Relevant bibliographies by topics / Cell surface antigen receptors

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

Academic literature on the topic 'Cell surface antigen receptors'

Author: Grafiati
Published: 4 June 2021
Last updated: 7 February 2022

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Journal articles on the topic "Cell surface antigen receptors"

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Sachen, Kacey L., Michael J. Strohman, Jonathan Singletary, Ash A. Alizadeh, Nicole H. Kattah, Chen Lossos, Elizabeth D. Mellins, Shoshana Levy, and Ronald Levy. "Self-antigen recognition by follicular lymphoma B-cell receptors." Blood 120, no. 20 (November 15, 2012): 4182–90. http://dx.doi.org/10.1182/blood-2012-05-427534.

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Abstract Follicular lymphoma is a monoclonal B-cell malignancy with each patient's tumor expressing a unique cell surface immunoglobulin (Ig), or B-cell receptor (BCR), that can potentially recognize antigens and/or transduce signals into the tumor cell. Here we evaluated the reactivity of tumor derived Igs for human tissue antigens. Self-reactivity was observed in 26% of tumor Igs (25 of 98). For one follicular lymphoma patient, the recognized self-antigen was identified as myoferlin. This patient's tumor cells bound recombinant myoferlin in proportion to their level of BCR expression, and the binding to myoferlin was preserved despite ongoing somatic hypermutation of Ig variable regions. Furthermore, BCR-mediated signaling was induced after culture of tumor cells with myoferlin. These results suggest that antigen stimulation may provide survival signals to tumor cells and that there is a selective pressure to preserve antigen recognition as the tumor evolves.
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Simon, Bianca, Dennis C. Harrer, Beatrice Schuler-Thurner, Gerold Schuler, and Ugur Uslu. "Arming T Cells with a gp100-Specific TCR and a CSPG4-Specific CAR Using Combined DNA- and RNA-Based Receptor Transfer." Cancers 11, no. 5 (May 20, 2019): 696. http://dx.doi.org/10.3390/cancers11050696.

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Tumor cells can develop immune escape mechanisms to bypass T cell recognition, e.g., antigen loss or downregulation of the antigen presenting machinery, which represents a major challenge in adoptive T cell therapy. To counteract these mechanisms, we transferred not only one, but two receptors into the same T cell to generate T cells expressing two additional receptors (TETARs). We generated these TETARs by lentiviral transduction of a gp100-specific T cell receptor (TCR) and subsequent electroporation of mRNA encoding a second-generation CSPG4-specific chimeric antigen receptor (CAR). Following pilot experiments to optimize the combined DNA- and RNA-based receptor transfer, the functionality of TETARs was compared to T cells either transfected with the TCR only or the CAR only. After transfection, TETARs clearly expressed both introduced receptors on their cell surface. When stimulated with tumor cells expressing either one of the antigens or both, TETARs were able to secrete cytokines and showed cytotoxicity. The confirmation that two antigen-specific receptors can be functionally combined using two different methods to introduce each receptor into the same T cell opens new possibilities and opportunities in cancer immunotherapy. For further evaluation, the use of these TETARs in appropriate animal models will be the next step towards a potential clinical use in cancer patients.
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Kamiya, Takahiro, Desmond Wong, Yi Tian Png, and Dario Campana. "A novel method to generate T-cell receptor–deficient chimeric antigen receptor T cells." Blood Advances 2, no. 5 (March 5, 2018): 517–28. http://dx.doi.org/10.1182/bloodadvances.2017012823.

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Key Points Newly designed PEBLs prevent surface expression of T-cell receptor in T cells without affecting their function. Combined with chimeric antigen receptors, PEBLs can rapidly generate powerful antileukemic T cells without alloreactivity.
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Apostolopoulos, Vasso, Theresia Thalhammer, Andreas G. Tzakos, and Lily Stojanovska. "Targeting Antigens to Dendritic Cell Receptors for Vaccine Development." Journal of Drug Delivery 2013 (October 8, 2013): 1–22. http://dx.doi.org/10.1155/2013/869718.

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Dendritic cells (DCs) are highly specialized antigen presenting cells of the immune system which play a key role in regulating immune responses. Depending on the method of antigen delivery, DCs stimulate immune responses or induce tolerance. As a consequence of the dual function of DCs, DCs are studied in the context of immunotherapy for both cancer and autoimmune diseases. In vaccine development, a major aim is to induce strong, specific T-cell responses. This is achieved by targeting antigen to cell surface molecules on DCs that efficiently channel the antigen into endocytic compartments for loading onto MHC molecules and stimulation of T-cell responses. The most attractive cell surface receptors, expressed on DCs used as targets for antigen delivery for cancer and other diseases, are discussed.
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Wang, Ninghai, Abhay Satoskar, William Faubion, Duncan Howie, Susumu Okamoto, Stefan Feske, Charles Gullo, et al. "The Cell Surface Receptor SLAM Controls T Cell and Macrophage Functions." Journal of Experimental Medicine 199, no. 9 (May 3, 2004): 1255–64. http://dx.doi.org/10.1084/jem.20031835.

