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Removal of this side chain enhances the binding affinity by more than fivefold, suggesting that access of Crb to Pals1 may be regulated by intradomain contacts or by protein-protein interaction.
The unique in-frame MPP5-FAM71D fusion product is important for proliferation of PC346C cells.
the crystal structure of a 4-L27 domain-containing heterotrimer derived from the tripartite complex Patj/Pals1/Mals2
Crystals of tripartite complex 1 of L27 (show RPL27 Proteins)(PATJ)-(L27N,L27C)(Pals1)-L27 (show RPL27 Proteins)(MALS (show NCR3 Proteins)) diffracted to 2.05 A resolution
Small irregularly shaped spots are detected throughout the Pals1-deficient retina of conditional knockdown mice by confocal scanning laser ophthalmoscopy and spectral domain optical coherence tomography.
The cell polarity protein PALS1 is expressed in T lymphocytes and participates to the optimal activation of NF-kappaB following TCR stimulation.
Data suggest that hijacking of PALS1 by SARS (show SARS Proteins)-CoV E plays a determinant role in the disruption of the lung epithelium in SARS (show SARS Proteins) patients.
Polycystin-2 activity is controlled by transcriptional coactivator with PDZ binding motif and PALS1-associated tight junction protein
Polarity protein associated with lin seven 1 (Pals1) plays an essential role in radical and longitudinal extension of the myelin sheath in peripheral nerves, likely involving membrane protein trafficking.
Pals1 functions as an adapter, linking mammalian homologues of Crumbs and Discs Lost.
Pals1 haploinsufficiency in mouse kidneys associated with the upregulation of Hippo pathway target genes and marker genes of TGF-beta (show TGFB1 Proteins) signaling, including biomarkers of renal diseases. These findings support a link between apical polarity proteins and renal diseases, especially renal cyst diseases
This study identifies Pals1 as a novel intrinsic factor (show GIF Proteins) that regulates the generation of cerebellar cells and Pals1 deficiency as a potential inhibitor of overactive mitogenic signaling.
This paper reveals the role of the canonical polarity protein Pals1 in radial sorting of axons by Schwann cells.
Data show the deletion of Pals1 leads to the disruption of the apical localization of Crb polarity complex proteins Crb1 (show CRB1 Proteins), Crb2 (show CRB2 Proteins) and Crb3 (show CRB3 Proteins) in retinal progenitors and the adult retina.
Genetic study demonstrates a near-complete abrogation of cortical development in the absence of the apical complex protein Pals1. Despite the absence of most cortical structures, Pals1 CKO mice survive and display relatively normal health.
association of Veli3 with MPP5 suggests that the MAGUKs recruit Veli3 and its binding partners to different cellular regions of the retina where they may participate in the organization of specialized intercellular junctions.
analysis of structures of tetrameric L27 (show RPL27A Proteins) domain complexes formed by mLin-2 (show CASK Proteins)/mLin-7 and Patj/Pals1 scaffold proteins
RNA interference-induced silencing of the Crb1 (show CRB1 Proteins)-interacting-protein Pals1 (protein associated with Lin7; Mpp5) in Muller glial cells resulted in loss of Crb1 (show CRB1 Proteins), Crb2 (show CRB2 Proteins), Mupp1 and Veli3 protein localization and partial loss of Crb3 (show CRB3 Proteins).
the importance of a conserved Crumbs-MPP5-EPB41L5 (show EPB41L5 Proteins) polarity complex in mammals for separation of the apical and basolateral domains through specialized cell-cell junctions
morphogenesis of the neural tube requires nok (show STYK1 Proteins) function
Heart and soul/PRKCi and nagie oko/Mpp5 regulate myocardial coherence and remodeling during cardiac morphogenesis.
Data show that nagie oko contains a predicted nuclear export and two conserved nuclear localization signals and loss of the predicted nuclear export signal results in nuclear protein accumulation.
deletion constructs of Nok in functional rescue experiments to define domains essential for cell polarity, maintenance of epithelial integrity and cardiac morphogenesis.Nok does not interact with Crumbs proteins upon deletion of the PDZ domain
that Nok (show STYK1 Proteins) is required for retinal pigment epithelium integrity in a tissue-autonomous manner
This gene encodes a member of the p55-like subfamily of the membrane-associated guanylate kinase (MAGUK) gene superfamily. The encoded protein participates in the polarization of differentiating cells, has been shown to regulate myelinating Schwann cells (PMID: 20237282), and is one of the components of the Crumbs complex in the retina. Mice which express lower levels of the orthologous protein have retinal degeneration and impaired vision (PMID: 22114289). Multiple transcript variants encoding different isoforms have been found for this gene.
MAGUK p55 subfamily member 5
, protein associated with lin seven 1
, protein associated with Lin Seven 1
, membrane protein, palmitoylated 3 (MAGUK p55 subfamily member 5)
, protein associated with Lin-7 1
, MAGUK family factor
, MAGUK p55 subfamily member 5-A
, membrane protein, palmitoylated 5 (MAGUK p55 subfamily member 5)
, nagie oko protein