Relevant bibliographies by topics / Antibody-toxin conjugates

Academic literature on the topic 'Antibody-toxin conjugates'

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Published: 4 June 2021
Last updated: 26 January 2023

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Journal articles on the topic "Antibody-toxin conjugates"

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Esteva, Francisco J., Kathy D. Miller, and Beverly A. Teicher. "What Can We Learn about Antibody-Drug Conjugates from the T-DM1 Experience?" American Society of Clinical Oncology Educational Book, no. 35 (May 2015): e117-e125. http://dx.doi.org/10.14694/edbook_am.2015.35.e117.

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Antibody conjugates are a diverse class of therapeutics that consist of a cytotoxic agent linked covalently to an antibody or antibody fragment directed toward a specific cell surface target expressed by tumor cells. The notion that antibodies directed toward targets on the surface of malignant cells could be used for drug delivery is not new. The history of antibody conjugates has been marked by hurdles identified and overcome. Early conjugates used mouse antibodies, drugs that either were not sufficiently potent, were immunogenic (proteins), or were too toxic, and linkers that were not sufficiently stable in circulation. Four main avenues have been explored using antibodies to target cytotoxic agents to malignant cells: antibody-protein toxin (or antibody fragment–protein toxin fusion) conjugates, antibody-chelated radionuclide conjugates, antibody-small molecule conjugates, and antibody-enzyme conjugates administered along with small molecule prodrugs that require metabolism by the conjugated enzyme to release the activated species. Technology is continuing to evolve regarding the protein and small molecule components, and it is likely that single chemical entities soon will be the norm for antibody-drug conjugates. Only antibody-radionuclide conjugates and antibody-drug conjugates have reached the regulatory approval stage, and there are more than 40 antibody conjugates in clinical trials. The time may have come for this technology to become a major contributor to improving treatment for patients with cancer.
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Ahmad, Ateeq, and Kevin Law. "Strategies for designing antibody-toxin conjugates." Trends in Biotechnology 6, no. 10 (October 1988): 246–51. http://dx.doi.org/10.1016/0167-7799(88)90056-x.

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Govindan, Serengulam V., and David M. Goldenberg. "New Antibody Conjugates in Cancer Therapy." Scientific World JOURNAL 10 (2010): 2070–89. http://dx.doi.org/10.1100/tsw.2010.191.

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Targeting of radiation, drugs, and protein toxins to cancers selectively with monoclonal antibodies (MAbs) has been a topic of considerable interest and an area of continued development. Radioimmunotherapy (RAIT) of lymphoma using directly labeled MAbs is of current interest after approval of two radiolabeled anti-CD20 MAbs, as illustrated with the near 100% overall response rate obtained in a recent clinical trial using an investigational radiolabeled anti-CD22 MAb,90Y-epratuzumab. The advantage of pretargeted RAIT over directly labeled MAbs is continuing to be validated in preclinical models of lymphoma and solid tumors. Importantly, the advantages of combining RAIT with radiation sensitizers, with immunotherapy, or a drug conjugate targeting a different antigen are being studied clinically and preclinically. The area of drug-conjugated antibodies is progressing with encouraging data published for the trastuzumab-DM1 conjugate in a phase I clinical trial in HER2-positive breast cancer. The Dock-and-Lock platform technology has contributed to the design and the evaluation of complex antibody-cytokine and antibody-toxin conjugates. This review describes the advances made in these areas, with illustrations taken from advances made in the authors' institutions.
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Liang, X. P., M. E. Lamm, and J. G. Nedrud. "Oral administration of cholera toxin-Sendai virus conjugate potentiates gut and respiratory immunity against Sendai virus." Journal of Immunology 141, no. 5 (September 1, 1988): 1495–501. http://dx.doi.org/10.4049/jimmunol.141.5.1495.