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Signaling lymphocyte activation molecule (SLAM), a glycoprotein expressed on activated lymphocytes and antigen-presenting cells, has been shown to be a coregulator of antigen-driven T cell responses and is one of the two receptors for measles virus. Here we show that T cell receptor–induced interleukin (IL)-4 secretion by SLAM−/− CD4+ cells is down-regulated, whereas interferon γ production by CD4+ T cells is only slightly up-regulated. Although SLAM controls production of IL-12, tumor necrosis factor, and nitric oxide in response to lipopolysaccharide (LPS) by macrophages, SLAM does not regulate phagocytosis and responses to peptidoglycan or CpG. Thus, SLAM acts as a coreceptor that regulates signals transduced by the major LPS receptor Toll-like receptor 4 on the surface of mouse macrophages. A defective macrophage function resulted in an inability of SLAM−/− C57Bl/6 mice to remove the parasite Leishmania major. We conclude that the coreceptor SLAM plays a central role at the interface of acquired and innate immune responses.
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Meiliana, Anna, Nurrani Mustika Dewi, and Andi Wijaya. "CAR T Cells: Precision Cancer Immunotherapy." Indonesian Biomedical Journal 10, no. 3 (December 28, 2018): 203–16. http://dx.doi.org/10.18585/inabj.v10i3.635.

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BACKGROUND: Current cancer drugs and treatments are aiming at eradicating tumor cells, but often are more toxic then effective, killing also the normal cells and not selectively the tumor cells. There is good personalized cancer therapy that involves administration to the cancer-bearing host of immune cells with direct anticancer activity, which called adoptive cell therapy (ACT). A review of the unique biology of T cell therapy and of recent clinical experience compels a reassessment of target antigens that traditionally have been viewed from the perspective of weaker immunotherapeutic modalities.CONTENT: Chimeric antigen receptors (CAR) are recombinant receptors which provide both antigen-binding and T cell-activating functions. Many kind of CARs has been reported for the past few years, targeting an array of cell surface tumor antigens. Their biologic functions have extremely changed following the introduction of tripartite receptors comprising a costimulatory domain, termed second-generation CARs. The combination of CARs with costimulatory ligands, chimeric costimulatory receptors, or cytokines can be done to further enhance T cell potency, specificity and safety. CARs reflects a new class of drugs with exciting potential for cancer immunotherapy.SUMMARY: CAR-T cells have been arising as a new modality for cancer immunotherapy because of their potent efficacy against terminal cancers. They are known to exert higher efficacy than monoclonal antibodies and antibodydrug conjugates, and act via mechanisms distinct from T cell receptor-engineered T cells. These cells are constructed by transducing genes encoding fusion proteins of cancer antigen-recognizing single-chain Fv linked to intracellular signaling domains of T cell receptors.KEYWORDS: chimeric antigen receptor, CAR T cells, adoptive cell therapy, ACT, T cell receptor, TCR, cancer, immunotherapy
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Ketchum, Christina M., Xiaoyu Sun, Alexandra Suberi, John T. Fourkas, Wenxia Song, and Arpita Upadhyaya. "Subcellular topography modulates actin dynamics and signaling in B-cells." Molecular Biology of the Cell 29, no. 14 (July 15, 2018): 1732–42. http://dx.doi.org/10.1091/mbc.e17-06-0422.

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B-cell signaling activation is most effectively triggered by the binding of B-cell receptors (BCRs) to membrane-bound antigens. In vivo, B-cells encounter antigen on antigen-presenting cells (APC), which possess complex surfaces with convoluted topographies, a fluid membrane and deformable cell bodies. However, whether and how the physical properties of antigen presentation affect B-cell activation is not well understood. Here we use nanotopographic surfaces that allow systematic variation of geometric parameters to show that surface features on a subcellular scale influence B-cell signaling and actin dynamics. Parallel nanoridges with spacings of 3 microns or greater induce actin intensity oscillations on the ventral cell surface. Nanotopography-induced actin dynamics requires BCR signaling, actin polymerization, and myosin contractility. The topography of the stimulatory surface also modulates the distribution of BCR clusters in activated B-cells. Finally, B-cells stimulated on nanopatterned surfaces exhibit intracellular calcium oscillations with frequencies that depend on topography. Our results point to the importance of physical aspects of ligand presentation, in particular, nanotopography for B-cell activation and antigen gathering.
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Crowther, Michael D., Inge Marie Svane, and Özcan Met. "T-Cell Gene Therapy in Cancer Immunotherapy: Why It Is No Longer Just CARs on The Road." Cells 9, no. 7 (June 30, 2020): 1588. http://dx.doi.org/10.3390/cells9071588.

