Relevant bibliographies by topics / Monoclonal

Academic literature on the topic 'Monoclonal'

Author: Grafiati
Published: 4 June 2021
Last updated: 30 January 2023

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Contents

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

Journal articles on the topic "Monoclonal":

1

Panda, Manasi. "Rabies-Monoclonal Antibody - A Perspective." Journal of Communicable Diseases 54, no. 03 (September 30, 2022): 22–26. http://dx.doi.org/10.24321/0019.5138.202285.

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Rabies is an acute viral zoonotic disease that affects the central nervous system (CNS) of all warm-blooded animals, including mammals. Research studies and experience from across the world have demonstrated that appropriate administration of a combination of (a) local wound treatment, (b) anti-rabies vaccination and (c) passive immunization have proved to be quite effective in preventing the occurrence of rabies. As far as passive immunization is concerned, polyclonal plasma-derived rabies immunoglobulins (RIG) pose a number of limitations with scarce supply, high cost, etc. amongst many others. On the contrary Rabies Monoclonal Antibodies (R-mAb) are much cheaper, permit longer-term storage, etc. and hence could offer a more standardized, accessible, affordable and equally efficacious and safer alternative to RIG. Accordingly, this article has tried to throw light on the transition from RIG to monoclonal antibody-based Post Exposure Prophylaxis (PEP) which has been recommended by the WHO strongly. The advantages, limitations and future scope of R-mAb have been discussed at length to give a comprehensive idea about this novel invention in the field of medicine.
2

Bauvois, Adeline, Mélusine Larivière, Hervé Watier, and François Maillot. "Actualités des anticorps monoclonaux dans les maladies monogéniques aujourd’hui." médecine/sciences 35, no. 12 (December 2019): 1026–28. http://dx.doi.org/10.1051/medsci/2019203.

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Les maladies monogéniques sont des maladies génétiques rares mais très nombreuses, avec une sévérité variable. Les premières utilisations des anticorps monoclonaux dans ces maladies remontent aux années 2000 et de nombreux essais sont désormais en cours. Les anticorps monoclonaux anti-(interleukine)IL-1β ont profondément transformé la prise en charge des maladies auto-inflammatoires en modulant la composante inflammatoire et en diminuant le risque d’amylose secondaire ; les anticorps monoclonaux anti-TNF-α et anti-IL-6 sont également prescrits dans ces maladies. Dans le syndrome hémolytique et urémique atypique lié à des défauts de régulation de la voie alterne du complément, l’éculizumab, un anticorps monoclonal anti-C5, a permis d’améliorer le pronostic rénal des patients traités. Plus récemment, le lanadélumab, un anticorps monoclonal anti-kallicréïne plasmatique, est venu renforcer l’arsenal thérapeutique des angiœdèmes héréditaires et le burosumab, un anticorps monoclonal anti-FGF23, celui du rachitisme hypophosphatémique lié à l’X. Ces exemples illustrent bien l’importance de l’utilisation des anticorps monoclonaux dans la prise en charge des maladies monogéniques, l’intérêt de considérer cette option thérapeutique dans ce domaine et la nécessité de poursuivre des recherches.
3

Fujita, T., T. Kamato, and N. Tamura. "Characterization of functional properties of C4-binding protein by monoclonal antibodies." Journal of Immunology 134, no. 5 (May 1, 1985): 3320–24. http://dx.doi.org/10.4049/jimmunol.134.5.3320.

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Abstract We prepared mouse monoclonal antibodies to human C4-binding protein (C4-bp) by fusing spleen cells from mice immunized with purified C4-bp to the mouse myeloma line P3U1. Of four monoclonal antibodies that reacted with intact C4-bp, two were specific for a 48K fragment, one of the chymotryptic cleavage products of C4-bp, and one was specific for another fragment (160K). The fourth monoclonal antibody did not react with either fragment. One of the monoclonals that reacted with the 48K fragment blocked the binding of C4-bp to cell-bound C4b. This monoclonal antibody (TK3) also inhibited two other functions of C4-bp, serving as an essential cofactor for C3b/C4b inactivator (I) in the cleavage of fluid-phase C4b and accelerating the decay of C2a from the C4b,2a complex. The other monoclonals had little or no effect on these activities of C4-bp. In addition, we found that the 48K fragment lost the binding affinity for C4b. However, it can function as a cofactor for I and as a decay-accelerator, although its activities were about 200 times weaker than intact C4-bp on a molar basis. The monoclonal antibody TK3 completely inhibited these activities of the 48K fragment. On the basis of these findings, we conclude that the functionally active site of C4-bp is located on the 48K fragment. Probably, the cofactor and decay-accelerating activities of C4-bp result from the binding of C4-bp to C4b.
4