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Abstract Successful oral immunization to prevent infectious diseases in the gastrointestinal tract as well as distant mucosal tissues may depend on the effectiveness of an Ag to induce gut immune responses. We and others have previously reported that cholera toxin possesses strong adjuvant effects on the gut immune response to co-administered Ag. To explore further adjuvant effects of cholera toxin, the holotoxin or its B subunit was chemically cross-linked to Sendai virus. The resulting conjugates, which were not infectious, were evaluated for their capacity to induce gut immune responses against Sendai virus after oral administration to mice. Conjugating cholera toxin to virus significantly enhanced the adjuvant activity of cholera toxin compared to simple mixing. Cholera toxin B subunit, however, did not show an adjuvant effect either by itself or conjugated with the virus. Oral administration of the Sendai virus-cholera toxin conjugate was also able to prime for protective anti-viral responses in the respiratory tract. Mice that were orally immunized with the conjugate and intra-nasally boosted with inactivated virus alone showed virus-specific IgA titers in nasal secretions that correlated with protection against direct nasal challenge with live Sendai virus. For comparison, s.c. immunization was also studied. Systemic immunization with the virus-cholera toxin conjugate induced virus-specific antibody responses in serum as well as in the respiratory tract but failed to protect the upper respiratory tract against virus challenge. Systemic immunization plus an intra-nasal boost did, however, confer a variable degree of protection to the upper respiratory tract, which correlated primarily with bronchoalveolar lavage (lung) antibody titers.
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Panjideh, Hossein, Nicole Niesler, Alexander Weng, and Hendrik Fuchs. "Improved Therapy of B-Cell Non-Hodgkin Lymphoma by Obinutuzumab-Dianthin Conjugates in Combination with the Endosomal Escape Enhancer SO1861." Toxins 14, no. 7 (July 13, 2022): 478. http://dx.doi.org/10.3390/toxins14070478.

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Immunotoxins do not only bind to cancer-specific receptors to mediate the elimination of tumor cells through the innate immune system, but also increase target cytotoxicity by the intrinsic toxin activity. The plant glycoside SO1861 was previously reported to enhance the endolysosomal escape of antibody-toxin conjugates in non-hematopoietic cells, thus increasing their cytotoxicity manifold. Here we tested this technology for the first time in a lymphoma in vivo model. First, the therapeutic CD20 antibody obinutuzumab was chemically conjugated to the ribosome-inactivating protein dianthin. The cytotoxicity of obinutuzumab-dianthin (ObiDi) was evaluated on human B-lymphocyte Burkitt’s lymphoma Raji cells and compared to human T-cell leukemia off-target Jurkat cells. When tested in combination with SO1861, the cytotoxicity for target cells was 131-fold greater than for off-target cells. In vivo imaging in a xenograft model of B-cell lymphoma in mice revealed that ObiDi/SO1861 efficiently prevents tumor growth (51.4% response rate) compared to the monotherapy with ObiDi (25.9%) and non-conjugated obinutuzumab (20.7%). The reduction of tumor volume and overall survival was also improved. Taken together, our results substantially contribute to the development of a combination therapy with SO1861 as a platform technology to enhance the efficacy of therapeutic antibody-toxin conjugates in lymphoma and leukemia.
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Faria, Morse, Marlking Peay, Brandon Lam, Eric Ma, Moucun Yuan, Michael Waldron, William Mylott, Meina Liang, and Anton Rosenbaum. "Multiplex LC-MS/MS Assays for Clinical Bioanalysis of MEDI4276, an Antibody-Drug Conjugate of Tubulysin Analogue Attached via Cleavable Linker to a Biparatopic Humanized Antibody against HER-2." Antibodies 8, no. 1 (January 11, 2019): 11. http://dx.doi.org/10.3390/antib8010011.

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Bioanalysis of complex biotherapeutics, such as antibody-drug conjugates (ADCs), is challenging and requires multiple assays to describe their pharmacokinetic (PK) profiles. To enable exposure-safety and exposure-efficacy analyses, as well as to understand the metabolism of ADC therapeutics, three bioanalytical methods are typically employed: Total Antibody, Antibody Conjugated Toxin or Total ADC and Unconjugated Toxin. MEDI4276 is an ADC comprised of biparatopic humanized antibody attached via a protease-cleavable peptide-based maleimidocaproyl linker to a tubulysin toxin (AZ13599185) with an approximate average drug-antibody ratio of 4. The conjugated payload of MEDI4276 can undergo ester hydrolysis to produce the conjugated payload AZ13687308, leading to the formation of MEDI1498 (de-acetylated MEDI4276). In this report, we describe the development, validation and application of three novel multiplex bioanalytical methods. The first ligand-binding liquid chromatography coupled with tandem mass spectrometry (LBA-LC-MS/MS) method was developed and validated for simultaneous measurement of total antibody and total ADC (antibody-conjugated AZ13599185) from MEDI4276. The second LBA-LC-MS/MS assay quantified total ADC (antibody-conjugated AZ13687308) from MEDI1498. The third multiplex LC-MS/MS assay was used for simultaneous quantification of unconjugated AZ13599185 and AZ13687308. Additional stability experiments confirmed that quantification of the released warhead in the presence of high concentrations of MEDI4276 was acceptable. Subsequently, the assays were employed in support of a first-in-human clinical trial (NCT02576548).
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Yu, Rui, Junjie Xu, Tao Hu, and Wei Chen. "The Pneumococcal Polysaccharide-Tetanus Toxin Native C-Fragment Conjugate Vaccine: The Carrier Effect and Immunogenicity." Mediators of Inflammation 2020 (July 4, 2020): 1–11. http://dx.doi.org/10.1155/2020/9596129.

