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Journal articles on the topic 'Cell receptors'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 August 2024

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1

Steverding, Dietmar. "Cycle Numbers of Cell Surface Recycling Receptors." Receptors 2, no. 2 (June 6, 2023): 160–65. http://dx.doi.org/10.3390/receptors2020010.

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The cycle number (nc) of a recycling receptor is defined as the average number of round trips (cell surface–endosome–cell surface) the receptor can make before it is degraded. This characteristic parameter of recycling receptors can be easily determined from the receptor’s half-life (t½, the time in which 50% of the receptor is degraded) and cycling time (Tc, the time a receptor needs to complete a round trip). Relationship analyses revealed that nc increases linearly with increasing t½ and decreases exponentially with increasing Tc. For commonly observed t½ and Tc values, it was calculated that recycling receptors have nc values of <300. In addition, it was found that recycling receptors in cancer cells have generally smaller nc values (<100), whereas recycling receptors in normal cells have larger nc values (>100). Based on this latter finding, the cycle number nc may be a useful criterion for distinguishing between cancer and normal cells.

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2

Gao, Yin, Xue Luan, Jacob Melamed, and Inka Brockhausen. "Role of Glycans on Key Cell Surface Receptors That Regulate Cell Proliferation and Cell Death." Cells 10, no. 5 (May 19, 2021): 1252. http://dx.doi.org/10.3390/cells10051252.

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Cells undergo proliferation and apoptosis, migration and differentiation via a number of cell surface receptors, most of which are heavily glycosylated. This review discusses receptor glycosylation and the known roles of glycans on the functions of receptors expressed in diverse cell types. We included growth factor receptors that have an intracellular tyrosine kinase domain, growth factor receptors that have a serine/threonine kinase domain, and cell-death-inducing receptors. N- and O-glycans have a wide range of functions including roles in receptor conformation, ligand binding, oligomerization, and activation of signaling cascades. A better understanding of these functions will enable control of cell survival and cell death in diseases such as cancer and in immune responses.

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3

Thermos, K., M. D. Meglasson, J. Nelson, K. M. Lounsbury, and T. Reisine. "Pancreatic beta-cell somatostatin receptors." American Journal of Physiology-Endocrinology and Metabolism 259, no. 2 (August 1, 1990): E216—E224. http://dx.doi.org/10.1152/ajpendo.1990.259.2.e216.

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The characteristics of somatostatin (SRIF) receptors in rat pancreatic beta-cells were investigated using rat islets and the beta-cell line HIT-T15 (HIT). The biochemical properties of the SRIF receptors were examined with 125I-labeled des-Ala-1,Gly-2-desamino-Cys-3-[Tyr-11]- dicarba3,14-somatostatin (CGP 23996). 125I-CGP 23996 bound to SRIF receptors in HIT cells with high affinity and in a saturable manner. The binding of 125I-CGP 23996 to SRIF receptors was blocked by SRIF analogues with a rank order of potency of somatostatin 28 (SRIF-28) greater than D-Trp-8-somatostatin greater than somatostatin 14 (SRIF-14). To investigate the physical properties of the HIT cell SRIF receptor, the receptor was covalently labeled with 125I-CGP 23996 using photo-cross-linking techniques. 125I-CGP 23996 specifically labeled a protein of 55 kDa in HIT cell membranes. The size of the SRIF receptor in HIT cells is similar to the size of the SRIF receptor labeled with 125I-CGP 23996 in membranes of freshly isolated islets, suggesting that the physical properties of SRIF receptors in HIT cells and rat islet cells are similar. The binding studies suggest that beta-cells predominantly express a SRIF-28-preferring receptor. In freshly isolated islets, glucose- and arginine-stimulated insulin release was effectively blocked by SRIF-28 but not by SRIF-14. SRIF-14 did inhibit arginine-stimulated glucagon secretion from freshly isolated islets. The dissociation of the inhibitory effects of SRIF-28 and SRIF-14 on insulin and glucagon release from freshly isolated islets suggests that the two peptides act through different receptors in islets to regulate hormone secretion.

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4

Ardaillou, R., D. Chansel, V. Stefanovic, and N. Ardaillou. "Cell surface receptors and ectoenzymes in mesangial cells." Journal of the American Society of Nephrology 2, no. 10 (April 1992): S107. http://dx.doi.org/10.1681/asn.v210s107.