Velez, D., J. D. Macmillan, and L. Miller. "Production and use of monoclonal antibodies for identification of Bradyrhizobium japonicum strains." Canadian Journal of Microbiology 34, no. 1 (January 1, 1988): 88–92. http://dx.doi.org/10.1139/m88-018.

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Thirteen murine hybridomas capable of producing monoclonal antibodies to somatic antigens on Bradyrhizobium japonicum were developed and an indirect enzyme-linked immunosorbent assay was used to test reactivity of the antibodies against 20 strains of B. japonicum. Although polyclonal antisera from mice immunized with strains of B. japonicum reacted with bacterial cells of all 20 strains, individual monoclonals were more specific. Some antibodies reacted with as few as 2 and one with as many as 11 strains. On the basis of reactivity with the set of 13 monoclonal antibodies, the 20 strains of B. japonicum could be divided arbitrarily into five groups. Three of five monoclonal antibodies tested reacted with bacteroids taken directly from soybean nodules. One monoclonal bound to cells of five species of Rhizobium, but none of the 13 reacted with gram-negative bacteria representing six other genera. Treatment of cells with reagents and heat indicated the chemical nature of the antigens to five of the monoclonals. Antigen reactive with one antibody was destroyed by periodate oxidation indicating that it was a polysaccharide. Two antigens were probably proteins as they could be digested by trypsin and denatured by heat. Two others were inactivated by all three treatments suggesting they were glycoproteins.
5

Campbell, AM, P. Whitford, and RE Leake. "Human monoclonal antibodies and monoclonal antibody multispecificity." British Journal of Cancer 56, no. 6 (December 1987): 709–13. http://dx.doi.org/10.1038/bjc.1987.275.

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Hanna, R. E. B., A. G. Trudgett, and A. Anderson. "Fasciola hepatica: development of monoclonal antibodies against somatic antigens and their characterization by ultrastructural localization of antibody binding." Journal of Helminthology 62, no. 1 (March 1988): 15–28. http://dx.doi.org/10.1017/s0022149x00011147.

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ABSTRACTA series of monoclonal antibodies was prepared against tegumental and internal antigens ofFasciola hepaticaby immunizing mice with whole adult-fluke homogenates prior to harvesting the splenic lymphocytes for fusion. Preliminary screening by the Indirect Fluorescent Antibody technique indicated the occurrence of discrete groups of monoclonals differing from one another in tissue-specificity but within which IFA labelling patterns were fairly consistent. Representative hybridomas for 5 of these groups were stabilized and used to produce ascites fluid in mice. By application of an immunogold labelling technique it was possible to map the distribution of antigens for which each monoclonal antibody had affinity throughout the tissues of 4-week and 12-week flukes. Several monoclonals specifically labelled antigenic determinants on the important tegumental antigen T1. However the distribution of gold colloid labelling suggested that epitopes other than that normally exposed to the infected host were recognized; and several monoclonals specifically attached to T1 antigen in the tegument of juvenile worms only. The glycocalyx of the gut and excretory system of flukes shared T1 antigenicity with the tegument. Monoclonal antibodies were produced against an internal immunogen associated with ribosomes and heterochromatin in active protein-producing cells, and against interstitial material of adult flukes. Monoclonals against antigens in parenchymal cell cytoplasm and in mature vitelline cells were recognized but the corresponding hybridomas were not stabilized.
7

Rieger, Paula Trahan. "Monoclonal Antibodies." American Journal of Nursing 87, no. 4 (April 1987): 469. http://dx.doi.org/10.2307/3470440.

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Kosmas, C., H. Kalofonos, and A. A. Epenetos. "Monoclonal Antibodies." Drugs 38, no. 5 (November 1989): 645–57. http://dx.doi.org/10.2165/00003495-198938050-00001.

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&NA;. "Monoclonal antibodies." Reactions Weekly &NA;, no. 1293 (March 2010): 36. http://dx.doi.org/10.2165/00128415-201012930-00100.

