Bode, Betsy Branscomb, and Janet Schnee. "ANTIBODY TARGETED FIBRINOLYSIS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643723.

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Chemical conjugates of fibrin-specificantibodies and plasminogen activators. Urokinase or tPA were linked covalently toamonoclonal antibody specific for the amino terminus of the beta chain of human fibrin (59D8) by means of the unidirectionalcross-linking reagent SPDP. The fibrinolytic potency of the conjugates at equal amidolytic activities was compared to the native plasminogen activators in an assay measuring lysis of 1251-fibrin monomer covalently linked to Sepharose CL-4B. Urokinase was least potent, tPA exhibited a 10fold increase in fibrinolysis whereas both the urokinase and tPA antib
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Pontes, Larissa, Marcus Bezerra, Marcela Fonseca, Marcos Lourenzoni, and Gilvan Furtado. "Construction, by rational design, and initial characterization of affinity mutants of Rituximab fragment antibody." In IV International Symposium on Immunobiologicals & VII Seminário Anual Científico e Tecnológico. Instituto de Tecnologia em Imunobiológicos, 2019. http://dx.doi.org/10.35259/isi.sact.2019_32703.

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Ishihara, Jun, Ako Ishihara, Aslan Mansurov, Koichi Sasaki, Steve S. Lee, John-Michael Williford, Lambert Potin, et al. "Abstract 1553: Collagen affinity improves safety and efficacy of antibody and cytokine cancer immunotherapies." 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.am2019-1553.

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Eun, So-Young, Mijung Lee, Hye-Young Park, Miyoung Oh, Hye In Yum, Aerin Yoon, Eunhee Lee, et al. "Abstract LB-113: Enhanced anti-tumor efficacy of CEACAM1-targeting antibody after affinity maturation." 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-lb-113.

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Ishihara, Jun, Ako Ishihara, Aslan Mansurov, Koichi Sasaki, Steve S. Lee, John-Michael Williford, Lambert Potin, et al. "Abstract 1553: Collagen affinity improves safety and efficacy of antibody and cytokine cancer immunotherapies." 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.sabcs18-1553.

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Doran, Ben, Christy Ritchie, Babu Dhokia, Paul Rogers, and David Jones. "Abstract B128: Affinity optimization of an anti‐MUC1 antibody, (HuHMFG1) also enhances ADCC activity." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-b128.

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YOUNG, D., M. W. GRIFFITHS, and L. BROVKO. "USE OF BIOLUMINESCENCE FOR THE EVALUATION OF AFFINITY CONSTANTS FOR BACTERIAL CELL-ANTIBODY INTERACTIONS." In Bioluminescence and Chemiluminescence - Progress and Current Applications - 12th International Symposium on Bioluminescence (BL) and Chemiluminescence (CL). WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776624_0098.

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