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The encapsulated bacteria, as Streptococcus pneumonia, Haemophilus influenzae type b, and Neisseria meningitidis, cause serious morbidity and mortality worldwide. The capsular polysaccharide (PS), which could elicit a weak T cell-independent immune response, is a vital virulence determinant. One of the strategies to improve the PS-specific immunogenicity is to conjugate PS with a nontoxic carrier protein. Tetanus toxoid (TT) and CRM197 are the typical carrier proteins for the PS conjugate vaccines. TT is the inactivated tetanus toxin manipulated with formaldehyde, which suffers from the pollution from residual formaldehyde and the incomplete detoxification. CRM197 has the disadvantage of low-yield purification with the requirement of sophisticated culture conditions. Thus, a novel carrier protein without these disadvantages is highly required. The tetanus toxin native C-fragment (Hc) is safe, low-cost, and highly immunogenic with easy purification, which can act as a promising carrier protein. Pneumococcal serogroups 14 and 23F were major epidemic causes of pneumococcal infections. In the present study, the capsular PSs (PS14 and PS23F) were conjugated with Hc, TT, and CRM197, respectively. TT- and CRM197-based conjugates acted as controls for Hc-based conjugates (PS14-Hc and PS23F-Hc). The structural properties of Hc were not fundamentally changed after conjugated with PS. PS14-Hc and PS23F-Hc could potentiate sound PS-specific antibody levels comparable to the controls. Thus, Hc exhibited a practical carrier effect to help the pneumococcal conjugate vaccines perform good immunogenicities.
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Marsh, J. W., and D. M. Neville. "A flexible peptide spacer increases the efficacy of holoricin anti-T cell immunotoxins." Journal of Immunology 140, no. 10 (May 15, 1988): 3674–78. http://dx.doi.org/10.4049/jimmunol.140.10.3674.

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Abstract Immunotoxins, constructed by chemically cross-linking an antibody and protein toxin, do not possess the high efficacy of the native toxin. Decreases in toxicity are due in part to the steric constraints imposed on the two macromolecules, which result in both decreased antibody binding and toxin function. In examining the structural features that influence efficacy in holotoxin-antibody conjugates, it was found that the incorporation of a 29-residue polypeptide, derived from the insulin B chain between the antibody and ricin moiety, resulted in an increase in both potency and efficacy. In a murine model system, potency of the peptide spacer conjugate was increased nearly 10-fold; however, when examined by the procedure used to purge bone marrow, the peptide spacer conjugate was not demonstrably more toxic to nontarget cells than the nonspacer conjugate. Thus, in addition to increases of efficacy and potency, this novel immunotoxin demonstrated increased specificity by approximately 10-fold. To test the general utility of peptide spacer inclusion, a T101-ricin conjugate was constructed with the peptide spacer. It yielded a protein synthesis inhibition rate of -0.6 log/h on MOLT-3 cells, greater than 10-fold more efficacious than a previously constructed nonspacer T101-ricin conjugate examined under similar conditions.
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Govindan, Serengulam V., Gary L. Griffiths, Hans J. Hansen, Ivan D. Horak, and David M. Goldenberg. "Cancer Therapy with Radiolabeled and Drug/Toxin-conjugated Antibodies." Technology in Cancer Research & Treatment 4, no. 4 (August 2005): 375–91. http://dx.doi.org/10.1177/153303460500400406.

