モエシン (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "モエシン" in Japanese language version.

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doi.org

“Moesin: a member of the protein 4.1-talin-ezrin family of proteins”. Proc. Natl. Acad. Sci. U.S.A. 88 (19): 8297-301. (Oct 1991). doi:10.1073/pnas.88.19.8297. PMC 52495. PMID 1924289.
“Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts”. Exp. Cell Res. 219 (1): 180-96. (Sep 1995). doi:10.1006/excr.1995.1218. PMID 7628534.
“Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2”. J. Cell Biol. 140 (4): 885-95. (Feb 1998). doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040.
“Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization”. J. Cell Biol. 138 (6): 1409-23. (Sep 1997). doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994.
“A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting”. J. Biol. Chem. 277 (12): 10400-9. (Mar 2002). doi:10.1074/jbc.M110694200. PMID 11784723.
“The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain”. Biochem. Biophys. Res. Commun. 289 (2): 382-8. (Nov 2001). doi:10.1006/bbrc.2001.5982. PMID 11716484.
“Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes”. J. Cell Biol. 157 (7): 1233-45. (Jun 2002). doi:10.1083/jcb.200112126. PMC 2173557. PMID 12082081.
“Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy”. J. Biol. Chem. 280 (12): 11641-7. (Mar 2005). doi:10.1074/jbc.M411781200. PMID 15659383.
“Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site”. Mol. Biol. Cell 6 (8): 1061-75. (Aug 1995). doi:10.1091/mbc.6.8.1061. PMC 301263. PMID 7579708.
“Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins”. Proc. Natl. Acad. Sci. U.S.A. 90 (22): 10846-50. (Nov 1993). doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180.

ensembl.org

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000147065 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000031207 - Ensembl, May 2017

nih.gov

pubmed.ncbi.nlm.nih.gov

“Moesin: a member of the protein 4.1-talin-ezrin family of proteins”. Proc. Natl. Acad. Sci. U.S.A. 88 (19): 8297-301. (Oct 1991). doi:10.1073/pnas.88.19.8297. PMC 52495. PMID 1924289.
“Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts”. Exp. Cell Res. 219 (1): 180-96. (Sep 1995). doi:10.1006/excr.1995.1218. PMID 7628534.
“CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts”. Blood 91 (12): 4632-44. (Jun 1998). PMID 9616160.
“Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2”. J. Cell Biol. 140 (4): 885-95. (Feb 1998). doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040.
“Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization”. J. Cell Biol. 138 (6): 1409-23. (Sep 1997). doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994.
“A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting”. J. Biol. Chem. 277 (12): 10400-9. (Mar 2002). doi:10.1074/jbc.M110694200. PMID 11784723.
“The NADPH oxidase components p47(phox) and p40(phox) bind to moesin through their PX domain”. Biochem. Biophys. Res. Commun. 289 (2): 382-8. (Nov 2001). doi:10.1006/bbrc.2001.5982. PMID 11716484.
“Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes”. J. Cell Biol. 157 (7): 1233-45. (Jun 2002). doi:10.1083/jcb.200112126. PMC 2173557. PMID 12082081.
“Cytoskeleton-mediated death receptor and ligand concentration in lipid rafts forms apoptosis-promoting clusters in cancer chemotherapy”. J. Biol. Chem. 280 (12): 11641-7. (Mar 2005). doi:10.1074/jbc.M411781200. PMID 15659383.
“Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site”. Mol. Biol. Cell 6 (8): 1061-75. (Aug 1995). doi:10.1091/mbc.6.8.1061. PMC 301263. PMID 7579708.
“Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins”. Proc. Natl. Acad. Sci. U.S.A. 90 (22): 10846-50. (Nov 1993). doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

wikipedia.org

en.wikipedia.org

GRCh38: Ensembl release 89: ENSG00000147065 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000031207 - Ensembl, May 2017