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Mesangial cells possess a variety of receptors for hormones and autacoids. They are also equipped with ectoenzymes whose function may be to control the availability of autacoids and hormones at their receptor sites. Several examples are considered. Receptors for angiotensin II (AII) are present both on murine and human mesangial cells. One single group of receptors has been demonstrated in each of these preparations. Mesangial cell AII receptors are linked to phospholipase C via a G protein. They belong to the AT1 subtype because (125I)AII is displaced from its binding sites preferentially by AT1 antagonists such as DUP 753 and EXP 3,174, whereas AT2 antagonists are much less potent. AT1 antagonists suppress the biological effects of AII in mesangial cells, including the stimulation of intracellular calcium concentration and the increase of prostaglandin synthesis and of (3H)leucine incorporation. Mesangial cells also have receptors for atrial natriuretic factor, but the distribution between B receptors with guanylate cyclase activity and clearance (C) receptors varies with the species. Both types are present in murine mesangial cells, whereas only C receptors are found in human mesangial cells. In contrast, human epithelial cells possess both B and C receptors. Ecto-5'-nucleotidase activity results in the production of adenosine, which acts on mesangial cells through A1 and A2 receptors. This enzyme is markedly induced in rat mesangial cells by interleukin-1, whose effect is mediated in part by prostaglandin E2 and cAMP. Various other cAMP-stimulating agents also induce 5'-nucleotidase expression in rat mesangial cells. Ectopeptidases are present in all glomerular cell types but essentially in epithelial cells.(ABSTRACT TRUNCATED AT 250 WORDS)

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5

Atif, Muhmmad, Abdullah Alsrhani, Farrah Naz, Muhammad Imran, Muhammad Imran, Muhammad Ikram Ullah, Ayman A. M. Alameen, Tanweer Aslam Gondal, and Qaisar Raza. "Targeting Adenosine Receptors in Neurological Diseases." Cellular Reprogramming 23, no. 2 (April 1, 2021): 57–72. http://dx.doi.org/10.1089/cell.2020.0087.

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6

Uings, I. J. "Cell receptors and cell signalling." Molecular Pathology 53, no. 6 (December 1, 2000): 295–99. http://dx.doi.org/10.1136/mp.53.6.295.

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7

Desforges, Jane F. "T-Cell Receptors." New England Journal of Medicine 313, no. 9 (August 29, 1985): 576–77. http://dx.doi.org/10.1056/nejm198508293130909.

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8

Abbas, Atheir, and Bryan L. Roth. "Electrifying cell receptors." Nature Nanotechnology 3, no. 10 (October 2008): 587–88. http://dx.doi.org/10.1038/nnano.2008.292.

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9

Deller, M. "Cell surface receptors." Current Opinion in Structural Biology 10, no. 2 (April 1, 2000): 213–19. http://dx.doi.org/10.1016/s0959-440x(00)00072-5.

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10

Primi, Daniele. "T cell receptors." FEBS Letters 384, no. 3 (April 22, 1996): 296. http://dx.doi.org/10.1016/s0014-5793(96)90958-8.

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11

Ryan, Una S. "Endothelial cell receptors." Advanced Drug Delivery Reviews 4, no. 1 (July 1989): 65–85. http://dx.doi.org/10.1016/0169-409x(89)90038-0.

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12

Caccia, Nicolette, and Tak W. Mak. "T cell receptors." American Journal of Medicine 85, no. 6 (December 1988): 9–11. http://dx.doi.org/10.1016/0002-9343(88)90371-3.

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13

Lanier, Lewis L. "NK CELL RECEPTORS." Annual Review of Immunology 16, no. 1 (April 1998): 359–93. http://dx.doi.org/10.1146/annurev.immunol.16.1.359.

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14

Viney, Joanne L. "T Cell receptors." Immunology Today 17, no. 7 (July 1996): 346–47. http://dx.doi.org/10.1016/0167-5699(96)80797-3.

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15

Mapstone, Timothy B. "Cell Surface Receptors." Pediatric Neurosurgery 27, no. 2 (1997): 57–62. http://dx.doi.org/10.1159/000121228.

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16

Ingber, Arieh. "Langerhans Cell Receptors." Dermatologic Clinics 25, no. 4 (October 2007): 559–62. http://dx.doi.org/10.1016/j.det.2007.06.019.

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17

Gao, Zihan. "The structure and function of cell membrane receptor." Highlights in Science, Engineering and Technology 74 (December 29, 2023): 441–47. http://dx.doi.org/10.54097/bncesw47.

