Relevant bibliographies by topics / Eph receptor

Academic literature on the topic 'Eph receptor'

Author: Grafiati
Published: 4 June 2021
Last updated: 31 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Contents

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Eph receptor.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Eph receptor"

1

Schweda, Frank, Jürgen Klar, Shuh Narumiya, Rolf M. Nüsing, and Armin Kurtz. "Stimulation of renin release by prostaglandin E2 is mediated by EP2 and EP4 receptors in mouse kidneys." American Journal of Physiology-Renal Physiology 287, no. 3 (September 2004): F427—F433. http://dx.doi.org/10.1152/ajprenal.00072.2004.

Full text
Abstract:
PGE2 is a potent stimulator of renin release. So far, the contribution of each of the four PGE2 receptor subtypes (EP1–EP4) in the regulation of renin release has not been characterized. Therefore, we investigated the effects PGE2 on renin secretion rates (RSR) from isolated, perfused kidneys of EP1−/−, EP2−/−, EP3−/−, EP4−/−, and wild-type mice. PGE2 concentration dependently stimulated RSR from kidneys of all four knockout strains with a threshold concentration of 1 nM in EP1−/−, EP2−/−, EP3−/−, and wild-type mice, whereas the threshold concentration was shifted to 10 nM in EP4−/− mice. Moreover, the maximum stimulation of RSR by PGE2 at 1 μM was significantly reduced in EP4−/− (12.8-fold of control) and EP2−/− (15.9-fold) compared with wild-type (20.7-fold), EP1−/− (23.8-fold), and EP3−/− (20.1-fold). In contrast, stimulation of RSR by either the loop diuretic bumetanide or the β-adrenoceptor agonist isoproterenol was similar in all strains. PGE2 exerted a dual effect on renal vascular tone, inducing vasodilatation at low concentrations (1 nmol/) and vasoconstriction at higher concentrations (100 nmol/) in kidneys of wild-type mice. In kidneys of EP2−/− as well as EP4−/− mice, vasodilatation at low PGE2 concentrations was prevented, whereas vasoconstriction at higher concentrations was augmented. In contrast, the vasodilatatory component was pronounced in kidneys of EP1 and EP3 knockout mice, whereas in both genotypes the vasoconstriction at higher PGE2 concentrations was markedly blunted. Our data provide evidence that PGE2 stimulates renin release via activation of EP2 and EP4 receptors, whereas EP1 and EP3 receptors appear to be without functional relevance in juxtaglomerular cells. In contrast, all four receptor subtypes are involved in the control of renal vascular tone, EP1 and EP3 receptors increasing, and EP2 as well as EP4 receptors, decreasing it.
APA, Harvard, Vancouver, ISO, and other styles
2

Breyer, Matthew D., and Richard M. Breyer. "Prostaglandin E receptors and the kidney." American Journal of Physiology-Renal Physiology 279, no. 1 (July 1, 2000): F12—F23. http://dx.doi.org/10.1152/ajprenal.2000.279.1.f12.

Full text
Abstract:
Prostaglandin E2 is a major renal cyclooxygenase metabolite of arachidonate and interacts with four G protein-coupled E-prostanoid receptors designated EP1, EP2, EP3, and EP4. Through these receptors, PGE2modulates renal hemodynamics and salt and water excretion. The intrarenal distribution and function of EP receptors have been partially characterized, and each receptor has a distinct role. EP1 expression predominates in the collecting duct where it inhibits Na+ absorption, contributing to natriuresis. The EP2 receptor regulates vascular reactivity, and EP2 receptor-knockout mice have salt-sensitive hypertension. The EP3 receptor is also expressed in vessels as well as in the thick ascending limb and collecting duct, where it antagonizes vasopressin-stimulated salt and water transport. EP4 mRNA is expressed in the glomerulus and collecting duct and may regulate glomerular tone and renal renin release. The capacity of PGE2 to bidirectionally modulate vascular tone and epithelial transport via constrictor EP1 and EP3 receptors vs. dilator EP2 and EP4 receptors allows PGE2 to serve as a buffer, preventing excessive responses to physiological perturbations.
APA, Harvard, Vancouver, ISO, and other styles
3

Mason, Emilia O., Yehuda Goldgur, Dorothea Robev, Andrew Freywald, Dimitar B. Nikolov, and Juha P. Himanen. "Structure of the EphB6 receptor ectodomain." PLOS ONE 16, no. 3 (March 26, 2021): e0247335. http://dx.doi.org/10.1371/journal.pone.0247335.

Full text
Abstract:
Eph receptors are the largest group amongst the receptor tyrosine kinases and are divided into two subgroups, A and B, based on ligand binding specificities and sequence conservation. Through ligand-induced and ligand-independent activities, Ephs play central roles in diverse biological processes, including embryo development, regulation of neuronal signaling, immune responses, vasculogenesis, as well as tumor initiation, progression, and metastasis. The Eph extracellular regions (ECDs) are constituted of multiple domains, and previous structural studies of the A class receptors revealed how they interact with ephrin ligands and simultaneously mediate Eph-Eph clustering necessary for biological activity. Specifically, EphA structures highlighted a model, where clustering of ligand-bound receptors relies on two distinct receptor/receptor interfaces. Interestingly, most unliganded A class receptors also form an additional, third interface, between the ligand binding domain (LBD) and the fibronectin III domain (FN3) of neighboring molecules. Structures of B-class Eph ECDs, on the other hand, have never been reported. To further our understanding of Eph receptor function, we crystallized the EphB6-ECD and determined its three-dimensional structure using X-ray crystallography. EphB6 has important functions in both normal physiology and human malignancies and is especially interesting because this atypical receptor innately lacks kinase activity and our understanding of the mechanism of action is still incomplete. Our structural data reveals the overall EphB6-ECD architecture and shows EphB6-LBD/FN3 interactions similar to those observed for the unliganded A class receptors, suggesting that these unusual interactions are of general importance to the Eph group. We also observe unique structural features, which likely reflect the atypical signaling properties of EphB6, namely the need of co-receptor(s) for this kinase-inactive Eph. These findings provide new valuable information on the structural organization and mechanism of action of the B-class Ephs, and specifically EphB6, which in the future will assist in identifying clinically relevant targets for cancer therapy.
APA, Harvard, Vancouver, ISO, and other styles
4

