Frizzled Domain
Mostrando 1-12 de 20 artigos, teses e dissertações.
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1. Estudo da regulação transcricional do COL18A1 e análise funcional do domínio Frizzled / Study COL18A1 transcription regulation and function analysis of Frizzled domain
A conclusão do seqüênciamento do genoma de múltiplos vertebrados trouxe um importante desafio para entender e predizer função, particularmente para seqüências não-codificantes, a partir de seqüências primarias de DNA. A hipótese de que a conservação evolutiva prediz seqüências funcionais é comumente aceita, inclusive para seqüências envolv
Publicado em: 2009
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2. A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors
This paper describes the identification of a new family of mammalian genes that encode secreted proteins containing homology to the cysteine-rich ligand-binding domain found in the frizzled family of transmembrane receptors. The secreted frizzled-related proteins (sFRPs) are approximately 30 kDa in size, and each contains a putative signal sequence, a frizzl
The National Academy of Sciences of the USA.
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3. The cysteine-rich frizzled domain of Frzb-1 is required and sufficient for modulation of Wnt signaling
Convincing evidence has accumulated to identify the Frizzled proteins as receptors for the Wnt growth factors. In parallel, a number of secreted frizzled-like proteins with a conserved N-terminal frizzled motif have been identified. One of these proteins, Frzb-1, binds Wnt-1 and Xwnt-8 proteins and antagonizes Xwnt-8 signaling in Xenopus embryos. Here we rep
The National Academy of Sciences of the USA.
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4. Evidence that the cysteine-rich domain of Drosophila Frizzled family receptors is dispensable for transducing Wingless
Members of the Frizzled family of serpentine transmembrane receptors are required to transduce Wingless/Int (Wnt) signals and contain in their N-terminal regions a conserved Wnt-binding cysteine-rich domain (CRD). Each CRD has specific affinities for particular Wnts, and it is generally believed that signal transduction depends on the strength of this intera
National Academy of Sciences.
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5. Purification and molecular cloning of a secreted, Frizzled-related antagonist of Wnt action
Frizzled polypeptides are integral membrane proteins that recently were shown to function as receptors for Wnt signaling molecules. Here, we report the identification of a novel, secreted 36-kDa protein that contains a region homologous to a putative Wnt-binding domain of Frizzleds. This protein, called Frizzled-related protein (FRP), was first identified as
The National Academy of Sciences of the USA.
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6. Biochemical characterization of Wnt-Frizzled interactions using a soluble, biologically active vertebrate Wnt protein
Biochemical studies of Wnt signaling have been hampered by difficulties in obtaining large quantities of soluble, biologically active Wnt proteins. In this paper, we report the production in Drosophila S2 cells of biologically active Xenopus Wnt8 (XWnt8). Epitope- or alkaline phosphatase-tagged XWnt8 proteins are secreted by concentrated S2 cells in a form t
The National Academy of Sciences.
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7. An antiproliferative factor from interstitial cystitis patients is a frizzled 8 protein-related sialoglycopeptide
Approximately 1 million people in the United States suffer from interstitial cystitis, a chronic painful urinary bladder disorder characterized by thinning or ulceration of the bladder epithelial lining; its etiology is unknown. We have identified a glycosylated frizzled-related peptide inhibitor of cell proliferation that is secreted specifically by bladder
National Academy of Sciences.
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8. Regulation of eye development by frizzled signaling in Xenopus
Eye development in both invertebrates and vertebrates is regulated by a network of highly conserved transcription factors. However, it is not known what controls the expression of these factors to regulate early eye formation and whether transmembrane signaling events are involved. Here we establish a role for signaling via a member of the frizzled fami
The National Academy of Sciences.
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9. The C-terminal cytoplasmic Lys-Thr-X-X-X-Trp motif in frizzled receptors mediates Wnt/β-catenin signalling
Frizzled receptors are components of the Wnt signalling pathway, but how they activate the canonical Wnt/β-catenin pathway is not clear. Here we use three distinct vertebrate frizzled receptors (Xfz3, Xfz4 and Xfz7) and describe whether and how their C-terminal cytoplasmic regions transduce the Wnt/β-catenin signal. We show that Xfz3 activates this pathway
Oxford University Press.
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10. Sequence requirement and subtype specificity in the high-affinity interaction between human frizzled and dishevelled proteins
Members of the Wnt family of lipoglycoproteins initiate signaling by binding to Frizzled (Fz) receptors, and the signal is then relayed by Disheveled (Dvl). The Dvl PDZ domain is known to interact directly with a peptide derived from the KTXXXW motif of Fz7, which is conserved in all known Fz subtypes. We found that an extended region spanning the KTXXXW mot
Wiley Subscription Services.
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11. A novel frizzled gene identified in human esophageal carcinoma mediates APC/β-catenin signals
A novel member of the human frizzled (Fz) gene family was cloned and found to be specifically expressed in 3 of 13 well differentiated (23%), 13 of 20 moderately differentiated (62%), and 12 of 14 poorly differentiated (86%) squamous cell esophageal carcinomas compared with the adjacent uninvolved normal mucosa. The FzE3 cDNA encodes a protein of 574 amino a
The National Academy of Sciences.
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12. Discovery and Characterization of a Small Molecule Inhibitor of the PDZ Domain of Dishevelled*
Dishevelled (Dvl) is an essential protein in the Wnt signaling pathways; it uses its PDZ domain to transduce the Wnt signals from the membrane receptor Frizzled to downstream components. Here, we report identifying a drug-like small molecule compound through structure-based ligand screening and NMR spectroscopy and show the compound to interact at low microm
American Society for Biochemistry and Molecular Biology.