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Radioimmunotherapy and antibody-directed chemotherapy have emerged as cancer treatment modalities with the regulatory approval of products for non-Hodgkin's lymphoma and acute myeloid leukemia. Antibody-toxin therapy is likewise on the verge of clinical fruition. Accumulating evidence suggests that radioimmunotherapy may have the best impact in minimal-disease and adjuvant settings, especially with radioresistant solid tumors. For the latter, ongoing efforts in ‘pretargeting’ to increase deliverable tumor radiation dose, combination therapies, and locoregional applications are also of importance. Antibody-drug conjugates have the potential to increase the therapeutic index of chemotherapy by minimizing systemic toxicity and improving tumor targeting. The design of optimal drug conjugates in this regard is predicated upon the proper choice of the target antigen, the cleavable-linker, and the drug. In respect of antibody-toxin conjugates, considerable progress has been made in chemical and recombinant immunotoxin designs, and in the advancement of many products to clinical trials. Continued development of antibody-directed therapies should expand the options available for the management of cancer.
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Lefeber, Dirk J., Barry Benaissa-Trouw, Johannes F. G. Vliegenthart, Johannis P. Kamerling, Wouter T. M. Jansen, Kees Kraaijeveld, and Harm Snippe. "Th1-Directing Adjuvants Increase the Immunogenicity of Oligosaccharide-Protein Conjugate Vaccines Related to Streptococcus pneumoniae Type 3." Infection and Immunity 71, no. 12 (December 2003): 6915–20. http://dx.doi.org/10.1128/iai.71.12.6915-6920.2003.

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ABSTRACT Oligosaccharide (OS)-protein conjugates are promising candidate vaccinesagainst encapsulated bacteria, such as Haemophilus influenzae, Neisseria meningitidis, and Streptococcus pneumoniae. Although the effects of several variables such as OS chain length and protein carrier have been studied, little is known about the influence of adjuvants on the immunogenicity of OS-protein conjugates. In this study, a minimal protective trisaccharide epitope of Streptococcus pneumoniae type 3 conjugated to the cross-reacting material of diphtheria toxin was used for immunization of BALB/c mice in the presence of different adjuvants. Subsequently, half of the mice received a booster immunization with conjugate alone. Independent of the use and type of adjuvant, all mice produced long-lasting anti-polysaccharide type 3 (PS3) antibody levels, which provided full protection against challenge with pneumococcal type 3 bacteria. All adjuvants tested increased the anti-PS3 antibody levels and opsonic capacities as measured by an enzyme-linked immunosorbent assay and an in vitro phagocytosis assay. The use of QuilA or a combination of the adjuvants CpG and dimethyl dioctadecyl ammonium bromide resulted in the highest phagocytic capacities and the highest levels of Th1-related immunoglobulin G (IgG) subclasses. Phagocytic capacity correlated strongly with Th1-associated IgG2a and IgG2b levels, to a lesser extent with Th2-associated IgG1 levels, and weakly with thiocyanate elution as a measure of avidity. Thus, the improved immunogenicity of OS-protein conjugates was most pronounced for Th1-directing adjuvants.
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Dissertations / Theses on the topic "Antibody-toxin conjugates"

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Ng, Wai-yun Louisa. "Production of variants of mitogillin with reduced IgE binding activity." Click to view the E-thesis via HKUTO, 2004. http://sunzi.lib.hku.hk/hkuto/record/B31972093.

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Ng, Wai-yun Louisa, and 吳慧欣. "Production of variants of mitogillin with reduced IgE bindingactivity." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2004. http://hub.hku.hk/bib/B31972093.

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Kwok, Hon Hung. "Immunolesioning in the rat brain." HKBU Institutional Repository, 1999. http://repository.hkbu.edu.hk/etd_ra/234.

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"Construction of a Recombinant Immunotoxin." University of Technology, Sydney. Faculty of Science, 1995. http://hdl.handle.net/2100/270.