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&NA;. "Monoclonal Antibodies." Journal of Pediatric Hematology/Oncology 25, no. 4 (April 2003): S5—S6. http://dx.doi.org/10.1097/00043426-200304000-00025.

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Journal articles Dissertations / Theses Books

Dissertations / Theses on the topic "Monoclonal":

1

Austin, Eric B. "Human monoclonal antibodies." Thesis, University of Nottingham, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.276187.

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Xu, Wenbin. "Studies of antigenic relationships among spotted fever group rickettsiae by monoclonal antibodies." Aix-Marseille 2, 1997. http://www.theses.fr/1997AIX20665.

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Plumpton, Christopher. "Monoclonal antibodies against phytochrome." Thesis, University of Cambridge, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.358677.

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Fernandes, Carla Sofia. "Análise retrospectiva do achado de pico monoclonal em proteinogramas de rotina." Master's thesis, Universidade da Beira Interior, 2010. http://hdl.handle.net/10400.6/770.

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Introdução: As gamapatias monoclonais constituem um grupo heterogéneo de patologias, caracterizado pela proliferação monoclonal de plasmócitos que produzem e secretam imunoglobulina ou fragmentos desta. Na maioria das vezes, trata-se de uma entidade benigna, usualmente referida como gamapatia monoclonal de significado indeterminado. Contudo, esta pode evoluir para uma situação mais grave como o mieloma múltiplo ou outras gamapatias malignas. A detecção de componente monoclonal através de electroforese e a identificação por imunofixação sérica e/ou urinária de rotina são fundamentais para o seu diagnóstico, dada a sua variabilidade de manifestações clínicas. O principal objectivo deste estudo é salientar a importância da componente laboratorial no diagnóstico das gamapatias monoclonais. Métodos: Efectuou-se uma análise retrospectiva das electroforeses e imunofixações realizadas no Serviço de Patologia Clínica do Centro Hospitalar Cova da Beira durante o ano de 2009. Resultados: Neste estudo, foram incluídos 3407 indivíduos, 1983 (58,2%) do sexo feminino e 1424 (41,8%) do sexo masculino, com uma idade média de 65 anos. Durante o ano de 2009, a incidência de picos monoclonais foi de 3,55%. Os serviços de Hematologia e de Medicina Interna foram os que detectaram o maior número de picos monoclonais. Do total de indivíduos com componente monoclonal, 74 (61,2%) eram do sexo masculino e 47 (38,8%) do sexo feminino, apresentando uma idade média de 72 anos. A incidência das cadeias pesadas foi de 59,5% para IgG, 22,4% para IgM e por último 15,6% para IgA. Em relação às cadeias leves, a incidência de kappa foi de 62% e de lambda 38%. Em 5 indivíduos foram detectados picos biclonais, tendo-se obtido uma incidência de 4,13%. Conclusão: A electroforese de proteínas pode ser considerada um bom método de triagem para detecção precoce de gamapatias monoclonais e a imunofixação para confirmação diagnóstica e para a caracterização das gamapatias monoclonais.
Introduction: Monoclonal gammopathies comprise of a heterogeneous group of pathologies, characterized by the monoclonal proliferation of plasmocytes, which produce and secrete immunoglobulins or fragments of these. In the majority of cases, this is a benign entity known as monoclonal gammopathy of undetermined significance. However, it is possible that these gammopathies may lead to the development of more serious conditions, mainly multiple myeloma and other malignant gammopathies. Critical to the diagnosis of these immunoglobinopathies is the routine detection of the monoclonal component by means of electrophoresis and serous/urinary immunofixation, as they may present with a wide variety of clinical manifestations. The main objective of this study is to emphasize the importance of laboratorial screening in the diagnosis of monoclonal gammopathies. Methods: A retrospective study was carried out, consisting in the analysis of electrophoresis and immunofixations applied to patients of the Clinical Pathology Department of the Cova da Beira Hospital Centre throughout the year 2009. Results: This study comprised of 3407 participants, 1983 (58.2%) females and 1424 (41.8%) males, with an average age of 65 years. Throughout the year 2009, the incidence of monoclonal peaks pregistered at the Cova da Beira Hospital Centre was 3.55%. The departments which detected the largest number of monoclonal peaks were Hematology and Internal Medicine. Within the total number of individuals presenting with monoclonal components, 74 (61.2%) were male and 47 (38.8%) were female, with an average age of 72 years. The incidence of heavy chains was 59.5% for IgG, 22.4% for IgM and 15.6 % for IgA. With respect to the light chains, the incidence of kappa chains was 62% and lambda chains 38%. Biclonal peaks were found in 5 individuals with a corresponding incidence of 4.13%. Conclusion: The electrophoresis of proteins may be considered as a good screening method for the early detection of monoclonal gammopathies, and immunofixation can be employed for confirmation of the diagnosis and characterization of the monoclonal gammopathies.
5