Wagner, Melany J., Marilyn S. Hsiung, Gerald D. Gish, Rick D. Bagshaw, Sasha A. Doodnauth, Mohamed A. Soliman, Claus Jørgensen, Monika Tucholska, and Robert Rottapel. "The Shb scaffold binds the Nck adaptor protein, p120 RasGAP, and Chimaerins and thereby facilitates heterotypic cell segregation by the receptor EphB2." Journal of Biological Chemistry 295, no. 12 (February 14, 2020): 3932–44. http://dx.doi.org/10.1074/jbc.ra119.009276.

Full text
Abstract:
Eph receptors are a family of receptor tyrosine kinases that control directional cell movement during various biological processes, including embryogenesis, neuronal pathfinding, and tumor formation. The biochemical pathways of Eph receptors are context-dependent in part because of the varied composition of a heterotypic, oligomeric, active Eph receptor complex. Downstream of the Eph receptors, little is known about the essential phosphorylation events that define the context and instruct cell movement. Here, we define a pathway that is required for Eph receptor B2 (EphB2)–mediated cell sorting and is conserved among multiple Eph receptors. Utilizing a HEK293 model of EphB2+/ephrinB1+ cell segregation, we found that the scaffold adaptor protein SH2 domain–containing adaptor protein B (Shb) is essential for EphB2 functionality. Further characterization revealed that Shb interacts with known modulators of cytoskeletal rearrangement and cell mobility, including Nck adaptor protein (Nck), p120-Ras GTPase-activating protein (RasGAP), and the α- and β-Chimaerin Rac GAPs. We noted that phosphorylation of Tyr297, Tyr246, and Tyr336 of Shb is required for EphB2–ephrinB1 boundary formation, as well as binding of Nck, RasGAP, and the chimaerins, respectively. Similar complexes were formed in the context of EphA4, EphA8, EphB2, and EphB4 receptor activation. These results indicate that phosphotyrosine-mediated signaling through Shb is essential in EphB2-mediated heterotypic cell segregation and suggest a conserved function for Shb downstream of multiple Eph receptors.
APA, Harvard, Vancouver, ISO, and other styles
5

Truitt, Luke, and Andrew Freywald. "Dancing with the dead: Eph receptors and their kinase-null partnersThis paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health and Disease, and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 89, no. 2 (April 2011): 115–29. http://dx.doi.org/10.1139/o10-145.

Full text
Abstract:
Eph receptor tyrosine kinases and their ligands, ephrins, are membrane proteins coordinating a wide range of biological functions both in developing embryos and in adult multicellular organisms. Numerous studies have implicated Eph receptors in the induction of opposing responses, including cell adhesion or repulsion, support or inhibition of cell proliferation and cell migration, and progression or suppression of multiple malignancies. Similar to other receptor tyrosine kinases, Eph receptors rely on their ability to catalyze tyrosine phosphorylation for signal transduction. Interestingly, however, Eph receptors also actively utilize three kinase-deficient receptor tyrosine kinases, EphB6, EphA10, and Ryk, in their signaling network. The accumulating evidence suggests that the unusual flexibility of the Eph family, allowing it to initiate antagonistic responses, might be partially explained by the influence of the kinase-dead participants and that the exact outcome of an Eph-mediated action is likely to be defined by the balance between the signaling of catalytically potent and catalytically null receptors. We discuss in this minireview the emerging functions of the kinase-dead EphB6, EphA10, and Ryk receptors both in normal biological responses and in malignancy, and analyze currently available information related to the molecular mechanisms of their action in the context of the Eph family.
APA, Harvard, Vancouver, ISO, and other styles
6

Blikslager, Anthony T., Susan M. Pell, and Karen M. Young. "PGE2 triggers recovery of transmucosal resistance via EP receptor cross talk in porcine ischemia-injured ileum." American Journal of Physiology-Gastrointestinal and Liver Physiology 281, no. 2 (August 1, 2001): G375—G381. http://dx.doi.org/10.1152/ajpgi.2001.281.2.g375.

Full text
Abstract:
16,16-Dimethyl-PGE2 (PGE2) may interact with one of four prostaglandin type E (EP) receptors, which signal via cAMP (via EP2 or EP4 receptors) or intracellular Ca2+ (via EP1 receptors). Furthermore, EP3 receptors have several splice variants, which may signal via cAMP or intracellular Ca2+. We sought to determine the PGE2 receptor interactions that mediate recovery of transmucosal resistance ( R) in ischemia-injured porcine ileum. Porcine ileum was subjected to 45 min of ischemia, after which the mucosa was mounted in Ussing chambers. Tissues were pretreated with indomethacin (5 μM). Treatment with the EP1, EP2, EP3, and EP4 agonist PGE2 (1 μM) elevated R twofold and significantly increased tissue cAMP content, whereas the EP2 and EP4 agonist deoxy-PGE1 (1 μM) or the EP1 and EP3 agonist sulprostone (1 μM) had no effect. However, a combination of deoxy-PGE1 and sulprostone stimulated synergistic elevations in R and tissue cAMP content. Furthermore, treatment of tissues with deoxy-PGE1 and the Ca2+ ionophore A-23187 stimulated synergistic increases in R and cAMP, indicating that PGE2 triggers recovery of R via EP receptor cross talk mechanisms involving cAMP and intracellular Ca2+.
APA, Harvard, Vancouver, ISO, and other styles
7

Buchert, Michael, Stefan Schneider, Virginia Meskenaite, Mark T. Adams, Eli Canaani, Thomas Baechi, Karin Moelling, and Christopher M. Hovens. "The Junction-associated Protein AF-6 Interacts and Clusters with Specific Eph Receptor Tyrosine Kinases at Specialized Sites of Cell–Cell Contact in the Brain." Journal of Cell Biology 144, no. 2 (January 25, 1999): 361–71. http://dx.doi.org/10.1083/jcb.144.2.361.

