Receptor, EphA4
Receptor, EphA2
Ephrin-A2
Ephrin-A5
Receptor, EphA7
Receptor, EphA5
Receptor, EphA1
Ephrin-A1
Receptors, Eph Family
Ephrin-A4
Ephrins
Ephrin-A3
Ephrin-B3
Topographic targeting and pathfinding errors of retinal axons following overexpression of ephrinA ligands on retinal ganglion cell axons. (1/52)
In the retinotectal projection, the Eph receptor tyrosine kinase ligands ephrinA2 and ephrinA5 are differentially expressed not only in the tectum, but also in a high-nasal-to-low-temporal pattern in the retina. Recently, we have shown that retrovirally driven overexpression of ephrinA2 on retinal axons leads to topographic targeting errors of temporal axons in that they overshoot their normal termination zones in the rostral tectum and project onto the mid- and caudal tectum. The behavior of nasal axons, however, was only marginally affected. Here, we show that overexpression of ephrinA5 affects the topographic targeting behavior of both temporal and nasal axons. These data reinforce the idea that differential ligand expression on retinal axons contributes to topographic targeting in the retinotectal projection. Additionally, we found that ectopic expression of ephrinA2 and ephrinA5 frequently leads to pathfinding errors at the chiasm, resulting in an increased stable ipsilateral projection. (+info)Axon guidance in the mouse optic chiasm: retinal neurite inhibition by ephrin "A"-expressing hypothalamic cells in vitro. (2/52)
In the mammalian visual system, retinal axons undergo temporal and spatial rearrangements as they project bilaterally to targets on the brain. Retinal axons cross the neuraxis to form the optic chiasm on the hypothalamus in a position defined by overlapping domains of regulatory gene expression. However, the downstream molecules that direct these processes remain largely unknown. Here we use a novel in vitro paradigm to study possible roles of the Eph family of receptor tyrosine kinases in chiasm formation. In vivo, Eph receptors and their ligands distribute in complex patterns in the retina and hypothalamus. In vitro, retinal axons are inhibited by reaggregates of isolated hypothalamic, but not dorsal diencephalic or cerebellar cells. Furthermore, temporal retinal neurites are more inhibited than nasal neurites by hypothalamic cells. Addition of soluble EphA5-Fc to block Eph "A" subclass interactions decreases both the inhibition and the differential response of retinal neurites by hypothalamic reaggregates. These data show that isolated hypothalamic cells elicit specific, position-dependent inhibitory responses from retinal neurites in culture. Moreover, these responses are mediated, in part, by Eph interactions. Together with the in vivo distributions, these data suggest possible roles for Eph family members in directing retinal axon growth and/or reorganization during optic chiasm formation. (+info)Ephrin-A5 modulates cell adhesion and morphology in an integrin-dependent manner. (3/52)
The ephrins are membrane-tethered ligands for the Eph receptor tyrosine kinases, which play important roles in patterning of the nervous and vascular systems. It is now clear that ephrins are more than just ligands and can also act as signalling-competent receptors, participating in bidirectional signalling. We have recently shown that ephrin-A5 signals within caveola-like domains of the plasma membrane upon engagement with its cognate Eph receptor, leading to increased adhesion of the cells to fibronectin. Here we show that ephrin-A5 controls sequential biological events that are consistent with its role in neuronal guidance. Activation of ephrin-A5 induces an initial change in cell adhesion followed by changes in cell morphology. Both effects are dependent on the activation of beta1 integrin involving members of the Src family of protein tyrosine kinases. The prolonged activation of ERK-1 and ERK-2 is required for the change in cell morphology. Our work suggests a new role for class A ephrins in specifying the affinity of the cells towards various extracellular substrates by regulating integrin function. (+info)An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors. (4/52)