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Cell membrane receptors play a key role in regulating cell communication and maintaining cell homeostasis. This paper explores the complex relationship between the structure and function of cell membrane receptors, and elucidates their multiple roles in signal transduction, cellular response, and disease pathways. Different receptor types, including as G protein-coupled receptors (GPCRs), ligand-gated ion channels, receptor tyrosine kinases (RTKs), and cytokine receptors, have varied structural properties that serve different biological purposes and are necessary for cell division, proliferation, and metabolism. The function of membrane receptors that translate extracellular signals into intracellular responses is diverse. The organization of lipid rafts and other receptors within membrane microdomains can influence signal transduction efficiency and specificity. There are inseparable interactions among receptor internalization, recycling and degradation, and regulating the duration and intensity of receptor signaling is closely related to the treatment of diseases. In summary, the current research status of cell membrane receptor structure and function is reviewed in this paper. It contributes to a broader understanding of how receptors regulate important cellular processes at the molecular level. Understanding the nuances of receptor structure-function relationships holds great promise for developing new therapeutic strategies and advancing drug discovery for a variety of diseases.

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18

Zambon, Alexander C., Richard J. Hughes, J. Gary Meszaros, J. Julie Wu, Brian Torres, Laurence L. Brunton, and Paul A. Insel. "P2Y2 receptor of MDCK cells: cloning, expression, and cell-specific signaling." American Journal of Physiology-Renal Physiology 279, no. 6 (December 1, 2000): F1045—F1052. http://dx.doi.org/10.1152/ajprenal.2000.279.6.f1045.

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Madin-Darby canine kidney (MDCK)-D1 cells, a canine renal epithelial cell line, co-express at least three different P2Y receptor subtypes: P2Y1, P2Y2, and P2Y11 (24). Stimulation of P2Y receptors in these cells results in the release of arachidonic acid (AA) and metabolites and the elevation of intracellular cAMP. To define in more precise terms the signaling contributed by the MDCK-D1 P2Y2(cP2Y2) receptor, we have cloned and heterologously expressed it in CF2Th (canine thymocyte) cells, a P2Y2-null cell. Analysis by RT-PCR indicated that canine P2Y2receptors are expressed in skeletal muscle, spleen, kidney, lung, and liver. When expressed in CF2Th cells, cP2Y2 receptors promoted phospholipase C-mediated phosphatidylinositol (PI) hydrolysis [uridine 5′-triphosphate ≥ ATP > adenosine 5′-diphosphate > 2MT-ATP] and mobilization of intracellular Ca2+. In contrast to their actions in MDCK-D1 cells, cP2Y2 receptors did not stimulate formation of cAMP or AA release when expressed in CF2Th cells. The data indicate that cell setting plays an essential role in the ability of P2Y receptors to regulate AA release and cAMP formation. In particular, renal epithelial cells preferentially express components critical for cP2Y2-induced cAMP formation, including the expression of enzymes involved in the generation and metabolism of AA and receptors that respond to PGE2.

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19

Penberthy, Kristen K., and Kodi S. Ravichandran. "Apoptotic cell recognition receptors and scavenger receptors." Immunological Reviews 269, no. 1 (December 19, 2015): 44–59. http://dx.doi.org/10.1111/imr.12376.

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20

Jaremko, William J., Zhen Huang, Wei Wen, Andrew Wu, Nicholas Karl, and Li Niu. "Identification and characterization of RNA aptamers: A long aptamer blocks the AMPA receptor and a short aptamer blocks both AMPA and kainate receptors." Journal of Biological Chemistry 292, no. 18 (March 21, 2017): 7338–47. http://dx.doi.org/10.1074/jbc.m116.774752.

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AMPA and kainate receptors, along with NMDA receptors, represent different subtypes of glutamate ion channels. AMPA and kainate receptors share a high degree of sequence and structural similarities, and excessive activity of these receptors has been implicated in neurological diseases such as epilepsy. Therefore, blocking detrimental activity of both receptor types could be therapeutically beneficial. Here, we report the use of an in vitro evolution approach involving systematic evolution of ligands by exponential enrichment with a single AMPA receptor target (i.e. GluA1/2R) to isolate RNA aptamers that can potentially inhibit both AMPA and kainate receptors. A full-length or 101-nucleotide (nt) aptamer selectively inhibited GluA1/2R with a KI of ∼5 μm, along with GluA1 and GluA2 AMPA receptor subunits. Of note, its shorter version (55 nt) inhibited both AMPA and kainate receptors. In particular, this shorter aptamer blocked equally potently the activity of both the GluK1 and GluK2 kainate receptors. Using homologous binding and whole-cell recording assays, we found that an RNA aptamer most likely binds to the receptor's regulatory site and inhibits it noncompetitively. Our results suggest the potential of using a single receptor target to develop RNA aptamers with dual activity for effectively blocking both AMPA and kainate receptors.