Full text
Abstract:
The AF-6/afadin protein, which contains a single PDZ domain, forms a peripheral component of cell membranes at specialized sites of cell–cell junctions. To identify potential receptor-binding targets of AF-6 we screened the PDZ domain of AF-6 against a range of COOH-terminal peptides selected from receptors having potential PDZ domain-binding termini. The PDZ domain of AF-6 interacts with a subset of members of the Eph subfamily of RTKs via its COOH terminus both in vitro and in vivo. Cotransfection of a green fluorescent protein-tagged AF-6 fusion protein with full-length Eph receptors into heterologous cells induces a clustering of the Eph receptors and AF-6 at sites of cell–cell contact. Immunohistochemical analysis in the adult rat brain reveals coclustering of AF-6 with Eph receptors at postsynaptic membrane sites of excitatory synapses in the hippocampus. Furthermore, AF-6 is a substrate for a subgroup of Eph receptors and phosphorylation of AF-6 is dependent on a functional kinase domain of the receptor. The physical interaction of endogenous AF-6 with Eph receptors is demonstrated by coimmunoprecipitation from whole rat brain lysates. AF-6 is a candidate for mediating the clustering of Eph receptors at postsynaptic specializations in the adult rat brain.
APA, Harvard, Vancouver, ISO, and other styles
8

Janes, Peter W., Bettina Griesshaber, Lakmali Atapattu, Eva Nievergall, Linda L. Hii, Anneloes Mensinga, Chanly Chheang, et al. "Eph receptor function is modulated by heterooligomerization of A and B type Eph receptors." Journal of Cell Biology 195, no. 6 (December 5, 2011): 1033–45. http://dx.doi.org/10.1083/jcb.201104037.

Full text
Abstract:
Eph receptors interact with ephrin ligands on adjacent cells to facilitate tissue patterning during normal and oncogenic development, in which unscheduled expression and somatic mutations contribute to tumor progression. EphA and B subtypes preferentially bind A- and B-type ephrins, respectively, resulting in receptor complexes that propagate via homotypic Eph–Eph interactions. We now show that EphA and B receptors cocluster, such that specific ligation of one receptor promotes recruitment and cross-activation of the other. Remarkably, coexpression of a kinase-inactive mutant EphA3 with wild-type EphB2 can cause either cross-activation or cross-inhibition, depending on relative expression. Our findings indicate that cellular responses to ephrin contact are determined by the EphA/EphB receptor profile on a given cell rather than the individual Eph subclass. Importantly, they imply that in tumor cells coexpressing different Ephs, functional mutations in one subtype may cause phenotypes that are a result of altered signaling from heterotypic rather from homotypic Eph clusters.
APA, Harvard, Vancouver, ISO, and other styles
9

Wang, Jia, Xiang Zheng, Qiu Peng, Xuemei Zhang, and Zailong Qin. "Eph receptors: the bridge linking host and virus." Cellular and Molecular Life Sciences 77, no. 12 (December 31, 2019): 2355–65. http://dx.doi.org/10.1007/s00018-019-03409-6.

Full text
Abstract:
AbstractEph (erythropoietin-producing hepatoma) receptors and Ephrin ligands constitute the largest subfamily of receptor tyrosine kinase (RTK), which were first discovered in tumors. Heretofore, Eph protein has been shown to be involved in various tumor biological behaviors including proliferation and progression. The occurrence of specific types of tumor is closely related to the virus infection. Virus entry is a complex process characterized by a series of events. The entry into target cells is an essential step for virus to cause diseases, which requires the fusion of the viral envelope and host cellular membrane mediated by viral glycoproteins and cellular receptors. Integrin molecules are well known as entry receptors for most herpes viruses. However, in recent years, Eph receptors and their Ephrin ligands have been reported to be involved in virus infections. The main mechanism may be the interaction between Eph receptors and conserved viral surface glycoprotein, such as the gH/gL or gB protein of the herpesviridae. This review focuses on the relationship between Eph receptor family and virus infection that summarize the processes of viruses such as EBV, KSHV, HCV, RRV, etc., infecting target cells through Eph receptors and activating its downstream signaling pathways resulting in malignancies. Finally, we discussed the perspectives to block virus infection, prevention, and treatment of viral-related tumors via Eph receptor family.
APA, Harvard, Vancouver, ISO, and other styles
10

Xu, Qiling, Georg Mellitzer, and David G. Wilkinson. "Roles of Eph receptors and ephrins in segmental patterning." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 355, no. 1399 (July 29, 2000): 993–1002. http://dx.doi.org/10.1098/rstb.2000.0635.