Appropriate development of nervous system connectivity involves a variety of processes, including neuronal life-and-death decisions, differentiation, axon guidance and migration, and synaptogenesis. Although these activities likely require specialized signaling events, few substrates unique to these neurotrophic functions have been identified. Here we describe the cloning of ankyrin repeat-rich membrane spanning (ARMS), which encodes a novel downstream target of neurotrophin and ephrin receptor tyrosine kinases, Trk and Eph, respectively. The amino acid sequence of ARMS is highly conserved from nematode to human, suggesting an evolutionarily conserved role for this protein. The ARMS protein consists of 1715 amino acids containing four putative transmembrane domains, multiple ankyrin repeats, a sterile alpha motif domain, and a potential PDZ-binding motif. In the rat, ARMS is specifically expressed in the developing nervous system and in highly plastic areas of the adult brain, regions enriched in Trks and Eph receptors. ARMS can physically associate with TrkA and p75 neurotrophin receptors. Moreover, endogenous ARMS protein is tyrosine phosphorylated after neurotrophin treatment of pheochromocytoma 12 cells and primary hippocampal neurons or ephrin B treatment of NG108-15 cells, demonstrating that ARMS is a downstream target for both neurotrophin and ephrin receptors. (+info)Centrosome duplication: three kinases come up a winner! (5/52)
Despite over one hundred years of research, the duplication of the centrosome is a poorly understood process. Three recent papers--exploring three different kinases--may have provided the answer. (+info)Topographic-specific axon branching controlled by ephrin-As is the critical event in retinotectal map development. (6/52)
The retinotectal projection is the predominant model for studying molecular mechanisms controlling development of topographic axonal connections. Our analyses of topographic mapping of retinal ganglion cell (RGC) axons in chick optic tectum indicate that a primary role for guidance molecules is to regulate topographic branching along RGC axons, a process that imposes unique requirements on the molecular control of map development. We show that topographically appropriate connections are established exclusively by branches that form along the axon shaft. Initially, RGC axons overshoot their appropriate termination zone (TZ) along the anterior-posterior (A-P) tectal axis; temporal axons overshoot the greatest distance and nasal axons the least, which correlates with the nonlinear increasing A-P gradient of ephrin-A repellents. In contrast, branches form along the shaft of RGC axons with substantial A-P topographic specificity. Topography is enhanced through the preferential arborization of appropriately positioned branches and elimination of ectopic branches. Using a membrane stripe assay and time-lapse microscopy, we show that branches form de novo along retinal axons. Temporal axons preferentially branch on their topographically appropriate anterior tectal membranes. After the addition of soluble EphA3-Fc, which blocks ephrin-A function, temporal axons branch equally on anterior and posterior tectal membranes, indicating that the level of ephrin-As in posterior tectum is sufficient to inhibit temporal axon branching and generate branching specificity in vitro. Our findings indicate that topographic branch formation and arborization along RGC axons are critical events in retinotectal mapping. Ephrin-As inhibit branching along RGC axons posterior to their correct TZ, but alone cannot account for topographic branching and must cooperate with other molecular activities to generate appropriate mapping along the A-P tectal axis. (+info)Eph receptor tyrosine kinase-mediated formation of a topographic map in the Drosophila visual system. (7/52)
Roles for Eph receptor tyrosine kinase signaling in the formation of topographic patterns of axonal connectivity have been well established in vertebrate visual systems. Here we describe a role for a Drosophila Eph receptor tyrosine kinase (EPH) in the control of photoreceptor axon and cortical axon topography in the developing visual system. Although uniform across the developing eye, EPH is expressed in a concentration gradient appropriate for conveying positional information during cortical axon guidance in the second-order optic ganglion, the medulla. Disruption of this graded pattern of EPH activity by double-stranded RNA interference or by ectopic expression of wild-type or dominant-negative transgenes perturbed the establishment of medulla cortical axon topography. In addition, abnormal midline fasciculation of photoreceptor axons resulted from the eye-specific expression of the dominant-negative EPH transgene. These observations reveal a conserved role for Eph kinases as determinants of topographic map formation in vertebrates and invertebrates. (+info)Ephrins regulate the formation of terminal axonal arbors during the development of thalamocortical projections. (8/52)