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In recent years a number of therapeutically useful immunotoxins have been produced using recombinant gene technology. In general, this involves fusion of a toxin gene with sequence encoding a variety of clinically relevant proteins or peptides. Using these techniques a recombinant immunotoxin has been engineered by fusing the genes encoding an antibody fragment with the sequence of a small cytolytic peptide, melittin. The antibody fragment consists of the antigen binding site derived from a murine monoclonal antibody K- 1-21, which binds to human free kappa light chains and recognises a specific epitope (KMA) expressed on the surface of human myeloma and lymphoma cells. The toxic portion of the molecule is melittin, a 26 amino acid, membrane lytic peptide which is a major component of bee venom. Using PCR a single chain Fv (scFv) was constructed by linking VH and VL genes with an oligonucleotide encoding a flexible, hydrophilic peptide. The melittin gene was synthesised as an oligonucleotide and extended by PCR. Nucleotide sequence encoding a linker peptide was added to the 5' end and a primer encoding a FLAG peptide was used to extend the 3' end. This gene construct was then ligated into the recombinant expression vector, pPOW scFv, to create the fusion gene encoding the recombinant immunotoxin. The gene construct was expressed in the periplasm of E.coli (TOPP2) using the secretion signal pelB . Expression of the foreign protein was monitored by western blot using a monoclonal antibody which recognises the FLAG peptide encoded at the carboxy terminal region of the gene construct. Expression of the recombinant immunotoxin was optimised and the resulting protein was purified using anti-FLAG M2 affinity chromatography. Antigen binding activity was assessed by ELISA and flow cytometry using a human myeloma cell line, HMy2, which expresses the KMA antigen.Binding of the immunotoxin to a control human cell line, K562, which does not express KMA on the cell surface was also assessed. The results indicated that the recombinant immunotoxin retained antigen binding specificity and it was cytotoxic towards the target cell line (HMy2).
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"Construction of a recombinant immunotoxin." Thesis, University of Technology, Sydney. Faculty of Science, 1995. http://hdl.handle.net/10453/20069.

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University of Technology, Sydney. Faculty of Science.
In recent years a number of therapeutically useful immunotoxins have been produced using recombinant gene technology. In general, this involves fusion of a toxin gene with sequence encoding a variety of clinically relevant proteins or peptides. Using these techniques a recombinant immunotoxin has been engineered by fusing the genes encoding an antibody fragment with the sequence of a small cytolytic peptide, melittin. The antibody fragment consists of the antigen binding site derived from a murine monoclonal antibody K- 1-21, which binds to human free kappa light chains and recognises a specific epitope (KMA) expressed on the surface of human myeloma and lymphoma cells. The toxic portion of the molecule is melittin, a 26 amino acid, membrane lytic peptide which is a major component of bee venom. Using PCR a single chain Fv (scFv) was constructed by linking VH and VL genes with an oligonucleotide encoding a flexible, hydrophilic peptide. The melittin gene was synthesised as an oligonucleotide and extended by PCR. Nucleotide sequence encoding a linker peptide was added to the 5' end and a primer encoding a FLAG peptide was used to extend the 3' end. This gene construct was then ligated into the recombinant expression vector, pPOW scFv, to create the fusion gene encoding the recombinant immunotoxin. The gene construct was expressed in the periplasm of E.coli (TOPP2) using the secretion signal pelB . Expression of the foreign protein was monitored by western blot using a monoclonal antibody which recognises the FLAG peptide encoded at the carboxy terminal region of the gene construct. Expression of the recombinant immunotoxin was optimised and the resulting protein was purified using anti-FLAG M2 affinity chromatography. Antigen binding activity was assessed by ELISA and flow cytometry using a human myeloma cell line, HMy2, which expresses the KMA antigen.Binding of the immunotoxin to a control human cell line, K562, which does not express KMA on the cell surface was also assessed. The results indicated that the recombinant immunotoxin retained antigen binding specificity and it was cytotoxic towards the target cell line (HMy2).
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XU, HAO-JI, and 徐鎬基. "Studies on immunotoxin-monoclonal antibody 9.5D-abrin toxin a chain conjugates-against the grith of human cervical cancer cell lines." Thesis, 1991. http://ndltd.ncl.edu.tw/handle/82906099079103529855.

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Books on the topic "Antibody-toxin conjugates"

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Mark, Chamow Steven, and Ashkenazi Avi, eds. Antibody fusion proteins. New York: Wiley-Liss, 1999.

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E, Frankel Arthur, ed. Immunotoxins. Boston: Kluwer Academic Publishers, 1988.

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Phan, Văn Chi. Trichobakin và Immunotoxin tái tổ hợp. Hà Nội: Nhà xuất bản Khoa học tự nhiên và công nghệ, 2008.

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Ramakrishnan, S. Cytotoxic conjugates. Austin: R.G. Landes Co., 1993.