Full text
Abstract:
Eph receptor tyrosine kinases and their membrane–bound ligands, ephrins, have key roles in patterning and morphogenesis. Interactions between these molecules are promiscuous, but largely fall into two groups: EphA receptors bind to glycosylphosphatidyl inositol–anchored ephrin–A ligands, and EphB receptors bind to transmembrane ephrin–B proteins. Ephrin–B proteins transduce signals, such that bidirectional signalling can occur upon interaction with the Eph receptor. In many tissues, there are complementary and overlapping expression domains of interacting Eph receptors and ephrins. An important role of Eph receptors and ephrins is to mediate cell contact–dependent repulsion, and this has been implicated in the pathfinding of axons and neural crest cells, and the restriction of cell intermingling between hindbrain segments. Studies in an in vitro system show that bidirectional activation is required to prevent intermingling between cell populations, whereas unidirectional activation can restrict cell communication via gap junctions. Recent work indicates that Eph receptors can also upregulate cell adhesion, but the biochemical basis of repulsion versus adhesion responses is unclear. Eph receptors and ephrins have thus emerged as key regulators that, in parallel with cell adhesion molecules, underlie the establishment and maintenance of patterns of cellular organization.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Eph receptor"

1

Tuzi, Nadia Lucia. "The Eph growth factor receptor." Thesis, Open University, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.294878.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Bovenkamp, Diane Elizabeth. "Eph receptor tyrosine kinases, nervous system development and angiogenesis, cloning and characterization of Eph receptors from zebrafish and mice." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0021/NQ54056.pdf.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Soskis, Michael. "A Chemical-Genetic Study of EphB Receptor Tyrosine Kinase Signaling in the Developing Nervous System." Thesis, Harvard University, 2012. http://dissertations.umi.com/gsas.harvard:10525.

Full text
Abstract:
EphB receptor tyrosine kinases regulate cell-cell contacts throughout nervous system development, mediating processes as diverse as axon guidance, topographic mapping, neuronal migration and synapse formation. EphBs bind to a group of ligands, ephrin-Bs, which span the plasma membrane, thus allowing for bidirectional signaling between cells. Since EphBs are capable of multiple modes of signaling, and since they regulate numerous interdependent stages of development, it has been challenging to define which signaling functions of EphBs mediate particular developmental events. To overcome this hurdle, we developed an approach combining chemical biology with genetic engineering to reversibly inhibit EphB receptors in vivo. By mutating a residue in the receptor’s ATP-binding pocket, we rendered its kinase activity sensitive to reversible inhibition by PP1 analogs that do not inhibit wild type receptors. We engineered triple knockin mice bearing this mutation in which the kinase activity of EphB1, EphB2, and EphB3 can be rapidly, reversibly, and specifically blocked. Since we are able to block the kinase activity of EphBs while leaving their scaffolding and reverse signaling capabilities intact, we can precisely isolate the role of the kinase domain. In addition, acute inhibition can circumvent the developmental compensation that may occur after genetic mutations and can even allow the controlled study of EphBs in the mature brain and in disease models. Using these mice, termed analog-sensitive EphB triple knockin (AS-EphB TKI) mice, we demonstrate a requirement for the kinase-dependent signaling of EphBs in the collapse of retinal ganglion cell growth cones in vitro and the guidance of retinal axons at the optic chiasm in vivo. In addition, we show that the formation of several cortical axon tracts, including the corpus callosum, requires EphB tyrosine kinase signaling. In contrast, we find that steps in synapse development that are thought to be EphB-dependent occur normally when the kinase activity of EphBs is inhibited. We conclude that a cardinal in vivo function of EphB signaling, the ability to mediate axon guidance via growth cone repulsion, requires the tyrosine kinase activity of EphBs, while the development of functional excitatory synapses is independent of EphB tyrosine kinase activity.
APA, Harvard, Vancouver, ISO, and other styles
4

Stanforth, Hannah Amy. "Transcriptional targets of Eph receptor and ephrin signalling in the zebrafish hindbrain." Thesis, University College London (University of London), 2018. http://discovery.ucl.ac.uk/10053620/.

Full text
Abstract:
In vertebrates, there is a large family of Eph receptor tyrosine kinases and their ephrin ligands, which have complex and varied roles during development and in adult homeostasis. The most researched role of Eph receptors and ephrins is in control of cell migration through the regulation of the actin cytoskeleton and cell adhesion. More recently, it has been found that in some tissues Eph-ephrin signalling also leads to changes in gene transcription, for example to control cell differentiation. In the zebrafish hindbrain, Eph receptors and ephrins are expressed segmentally in the rhombomeres in a complementary pattern with respect to their binding partner. Signalling via this pathway induces a unique cell population to arise at rhombomere borders, known as the boundary cells. In order to understand more about Eph receptor and ephrin function in the hindbrain, RNA-sequencing was carried out on dissected hindbrains of zebrafish with endogenous Eph-ephrin signalling and fish that lack Eph-ephrin signalling. The transcriptional profiles were then compared to identify potential downstream targets, which were verified using RT-qPCR and in situ hybridisation. This identified four genes regulated downstream of Eph-ephrin signalling that are markers of progenitor cells and neural differentiation. When Eph-ephrin signalling is disrupted the expression of these genes alters, and the expression pattern of one gene, mdka, was consistent with loss of hindbrain boundary cells. To investigate this observation further, the expression of progenitor and neurogenic markers was determined when Eph-ephrin signalling was disrupted. This supported previous studies which found that Eph-ephrin signalling is required for formation of boundary cells and that boundary cell loss results in ectopic neurogenesis. In addition, it was found that ectopic neurogenesis was accompanied by the depletion of nestin-expressing neural progenitor cells at later stages of development. Together these findings support previous work showing that hindbrain boundary cells are essential for restricting neurogenesis to neurogenic zones adjacent to the boundaries.
APA, Harvard, Vancouver, ISO, and other styles
5

Scully, Audra L. "Isolation and characterization of Dek, a Drosophila Eph receptor protein tyrosine kinase /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 1998. http://wwwlib.umi.com/cr/ucsd/fullcit?p9904821.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Falivelli, Giulia <1985&gt. "Attenuation of Eph Receptor Kinase Activation in Cancer Cells by Coexpressed Ephrin Ligands." Doctoral thesis, Alma Mater Studiorum - Università di Bologna, 2014. http://amsdottorato.unibo.it/6264/.