The development of connections between thalamic afferents and their cortical target cells occurs in a highly precise manner. Thalamic axons enter the cortex through deep cortical layers, then stop their growth in layer 4 and elaborate terminal arbors specifically within this layer. The mechanisms that underlie target layer recognition for thalamocortical projections are not known. We compared the growth pattern of thalamic explants cultured on membrane substrates purified from cortical layer 4, the main recipient layer for thalamic axons, and cortical layer 5, a non-target layer. Thalamic axons exhibited a reduced growth rate and an increased branching density on their appropriate target membranes compared with non-target substrate. When confronted with alternating stripes of both membrane substrates, thalamic axons grew preferentially on their target membrane stripes. Enzymatic treatment of cortical membranes revealed that growth, branching and guidance of thalamic axons are independently regulated by attractive and repulsive cues differentially expressed in distinct cortical layers. These results indicate that multiple membrane-associated molecules collectively contribute to the laminar targeting of thalamic afferents. Furthermore, we found that interfering with the function of Eph tyrosine kinase receptors and their ligands, ephrins, abolished the preferential branching of thalamic axons on their target membranes, and that recombinant ephrin-A5 ligand elicited a branch-promoting activity on thalamic axons. We conclude that interactions between Eph receptors and ephrins mediate branch formation of thalamic axons and thereby may play a role in the establishment of layer-specific thalamocortical connections. (+info)EphA4 is a type of receptor tyrosine kinase that belongs to the Eph (Erythropoietin-producing hepatocellular) family of receptors. It is a transmembrane protein found on the surface of various types of cells, including neurons and glial cells in the nervous system.
EphA4 receptors play critical roles in several biological processes, such as cell migration, axon guidance, and synaptic plasticity during development and throughout adulthood. They interact with ephrin proteins, which are ligands (molecules that bind to receptors) found on adjacent cells. The interaction between EphA4 and ephrins triggers a cascade of intracellular signaling events that ultimately influence cell behavior.
In summary, EphA4 is a type of receptor involved in cell-cell communication, particularly during the development and functioning of the nervous system. Its dysfunction has been implicated in several neurological disorders, such as spinal cord injuries, Alzheimer's disease, and various forms of cancer.
EphA2 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph (Erythropoietin-producing hepatocellular) family of receptors. It is a transmembrane protein found on the surface of many types of cells, including epithelial, endothelial, and cancer cells.
EphA2 receptors play critical roles in various biological processes such as cell growth, survival, migration, and angiogenesis. They interact with their ligands, called ephrins, which are also transmembrane proteins expressed on adjacent cells. The interaction between EphA2 and ephrins triggers bidirectional signaling that can regulate the adhesion, repulsion, or movement of cells in response to contact with other cells.
In cancer biology, EphA2 receptors have been implicated in tumor progression and metastasis. Overexpression of EphA2 has been observed in various types of human cancers, including breast, lung, prostate, ovarian, and colon cancer. High levels of EphA2 are often associated with poor clinical outcomes, making it an attractive therapeutic target for cancer treatment.
Ephrin-A2 is a type of protein that belongs to the ephrin family. It is a membrane-bound ligand for Eph receptors, which are tyrosine kinase receptors located on the cell surface. Ephrin-A2 and Eph receptors play critical roles in various biological processes, including axon guidance, tissue boundary formation, and tumorigenesis.
Ephrin-A2 is encoded by the EFNB2 gene and is expressed on the cell membrane as a glycosylphosphatidylinositol (GPI)-anchored protein. It can interact with several Eph receptors, including EphA3, EphA4, EphA5, and EphA7, leading to bidirectional signaling that regulates cell-cell interactions and communication.
In the nervous system, ephrin-A2 and its receptors are essential for the development and maintenance of neural circuits. They help to establish precise connections between neurons by mediating repulsive interactions that guide axon growth and fasciculation. Additionally, ephrin-A2 has been implicated in various pathological conditions, such as cancer, where it can contribute to tumor progression and metastasis.