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T-cells have a natural ability to fight cancer cells in the tumour microenvironment. Due to thymic selection and tissue-driven immunomodulation, these cancer-fighting T-cells are generally low in number and exhausted. One way to overcome these issues is to genetically alter T-cells to improve their effectiveness. This process can involve introducing a receptor that has high affinity for a tumour antigen, with two promising candidates known as chimeric-antigen receptors (CARs), or T-cell receptors (TCRs) with high tumour specificity. This review focuses on the editing of immune cells to introduce such novel receptors to improve immune responses to cancer. These new receptors redirect T-cells innate killing abilities to the appropriate target on cancer cells. CARs are modified receptors that recognise whole proteins on the surface of cancer cells. They have been shown to be very effective in haematological malignancies but have limited documented efficacy in solid cancers. TCRs recognise internal antigens and therefore enable targeting of a much wider range of antigens. TCRs require major histocompatibility complex (MHC) restriction but novel TCRs may have broader antigen recognition. Moreover, there are multiple cell types which can be used as targets to improve the “off-the-shelf” capabilities of these genetic engineering methods.
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Franco, A., M. Paroli, U. Testa, R. Benvenuto, C. Peschle, F. Balsano, and V. Barnaba. "Transferrin receptor mediates uptake and presentation of hepatitis B envelope antigen by T lymphocytes." Journal of Experimental Medicine 175, no. 5 (May 1, 1992): 1195–205. http://dx.doi.org/10.1084/jem.175.5.1195.

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Human activated T lymphocytes expressing class II molecules are able to present only complex antigens that bind to their own surface receptors, and thus can be captured, internalized, and processed through the class II major histocompatibility complex processing pathway. We have used the antigen-presenting T cell system to identify the viral receptor used by hepatitis B virus (HBV) to enter cells, as well as the sequence of HB envelope antigen (HBenvAg) involved in this interaction. Results show that both CD4+ and CD8+ T clones can process and present HBenvAg to class II-restricted cytotoxic T lymphocytes and that the CD71 transferrin receptor (TfR) is involved in efficient HBenvAg uptake by T cells. Moreover, we provide evidence that the HBenvAg sequence interacting with the T cell surface is contained within the pre-S2 region. Since TfR is also expressed on hepatocytes, it might represent a portal of cellular entry for HBV infection. This system of antigen presentation by T cells may serve as a model to study both lymphocyte receptors used by lymphocytotropic viruses and viral proteins critical to bind them.
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Moores, Sheri L., Laura M. Selfors, Jessica Fredericks, Timo Breit, Keiko Fujikawa, Frederick W. Alt, Joan S. Brugge, and Wojciech Swat. "Vav Family Proteins Couple to Diverse Cell Surface Receptors." Molecular and Cellular Biology 20, no. 17 (September 1, 2000): 6364–73. http://dx.doi.org/10.1128/mcb.20.17.6364-6373.2000.

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ABSTRACT Vav proteins are guanine nucleotide exchange factors for Rho family GTPases which activate pathways leading to actin cytoskeletal rearrangements and transcriptional alterations. Vav proteins contain several protein binding domains which can link cell surface receptors to downstream signaling proteins. Vav1 is expressed exclusively in hematopoietic cells and tyrosine phosphorylated in response to activation of multiple cell surface receptors. However, it is not known whether the recently identified isoforms Vav2 and Vav3, which are broadly expressed, can couple with similar classes of receptors, nor is it known whether all Vav isoforms possess identical functional activities. We expressed Vav1, Vav2, and Vav3 at equivalent levels to directly compare the responses of the Vav proteins to receptor activation. Although each Vav isoform was tyrosine phosphorylated upon activation of representative receptor tyrosine kinases, integrin, and lymphocyte antigen receptors, we found unique aspects of Vav protein coupling in each receptor pathway. Each Vav protein coprecipitated with activated epidermal growth factor and platelet-derived growth factor (PDGF) receptors, and multiple phosphorylated tyrosine residues on the PDGF receptor were able to mediate Vav2 tyrosine phosphorylation. Integrin-induced tyrosine phosphorylation of Vav proteins was not detected in nonhematopoietic cells unless the protein tyrosine kinase Syk was also expressed, suggesting that integrin activation of Vav proteins may be restricted to cell types that express particular tyrosine kinases. In addition, we found that Vav1, but not Vav2 or Vav3, can efficiently cooperate with T-cell receptor signaling to enhance NFAT-dependent transcription, while Vav1 and Vav3, but not Vav2, can enhance NFκB-dependent transcription. Thus, although each Vav isoform can respond to similar cell surface receptors, there are isoform-specific differences in their activation of downstream signaling pathways.
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Dissertations / Theses on the topic "Cell surface antigen receptors"

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Mallett, Susan. "Characterization of T lymphocyte antigens." Thesis, University of Oxford, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293461.

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Deftos, Michael Laing. "Notch signaling in T cell development /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/8364.