Full text
Abstract:
The Eph receptor tyrosine kinases mediate juxtacrine signals by interacting “in trans” with ligands anchored to the surface of neighboring cells via a GPI-anchor (ephrin-As) or a transmembrane segment (ephrin-Bs), which leads to receptor clustering and increased kinase activity. Additionally, soluble forms of the ephrin-A ligands released from the cell surface by matrix metalloproteases can also activate EphA receptor signaling. Besides these trans interactions, recent studies have revealed that Eph receptors and ephrins coexpressed in neurons can also engage in lateral “cis” associations that attenuate receptor activation by ephrins in trans with critical functional consequences. Despite the importance of the Eph/ephrin system in tumorigenesis, Eph receptor-ephrin cis interactions have not been previously investigated in cancer cells. Here we show that in cancer cells, coexpressed ephrin-A3 can inhibit the ability of EphA2 and EphA3 to bind ephrins in trans and become activated, while ephrin-B2 can inhibit not only EphB4 but also EphA3. The cis-inhibition of EphA3 by ephrin-B2 implies that in some cases ephrins that cannot activate a particular Eph receptor in trans can nevertheless inhibit its signaling ability through cis association. We also found that an EphA3 mutation identified in lung cancer enhances cis interaction with ephrin-A3. These results suggest a novel mechanism that may contribute to cancer pathogenesis by attenuating the tumor suppressing effects of Eph receptor signaling pathways activated by ephrins in trans (Falivelli et al. 2013).
APA, Harvard, Vancouver, ISO, and other styles
7

McCarron, Jennifer Kylie. "The role of the Eph and ephrin proteins in prostate cancer." Thesis, Queensland University of Technology, 2011. https://eprints.qut.edu.au/67918/1/Jennifer_McCarron_Thesis.pdf.

Full text
Abstract:
Prostate cancer is the most commonly diagnosed malignancy and the second leading cause of cancer related deaths in Australian men. Treatment in the early stages of the disease involves surgery, radiation and/or hormone therapy. However, in late stages of the disease these treatments are no longer effective and only palliative care is available. Therefore, there is a focus on exploration of novel therapies to increase survival and treatment efficacy. Advanced prostate cancer is characterised by bone or other distant metastasis. Spreading of the primary tumour to a secondary location is a complex process requiring an initial loss in cell-cell adhesion followed by increased cell migration and invasion. One gene family that has been known to affect cell-to-cell contact in other model systems are the Eph receptor tyrosine kinases. They are the largest family of receptor tyrosine kinases made up of 14 vertebrate Eph receptors that bind to nine cell membrane bound ephrin ligands. Eph-ephrin interaction is crucial in regulating cell behaviour in developmental processes and it is now thought that the underlying mechanisms involved in development may also be involved in cancer. Aberrant expression has been reported in many human malignancies including prostate cancer. Furthermore, expression has been linked with metastasis and poor prognosis in other tumour models. This study explores the potential role of the Eph receptor family in prostate cancer, in particular the roles of EphA2, EphA3 and ephrin-A5. Gene expression profiles were established for the Eph family in a series of prostate cancer cell lines using quantitative real time RT-PCR. A smaller subset of the most prominently expressed genes was chosen to screen a cohort of clinical samples. Elevated levels of EphA2, EphA3 and their ligands, ephrin-A1 and ephrin-A5 were observed in individual cell lines. Interestingly high EphA3 expression was observed in the androgen responsive cell lines while EphA2 was more prominent in the androgen independent cell lines. However, studies using 5-dihydrotestosterone suggest that EphA3 expression in not regulated by androgen. Cells expressing EphA2 showed a greater ability for migration and invasion while cells expressing EphA3 showed poor migration and invasion. Forced expression of EphA2 in the LNCaP cell line resulted in a more invasive phenotype while forced expression of EphA3 in the PC-3 cell line suggests a possible negative effect for EphA3 on cell migration and invasion. Cell signalling studies show activation of EphA2 decreases activity of proteins thought to be involved in pathways regulating cell movement including Akt, Src and FAK. Changes to the activation status of Rho family members, including RhoA and Rac1, associated with reorganisation of the actin cytoskeleton, an important part of cell migration was also observed. As a result, activation of EphA2 in PC-3 cells resulted in a less invasive phenotype. A novel finding in this study was the discovery of a combination of two EphA2 Mabs able to activate EphA2. Preliminary results show a potential for this antibody combination to reduce prostate cancer invasion in vitro. A unique aspect of Eph-ephrin interaction is the resulting bi-directional signalling that occurs through both the receptor and ligand. In this study a potential role for ephrin-A5 mediated signalling in prostate cancer was observed. LNCaP cells express high levels of EphA3 and its high affinity ligand ephrin-A5. In stripe assays, used to study guidance cues, LNCaP cells show strong attraction/migration to EphA3-Fc stripes but not ephrin-A5-Fc stripes suggesting ephrin-A5 mediated reverse cell signalling is involved. Knockdown of ephrin-A5 using shRNA resulted in a decrease in attraction/migration to EphA3-Fc stripes. Furthermore a reduction in proliferation was also observed in vitro. A subcutaneous xenograft model using ephrin-A5 shRNA cells versus controls showed a decrease in tumour formation. This study demonstrates a difference in EphA2 and EphA3 function in prostate cancer migration/invasion and a potential role for ephrin-A5 in prostate cancer cell adhesion and growth.
APA, Harvard, Vancouver, ISO, and other styles
8