Benjamin, Richard John. "Tolerance induction with monoclonal antibodies." Thesis, University of Cambridge, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.253988.

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Qin, Shi-Xin. "Transplantation tolerance with monoclonal antibodies." Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305697.

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Heron, Andrew David. "The stability of monoclonal antibodies." Thesis, University of Glasgow, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.252169.

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Isaacs, John Dudley. "Improving serotherapy with monoclonal antibodies." Thesis, University of Cambridge, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386115.

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Paudel, Subhash. "Shear thinning in monoclonal antibodies." Thesis, Kansas State University, 2016. http://hdl.handle.net/2097/32833.

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Abstract:
Master of Science
Department of Physics
Jeremy D. Schmit
Antibodies are large Y-shaped proteins which are used by immune system to identify and neutralize pathogens. Monoclonal antibody therapy is used to treat different patient conditions. There are problems associated with the manufacturability and deliverability of mAb solutions due to the viscous nature of the protein. The viscosity of antibody solutions increases with the increase in concentration and decreases with applied shear. We want to know why these behaviours are seen and to address this problem we have developed a theory describing the rapid viscosity increase with increasing concentration. We use the polymer theory to explain this behaviour. Here antibodies are treated as polymers. The length of the polymer depend on the aggregation. The reptation time increases approximately as the cubic power of size of aggregate (N³ ). We see the shear thinning behaviour is dependent on the Ab-Ab binding energy and find the relationship between the size of the aggregate and the binding energy. We find aggregate size and morphology using several models for Ab-Ab interaction sites. We use the head to head binding (fAb-fAb binding) model to describe aggregation state in our viscosity theory. The size of the aggregate and hence the reptation time is captured by the binding energy. When the binding energy increases the zero shear viscosity increases and the reptation time decreases. Likewise when the binding energy decreases the zero shear viscosity decreases and the reptation time increases. We have yet to find the correct exponents for the shear thinning behaviour of different mAbs which would be our future work.
10

Ueda, Yasuji. "MONOCLONAL ANTIBODIES TO CHICK CRYSTALLINS." 京都大学 (Kyoto University), 1989. http://hdl.handle.net/2433/86412.

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Books on the topic "Monoclonal":

1

L, Beverley Peter C., ed. Monoclonal antibodies. Edinburgh: Churchill Livingstone, 1986.

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Ossipow, Vincent, and Nicolas Fischer, eds. Monoclonal Antibodies. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-992-5.

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Albitar, Maher, ed. Monoclonal Antibodies. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-323-3.

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Peters, Johann Hinrich, and Horst Baumgarten, eds. Monoclonal Antibodies. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4.

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L, Macario Alberto J., and Conway de Macario Everly, eds. Monoclonal antibodies against bacteria. Orlando: Academic Press, 1985.

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Davis, William C. Monoclonal Antibody Protocols. New Jersey: Humana Press, 1995. http://dx.doi.org/10.1385/0896033082.

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Borrebaeck, Carl A. K., and James W. Larrick, eds. Therapeutic Monoclonal Antibodies. London: Palgrave Macmillan UK, 1990. http://dx.doi.org/10.1007/978-1-349-11894-6.

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Steinitz, Michael, ed. Human Monoclonal Antibodies. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-586-6.

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An, Zhiqiang, ed. Therapeutic Monoclonal Antibodies. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2009. http://dx.doi.org/10.1002/9780470485408.

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Steinitz, Michael, ed. Human Monoclonal Antibodies. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8958-4.

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Book chapters on the topic "Monoclonal":

1

Peters, J. H., and D. Baron. "Introduction." In Monoclonal Antibodies, 1–17. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_1.

