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関連文献

“ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction”. Curr. Opin. Cell Biol. 9 (1):  70-5. (1997). doi:10.1016/S0955-0674(97)80154-8. PMID 9013673.
“The ezrin protein family: membrane-cytoskeleton interactions and disease associations”. Curr. Opin. Cell Biol. 9 (5):  659-66. (1997). doi:10.1016/S0955-0674(97)80119-6. PMID 9330869.
“Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death”. Cell Death Differ. 12 Suppl 1:  932-41. (2005). doi:10.1038/sj.cdd.4401582. PMID 15818415.
“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. (1995). doi:10.1091/mbc.6.8.1061. PMC 301263. PMID 7579708. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC301263/.
“Differential expression of the microspike-associated protein moesin in human tissues”. Eur. J. Cell Biol. 67 (3):  189-98. (1995). PMID 7588875.
“Physical association of moesin and CD46 as a receptor complex for measles virus”. J. Virol. 69 (4):  2248-56. (1995). PMC 188894. PMID 7884872. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC188894/.
“Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN)”. Genomics 19 (2):  326-33. (1994). doi:10.1006/geno.1994.1065. PMID 8188263.
“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. (1993). doi:10.1073/pnas.90.22.10846. PMC 47875. PMID 8248180. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC47875/.
“Moesin: a cell membrane protein linked with susceptibility to measles virus infection” (Submitted manuscript). Virology 198 (1):  265-74. (1994). doi:10.1006/viro.1994.1029. PMID 8259662. https://opus.bibliothek.uni-wuerzburg.de/frontdoor/index/index/docId/5873.
“Phosphorylation of threonine 558 in the carboxyl-terminal actin-binding domain of moesin by thrombin activation of human platelets”. J. Biol. Chem. 270 (52):  31377-85. (1995). doi:10.1074/jbc.270.52.31377. PMID 8537411.
“Cytoskeletal proteins inside human immunodeficiency virus type 1 virions”. J. Virol. 70 (11):  7734-43. (1996). PMC 190843. PMID 8892894. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC190843/.
“Specific binding of HIV-1 envelope protein gp120 to the structural membrane proteins ezrin and moesin”. Virus Res. 49 (2):  215-23. (1997). doi:10.1016/S0168-1702(97)00039-7. PMID 9213396.
“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. (1997). doi:10.1083/jcb.138.6.1409. PMC 2132557. PMID 9298994. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132557/.
“Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family”. J. Cell Biol. 139 (1):  169-79. (1997). doi:10.1083/jcb.139.1.169. PMC 2139813. PMID 9314537. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2139813/.
“NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins”. J. Biol. Chem. 273 (3):  1273-6. (1998). doi:10.1074/jbc.273.3.1273. PMID 9430655.
“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. (1998). doi:10.1083/jcb.140.4.885. PMC 2141743. PMID 9472040. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2141743/.