Ephrin-A5 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that interact with Eph receptors, which are tyrosine kinase receptors found on the surface of cells. The interaction between ephrins and Eph receptors plays a crucial role in the development and function of the nervous system, including axon guidance, cell migration, and synaptic plasticity.
Ephrin-A5 is specifically classified as a glycosylphosphatidylinositol (GPI)-anchored protein, which means it is attached to the outer layer of the cell membrane through a GPI anchor. It is primarily expressed in various tissues, including the brain, heart, and lungs.
In the nervous system, Ephrin-A5 and its receptor, EphA4, are involved in repulsive guidance cues that help to establish proper neuronal connections during development. Dysregulation of this interaction has been implicated in several neurological disorders, such as spinal cord injuries, Alzheimer's disease, and schizophrenia.
EphA7 is a type of receptor that belongs to the EPH receptor tyrosine kinase family. These receptors are involved in intracellular signaling and play crucial roles in various biological processes, including cell growth, differentiation, and migration.
EphA7 receptors are specifically activated by ephrin-A ligands, which are membrane-bound proteins expressed on adjacent cells. When an ephrin-A ligand binds to an EphA7 receptor, it triggers a cascade of intracellular signaling events that can affect various cellular functions.
EphA7 receptors have been implicated in several physiological and pathological processes, including nervous system development, angiogenesis, and cancer. In the nervous system, EphA7 receptors help to establish connections between neurons and guide their migration during development. In cancer, abnormal expression or activation of EphA7 receptors has been linked to tumor growth, progression, and metastasis.
It's worth noting that while I strive to provide accurate and up-to-date information, medical definitions can be complex and nuanced. Therefore, it may be helpful to consult authoritative medical resources or speak with a healthcare professional for more detailed information on this topic.
EphA5 is a type of receptor tyrosine kinase that belongs to the Eph receptor family. Eph receptors are the largest subfamily of receptor tyrosine kinases and play critical roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development.
EphA5 receptor specifically binds to ephrin-A5 ligand, which is a member of the ephrin family of membrane-bound proteins. The binding of ephrin-A5 to EphA5 triggers bidirectional signaling, meaning that both the receptor and the ligand can transmit signals into their respective cells. This interaction leads to various cellular responses, such as changes in cytoskeletal organization, cell adhesion, and intracellular signaling pathways.
EphA5 has been implicated in several physiological and pathological processes, including neural development, vascular remodeling, tumor angiogenesis, and cancer metastasis. Mutations in the EPHA5 gene have been associated with various human diseases, such as intellectual disability, epilepsy, and congenital heart defects.
EphA1 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. It is a single-pass transmembrane protein that contains an extracellular domain with a binding site for its ligand, ephrin-A5, and an intracellular domain with tyrosine kinase activity.
EphA1 receptors are involved in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. They also play a role in angiogenesis, neuroprotection, and tumorigenesis in adults.
The binding of ephrin-A5 to EphA1 receptors triggers bidirectional signaling, affecting both the receptor-expressing cell and the ephrin-presenting cell. This interaction can lead to repulsion, adhesion, or collapse of the growth cone, depending on the context and the specific Eph/ephrin pair involved.
Mutations in EphA1 have been associated with various diseases, including cancer, neurodevelopmental disorders, and cardiovascular disease.
Ephrin-A1 is a type of protein that belongs to the ephrin family. It is a membrane-bound ligand for Eph receptors, which are tyrosine kinase receptors located on the cell surface. Ephrin-A1 and its receptors play critical roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. Ephrin-A1 is also involved in angiogenesis, tumorigenesis, and metastasis in cancer. It is encoded by the EFNAs gene in humans.
Eph family receptors are a group of tyrosine kinase receptors that play crucial roles in the development and function of the nervous system, as well as in other tissues. They are named after the first discovered member of this family, EPH (Erythropoietin-Producing Human Hepatocellular carcinoma) receptor.