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Peters, J. H., M. Schulze, M. Grol, S. Schiefer, H. Baumgarten, J. Endl, H. Xu, et al. "Demonstration of Monoclonal Antibodies." In Monoclonal Antibodies, 316–461. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_10.

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Baron, D. "Safety Precautions at Work." In Monoclonal Antibodies, 463–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_11.

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Peters, Johann Hinrich, and Horst Baumgarten. "Appendix." In Monoclonal Antibodies, 466–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_12.

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Wiggenhauser, A., J. H. Peters, and H. Baumgarten. "Preconditions for Hybridoma Technology." In Monoclonal Antibodies, 18–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_2.

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Baumgarten, H., M. Schulze, J. H. Peters, and T. Hebell. "Immunization." In Monoclonal Antibodies, 39–70. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_3.

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Wiggenhauser, A., J. H. Peters, H. Baumgarten, and A. Borgya. "Taking Blood and Isolating Cells." In Monoclonal Antibodies, 71–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_4.

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Peters, J. H., E. Debus, H. Baumgarten, R. Würzner, M. Schulze, and Helga Gerlach. "Cell Culture." In Monoclonal Antibodies, 88–136. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_5.

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Baron, D., J. H. Peters, R. K. H. Gieseler, S. Lenzner, H. Baumgarten, R. Würzner, B. Goller, and Th Werfel. "Production of Hybridomas." In Monoclonal Antibodies, 137–222. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_6.

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Baumgarten, H., R. Franze, J. H. Peters, A. Borgya, D. Baron, E. Debus, and M. Kubbies. "Mass Production of Monoclonal Antibodies." In Monoclonal Antibodies, 223–57. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-74532-4_7.

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Conference papers on the topic "Monoclonal":

1

Clemetson, K. J., R. Weber, and J. L. McGregor. "TOPOLOGY OF PLATELET GPIb INVESTIGATED BY LOCATION OF MONOCLONAL ANTIBODY EPITOPES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643625.

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A large number of monoclonal antibodies to platelet membrane glycoprotein lb (GPIb) have been described but for most of these the position of the epitope is not known. Since many of these influence platelet function, a better understanding of struc-ture-function relationships requires this knowledge. The position of the epitopes for the monoclonal antibodies API (Dr. T.J. Kunicki), AN51 and SZ-2 (Dr. C-G. Ruan), WM23 (Dr. M.C. Berndt) and PI were determined by analysis of proteolytic cleavage fragments of glycocalicin via affinity chromatography on the monoclonal antibodies coupled to Sepharose, elution with diethyl ami ne solution, separation on SDS-gel electrophoresis and detection by silver-staining. First, intact glycocalicin was examined and was found to bind to all monoclonals with the exception of PI. All monoclonals bound intact GPIb. WM23 bound a 70 kDa glycopeptide from the highly-glycosylated 90 kDa tryptic fragment of glycocalicin. API, AN51 and SZ-2 all bound to 45 kDa and 40 kDa, poorly glycosylated tryptic fragments. The 40 kDa fragment is derived from the 45 kDa fragment and has been shown to be the N-terminal region of GPIb. All these monoclonals have been shown to inhibit von Willebrand factor induced platelet agglutination. Platelets were treated with either elastase or calcium activated protease and monoclonal binding checked by immunofluorescence. The immunofluorescence with API, AN51 and SZ-2 was minimal compared to control platelets whereas that of PI remained as strong as the controls. This indicates that the epitope for PI lies on GPIb in a region other than glycocalicin and its absence from glycocalicin is not simply due to conformational changes in that fragment. Since PI inhibits platelet activation by thrombin and ADP it must act via conformational effects and not by blocking the thrombin receptor which lies on the 45 kDa region of glycocalicin. These results support a more complex role for GPIb in platelet activation.
2

Hessing, Martin, Joost C. M. Meijers, Jan A. van Mourik, and Bonno N. Bouma. "MONOCLONAL ANTIBODIES TO HUMAN PROTEIN S AND C4b-BINDING PROTEIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644291.

