LDL-receptor-related proteins in Wnt signal transduction
By K. Tamai, Mikhail V. Semenov, Y. Kato, Rebecca Spokony, Chunming Liu, Y. Katsuyama, Fred J Hess, J. Saint-jeannet, Xi He. Nature, 2000
1,422 citations recorded by the source corpus.
Subfields: Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/775c355f8bc120fc30e4d0f674a84a45566c45af
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Citations in the corpus
- Signalling in neural development: WNTS in the vertebrate nervous system: from patterning to neuronal connectivity (2005, background): “fcgi?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=16974">LRP6 — single-pass transmembrane proteins — is specifically required for signalling through the canonical pathwa”
- An LDL-receptor-related protein mediates Wnt signalling in mice (2000, background): “and by overexpression of LRP6 in Xenopus embryo”
- Wnt signaling in the intestinal epithelium: from endoderm to cancer. (2005, background): “Wnts activate responding cells by interacting with the seven-span transmembrane protein Frizzled (Fz) and the single-span transmembrane protein LRP (Bhanot et al. 1996; Pinson et al. 2000; Tamai et al. 2000; Wehrli et al. 2000).”
- Lrp5 controls bone formation by inhibiting serotonin synthesis in the duodenum: an entero-bone endocrine axis (2008, background): “Lrp5 is a member of the family of lipoprotein receptor related proteins (Lrps), a small group of single-pass transmembrane proteins (Tamai et al., 2000).”
- α4β1- and α6β1-integrins are functional receptors for midkine, a heparin-binding growth factor (2004, methodology): “The coding sequences of human β1-integrin (Argraves et al., 1987) and human α6-integrin (Tamura et al., 1990) were ligated into an expression vector pcDNA3.”
- Sclerostin Mediates Bone Response to Mechanical Unloading Through Antagonizing Wnt/β‐Catenin Signaling (2009, background): “(20) In addition, sclerostin protein expression was relatively restricted in bone postnatally, unlike Lrp5.”
- Secreted antagonists of the Wnt signalling pathway (2003, background): “…a member of the frizzled (Fz) family (there are 10 of these seven-transmembrane-span proteins in humans) and either one of two single-span transmembrane proteins, low-density-lipoprotein-receptorrelated proteins [LRP-5 and LRP-6 (Pinson et al., 2000; Tamai et al., 2000; Wehrli et al., 2000)] (Fig.”
- Mutations in LRP5 or FZD4 underlie the common familial exudative vitreoretinopathy locus on chromosome 11q. (2004, background): “Consistent with this notion, LRP5 has been shown to interact with different Wnt/frizzled complexes (Tamai et al. 2000; Semënov et al. 2001; Kato et al. 2002; Caricasole et al. 2003), although the binding sites have not been determined.”
- Nucleo-cytoplasmic distribution of β-catenin is regulated by retention (2006, methodology): “, 1996) and LRP5/6 (Pinson et al., 2000; Tamai et al., 2000), this destruction complex is inactivated, which leads to accumulation of -catenin in the cytoplasm and its entry into the nucleus.”