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The following terms were not found in PubMed: LINC01950, LINC01950
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Mapping of breakpoints in balanced chromosomal translocations by shallow whole-genome sequencing points to EFNA5, BAHD1 and PPP2R5E as novel candidates for genes causing human Mendelian disorders.
Murcia Pienkowski V, Kucharczyk M, Młynek M, Szczałuba K, Rydzanicz M, Poszewiecka B, Skórka A, Sykulski M, Biernacka A, Koppolu AA, Posmyk R, Walczak A, Kosińska J, Krajewski P, Castaneda J, Obersztyn E, Jurkiewicz E, Śmigiel R, Gambin A, Chrzanowska K, Krajewska-Walasek M, Płoski R. Murcia Pienkowski V, et al. J Med Genet. 2019 Feb;56(2):104-112. doi: 10.1136/jmedgenet-2018-105527. Epub 2018 Oct 23. J Med Genet. 2019. PMID: 30352868
In one case (BCT disrupting BAHD1 and RET) cDNA analysis was used to verify expression of a fusion transcript in cultured fibroblasts. RESULTS: In all nine probands 11 disrupted genes were found, that is, EFNA5, EBF3, LARGE, PPP2R5E, TXNDC5, ZNF423, NIPBL, BAHD1, RE …
In one case (BCT disrupting BAHD1 and RET) cDNA analysis was used to verify expression of a fusion transcript in cultured fibroblasts …
Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.
Laing ED, Navaratnarajah CK, Cheliout Da Silva S, Petzing SR, Xu Y, Sterling SL, Marsh GA, Wang LF, Amaya M, Nikolov DB, Cattaneo R, Broder CC, Xu K. Laing ED, et al. Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20707-20715. doi: 10.1073/pnas.1911773116. Epub 2019 Sep 23. Proc Natl Acad Sci U S A. 2019. PMID: 31548390 Free PMC article.
We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. ...We also show that CedV can enter …
We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and …
Protein targeting in the analysis of learning and memory: a potential alternative to gene targeting.
Gerlai R, Williams SP, Cairns B, Van Bruggen N, Moran P, Shih A, Caras I, Sauer H, Phillips HS, Winslow JW. Gerlai R, et al. Exp Brain Res. 1998 Nov;123(1-2):24-35. doi: 10.1007/s002210050541. Exp Brain Res. 1998. PMID: 9835389
Here, we suggest a potentially useful in vivo strategy based on systemic application of immunoadhesins, genetically engineered fusion proteins possessing the Fc portion of the human IgG molecule and, for example, a binding domain of a receptor of interest. ...
Here, we suggest a potentially useful in vivo strategy based on systemic application of immunoadhesins, genetically engineered fusion …
Recruitment of Eph receptors into signaling clusters does not require ephrin contact.
Wimmer-Kleikamp SH, Janes PW, Squire A, Bastiaens PI, Lackmann M. Wimmer-Kleikamp SH, et al. J Cell Biol. 2004 Mar 1;164(5):661-6. doi: 10.1083/jcb.200312001. J Cell Biol. 2004. PMID: 14993233 Free PMC article.
We demonstrate by confocal time-lapse and fluorescence resonance energy transfer microscopy that within minutes of binding ephrin-A5-coated beads, EphA3 receptors assemble into large clusters. ...
We demonstrate by confocal time-lapse and fluorescence resonance energy transfer microscopy that within minutes of binding ephrin- …
Reconstitution of Fusion Proteins in Supported Lipid Bilayers for the Study of Cell Surface Receptor-Ligand Interactions in Cell-Cell Contact.
Ghosh Moulick R, Afanasenkau D, Choi SE, Albers J, Lange W, Maybeck V, Utesch T, Offenhäusser A. Ghosh Moulick R, et al. Langmuir. 2016 Apr 12;32(14):3462-9. doi: 10.1021/acs.langmuir.5b04644. Epub 2016 Apr 1. Langmuir. 2016. PMID: 26986674
This platform consists of a supported lipid bilayer modified with incorporated neuronal adhesion proteins conjugated with the Fc-domain of IgG (ephrin A5 Fc-chimera). We extensively characterized properties of these protein containing bilayers using fluorescence rec …
This platform consists of a supported lipid bilayer modified with incorporated neuronal adhesion proteins conjugated with the Fc-domain of I …
Alkaline phosphatase fusion proteins as affinity probes for protein localization studies.
Brennan C, Fabes J. Brennan C, et al. Sci STKE. 2003 Feb 4;2003(168):PL2. doi: 10.1126/stke.2003.168.pl2. Sci STKE. 2003. PMID: 12582203
The technique permits localization of both receptors and ligands and is readily quantifiable for cell-surface binding assays. Soluble ectodomain placental alkaline phosphatase fusion proteins are therefore highly sensitive reagents that permit the direct localization of av …
The technique permits localization of both receptors and ligands and is readily quantifiable for cell-surface binding assays. Soluble ectodo …
Compartmentalized signaling by GPI-anchored ephrin-A5 requires the Fyn tyrosine kinase to regulate cellular adhesion.
Davy A, Gale NW, Murray EW, Klinghoffer RA, Soriano P, Feuerstein C, Robbins SM. Davy A, et al. Genes Dev. 1999 Dec 1;13(23):3125-35. doi: 10.1101/gad.13.23.3125. Genes Dev. 1999. PMID: 10601038 Free PMC article.
Eph receptor tyrosine kinases and their corresponding surface-bound ligands, the ephrins, provide cues to the migration of cells and growth cones during embryonic development. Here we show that ephrin-A5, which is attached to the outer leaflet of the plasma membrane …
Eph receptor tyrosine kinases and their corresponding surface-bound ligands, the ephrins, provide cues to the migration of cells and growth …
Kinetic analysis of the binding of monomeric and dimeric ephrins to Eph receptors: correlation to function in a growth cone collapse assay.
Pabbisetty KB, Yue X, Li C, Himanen JP, Zhou R, Nikolov DB, Hu L. Pabbisetty KB, et al. Protein Sci. 2007 Mar;16(3):355-61. doi: 10.1110/ps.062608807. Protein Sci. 2007. PMID: 17322526 Free PMC article.
Our results indicate that the Eph receptor binding of dimeric ephrins, formed through fusion with disulfide-linked Fc fragments, is best described using a bivalent analyte model as a two-step process involving an initial monovalent 2:1 binding followed by a second bivalent …
Our results indicate that the Eph receptor binding of dimeric ephrins, formed through fusion with disulfide-linked Fc fragments, is b …
Three distinct molecular surfaces in ephrin-A5 are essential for a functional interaction with EphA3.
Day B, To C, Himanen JP, Smith FM, Nikolov DB, Boyd AW, Lackmann M. Day B, et al. J Biol Chem. 2005 Jul 15;280(28):26526-32. doi: 10.1074/jbc.M504972200. Epub 2005 May 18. J Biol Chem. 2005. PMID: 15901737 Free article.
However, Eph signal initiation requires the assembly of higher order oligomers, suggesting additional points of contact. By screening a random library of EphA3 binding-compromised ephrin-A5 mutants, we have now determined ephrin-A5 residues that are es …
However, Eph signal initiation requires the assembly of higher order oligomers, suggesting additional points of contact. By screening a rand …