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Gadd, Stephen J. "Analysis of acute mycloid leukaemia cell surface antigens with monoclonal antibodies." Title page, contents and abstract only, 1985. http://web4.library.adelaide.edu.au/theses/09PH/09phg123.pdf.

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Watanabe, Norihiko. "Antigen receptor cross-linking by anti-immunoglobulin antibodies coupled to cell surface membrane induces rapid apoptosis of normal spleen B cells." Kyoto University, 1998. http://hdl.handle.net/2433/182246.

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Gray, Daniel Herbert Donald. "Thymic stromal cells : population dynamics and their role in thymopoiesis." Monash University, Dept. of Pathology and Immunity, 2003. http://arrow.monash.edu.au/hdl/1959.1/9409.

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Clarke, Raedun Laurie. "The signal transduction pathways initiated by CD8 during apoptosis of thymocytes /." Connect to full text via ProQuest. Limited to UCD Anschutz Medical Campus, 2007.

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Thesis (Ph.D. in Immunology) -- University of Colorado Denver, 2007.
Typescript. Includes bibliographical references (leaves 236-251). Free to UCD affiliates. Online version available via ProQuest Digital Dissertations;
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Alheim, Mats. "Inhibitory receptors of natural killer cells : specificity and regulation /." Stockholm, 1998. http://diss.kib.ki.se/search/diss.se.cfm?19981009alhe.

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Leprince, Corinne. "Regulation de la fonction des lymphocytes b humains : interactions entre proteines membranaires et facteurs solubles." Paris 6, 1988. http://www.theses.fr/1988PA066361.

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Etude de la regulation de la reponse immune due aux lymphocytes b a travers leur sensibilite a des signaux regulateurs solubles (interleukines et facteurs bcgf) et l'expression de deux molecules de surface, les antigenes cd5 et b8. 7
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Hauser, Jannek. "Regulation of B cell development by antigen receptors." Doctoral thesis, Umeå universitet, Institutionen för molekylärbiologi (Medicinska fakulteten), 2011. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-40819.

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The developmental processes of lymphopoiesis generate mature B lymphocytes from hematopoietic stem cells through increasingly restricted intermediates. Networks of transcription factors regulate these cell fate choices and are composed of both ubiquitously expressed and B lineage-specific factors. E-protein transcription factors are encoded by the three genes E2A, E2-2 (SEF2-1), and HEB. The E2A gene is required for B cell development and encodes the alternatively spliced proteins E12 and E47. During B lymphocyte development, the cells have to pass several checkpoints verifying the functionality of their antigen receptors. Early in the development, the expression of a pre-B cell receptor (pre-BCR) with membrane-bound immunoglobulin (Ig) heavy chain protein associated with surrogate light chain (SLC) proteins is a critical checkpoint that monitors for functional Ig heavy chain rearrangement. Signaling from the pre-BCR induces survival and a limited clonal expansion. Here it is shown that pre-BCR signaling rapidly down-regulates the SLCs l5 and VpreB and also the co-receptor CD19. Ca2+ signaling and E2A were shown to be essential for this regulation. E2A mutated in its binding site for the Ca2+ sensor protein calmodulin (CaM), and thus with CaM-resistant DNA binding, makes l5, VpreB and CD19 expression resistant to the inhibition following pre-BCR stimulation. Thus, Ca2+ down-regulates SLC and CD19 gene expression upon pre-BCR stimulation through inhibition of E2A by Ca2+/CaM. A general negative feedback regulation of the pre-BCR proteins as well as many co-receptors and proteins in signal pathways from the receptor was also shown. After the ordered recombination of Ig heavy chain gene segments, also Ig light chain gene segments are recombined together to create antibody diversity. The recombinations are orchestrated by the recombination activating gene (RAG) enzymes, other enzymes that cleave/mutate/assemble DNA of the Ig loci, and the transcription factor Pax5. A key feature of the immune system is the concept that one lymphocyte has only one antigen specificity that can be selected for or against. This requires that only one of the alleles of genes for Ig chains is made functional. The mechanism of this allelic exclusion has however been an enigma. Here pre-BCR signaling was shown to down-regulate several components of the recombination machinery including RAG1 and RAG2 through CaM inhibition of E2A. Furthermore, E2A, Pax5 and the RAGs were shown to be in a complex bound to key sequences on the IgH gene before pre-BCR stimulation and instead bound to CaM after this stimulation. Thus, the recombination complex is directly released through CaM inhibition of E2A. Upon encountering antigens, B cells must adapt to produce a highly specific and potent antibody response. Somatic hypermutation (SH), which introduces point mutations in the variable regions of Ig genes, can increase the affinity for antigen, and antibody effector functions can be altered by class switch recombination (CSR), which changes the expressed constant region exons. Activation-induced cytidine deaminase (AID) is the mutagenic antibody diversification enzyme that is essential for both SH and CSR. The AID enzyme has to be tightly controlled as it is a powerful mutagen. BCR signaling, which signals that good antibody affinity has been reached, was shown to inhibit AID gene expression through CaM inhibition of E2A.  SH increases the antigen binding strength by many orders of magnitude. Each round of SH leads to one or a few mutations, followed by selection for increased affinity. Thus, BCR signaling has to enable selection for successive improvements in antibodies (Ab) over an extremely broad range of affinities. Here the BCR is shown to be subject to general negative feedback regulation of the receptor proteins as well as many co-receptors and proteins in signal pathways from the receptor. Thus, the BCR can down-regulate itself to enable sensitive detection of successive improvements in antigen affinity. Furthermore, the feedback inhibition of the BCR signalosome and most of its protein, and most other gene regulations by BCR stimulation, is through inhibition of E2A by Ca2+/CaM. Differentiation to Ab-secreting plasmablasts and plasma cells is antigen-driven. The interaction of antigen with the membrane-bound Ab of the BCR is critical in determining which clones enter the plasma cell response. Genome-wide analysis showed that differentiation of B cells to Ab-secreting cell is induced by BCR stimulation through very fast regulatory events, and induction of IRF-4 and down-regulation of Pax5, Bcl-6, MITF, Ets-1, Fli-1 and Spi-B gene expressions were identified as immediate early events. Ca2+ signaling through CaM inhibition of E2A was essential for these rapid down-regulations of immediate early genes after BCR stimulation in initiation of plasma cell differentiation.
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Wilson, Keith Michael. "Single particle fluorescent imaging analysis of cell surface HLA-DR and associated CD74 antigens." Thesis, University of Essex, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.361022.

