منابع مشابه
RSPO1 (R-spondin homolog (Xenopus laevis))
mRNA about 2.5 kb, 263 residues in full-length translated protein, which contains an N-terminal signal peptide, followed by two cysteine-rich furin-like domains, one thrombospondin type 1 domain (TSP1 domain) and a putative C-terminal nuclear localization signal domain. Three alternatively spliced isoforms have been identified: one lacking the signal peptide encoded by exon 4, one lacking the t...
متن کاملMIER1 (mesoderm induction early response 1 homolog (Xenopus laevis))
A. Schematic illustrating the exon-intron organization of the human MIER1 gene Exons are shown as red bars/vertical lines and introns as horizontal lines; exon numbers are indicated below each schematic. The light red bar indicates the facultative intron 16 and the position of the alpha and beta carboxy-terminal coding regions are indicated. Note that the beta coding region is located within th...
متن کاملR-Spondin 1 Regulates WNT Signaling Pathway by Antagonizing the Function of Dickkopf Homolog 1
Yang Wang1, Bingqiang Zhang2 and Wei Zou2,3* 1Department of Medical Microbiology and Immunology, Creighton University School of Medicine, Omaha, USA 2Expert Work station, Restore Life Science Co, Qingdao, China 3College of Life Science, Liaoning Normal University, Dalian, PR China *Corresponding author: Wei Zou, Expert Work station, Restore Life Science Co, Qingdao, College of Life Science, Lia...
متن کاملStructures of Wnt-Antagonist ZNRF3 and Its Complex with R-Spondin 1 and Implications for Signaling
Zinc RING finger 3 (ZNRF3) and its homolog RING finger 43 (RNF43) antagonize Wnt signaling in adult stem cells by ubiquitinating Frizzled receptors (FZD), which leads to endocytosis of the Wnt receptor. Conversely, binding of ZNRF3/RNF43 to LGR4-6 - R-spondin blocks Frizzled ubiquitination and enhances Wnt signaling. Here, we present crystal structures of the ZNRF3 ectodomain and its complex wi...
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ژورنال
عنوان ژورنال: Atlas of Genetics and Cytogenetics in Oncology and Haematology
سال: 2011
ISSN: 1768-3262
DOI: 10.4267/2042/44472