EFNA5

Ephrin-A5, also known as EFNA5, is a human gene.cite web | title = Entrez Gene: EFNA5 ephrin-A5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1946| accessdate = ]

PBB_Summary
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summary_text = Ephrin-A5, a member of the ephrin gene family, prevents axon bundling in cocultures of cortical neurons with astrocytes, a model of late stage nervous system development and differentiation. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. EPH receptors typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997). Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are similarly divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.cite web | title = Entrez Gene: EFNA5 ephrin-A5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1946| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Flanagan JG, Vanderhaeghen P |title=The ephrins and Eph receptors in neural development. |journal=Annu. Rev. Neurosci. |volume=21 |issue= |pages= 309–45 |year= 1998 |pmid= 9530499 |doi= 10.1146/annurev.neuro.21.1.309
*cite journal | author=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151–81 |year= 1998 |pmid= 9576626 |doi=
*cite journal | author=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis. |journal=Development |volume=126 |issue= 10 |pages= 2033–44 |year= 1999 |pmid= 10207129 |doi=
*cite journal | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly. |journal=Int. Rev. Cytol. |volume=196 |issue= |pages= 177–244 |year= 2000 |pmid= 10730216 |doi=
*cite journal | author=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=355 |issue= 1399 |pages= 993–1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635
*cite journal | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155–64 |year= 2001 |pmid= 11256076 |doi=
*cite journal | author=Winslow JW, Moran P, Valverde J, "et al." |title=Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor involved in axon bundle formation. |journal=Neuron |volume=14 |issue= 5 |pages= 973–81 |year= 1995 |pmid= 7748564 |doi=
*cite journal | author=Cerretti DP, Copeland NG, Gilbert DJ, "et al." |title=The gene encoding LERK-7 (EPLG7, Epl7), a ligand for the Eph-related receptor tyrosine kinases, maps to human chromosome 5 at band q21 and to mouse chromosome 17. |journal=Genomics |volume=35 |issue= 2 |pages= 376–9 |year= 1996 |pmid= 8661153 |doi= 10.1006/geno.1996.0371
*cite journal | author=Gale NW, Holland SJ, Valenzuela DM, "et al." |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. |journal=Neuron |volume=17 |issue= 1 |pages= 9–19 |year= 1996 |pmid= 8755474 |doi=
*cite journal | author=Lackmann M, Mann RJ, Kravets L, "et al." |title=Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16521–30 |year= 1997 |pmid= 9195962 |doi=
*cite journal | author=Kozlosky CJ, VandenBos T, Park L, "et al." |title=LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain. |journal=Cytokine |volume=9 |issue= 8 |pages= 540–9 |year= 1997 |pmid= 9245480 |doi= 10.1006/cyto.1997.0199
*cite journal | author= |title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. |journal=Cell |volume=90 |issue= 3 |pages= 403–4 |year= 1997 |pmid= 9267020 |doi=
*cite journal | author=Ciossek T, Monschau B, Kremoser C, "et al." |title=Eph receptor-ligand interactions are necessary for guidance of retinal ganglion cell axons in vitro. |journal=Eur. J. Neurosci. |volume=10 |issue= 5 |pages= 1574–80 |year= 1998 |pmid= 9751130 |doi=
*cite journal | author=Janis LS, Cassidy RM, Kromer LF |title=Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum. |journal=J. Neurosci. |volume=19 |issue= 12 |pages= 4962–71 |year= 1999 |pmid= 10366629 |doi=
*cite journal | author=Gerlai R, Shinsky N, Shih A, "et al." |title=Regulation of learning by EphA receptors: a protein targeting study. |journal=J. Neurosci. |volume=19 |issue= 21 |pages= 9538–49 |year= 1999 |pmid= 10531456 |doi=
*cite journal | author=Davy A, Gale NW, Murray EW, "et al." |title=Compartmentalized signaling by GPI-anchored ephrin-A5 requires the Fyn tyrosine kinase to regulate cellular adhesion. |journal=Genes Dev. |volume=13 |issue= 23 |pages= 3125–35 |year= 2000 |pmid= 10601038 |doi=

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