These receptors are divided into two subfamilies: EphA and EphB, based on their binding preferences for ephrin ligands. Ephrins are membrane-bound proteins that can be either GPI-anchored (ephrin-A) or transmembrane (ephrin-B), and they interact with Eph receptors in a bidirectional manner, activating both forward signaling in the receptor-expressing cell and reverse signaling in the ephrin-expressing cell.
Eph receptors and ephrins are essential for axon guidance, topographic mapping, and synaptic plasticity during neural development. They also participate in various processes in adult tissues, such as angiogenesis, tumorigenesis, and immune responses. Dysregulation of Eph family receptors has been implicated in several diseases, including cancer, neurological disorders, and vascular diseases.
Ephrin-A4 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that play crucial roles in various biological processes, including cell signaling and communication during development. Specifically, Ephrin-A4 is a ligand for Eph receptors, which are tyrosine kinase receptors located on the cell membrane.
Ephrin-A4 is composed of a glycosylphosphatidylinositol (GPI) anchor that attaches it to the cell membrane and an extracellular domain that interacts with Eph receptors. When Ephrin-A4 binds to an Eph receptor on a neighboring cell, it triggers a cascade of intracellular signaling events that can regulate various cellular processes, such as cell adhesion, migration, and proliferation.
In the medical field, Ephrin-A4 has been studied in the context of various diseases, including cancer. For example, abnormal expression of Ephrin-A4 has been observed in several types of tumors, and it has been suggested to play a role in tumor progression and metastasis. However, more research is needed to fully understand the functional significance of Ephrin-A4 in health and disease.
Ephrins are a family of membrane-bound proteins that play crucial roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. They interact with Eph receptors, which are tyrosine kinase receptors found on the surface of neighboring cells. This interaction results in bidirectional signaling between the two cells, affecting their behaviors and influencing the organization of tissues and organs.
There are two main types of ephrins: Ephrin-A (also known as GPI-anchored ephrins) and Ephrin-B (transmembrane ephrins). Ephrin-A proteins are attached to the cell membrane through a glycosylphosphatidylinositol (GPI) anchor, while Ephrin-B proteins have a transmembrane domain and a cytoplasmic tail. Both types of ephrins interact with Eph receptors, leading to the initiation of intracellular signaling cascades that regulate various cellular responses.
Dysregulation of ephrin/Eph receptor interactions has been implicated in several human diseases, including cancer, where they can contribute to tumor growth, progression, and metastasis. Therefore, understanding the functions and regulation of ephrins and their receptors is essential for developing novel therapeutic strategies to treat various diseases.
Ephrin-A3 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that play crucial roles in various biological processes, including cell signaling and communication during development. Specifically, Ephrin-A3 binds to Eph receptors, which are tyrosine kinase receptors found on the surface of neighboring cells. This binding leads to bidirectional signals that regulate cell adhesion, repulsion, and migration, thereby helping to establish proper tissue and organ architecture during development. Additionally, Ephrin-A3 has been implicated in various physiological and pathological processes, such as angiogenesis, neurogenesis, and cancer.
Ephrin-B3 is a type of protein that belongs to the ephrin family and is involved in cell signaling, particularly during the development and functioning of the nervous system. It is a transmembrane protein, which means it spans the membrane of the cell and has a domain outside the cell and a domain inside the cell.
Ephrin-B3 interacts with Eph receptors on neighboring cells to initiate bidirectional signaling, which means that both the cells that express ephrin-B3 and the cells that express the Eph receptor are affected by this interaction. This signaling is important for various processes such as axon guidance, cell migration, and tissue boundaries formation during development. In addition, ephrin-B3 has been implicated in the regulation of synaptic plasticity and vascular remodeling in adults.
Mutations in the gene that encodes ephrin-B3 have been associated with certain neurological disorders, such as intellectual disability and epilepsy.