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21

Lucianò, Anna Maria, Francesca Mattei, Elisa Damo, Elisa Panzarini, Luciana Dini, and Ada Maria Tata. "Effects mediated by M2 muscarinic orthosteric agonist on cell growth in human neuroblastoma cell lines." Pure and Applied Chemistry 91, no. 10 (October 25, 2019): 1641–50. http://dx.doi.org/10.1515/pac-2018-1224.

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Abstract The role of muscarinic receptors has been largely documented over the past few decades. Recently we demonstrated that the activation of M2 muscarinic receptors arrested cell proliferation and induced apoptosis in glioblastoma and in other tumour types. This paper aims to evaluate the expression of the M2 muscarinic receptor subtypes in different neuroblastoma cell lines and its role in the control of cell proliferation and survival. Neuroblastoma is the most common solid extracranial tumour, appearing during childhood and displaying a differentiated clinical behaviour. Considering the high homology between muscarinic receptor subtypes, we have identified Arecaidine Propargyl Ester (APE) as a selective orthosteric agonist for M2 muscarinic receptors. Using this agonist, we demonstrate how a selective activation of the M2 receptor subtype negatively modulates cell growth without affecting cell survival in different human neuroblastoma cell lines. As similarly demonstrated in other cell types, following the M2 receptor silencing by short-interference RNA, the effects of APE are completely abolished. We conclude by confirming the ability of APE to bind selectively M2 muscarinic receptor subtypes. Moreover, for the first time we demonstrate that M2 receptor activation inhibits cell growth also in human neuroblastoma cells, indicating that M2 receptors may be an interesting therapeutic target in several solid tumours.

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22

Finbloom, D. S. "Regulation of cell-surface receptors for human interferon-γ on the human histiocytic lymphoma cell line U937." Biochemical Journal 274, no. 3 (March 15, 1991): 775–80. http://dx.doi.org/10.1042/bj2740775.

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Interferon-gamma (IFN gamma) binds to high-affinity receptors on monocytes and is rapidly internalized. This study investigates the ability of the human monocyte-like cell line, U937, to regulate the cell-surface expression of the IFN gamma receptor (IFN gamma R) during endocytosis of ligand. Recombinant IFN gamma was radiolabelled to high specific radioactivity with Bolton-Hunter reagent and used to enumerate IFN gamma R on treated U937 cells. Cells which had internalized IFN gamma for up to 3 h displayed maximal levels of IFN gamma R at all time points tested after all unlabelled IFN gamma had been acid-stripped from the cell at pH 2.78. Therefore there was no evidence of down-modulation of the receptor. After trypsin treatment of the IFN gamma R, the cells were able to synthesize and insert into the cell membrane up to 1000 IFN gamma R molecules/h after a 60 min lag. Since biosynthesis played a minor role during the first 30 min of endocytosis, I examined other possibilities to explain the lack of down-modulation of the receptor. A solubilized-receptor assay revealed the presence of an intracellular pool of receptors equal to about 25% of the number of cell surface receptors. Using trypsin to differentiate between intracellular and surface receptors, I observed that 43% of those receptors that were internalized after a 30 min exposure to IFN gamma (580 molecules) could be recycled back to the plasma membrane. In addition, equal rates of receptor decay (t1/2 = 5 h) were observed in the presence of cycloheximide with or without IFN gamma. All the data taken together suggest that during the first 30 min of endocytosis both the expression of an intracellular source of receptor and recycling of internalized receptors contribute to maintain optimal receptor expression.

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23

Mehta, S. R., S. R. Grant, and A. L. Maizel. "Characterization of the cell surface receptors for human B cell growth factor of 12,000 molecular weight." Journal of Immunology 137, no. 7 (October 1, 1986): 2210–14. http://dx.doi.org/10.4049/jimmunol.137.7.2210.