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Books on the topic "Cell surface antigen receptors"

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Cell surface and differentiation. London: Chapman and Hall, 1990.

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Recognition receptors in biosensors. New York: Springer, 2010.

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Cell surface receptors: A short course on theory & methods. 3rd ed. New York: Springer, 2004.

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BLyS ligands and receptors. New York: Humana Press, 2010.

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Cell surface receptors: A short course on theory and methods. Boston: Nijhoff, 1986.

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Limbird, Lee E. Cell surface receptors: A short course on theory and methods. 2nd ed. Boston: Kluwer Academic Publishers, 1996.

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Limbird, Lee E. Cell Surface Receptors: A Short Course on Theory and Methods. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4757-1882-9.

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Limbird, Lee E. Cell Surface Receptors: A Short Course on Theory and Methods. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1255-0.

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Van den Elsen, Peter J., 1951-. The human T-cell receptor repertoire and transplantation. New York: Springer Verlag, 1995.

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Z, Atassi M., and Abbott Laboratories, eds. Immunobiology of proteins and peptides IV: T-cell recognition and antigen presentation. New York: Plenum Press, 1987.

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Book chapters on the topic "Cell surface antigen receptors"

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Mage, Rose G., and Claire Rogel-Gaillard. "Immunogenetics in the rabbit." In The genetics and genomics of the rabbit, 66–83. Wallingford: CABI, 2021. http://dx.doi.org/10.1079/9781780643342.0005.

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Abstract This chapter on immunogenetics in the rabbit focused on some genes with genetic and genomic sequence information including those encoding: soluble circulating immunoglobulin molecules (Igs) and their surface-bound forms on B lymphocytes (BCRs); T-cell receptors on T lymphocyte surfaces, (TCRs); the rabbit Leukocyte Antigen (RLA) complex (proteins on cells that function to present antigen fragments to TCRs); and some cytokine genes that encode key regulators of T- and B-cell responses.
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Schreiber, Hans, Carter van Waes, and Hans Josef Stauss. "Unique Tumor-Specific Antigens as Altered Cell-Surface Receptors." In Mechanisms of Receptor Regulation, 375–94. Boston, MA: Springer US, 1985. http://dx.doi.org/10.1007/978-1-4613-2131-6_19.

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Rhode, Peter R. "Soluble T-Cell Antigen Receptors." In Fusion Protein Technologies for Biopharmaceuticals, 475–93. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2013. http://dx.doi.org/10.1002/9781118354599.ch31.

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Tailor, C. S., D. Lavillette, M. Marin, and D. Kabat. "Cell Surface Receptors for Gammaretroviruses." In Current Topics in Microbiology and Immunology, 29–106. Berlin, Heidelberg: Springer Berlin Heidelberg, 2003. http://dx.doi.org/10.1007/978-3-642-19012-4_2.

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Hardie, D. G. "Cell Surface Receptors — Signal Transduction." In Biochemical Messengers, 147–89. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3108-7_7.

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Manger, Bernard, John Imboden, and Arthur Weiss. "Role of the T3/T-Cell Antigen Receptor Complex in T-Cell Activation." In The T-Cell Receptors, 133–49. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-5406-2_7.

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Xiao, Jiping, and Clare Bergson. "Detection of Cell Surface Dopamine Receptors." In Methods in Molecular Biology, 3–13. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-251-3_1.

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Hardie, D. G. "Cell Surface Receptors — Analysis and Identification." In Biochemical Messengers, 109–46. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3108-7_6.