Schaupp, Andreas. "Eph receptor clustering is the central integrator in eliciting graded Kinase-dependent signaling responses." Diss., lmu, 2012. http://nbn-resolving.de/urn:nbn:de:bvb:19-147651.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Karam, Sana. "Mechanisms of pattern formation in the developing cerebellum : role for Eph receptor gene family /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/10557.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Sabet, Ola [Verfasser], Philippe [Akademischer Betreuer] Bastiaens, and Roland [Akademischer Betreuer] Winter. "The spatial organization of EPH receptor tyrosine kinase activity / Ola Sabet. Betreuer: Philippe Bastiaens. Gutachter: Roland Winter." Dortmund : Universitätsbibliothek Dortmund, 2013. http://d-nb.info/1100168591/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "Eph receptor"

1

Wybenga-Groot, Leanne Elizabeth. Regulation of Eph receptor tyrosine kinase catalytic function. 2005.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Elowe, Sabine. Regulation of the ERK MAP kinase cascade by the Eph family of receptor tyrosine kinases. 2005.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

D. Shao, Y. Hu, Q. Wang, Y. Shen, X. Zhao, H.B. Tong*, and S.R. Shi*. The Growth hormone receptor is involved in the effects of dietary microencapsulated sodium butyrate on growth performance and intestinal morphology of yellow-feathered broilers. Verlag Eugen Ulmer, 2016. http://dx.doi.org/10.1399/eps.2016.167.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Litwa, M. David. The Evil Creator. Oxford University Press, 2021. http://dx.doi.org/10.1093/oso/9780197566428.001.0001.

Full text
Abstract:
This book examines the origins of the evil creator idea chiefly in light of early Christian biblical interpretation. It is divided into two main parts. In Part I, the focus is on the interpretation of a variety of alternative Christian groups (e.g., “Phibionite,” “Sethian,” “Ophite”). First, the pre-Christian Egyptian assimilation of the Jewish god to the evil deity Seth-Typhon is studied to understand its reapplication by alternative Christians to the Judeo-catholic creator. Second, an alternative Christian reception of John 8:44 (understood to refer to the devil’s father) is shown to implicate the Judeo-catholic creator in murdering Christ. Part II focuses on Marcionite Christian biblical interpretations. It begins with Marcionite interpretations of the creator’s character in Jewish scripture(Chapter 3), analyzes the reception of 2 Corinthians 4:4 (in which “the god of this world” blinds people, Chapter 4), examines Christ’s so-called destruction of the Law (Eph 2:15) and the Lawgiver (Chapters 5–6), and shows how Christ finally succumbs to the curse of the Law (Gal 3:13) inflicted by the creator (Chapter 7). A concluding chapter sums up the findings and shows how still today many readers of the Bible conclude that the creator is evil.
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Eph receptor"

1

Lai, Kwok-On, and Nancy Y. Ip. "Eph Receptor." In Encyclopedia of Signaling Molecules, 1565–73. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_428.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Miki, Toru, Randa Hilal-Dandan, Laurence L. Brunton, Jean Sévigny, Kwok-On Lai, Nancy Y. Ip, Renping Zhou, et al. "Eph Receptor." In Encyclopedia of Signaling Molecules, 560–67. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_428.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Gaitanos, Thomas, Irina Dudanova, Maria Sakkou, Rüdiger Klein, and Sónia Paixão. "The Eph Receptor Family." In Receptor Tyrosine Kinases: Family and Subfamilies, 165–264. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-11888-8_5.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Krull, Catherine E., and Daniel J. Liebl. "Ephrins and Eph Receptor Tyrosine Kinases in Synapse Formation." In The Sticky Synapse, 333–45. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-92708-4_16.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Drescher, U. "Eph Receptor Tyrosine Kinases and Their Ligands in Development." In Of Fish, Fly, Worm, and Man, 151–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-662-04264-9_9.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Jorgensen, Claus, and Alexei Poliakov. "Proteomics Analysis of Contact-Initiated Eph Receptor–Ephrin Signaling." In Cell-Cell Interactions, 1–16. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-604-7_1.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Zhou, Renping. "Regulation of topographic projection by the Eph family receptor Bsk (EphA5) and its ligands." In Molecular Bases of Axonal Growth and Pathfinding, 251–59. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-60905-3_10.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Arango, Diego. "Eph Receptors." In Encyclopedia of Cancer, 1–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_1928-2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Arango, Diego. "Eph Receptors." In Encyclopedia of Cancer, 1549–51. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46875-3_1928.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Arango, Diego. "Eph Receptors." In Encyclopedia of Cancer, 1268–69. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_1928.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "Eph receptor"