EPH receptor A1
Ephrin
Ephrin receptor
List of MeSH codes (D08)
EPHA
List of MeSH codes (D12.776.543)
ABCA7
TCF7L2
Tyrosine kinase
Sterile alpha motif
Fibronectin type III domain
EPH receptor A1 - Wikipedia
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RCSB PDB - 2K9Y: EphA2 dimeric structure in the lipidic bicelle at pH 5.0
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Eph
Calmodulin binding proteins and neuroinflammation in multiple neurodegenerative diseases | BMC Neuroscience | Full Text
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C) Log concentration-response relaxation curves to 5-HT and 5-HT receptor agonists - TNF-mediated apoptosis in cardiac myocytes
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Epidermal growth f6
- EPHA1, EPHA2, EFNA3, and EFNA4 mRNA expression was significantly higher in human epidermal growth factor receptor 2- (HER2-) positive tumors than in HER2-negative tumors. (hindawi.com)
- The epidermal growth factor receptor (EGFR) is a receptor tyrosine kinase (RTK) commonly targeted for inhibition by anti-cancer therapeutics. (biorxiv.org)
- The epidermal growth factor receptor (EGFR) is a HER-family receptor tyrosine kinase (RTK) that is involved in cell signaling in healthy tissue. (biorxiv.org)
- It is also frequently called HER2 (from human epidermal growth factor receptor 2 ) or HER2/neu . (iiab.me)
- HER2 is a member of the human epidermal growth factor receptor (HER/EGFR/ERBB) family. (iiab.me)
- HER2 is so named because it has a similar structure to human epidermal growth factor receptor, or HER1. (iiab.me)
Type-A receptor1
- EPH receptor A1 (ephrin type-A receptor 1) is a protein that in humans is encoded by the EPHA1 gene. (wikipedia.org)
EPHA6
- Family A receptors (EPHA) and ligands (EFNA) can act as oncogenes or tumor suppressors and are implicated in chemoresistance. (hindawi.com)
- Ephrin family A includes ten receptors named EPHA (1-10) and five ligands designated as EFNA (1-5) [ 6 ]. (hindawi.com)
- In general, class EphA receptors bind GPI-anchored ephrin-A ligands. (umbc.edu)
- There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. (umbc.edu)
- The Eph family of receptor tyrosine kinases (comprising EphA and EphB receptors) has been implicated in synapse formation and the regulation of synaptic function and plasticity6. (betalifesci.com)
- It binds preferentially to ephA receptors ( EPH FAMILY RECEPTORS ) with the exception of the EPHA1 RECEPTOR . (nih.gov)
Ligands9
- The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. (wikipedia.org)
- Unified nomenclature for Eph family receptors and their ligands, the ephrins. (wikipedia.org)
- The Eph receptor tyrosine kinases and their membrane-bound ephrin ligands control a diverse array of cell-cell interactions in the developing and adult organisms. (rcsb.org)
- Ephrins, also known as ephrin ligands, and Eph receptors (Ephs), which are RTKs, are key regulators of physiological and pathological processes involved in development and disease, such as cellular motility, cell repulsion, and cell adhesion [ 4 ]. (hindawi.com)
- Both receptors and ligands are membrane-bound proteins that require direct cell-cell interaction for activation. (hindawi.com)
- The interaction between ligands and receptors via bidirectional signaling and its involvement in cancer biology are mediated by complex processes [ 7 , 8 ]. (hindawi.com)
- The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date and their ligands, the ephrins,can be subdivided into two major subclasses, ephrin-A and ephrin-B. Interaction of Eph receptor tyrosine kinases with their membrane bound ephrin ligands initiates bidirectional signaling events that regulate cell migratory and adhesive behavior, particularly in the nervous system. (affbiotech.cn)
- Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. (affbiotech.cn)
- The conserved Eph receptors and their Ephrin ligands regulate a number of developmental processes, including axon guidance. (arizona.edu)
EphA22