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Shen, T. Y. "Drug Delivery via Cell-Surface Receptors." In Directed Drug Delivery, 231–45. Totowa, NJ: Humana Press, 1985. http://dx.doi.org/10.1007/978-1-4612-5186-6_13.

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Hynes, Richard O. "Cellular Adhesion and Cell Surface Receptors." In Fibronectins, 200–230. New York, NY: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4612-3264-3_8.

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Conference papers on the topic "Cell surface antigen receptors"

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Altieri, Dario C., Rossella Bader, and Pier M. Mannucci. "STRUCTURAL DIVERSITY AMONG CELLULAR ADHESION RECEPTORS: FIBRINOGEN BINDING IS A NOVEL BIOLOGICAL PROPERTY OF THE MONOCYTE DIFFERENTIATION ANTIGEN OKM1." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643851.

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A family of related glycoproteins (GP) mediate the interaction between the circulating adhesive proteins and a variety of cells (cytyoadhesins). In this study we have compared two cell-surface antigens which share the property to bind fibrinogen: the platelet GP IIb/IIIa, prototype of the cytoadhesins, and the receptor for fibrinogen costitutively synthesized by monocytes. Two anti-GP IIb/IIIa monoclonal antibodies (Mabs) (LJP9, LJP5), recognizing functionally distinct epitopes of the GP IIb/IIIa did not react with monocytes nor inhibited 125I-fibrinogen binding to monocytes. Similarly, an Arg-Gly-Asp containing peptide which completely abolished platelet-fibrinogen interaction, had no effect on monocytes. Structurally, the monocyte fibrinogen receptor was dimeric and composed of two subunits with molecular weight (Mr) of 155,000 and 95,000. This structural organization was different from that of the GP IIb/IIIa (Mr= 116,000), but in close analogy with the family of leukocyte differentiation antigens OKM1, LFA-1. Therefore, this possible relationship was investigated. A Mab to OKM1 antigen (10 μg/ml) completely suppressed fibrinogen binding to monocytes while it was ineffective on plateles. Iodinated monocyte lysate subjected to immunoprecipitation with OKM1 Mab (60 μg/ml) showed a dimeric antigen with the same molecular size of the monocyte fibrinogen receptor. Moreover, preclearing of the monocyte lysate with OKM1 Mab removed the immunoprecipitate corresponding to the monocyte fibrinogen receptor. These data indicate that the immunologic differentiation antigen OKM1, in addition to function as a complement receptor, displays also the novel biological adhesion property to mediate the binding of fibrinogen to monocytes.
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Phillips, David R., Laurence A. Fitzgerald, Leslie V. Parise, and Israel F. Charo. "The Platelet Membrane Glycoprotein IIb-III a Complex: Member of a Superfamily of Adhesive Protein Receptors." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643727.

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The glycoprotein (GP) IIb-IIIa complex isthe receptor for fibrinogen,fibronectin and von Willebrand factor on the surface of activated platelets that mediates platelet aggregation.The GP IIb-IIIa complex contains two subunits; an a subunit, GP IIb, and a smaller 8 subunit, GP IIIa. To identify the subunits of GP IIb-IIIa responsible for fibrinogen binding, we examined the ability of purified subunitsto bind to immobilized fibrinogen. Both the GP IIb and the GP III a subunits have fibrinogen binding activity, suggesting that fibrinogen binds to multiple sites onthe GP I Ib-IIIa complex.A GP Ilb-IIIa-like complex has been identified on endothelial cells which is immunoreactive with antibodies raised against platelet GP IIb-III a. This complex binds a similar broadspectrum of adhesive proteins as plateletGP IIb-IIIa and appears to mediate the attachment of endothelial cells to the extracellular matrix. We have established, however, that while GP Ilia in endothelial cells is the same primary translation product as platelet GP Ilia, the endothelialcell "GP lib" is a different, but closely related, protein from platelet GP lib. This close relationship of the receptors on these two cells is reflective of recent observations in several laboratories which have shown that a wide variety of cells contain surface glycoproteins which have structural and functionalsimilarities to the GP IIb-IIIa complexinplatelets and the "GP IIb-IIIa-like" complex in endothelial cells.These glycoproteins, which have been termed "integrins" or "cytoadhesins", are complexes of highly homologous a and 8 subunits, mediate cell-cell or cel 1-substrata interactions, and may also bind the RGD sequence on adhesive proteins. Although in vertebrates this family includes at least ten receptor complexes, there are only three known 8 subunits, each of which defines a subset of receptors. One is GP IIIa, the 8 subunit for GP IIb-IIIa and the vitronectin receptor; another is the 8 subunit for the fibronectin receptors and the very late antigens on lymphocytes; the third is the 8subunit of the Mac-1, LFA-1, and P150/95 antigens on leukocytes. These three 6 subunits have been cloned and sequenced. Each contains 746-777 amino acids, a singletransmembrane domain near the carboxy terminus, 56 cysteines in identical positionsof the proteins, 31 of which are clustered into four repeats, and an overall identity in 45-47% of their amino acids. The asubunits are more diverse in size but appear to have a similar degree of homology.The available sequence information indicates that they contain a single transmembrane domain near their carbody terminii and four tandem repeats near their amino terminii which include sequences indicativeof four Ca2+-binding sites. These may account for the known Ca2+-binding properties of GP IIb. GP I Ib-IIIa and the other adhesive protein receptors therefore appear to have two membrane insertion sites, one on each subunit,with short cytoplasmic domains derived from the carboxy terminii of the two subunits. The amino terminii along with most ofthe mass of these proteins is extracellular. It can be anticipated that the highlyhomologous sequences between GP IIb-IIIa and the other adhesive protein receptors will help identify the functional domainswhich have been conserved since their evolutionary divergences.
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Majzner, Robbie G., Alec J. Walker, Meera Murgai, Ling Zhang, Adrienne H. Long, Kelsey M. Wanhainen, Rimas J. Orentas, and Crystal L. Mackall. "Abstract 2648: Chimeric antigen receptor T-cell therapy against anaplastic lymphoma kinase (ALK) is limited by target antigen density and CAR surface expression." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-2648.