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Abstract Quiescent normal human B cells have been shown to require an activation step before proliferating in response to B cell growth factor (BCGF) of 12,000 m.w. (12 kd). One effect of cell activation has been the putative acquisition of specific cell surface growth factor receptors. In this report, the existence of such receptors has been confirmed by using purified radioiodinated BCGF-12 kd. BCGF-12 kd receptors on activated B cells have been shown to be distinct form those interacting with IL 2. Scatchard analysis revealed both high affinity receptor sites with an apparent Kd of 28.6 pM and low affinity receptor sites with Kd of 1.2 nM on freshly prepared, anti-IgM activated peripheral blood B cells. Human B cells grown in culture for extended periods of time in the presence of BCGF-12 kd also displayed high affinity receptor sites (Kd, 41.4 pM) and low affinity receptor sites (Kd, 0.9 nM). The action of BCGF-12 kd therefore appears to be mediated by binding to its lineage-specific receptors on the cell surface.

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24

Hendrickson, Wayne A. "Transduction of biochemical signals across cell membranes." Quarterly Reviews of Biophysics 38, no. 4 (November 2005): 321–30. http://dx.doi.org/10.1017/s0033583506004136.

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1. Introduction 3212. Tyrosine kinase receptors 3223. Histidine kinase sensors 3254. G-protein coupled receptors 3275. Principles 3286. Acknowledgments 3297. References 330Biological cells need to be responsive to various stimuli, primarily chemical ligands from their environments. Specific receptor molecules embedded in the plasma membrane detect the different biochemical signals that impact the cell, and these receptors are the conduits for transmission of this information to the cell interior for action. There are several classes of signal transduction receptors and many specific receptors within each of the major classes. This review emphasizes the structural biology of three major classes of transmembrane receptors – tyrosine kinase receptors, histidine kinase sensors, and G-protein coupled receptors. Biophysical principles that govern the processes of signal transduction across cell membranes are also discussed.

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25

Park, Seung-Yoon, and In-San Kim. "Stabilin Receptors: Role as Phosphatidylserine Receptors." Biomolecules 9, no. 8 (August 20, 2019): 387. http://dx.doi.org/10.3390/biom9080387.

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Phosphatidylserine is a membrane phospholipid that is localized to the inner leaflet of the plasma membrane. Phosphatidylserine externalization to the outer leaflet of the plasma membrane is an important signal for various physiological processes, including apoptosis, platelet activation, cell fusion, lymphocyte activation, and regenerative axonal fusion. Stabilin-1 and stabilin-2 are membrane receptors that recognize phosphatidylserine on the cell surface. Here, we discuss the functions of Stabilin-1 and stabilin-2 as phosphatidylserine receptors in apoptotic cell clearance (efferocytosis) and cell fusion, and their ligand-recognition and signaling pathways.

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26

Ciccone, Ermanno, Carlo Enrico Grossi, and Andrea Velardi. "Opposing functions of activatory T-cell receptors and inhibitory NK-cell receptors on cytotoxic T cells." Immunology Today 17, no. 10 (October 1996): 450–53. http://dx.doi.org/10.1016/0167-5699(96)30054-v.

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27

Modlin, Robert L., Michael B. Brenner, Michael S. Krangel, Allan D. Duby, and Barry R. Bloom. "T-cell receptors of human suppressor cells." Nature 329, no. 6139 (October 1987): 541–45. http://dx.doi.org/10.1038/329541a0.

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28

Kalász, Vera, Tihamér Pap, György Csanaky, and Gábor Kelényi. "Endothelial cell receptors on leukemic plasma cells." Leukemia Research 13, no. 9 (January 1989): 863–68. http://dx.doi.org/10.1016/0145-2126(89)90100-8.

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29

Csanaky, György. "Cell adhesion receptors on neoplastic plasma cells." American Journal of Hematology 49, no. 4 (August 1995): 361–62. http://dx.doi.org/10.1002/ajh.2830490425.

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30

Biassoni, Roberto, Claudia Cantoni, Daniela Pende, Simona Sivori, Silvia Parolini, Massimo Vitale, Cristina Bottino, and Alessandro Moretta. "Human natural killer cell receptors and co-receptors." Immunological Reviews 181, no. 1 (July 2001): 203–14. http://dx.doi.org/10.1034/j.1600-065x.2001.1810117.x.

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31

Bąbolewska, Edyta, and Ewa Brzezińska-Błaszczyk. "Mast cell inhibitory receptors." Postępy Higieny i Medycyny Doświadczalnej 66 (October 22, 2012): 739–51. http://dx.doi.org/10.5604/17322693.1015039.

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32

MILES, LINDSEY A., STEPHEN B. HAWLEY, and ROBERT J. PARMER. "Chromaffin Cell Plasminogen Receptors." Annals of the New York Academy of Sciences 971, no. 1 (October 2002): 454–59. http://dx.doi.org/10.1111/j.1749-6632.2002.tb04508.x.