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Protein S (PS) circulates in plasma both free and in reversible association with the complement component C4b-binding protein (C4bp). Only free PS is functional as a cofactor for activated protein C (APC). Cleavage of PS by thrombin at a site near the r-carboxyglutamic acid domain is associated with a loss of cofactor activity. This may be a control mechanism for the anticoagulant activity of APC. These observations led us to investigate the role of C4bp and thrombin in the regulation of PS. Complex formation between purified PS and C4bp was studied in plasma and in a system with purified components. 125I-labeled PS was first incubated with either C4bp or citrated plasma and then subjected to polyacrylamide gelelectrophoresis in the absence of SDS. The formation of the C4bp-PS complex in plasma and in the purified system was demonstrated by autoradiography. Crossed immuno-electrophoresis using an antiserum against PS was performed in the presence of 8 mM EDTA. Human citrated plasma showed two precipitin peaks. Free PS migrated rapidly in the first dimension, whereas the C4bp-PS complex was just anodal to the application slot. The addition of C4bp to either plasma or purified PS resulted in the disappearance of the free PS peak and an increase of the slower migrating peak. The effect of purified C4bp on the PS-cofactor function of APC was studied in citrated plasma. The prolongation of the APTT induced by the addition of APC could be inhibited by the addition of increasing amounts of C4bp. Monoclonal antibodies to PS and C4bp were prepared and characterized. The monoclonal antibodies to either PS or C4bp did not block the complex formation between and PS, as was demonstrated by dot blotting of C4bp with 125I-PS and agarose gelelectrophoresis followed by Western blotting. Three out of 7 monoclonal antibodies to PS did not detect PS after thrombin cleavage on an immunoblot after non-reduced SDS polyacrylamide gelelectrophoresis. These 3 antibodies gave a significant shortening of the prolonged APTT induced by the addition of APC to normal plasma, indicating that these monoclonals inhibited the cofactor function of PS. The other 4 monoclonals to PS that did detect PS after thrombin cleavage on an immunoblot, gave only a minor inhibition of the PS cofactor function.
3

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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Abstract:
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 = 0.03; 39MH8, K = 6.0 x 1011 M-1, n = 0.03. The binding constants for C7F7 to the purified carboxy-terminal (residues 1649-2332) 80 kD functional region of the Factor VIII:c molecule were also determined: KO = 1.0 x 1011 M-1, n = 0.55. On the basis of these results the following conclusions can be drawn: 1) the antibodies can be divided into two groups: high affinity (suitable for use in immunopurification), C7F7 and 39MH8; low affinity: BD10 and AD7; 2) the antibodies in the low affinity group have valance values two orders of magnitude higher than the high affinity antibodies, C7F7 and 39MH8. The difference might be explained by the high affinity antibody epitopes on the immobilized Factor VIII:c being less exposed to the solution; 3) C7F7 binding to the 80 kD polypeptide, compared to the whole Factor VIII:c molecule, gave virtually identical Kc values, but dramatically different valance values. This suggests that the C7F7 epitope is more accessible on the 80 kD polypeptide.
4

Yang, Wu, Li-ming Wang, Zhao Wei, and Yuan Junlin. "Preliminary Production of Anti- Glufosinate Monoclonal Antibodies." In 2007 1st International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2007. http://dx.doi.org/10.1109/icbbe.2007.18.

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5

Hasan, T. "Selective Phototoxicity Using Monoclonal Antibody-Chromophore Conjugates." In O-E/Fiber LASE '88, edited by Tayyaba Hasan. SPIE, 1989. http://dx.doi.org/10.1117/12.960183.

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6

Young, Colin R., Alice Lee, and Larry H. Stanker. "Detection of Campylobacter species using monoclonal antibodies." In Photonics East (ISAM, VVDC, IEMB), edited by Yud-Ren Chen. SPIE, 1999. http://dx.doi.org/10.1117/12.335779.

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7

Gdowski, Andrew, Amalendu Ranjan, Anindita Mukerjee, and Jamboor Vishwanatha. "Abstract 4396: Nanocarrier for monoclonal antibody delivery." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4396.

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8

Ray, Jason C., Penelope Allen, Ann Bacsi, Julian Bosco, Luke Chen, Michael Eller, Lyndell Lim, et al. "076 Inflammatory complications of CGRP monoclonal antibodies." In ANZAN Annual Scientific Meeting 2021 Abstracts. BMJ Publishing Group Ltd, 2021. http://dx.doi.org/10.1136/bmjno-2021-anzan.76.

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9

Varlamova, EY, VI Vasiliev, EY Saridi, MV Simonova, NS Shornikova, VR Gorodetsky, NN Tupizyn, and EN Sholokhova. "FRI0227 Monoclonal secretion duiring sjogren’s syndrome (ss)." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.320.

