アネキシンV
関連文献

“Annexin A5 as a novel player in prevention of atherothrombosis in SLE and in the general population”. Annals of the New York Academy of Sciences 1108 (1):  96–103. (Jun 2007). doi:10.1196/annals.1422.011. PMID 17893975.
“Inhibition of protein kinase C by annexin V”. Biochemistry 31 (6):  1886–91. (Feb 1992). doi:10.1021/bi00121a043. PMID 1310621.
“Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins”. Journal of Molecular Biology 223 (3):  683–704. (Feb 1992). doi:10.1016/0022-2836(92)90984-R. PMID 1311770.
“Selective binding of anchorin CII (annexin V) to type II and X collagen and to chondrocalcin (C-propeptide of type II collagen). Implications for anchoring function between matrix vesicles and matrix proteins”. FEBS Letters 310 (2):  143–7. (Sep 1992). doi:10.1016/0014-5793(92)81316-E. PMID 1397263.
“Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin”. The Journal of Infection 24 (3):  317–20. (May 1992). doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
“Chromosomal localization of the human gene for annexin V (placental anticoagulant protein I) to 4q26----q28”. Cytogenetics and Cell Genetics 57 (4):  187–92. (1992). doi:10.1159/000133143. PMID 1683830.
“The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes”. The EMBO Journal 9 (12):  3867–74. (Dec 1990). doi:10.1002/j.1460-2075.1990.tb07605.x. PMC 552154. PMID 2147412. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC552154/.
“The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity”. FEBS Letters 275 (1–2):  15–21. (Nov 1990). doi:10.1016/0014-5793(90)81428-Q. PMID 2148156.
“Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein”. European Journal of Biochemistry 174 (4):  585–92. (Jul 1988). doi:10.1111/j.1432-1033.1988.tb14139.x. PMID 2455636.
“A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation”. The Biochemical Journal 263 (3):  929–35. (Nov 1989). doi:10.1042/bj2630929. PMC 1133519. PMID 2532007. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1133519/.
“Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein”. Proceedings of the National Academy of Sciences of the United States of America 84 (17):  6078–82. (Sep 1987). doi:10.1073/pnas.84.17.6078. PMC 299011. PMID 2957692. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC299011/.
“Human placental anticoagulant protein: isolation and characterization”. Biochemistry 26 (17):  5572–8. (Aug 1987). doi:10.1021/bi00391a053. PMID 2960376.
“Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein”. Journal of Biochemistry 102 (5):  1261–73. (Nov 1987). doi:10.1093/oxfordjournals.jbchem.a122165. PMID 2963810.
“Primary structure of human placental anticoagulant protein”. Biochemistry 26 (25):  8087–92. (Dec 1987). doi:10.1021/bi00399a011. PMID 2964863.
“Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein”. The Journal of Biological Chemistry 263 (17):  8037–43. (Jun 1988). doi:10.1016/S0021-9258(18)68438-8. PMID 2967291.
“Characterization of cDNA encoding human placental anticoagulant protein (PP4): homology with the lipocortin family”. Proceedings of the National Academy of Sciences of the United States of America 85 (11):  3708–12. (Jun 1988). doi:10.1073/pnas.85.11.3708. PMC 280287. PMID 2967495. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC280287/.
“Five distinct calcium and phospholipid binding proteins share homology with lipocortin I”. The Journal of Biological Chemistry 263 (22):  10799–811. (Aug 1988). doi:10.1016/S0021-9258(18)38041-4. PMID 2968983.
“Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor”. The Journal of Biological Chemistry 263 (35):  18657–63. (Dec 1988). doi:10.1016/S0021-9258(18)37335-6. PMID 2974032.
“Annexin V: the key to understanding ion selectivity and voltage regulation?”. Trends in Biochemical Sciences 19 (7):  272–6. (Jul 1994). doi:10.1016/0968-0004(94)90002-7. PMID 7519374.
“The gene encoding human annexin V has a TATA-less promoter with a high G+C content”. Gene 149 (2):  253–60. (Nov 1994). doi:10.1016/0378-1119(94)90157-0. PMID 7958998.