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4

Morrissey, J. H., S. A. Gregory, and T. S. Edgington. "DIFFERENTIAL EXPRESSION AND SUBCELLULAR LOCALIZATION OF TISSUE FACTORIN A CONSTITUTIVE VERSUS AN INDUCIBLE CELL TYPE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643739.

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Tissue factor (TF) is an integral membraneglycoprotein and receptor present on a variety of cells outside of the vasculature, but normally absent from intravascular cells. TF plays a central role in initiation of coagulation by rapidly binding and allosterically activating bound factor Vll/VIIa, which proteoly-tically activates coagulation factors IX and X. This protease cascade appears to play a role in the cellular inflammatory response, during which endothelial cells and monocytes/macrophages can be induced to express cell surface TF.Monocyte TF can be induced in response to endotoxin and also via direct interaction with activated T cells and by a specific lymphokine.We have developed a panel of polyclonaland twenty-nine high affinity monoclonal antibodies to human TF. The antibodies recognize TF epitopes under a broad range of conditions, some of which rapidly and efficiently neutralize <95% of TF activity isolated from brain, placenta and expressed bycultured cells. Using these antibodies in immunohistochemical assays, we haveobserved little or no TF antigen cytologically associated with resting monocytes, noTF activity, and following stimulation, the cytologic appearance of TF antigen parallels the acquisition of TF activity.Immunohistochemical staining of stimulated monocytesis diffuse, consistent with homogeneous cell-surface distribution of the TF molecule.In addition, the normal human fibroblastic cell lines GM1380 and GM1381, whichexpress TF const itutively, show a cytologically different and much more intense pattern of intracellular inclusions of TF. This is consistent with previous observationsthat lysed cells show about five-fold moreTF activity than do intact cells. These findings indicate the presence of an intracellular storage site for TF in some cell types, a pattern presently associated only with constitutive expression of this receptor protein. In addition, they confirm thatTF is induced in stimulated monocytes rather than translocation or modification. Supported by NIH grants HL-16411 and CA-41085.
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5

Bau, I.-Jiuan, and Gou-Jen Wang. "A Highly Sensitive Electrochemical Impedimetric Nanobiosensor for Dust Mite Antigen Der p2 Detection." In ASME 2011 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2011. http://dx.doi.org/10.1115/detc2011-47123.

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The group 2 allergen, Der p2, has been reported to activate innate toll-like receptors (TLRs) on respiratory epithelial cells and thus aggravate respiratory diseases. In this study, a high sensitive nanobiosensor based on a 3D sensing element that has uniformly deposited gold nanoparticles for the detection of the dust mite antigen Der p2 is proposed. The barrier layer of an anodic aluminum oxide (AAO) film is used as the template in this highly sensitive nanobiosensor fabricated with a reducing agent and stabilizer-free method. Electrochemical deposition is utilized to synthesize uniformly distributed gold nanoparticles on the surface of the barrier layer. The size and the distribution density of the nanoparticles can be well controlled by the potential applied during electrochemical deposition. Following this procedure, monoclonal antibodies were immobilized against the dust mite antigen Der p2 by the gold nanoparticles through the 11-MUA (11-mercaptoundecanoic acid), EDC (1-Ethyl-3-(3-dimethyl-aminopropyl)-carbodiimide)/NHS (N-hydroxysuccinimide) self-assembled monolayer approach. The proposed nanobiosensor was successfully used to examine the Der p2 down to a concentration of 1pg/mL through the electrochemical impedance spectroscopy analysis. The high sensitivity of the proposed 3D nanobiosensor can be attributed to the high intensity and uniformity of the Au nanoparticles on the sensor. The proposed nanobiosensor would be useful for the fast detection of rare molecules in a solution.
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LeFebvre, Aaron K., Melissa Frenchmeyer, Kyle M. McQuaid, MRussell Williams, Charles M. McBrairty, and Joseph D. Kittle. "Abstract 706: Rapid detection of SARS-CoV-2 antigen and antibody seroconversion in clinical specimens using a novel Surface Programmable Activation Receptor (SPAR) modified T cell diagnostic method." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-706.