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10

Metzelaar, M. J., H. K. Nieuwenhuis, and J. J. Sixma. "DETECTION OF ACTIVATED PLATELETS WITH MONOCLONAL ANTIBODIES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643829.

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Abstract:
Blood tests reflecting in-vivo activation of platelets are potentially useful in evaluating patients with thrombotic diseases. Recently monoclonal antibodies have been described that react preferentially with activated platelets. We prepared an IgG2b antibody, designated RUU-AP 2.28, that reacted with a 53.000 MW protein that is located in a special subclass of platelet granules in unstimulated platelets and that is exposed on the surface of activated platelets. Increased numbers of platelets that expressed the 2.28 antigen on their surface were observed in patients undergoing cardiopulmonary bypass and in patients with acute deep venous thrombosis. The percentage of RUU-AP 2.28 positive platelets in the circulation was 3,9 ± 2.7 (SD)% in the controls, (n = 20), 24.6 ± 13.5% in patients after cardiopulmonary surgery (n = 10) and 8.5% in patients with acute deep venous thrombosis (n = 2).In order to detect also earlier stages of platelet activation, such as secretion-independent phenomena, we produced new monoclonal antibodies by fusing spleen cells from Balb/c mice, immunized with thrombin stimulated, paraformaldehyde fixed platelets, with Ag 8653 myeloma cells. As a screening assay we used an ELISA with freshly fixed platelets or fixed thrombin-activated platelets. We detected six monoclonal antibodies (RUU-AP 1-6) specific for thrombin-activated platelets. The results of the ELISA were confirmed by flow cytofluorometry.None of the antibodies inhibited platelet aggregation induced by ADP, collagen or ristocetin. Ascites of IgGl antibody RUU-AP 3 reacted with normal thrombin-activated platelets but did not react with thrombin-activated platelets from a patient with Glanzmann’s disease. In addition antibody RUU-AP 3 reacted with normal platelets stimulated with 1 pM of ADP. These data suggest that antibody RUU-AP 3 detects a secretion-independent conformational change in the platelet membrane glycoprotein IIb-IIIa complex.

Reports on the topic "Monoclonal":

1

Snyder, Christopher M., and Lawrence J. Wysocki. Dissecting Immunogenicity of Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, June 2002. http://dx.doi.org/10.21236/ada407659.

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2

Snyder, Christopher M., and Lawrence J. Wysocki. Dissecting Immunogenicity of Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, June 2003. http://dx.doi.org/10.21236/ada417364.

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3

Jaszczak, R. J. SPECT assay of radiolabeled monoclonal antibodies. Office of Scientific and Technical Information (OSTI), February 1992. http://dx.doi.org/10.2172/7197646.

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Jaszczak, R. J. SPECT assay of radiolabeled monoclonal antibodies. Office of Scientific and Technical Information (OSTI), February 1992. http://dx.doi.org/10.2172/7288347.

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Chia, John K. Polymyxin B(PMB)-Specific Monoclonal Antibodies. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada231817.

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Sato, J. D. Receptor Monoclonal Antibodies that Inhibit Tumor Angiogenesis. Fort Belvoir, VA: Defense Technical Information Center, August 2001. http://dx.doi.org/10.21236/ada398146.

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Sato, J. D. Receptor Monoclonal Antibodies that Inhibit Tumor Angiogenesis. Fort Belvoir, VA: Defense Technical Information Center, August 1999. http://dx.doi.org/10.21236/ada383129.

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Glassy, Mark C. Neutralizing Monoclonal Antibodies against Biological Toxins. Phase 1. Fort Belvoir, VA: Defense Technical Information Center, August 1993. http://dx.doi.org/10.21236/adb176298.

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Jaszczak, Ronald, J. Final Progress Report: SPECT Assay of Radiolabeled Monoclonal Antibodies. Office of Scientific and Technical Information (OSTI), September 2004. http://dx.doi.org/10.2172/886018.

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Volkert, W. A., A. R. Ketring, R. R. Kuntz, R. A. Holmes, E. P. Mitchell, and T. L. Feldbush. Production of radiolabeled monoclonal antibody conjugates by photoaffinity labeling. Office of Scientific and Technical Information (OSTI), June 1990. http://dx.doi.org/10.2172/6445745.

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To the bibliography