- Spatial structure of dimeric transmembrane domain of EphA2 receptor embedded into lipid bicelle was obtained by solution NMR, showing a left-handed parallel packing of the transmembrane helices (535-559)(2). (rcsb.org)
- The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. (umbc.edu)
Protein7
- This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. (wikipedia.org)
- These findings serve as an instructive example of the diversity of transmembrane domain formation within the same family of protein kinases and seem to favor the assumption that the so-called rotation-coupled activation mechanism may take place during the Eph receptor signaling. (rcsb.org)
- EPH receptor A1 (EphA1), with 976-amino acid protein(about 107 kDa), belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. (affbiotech.cn)
- In a cross-sectional study of 48 AD patients without diabetes, 20 cognitively normal diabetic patients, 16 patients with frontotemporal dementia, and 84 cognitively normal controls, researchers found that dysfunctionally phosphorylated insulin receptor substrate-1 (IRS-1), a neuronal protein, is detectable in blood using exosome-based technology and may be able to predict AD up to 10 years before the appearance of symptoms. (medscape.com)
- Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10. (umbc.edu)
- G protein-coupled P2Y receptors participate in the nucleotide receptor G protein-coupled receptor (GPCR) family members and also have eight mammalian subtypes (P2Y1, 2, 4, 6, 11-14) (Kim et al. (aboutsciencenow.info)
- Receptor tyrosine-protein kinase erbB-2 , also known as CD340 (cluster of differentiation 340), proto-oncogene Neu , Erbb2 (rodent), or ERBB2 (human), is a protein that in humans is encoded by the ERBB2 gene. (iiab.me)
Monoclonal2
- The pieces had been precontracted with 1 molL?1 phenylephrine which induced a suffered contraction Mouse monoclonal to EphA1 above basal pressure of just one 1.9 0.4 g (= 71). (nonamimaho.com)
- The pocket for MRS2500 binding to Mouse monoclonal to EphA1 P2Y1R described by residues through the N terminus generally, ECL2, and its own helices buildings. (aboutsciencenow.info)
RTKs3
- Receptor tyrosine kinases (RTKs) play an important role in a variety of cellular processes in cancer [ 3 ]. (hindawi.com)
- EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). (umbc.edu)
- Ephrin receptors are components of cell signalling pathways involved in animal growth and development, forming the largest sub-family of receptor tyrosine kinases (RTKs). (betalifesci.com)
CD332
- Common variants at ABCA7 , MS4A6A/MS4A4E , EPHA1 , CD33 and CD2AP are associated with Alzheimer's disease. (jamanetwork.com)
- Common variants at MS4A4/MS4A6E , CD2AP , CD33 and EPHA1 are associated with late-onset Alzheimer's disease. (jamanetwork.com)
Vertebrate2
- Roles for Eph receptor tyrosine kinase signaling in the formation of topographic patterns of axonal connectivity have been well established in vertebrate visual systems. (sdbonline.org)
- In contrast to the large vertebrate Eph/Ephrin family, Drosophila has a single Eph receptor and a single Ephrin ligand, both of which are expressed within the developing nervous system. (arizona.edu)
Subfamily1
- Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. (wikipedia.org)
Drosophila Eph2
- A role for a Drosophila Eph receptor tyrosine kinase (Eph) in the control of photoreceptor axon and cortical axon topography in the developing visual system is described. (sdbonline.org)
- Thomas, John B. / Drosophila Eph receptor guides specific axon branches of mushroom body neurons . (arizona.edu)
Transmembrane1
- Importantly, a similar motif AX(3)GX(3)G as was found is responsible for right-handed dimerization of transmembrane domain of the EphA1 receptor. (rcsb.org)
EPHA101
- EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. (umbc.edu)
Membrane-bound1
- The ErbB family consists of four plasma membrane-bound receptor tyrosine kinases. (iiab.me)
Proteins1