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Wu, Ling, Joanna Brzostek, Shvetha Sankaran, Triscilla Tan, Conrad Chan, Jiawei Yap, Junyun Lai, Paul MacAry, and Nicholas Gascoigne. "Abstract 1425: Chimeric antigen receptors based on T cell receptor-like antibodies." 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.am2019-1425.

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Wu, Ling, Joanna Brzostek, Shvetha Sankaran, Triscilla Tan, Conrad Chan, Jiawei Yap, Junyun Lai, Paul MacAry, and Nicholas Gascoigne. "Abstract 1425: Chimeric antigen receptors based on T cell receptor-like antibodies." 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.sabcs18-1425.

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Nawroth, Peter P., Jerry Brett, Susan Steinberg, Charles T. Esmon, and David M. Stern. "ENDOTHELIUM AND PROTEIN S: SYNTHESIS, RELEASE AND REGULATION OF ANTICOAGULANT ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642962.

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The protein C-protein S pathway is closely linked to the vessel wall. In terms of protein C, endothelium has been shown to provide the receptor thrombomodulin, which promotes thrombin-mediated formation of activated protein C. Optimal anticoagulant function of activated protein C requires protein S and a cellular surface. Recent studies have indicated that endothelium can facilitate assembly of the activated protein C-protein S complex and that bovine endothelium expresses specific binding site(s) for protein S which promote its anticoagulant function. Expression of protein S binding sites is subject to down-regulation by Tumor Necrosis Factor (TNF) . Exposure of cultured bovine endothelium to TNF results in decreased 125I-protein s binding and attenuated rates of Factor Va inactivation after 2 hrs followed by negligible 125I-protein S binding and Factor Va inactivation by 10 hrs. These changes persist for over 48 hrs, in contrast to the more transient rise in endothelial cell tissue factor induced by TNF which returns to baseline by 24 hrs.In addition to providing binding sites for protein S, endothelium constitutively synthesizes and releases this vitamin K-dependent anticoagulant cofactor. Release of protein S is blocked by addition of warfarin, indicating that y-carboxylation facilitates the release of intracellular protein S. Morphologic studies, at the level of electron microscope, have shown protein S antigen to be present in cisternae of rough endoplasmic reticulum, the trans face of the golgi and a population of intracellular vesicles which appear to be distributed at the cellular periphery. By immunofluorescence, the distribution of protein S is distinct from that of von Willebrand Factor. The intracellular vesicles containing protein S constitute a storage pool potentially available for rapid release. Treatment of endothelium with norepinephrine results in release of protein S over the next 20 min. Release is half-maximal at a norepinephrine concentration of about 0.1 uM and is not observed with the biologically inactive entantiomer (+) norepinephrine. Norepinephrine-induced release of intracellular protein S can be blocked by prazosine (10-7 7 M), but not by propranolol (10-6 M) or yohimbine (10-5 M). These data are consistent with release of protein S being a receptor-mediated process dependent on an endothelial cell alpha 1 adrenergic receptor. Blockade of norepinephrine-induced release of protein S by pertussis toxin treatment of endothelium further defines the intracellular pathway of protein S and implicates regulatory G proteins in the stimulus-response coupling. Electron microscopic studies have shown that following exposure of endothelium to norepinephrine the intracellular vesicles containing protein S undergo exocytosis at the plasma membrane. These data define a new relationship between the autonomic nervous system and the coagulation mechanism.Protein S is clearly an endothelial cell-associated anticoagulant protein. A specific binding site on the endothelial cell surface can regulate its anticoagulant function on the vessel wall. Endothelial cell synthesis and release of protein S defines a new level of participation of endothelium in the protein C-protein S pathway.
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Sharma, Preeti, Venkata VVR Marada, Monika Kizerwetter, Claire P. Schane, Yanran He, Steven P. Wolf, Karin Schreiber, et al. "Abstract 3238: Engineering chimeric antigen receptors for adoptive T cell therapy of cancers that express the Tn antigen." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-3238.

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Reports on the topic "Cell surface antigen receptors"

1

Silver, Pamela A. The Identification of Novel Ligands for Cell Surface Receptors. Fort Belvoir, VA: Defense Technical Information Center, September 1999. http://dx.doi.org/10.21236/ada382512.

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Silver, Pamela A. The Identification of Novel Ligands for Cell Surface Receptors. Fort Belvoir, VA: Defense Technical Information Center, October 2000. http://dx.doi.org/10.21236/ada392930.

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