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1960-, Tyle Praveen, and Ram Bhanu P. 1951-, eds. Targeted therapeutic systems. New York: Dekker, 1990.

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1947-, Wiley Ronald G., and Lappi Douglas A, eds. Molecular neurosurgery with targeted toxins. Totowa, N.J: Humana Press, 2005.

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A, Lappi Douglas, ed. Suicide transport and immunolesioning. Austin: R.G. Landes, 1994.

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Frankel, Arthur E. Immunotoxins. Springer, 2012.

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Immunotoxin Methods and Protocols. Humana Press, 2001.

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Frankel, A. Clinical Applications of Immunotoxins (Current Topics in Microbiology and Immunology). Springer-Verlag Telos, 1998.

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Book chapters on the topic "Antibody-toxin conjugates"

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Cumber, Alan J., and Edward J. Wawrzynczak. "Preparation of Cytotoxic Antibody—Toxin Conjugates." In Immunochemical Protocols, 135–44. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-257-9_13.

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Pietersz, Geoffrey, and Ian McKenzie. "Immunotherapy for Cancer—Toxin-Antibody Conjugates." In Toxins and Targets, 65–74. London: Routledge, 2022. http://dx.doi.org/10.4324/9781315076911-8.

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Neville, David M. "Monoclonal Antibody Mediated Drug Delivery and Antibody Toxin Conjugates." In Directed Drug Delivery, 211–30. Totowa, NJ: Humana Press, 1985. http://dx.doi.org/10.1007/978-1-4612-5186-6_12.

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Blakey, David C., Edward J. Wawrzynczak, Philip M. Wallace, and Philip E. Thorpe. "Antibody Toxin Conjugates: A Perspective (Part 1 of 2)." In Monoclonal Antibody Therapy, 50–70. Basel: KARGER, 1988. http://dx.doi.org/10.1159/000318800.

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Blakey, David C., Edward J. Wawrzynczak, Philip M. Wallace, and Philip E. Thorpe. "Antibody Toxin Conjugates: A Perspective (Part 2 of 2)." In Monoclonal Antibody Therapy, 71–90. Basel: KARGER, 1988. http://dx.doi.org/10.1159/000318801.

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Wawrzynczak, Edward J., and Alan J. Cumber. "Immunoaffinity Purification and Quantification of Antibody—Toxin Conjugates." In Immunochemical Protocols, 145–53. Totowa, NJ: Humana Press, 1998. http://dx.doi.org/10.1007/978-1-59259-257-9_14.

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Ohtani, Katsumi, and Yoshio Ueno. "Selective Antitumor Activity of T-2 Toxin-Antibody Conjugates." In Microbial Toxins in Foods and Feeds, 403–9. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4613-0663-4_38.

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Colombatti, M., M. Bisconti, P. Lorenzi, G. Stevanoni, B. Dipasquale, M. Gerosa, and G. Tridente. "Human Glioma Cell Lines: Tumour Associated Antigens Distribution and Sensitivity to Antibody-Toxin or Ligand-Toxin Conjugates. A Preliminary Report." In Proceedings of the 8th European Congress of Neurosurgery, Barcelona, September 6–11, 1987, 121–25. Vienna: Springer Vienna, 1988. http://dx.doi.org/10.1007/978-3-7091-8978-8_26.

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Oldham, Robert K. "Antibody-Drug and Antibody-Toxin Conjugates." In Immunity to Cancer, 575–85. Elsevier, 1985. http://dx.doi.org/10.1016/b978-0-12-586270-7.50053-7.

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"Antibody Toxin Fusions or Conjugates." In Encyclopedia of Cancer, 268. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-46875-3_100201.

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Conference papers on the topic "Antibody-toxin conjugates"

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Terrett, Jonathan A., Rachel Dusek, Dee Aud, Rahel Awdew, Sudha Swaminathan, San Lin Lou, Michael Trang, et al. "Abstract 661: Proteomics and selecting the right combination of target and toxin for antibody-drug-conjugate (ADC) development." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-661.

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Rickles, Richard J., Thomas P. Giordano, Shakira F. Cotard, Jill M. Grenier, Angela Romanelli, and Ti Cai. "Abstract 4765: Drug synergies observed for antibody and toxin components of SAR3419 ADC contribute to overall conjugate efficacy and can be combination drug or tumor cell line dependent." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4765.

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