- The individual P2Y1 receptor proteins framework and its own two ligand-binding sites for the nucleotide-like antagonist MRS2500 and allosteric antagonist 1-(2-(2-tert-butylphenoxy)pyridin-3-yl)-3-(4-(trifluoromethoxy)phenyl)urea (BPTU) had been reported in 2015 (Proteins Database [PDB] Identification: 4XNW, 4XNV) (Zhang et al. (aboutsciencenow.info)
Binds2
- This substance binds the recombinant individual P2Y1 receptor and inhibits the platelet aggregation due to ADP with an 50% inhibitory focus (IC50) worth in the nanomolar range. (aboutsciencenow.info)
- EphA5, also known as Ehk1, Bsk, Cek7, Hek7, and Rek7, is a member of the Eph receptor tyrosine kinase family which binds members of the Ephrin ligand family (1 - 4). (rndsystems.com)
Recombinant1
- Purified recombinant fragment of human EphA1 expressed in E. Coli. (affbiotech.cn)
HER21
- [10] [11] HER2 can heterodimerise with any of the other three receptors and is considered to be the preferred dimerisation partner of the other ErbB receptors. (iiab.me)
Roles1
- Ligand-mediated activation of Ephs induce various important downstream effects and Eph receptors have been studied for their potential roles in the development of cancer. (betalifesci.com)
Mammalian1
- Comparative studies of mammalian estrogen receptors from tissue culture and rats. (edu.au)
Serotonin1
- 2015). ADP may be the initial small-molecular pounds platelet agonist, and its own receptors, such as for example P2Y1 receptors, can few to turned on phospholipase C. The activation of serotonin receptor products signaling through the P2Y1 receptor, demonstrating that it's a particular antagonist in a position to stop ADP-induced platelet aggregation (Jin and Kunapuli, 1998). (aboutsciencenow.info)
Residues1
- Dimerisation results in the autophosphorylation of tyrosine residues within the cytoplasmic domain of the receptors and initiates a variety of signaling pathways. (iiab.me)
Antagonist2
- Ivacaftor hydrate Ramifications of 5-HT receptor antagonists on relaxations to 5-HT The 5-HT7 receptor selective antagonist SB 269970 (100 nmolL?1 and 300 nmolL?1) caused maximal rightwards displacements from the rest concentration-response curve to 5-HT (Shape 2A,B, Desk 2) and 5-CT (Shape 2C, Desk 2). (nonamimaho.com)
- In P2Y1R, the antagonist MRS2500 possibly prevents the actions of the helices and stabilized the receptor within an inactive condition by getting together with helices In the P2Y1RCMRS2500 framework, each terminal air of both phosphates forms at least one connection with the receptor. (aboutsciencenow.info)
Apoptosis1
- In summary, signaling through the ErbB family of receptors promotes cell proliferation and opposes apoptosis, and therefore must be tightly regulated to prevent uncontrolled cell growth from occurring. (iiab.me)
Signal1
- Eph/ephrin signal transduction occurs not only in the receptor-expressing cell but also in the ligand-expressing cell via bidirectional signaling [ 5 ]. (hindawi.com)
Human1
- Utilising fly genetics, this study generated the first Drosophila model of human wild-type and P460L mutant EphA1 and tested the effects of Eph /ephrin signalling on AD-relevant behaviour and neurophysiology. (sdbonline.org)
Channels1
- Prejunctional 5-HT1A Kv and receptors channels modulated 5-HT-induced relaxations whereas postjunctional K+ channels weren't involved with such responses. (nonamimaho.com)
Developmental1
- EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. (wikipedia.org)
Activation1
- Eph receptor-mediated signaling, which is triggered by ephrins7, probably modifies the properties of synapses during synaptic activation and remodeling. (betalifesci.com)
Expression2
- EphA1 mis-expression did not cause neurodegeneration, shorten lifespan or affect memory but flies mis-expressing the wild-type or mutant receptor were hyper-aroused, had reduced sleep , a stronger circadian rhythm and increased clock neuron activity and excitability. (sdbonline.org)
- Furthermore, diverse structural alterations have been identified that cause ligand-independent firing of this receptor, doing so in the absence of receptor over-expression. (iiab.me)