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33

Nemazee, David, and Martin Weigert. "Revising B Cell Receptors." Journal of Experimental Medicine 191, no. 11 (May 30, 2000): 1813–18. http://dx.doi.org/10.1084/jem.191.11.1813.

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34

Jaffe, Iris Z., and Frédéric Jaisser. "Endothelial Cell Mineralocorticoid Receptors." Hypertension 63, no. 5 (May 2014): 915–17. http://dx.doi.org/10.1161/hypertensionaha.114.01997.

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35

Degitz, Klaus, and S. Wright Caughman. "T-Cell Antigen Receptors." Dermatologic Clinics 8, no. 4 (October 1990): 663–72. http://dx.doi.org/10.1016/s0733-8635(18)30453-4.

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36

Gravitz, Lauren. "Shape-Shifting Cell Receptors." American Scientist 108, no. 1 (2020): 6. http://dx.doi.org/10.1511/2020.108.1.6.

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37

Carpentier, J. L. "3 Cell Surface Receptors." Progress in Histochemistry and Cytochemistry 26, no. 1-4 (January 1992): 77–87. http://dx.doi.org/10.1016/s0079-6336(11)80081-1.

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38

Moretta, Lorenzo, Roberto Biassoni, Cristina Bottino, Maria C. Mingari, and Alessandro Moretta. "Human NK-cell receptors." Immunology Today 21, no. 9 (September 2000): 420–22. http://dx.doi.org/10.1016/s0167-5699(00)01673-x.

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39

Long, Eric O., and Nicolai Wagtmann. "Natural killer cell receptors." Current Opinion in Immunology 9, no. 3 (June 1997): 344–50. http://dx.doi.org/10.1016/s0952-7915(97)80080-5.

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40

Yokoyama, Wayne M. "Natural killer cell receptors." Current Opinion in Immunology 10, no. 3 (June 1998): 298–305. http://dx.doi.org/10.1016/s0952-7915(98)80168-4.

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41

Born, W. "The T-cell receptors." Trends in Genetics 5 (1989): 162–63. http://dx.doi.org/10.1016/0168-9525(89)90063-2.

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42

Dejana, Elisabetta. "Endothelial Cell Adhesive Receptors." Journal of Cardiovascular Pharmacology 21 (1993): S18—S21. http://dx.doi.org/10.1097/00005344-199321001-00004.

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43

Pule, M., H. Finney, and A. Lawson. "Artificial T-cell receptors." Cytotherapy 5, no. 3 (2003): 211–26. http://dx.doi.org/10.1080/14653240310001488.

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44

Bannister, P., and M. S. Losowsky. "Cell Receptors and Ethanol." Alcoholism: Clinical and Experimental Research 10, s1 (December 1986): 50S—54S. http://dx.doi.org/10.1111/j.1530-0277.1986.tb05180.x.

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45

Straub, Christian, Marie-Luise Neulen, Beatrice Sperling, Katharina Windau, Maria Zechmann, Christine A. Jansen, Birgit C. Viertlboeck, and Thomas W. Göbel. "Chicken NK cell receptors." Developmental & Comparative Immunology 41, no. 3 (November 2013): 324–33. http://dx.doi.org/10.1016/j.dci.2013.03.013.

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46

Wagner, Gerhard, and Daniel F. Wyss. "Cell surface adhesion receptors." Current Opinion in Structural Biology 4, no. 6 (January 1994): 841–51. http://dx.doi.org/10.1016/0959-440x(94)90265-8.

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47

Reth, Michael. "B cell antigen receptors." Current Opinion in Immunology 6, no. 1 (February 1994): 3–8. http://dx.doi.org/10.1016/0952-7915(94)90026-4.

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48

Yokoyama, Wayne M. "Natural killer cell receptors." Current Opinion in Immunology 7, no. 1 (February 1995): 110–20. http://dx.doi.org/10.1016/0952-7915(95)80036-0.

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49

Bazzoni, Gianfranco, Inés Martín-Padura, Amada Beltràn-Nuñez, and Elisabetta Dejana. "Tumor cell adhesion receptors." Journal of Surgical Oncology 53, S3 (1993): 24–27. http://dx.doi.org/10.1002/jso.2930530508.

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50

Hide, Michihiro, Yuhki Yanase, and Malcolm W. Greaves. "Cutaneous Mast Cell Receptors." Dermatologic Clinics 25, no. 4 (October 2007): 563–75. http://dx.doi.org/10.1016/j.det.2007.06.013.

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