1

Nick, Alpa M., Rebecca L. Stone, Bin Chang, Jinsong Liu, Diana Urbauer, Edna Mora, Chad Pecot, et al. "Abstract 4457: In Search of a novel EPO receptor: The clinical significance of the Eph connection." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-4457.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Al-Mathkour, Marwah M., and Bekir Cinar. "Abstract 2634: The role of Eph A receptor 3 tyrosine kinase signaling in prostate cancer progression." 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.sabcs18-2634.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Al-Mathkour, Marwah M., and Bekir Cinar. "Abstract 2634: The role of Eph A receptor 3 tyrosine kinase signaling in prostate cancer progression." 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.am2019-2634.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Wang, Ying-Nai, Heng-Huan Lee, Wen-Hao Yang, Gabriel N. Hortobagyi, Dihua Yu, and Mien-Chie Hung. "Abstract 3081: Secretory human ribonuclease 1 functions as Eph receptor A4 ligand to promote breast tumor initiation." 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.am2021-3081.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Pujuguet, Philippe, Filip Beirinckx, Carole Delachaume, Jacques Huck, Ellen Van der Aar, Reginald Brys, Luc Van Rompaey, Piet Wigerinck, and Laurent Saniere. "Abstract 1753: GLPG1790: The first Ephrin (EPH) receptor tyrosine kinase inhibitor for the treatment of triple negative breast cancer." 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.am2014-1753.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Nagano, Kazuya, Yuka Maeda, Takuya Yamashita, Yohei Mukai, Haruhiko Kamada, Kazuma Higashisaka, Yasuo Yoshioka, Yasuo Tsutsumi, and Shin-ichi Tsunoda. "Abstract 4377: Biodistribution and therapeutic effects of a monoclonal antibody against Eph receptor A10 in a breast cancer xenograft model." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4377.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Authi, K. S., B. J. Evenden, E. J. Hornby, and N. Crawford. "THROMBOXANE-A2 MEDIATES THE ACTION OF INOSITOL (1.4.5) TRISPHOSPHATE (IP3) IN SAPONIN-PERMEABILISED PLATELETS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644519.

Full text
Abstract:
Inositol trisphosphate (IP3) has now been identified as an important intracellular second messenger that can initiate the release of Ca2+ from intracellular stores in a variety of cells, including platelets. We have studied the effects of IP3 on washed platelets permeabilised with saponin (12-14 μg/mi) which allows penetration into the cell of low M.Wt polar molecules. The permeabilised cells show normal responses to the agonists thrombin and collagen. The addition of IP (1-20 μM) after saponin treatment induces shape change, aggregation and secretion of preloaded [14C] 5HT. Concomitant with these responses, thromboxane is produced in a dose related manner. With 20 μM IP3 thromboxane B2 increases from basal levels of 5-4 ± 3-0 ng/ml to 140 ± 23 ng/ml. Both thromboxane production and the platelet responses induced by IP3 are inhibited by pretreatment with the cyclooxygenase inhibitors, indomethacin (EC50 50 μM) and aspirin (EC50 30 μM). Aggregation and secretion responses to IP3 are also inhibited by thromboxane B2 receptor agonists; EPO 92 (R. Jones, Edinburgh) and AH 23848 (Glaxo Ltd.). If Ca2+ EGTA buffers age used with permeabilised platelets to "lock" the cytosolic [Ca2+] at 0.1 μM, thromboxane production is reduced to the basal level. Intact platelets were labelled with Ca2+ (4h incubation) and after washing, resuspension and saponisation, IP3 induced the release of 20% of the cell associated Ca2+. The release was unaffected by pretreatment with antimycin and oligomycin indicating an gndoplasmic reticulum-lige storage site for the sequestered Ca2+. This IP3 -induced Ca2+ release was also not affected by pretreatment with either cyclooxygenase inhibitors or thromboxane receptor antagonists (EPO 92 and AH 23848). We believe these studies indicate that the action of IP3 in sagonised platelets involves release of intracellularly stored Ca2+, activation of phospholipase A2 and cyclooxygenase, and production of thromboxane A2. The release of thromboxane mediates and/or attenuates platelet responses by acting upon platelet surface receptors.
APA, Harvard, Vancouver, ISO, and other styles
8

Vaapil, Marica C., Susann Reinbothe, Anna-Maria Larsson, Caroline Wigerup, Jianmin Sun, Annika Jögi, Drorit Neumann, Lars Rönnstrand, and Sven Påhlman. "Abstract 3464: The effect of EPO-receptor in estrogen receptor positive breast cancer." 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.am2014-3464.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Shaikh, Saame (Raz), Anandita Pal, and Ian Carroll. "Eicosapentaenoic acid ethyl esters prevent obesity-driven impairments to glucose homeostasis through the biosynthesis of downstream hydroxylated metabolites." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/colx6433.

Full text
Abstract:
There is considerable debate on the clinical utility of the long n-3 polyunsaturated fatty acids eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) for preventing dysregulation of obesity-driven glucose homeostasis. Herein, we first show that administration of ethyl esters of EPA, but not DHA, to C57BL/6J male mice improves hyperglycemia, hyperinsulinemia, and glucose tolerance. Mechanistically, we demonstrate that EPA reverses the obesity-driven decrease in the concentration of white adipose tissue and liver 18-hydroxyeicosapentaenoic acid (18-HEPE), the precursor for resolvin E1 (RvE1). A combination of add-back and receptor knockout experiments reveal that RvE1 is specifically driving the improvement in hyperinsulinemia and hyperglycemia through the receptor known as ERV1/ChemR23 by controlling pathways related to hepatic glucose metabolism and inflammation. Next, we show that EPA’s effects are distinct in female mice as EPA administration leads to improvements in body weight, hyperinsulinemia and hyperglycemia but not glucose tolerance. In this case, EPA exerts its effects through a mechanism potentially mediated by 8-HEPE and upregulation of key intestinal microbes. Finally, we present translation data showing that glucose levels in humans with obesity are inversely related to EPA but not DHA in a sex-specific manner. Furthermore, data from our pilot clinical trial demonstrate that an 18-HEPE-enriched marine oil supplement increases RvE1 levels by 3-fold in humans with obesity. Taken together, these results provide clarity to the field by suggesting that EPA but not DHA ethyl esters can prevent glucose dysregulation in a sex-specific manner through distinct mechanisms mediated by downstream hydroxylated metabolites.
APA, Harvard, Vancouver, ISO, and other styles
10

Fulton, Amy M., Xinrong Ma, Namita Kundu, Olga Ioffe, Olga Goloubeva, Raymond Konger, Claudia Baquet, and Jocelyn Reader. "Abstract 5764: Opposing roles of the COX-2 pathway receptors EP1 and EP4 in metastasis and contribution to disparities." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-5764.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "Eph receptor"

1

Altstein, Miriam, and Ronald J. Nachman. Rational Design of Insect Control Agent Prototypes Based on Pyrokinin/PBAN Neuropeptide Antagonists. United States Department of Agriculture, August 2013. http://dx.doi.org/10.32747/2013.7593398.bard.

Full text
Abstract:
The general objective of this study was to develop rationally designed mimetic antagonists (and agonists) of the PK/PBAN Np class with enhanced bio-stability and bioavailability as prototypes for effective and environmentally friendly pest insect management agents. The PK/PBAN family is a multifunctional group of Nps that mediates key functions in insects (sex pheromone biosynthesis, cuticular melanization, myotropic activity, diapause and pupal development) and is, therefore, of high scientific and applied interest. The objectives of the current study were: (i) to identify an antagonist biophores (ii) to develop an arsenal of amphiphilic topically active PK/PBAN antagonists with an array of different time-release profiles based on the previously developed prototype analog; (iii) to develop rationally designed non-peptide SMLs based on the antagonist biophore determined in (i) and evaluate them in cloned receptor microplate binding assays and by pheromonotropic, melanotropic and pupariation in vivo assays. (iv) to clone PK/PBAN receptors (PK/PBAN-Rs) for further understanding of receptor-ligand interactions; (v) to develop microplate binding assays for screening the above SMLs. In the course of the granting period A series of amphiphilic PK/PBAN analogs based on a linear lead antagonist from the previous BARD grant was synthesized that incorporated a diverse array of hydrophobic groups (HR-Suc-A[dF]PRLa). Others were synthesized via the attachment of polyethylene glycol (PEG) polymers. A hydrophobic, biostablePK/PBAN/DH analog DH-2Abf-K prevented the onset of the protective state of diapause in H. zea pupae [EC50=7 pmol/larva] following injection into the preceding larval stage. It effectively induces the crop pest to commit a form of ‘ecological suicide’. Evaluation of a set of amphiphilic PK analogs with a diverse array of hydrophobic groups of the formula HR-Suc-FTPRLa led to the identification of analog T-63 (HR=Decyl) that increased the extent of diapause termination by a factor of 70% when applied topically to newly emerged pupae. Another biostablePK analog PK-Oic-1 featured anti-feedant and aphicidal properties that matched the potency of some commercial aphicides. Native PK showed no significant activity. The aphicidal effects were blocked by a new PEGylated PK antagonist analog PK-dF-PEG4, suggesting that the activity is mediated by a PK/PBAN receptor and therefore indicative of a novel and selective mode-of-action. Using a novel transPro mimetic motif (dihydroimidazole; ‘Jones’) developed in previous BARD-sponsored work, the first antagonist for the diapause hormone (DH), DH-Jo, was developed and shown to block over 50% of H. zea pupal diapause termination activity of native DH. This novel antagonist development strategy may be applicable to other invertebrate and vertebrate hormones that feature a transPro in the active core. The research identifies a critical component of the antagonist biophore for this PK/PBAN receptor subtype, i.e. a trans-oriented Pro. Additional work led to the molecular cloning and functional characterization of the DH receptor from H. zea, allowing for the discovery of three other DH antagonist analogs: Drosophila ETH, a β-AA analog, and a dF analog. The receptor experiments identified an agonist (DH-2Abf-dA) with a maximal response greater than native DH. ‘Deconvolution’ of a rationally-designed nonpeptide heterocyclic combinatorial library with a cyclic bis-guanidino (BG) scaffold led to discovery of several members that elicited activity in a pupariation acceleration assay, and one that also showed activity in an H. zea diapause termination assay, eliciting a maximal response of 90%. Molecular cloning and functional characterization of a CAP2b antidiuretic receptor from the kissing bug (R. prolixus) as well as the first CAP2b and PK receptors from a tick was also achieved. Notably, the PK/PBAN-like receptor from the cattle fever tick is unique among known PK/PBAN and CAP2b receptors in that it can interact with both ligand types, providing further evidence for an evolutionary relationship between these two NP families. In the course of the granting period we also managed to clone the PK/PBAN-R of H. peltigera, to express it and the S. littoralis-R Sf-9 cells and to evaluate their interaction with a variety of PK/PBAN ligands. In addition, three functional microplate assays in a HTS format have been developed: a cell-membrane competitive ligand binding assay; a Ca flux assay and a whole cell cAMP ELISA. The Ca flux assay has been used for receptor characterization due to its extremely high sensitivity. Computer homology studies were carried out to predict both receptor’s SAR and based on this analysis 8 mutants have been generated. The bioavailability of small linear antagonistic peptides has been evaluated and was found to be highly effective as sex pheromone biosynthesis inhibitors. The activity of 11 new amphiphilic analogs has also been evaluated. Unfortunately, due to a problem with the Heliothis moth colony we were unable to select those with pheromonotropic antagonistic activity and further check their bioavailability. Six peptides exhibited some melanotropic antagonistic activity but due to the low inhibitory effect the peptides were not further tested for bioavailability in S. littoralis larvae. Despite the fact that no new antagonistic peptides were discovered in the course of this granting period the results contribute to a better understanding of the interaction of the PK/PBAN family of Nps with their receptors, provided several HT assays for screening of libraries of various origin for presence of PK/PBAN-Ragonists and antagonists and provided important practical information for the further design of new, peptide-based insecticide prototypes aimed at the disruption of key neuroendocrine physiological functions in pest insects.
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Eph receptor' for particular source types:
Journal articles Dissertations / Theses
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography