Effie C. Tsilibary, MD PhD
Former Member of the Brain Sciences CenterBrain Sciences Center (BSC)
Publications
Pages:
1August 2021 through August 2016 •
2July 2016 through December 2007 •
3November 2007 through December 1993 •
4May 1993 through June 1985 •
5November 1983 through May 1977An Apolipoprotein EApolipoprotein E (ApoE)a plasma lipoprotein discovered in 1973 (Shore and Shore 1973). It binds low-density lipoprotein receptors, thereby facilitating cellular lipoprotein exchange and metabolism. The human apoE polypeptide consists of 299 amino acids and comprises three polymorphisms resulting from single amino acid substitutions. Three isoforms (E4, E3, and E2) are the result of cysteine^aEUR"arginine interchanges at two sites, namely residues 112 and 158; however, other genetic variants have been described. These three isoforms, each differentially affecting protein function, result in six phenotypes: three homozygotes (E4/4, E3/3, E2/2) and three heterozygotes (E4/3, E4/2, E3/2). With respect to the number of cysteine residues per mole, E2/2 contains 4, E3/2 contains 3, E4/2 and E3/3 each contain 2, E4/3 contains 1, and E4/4 contains 0. The number of cysteine residues per mole (CysR/mole) provides a numerical, biochemical scale in lieu of the genotype-based categories.4 fragment affects matrix metalloproteinase 9, tissue inhibitor of metalloproteinase 1 and cytokine levels in brain cell lines Neuroscience (2012, May) Dafnis I, Tzinia AK, Tsilibary EC, Zannis VI, & Chroni A Rapid magnetic heating treatment by highly charged maghemite nanoparticles on Wistar rats exocranial glioma tumors at microliter volume Biomicrofuidics (2010, June) Rabias I, Tsitrouli D, Karakosta E, Kehagias T, Diamantopoulos G, Fardis M, Stamopoulos D, Maris TG, Falaras P, Zouridakis N, Diamantis N, Panayotou G, Verganelakis DA, Drossopoulou GI, Tsilibary EC, & Papavassiliou G An ApoEApolipoprotein E (ApoE)a plasma lipoprotein discovered in 1973 (Shore and Shore 1973). It binds low-density lipoprotein receptors, thereby facilitating cellular lipoprotein exchange and metabolism. The human apoE polypeptide consists of 299 amino acids and comprises three polymorphisms resulting from single amino acid substitutions. Three isoforms (E4, E3, and E2) are the result of cysteine^aEUR"arginine interchanges at two sites, namely residues 112 and 158; however, other genetic variants have been described. These three isoforms, each differentially affecting protein function, result in six phenotypes: three homozygotes (E4/4, E3/3, E2/2) and three heterozygotes (E4/3, E4/2, E3/2). With respect to the number of cysteine residues per mole, E2/2 contains 4, E3/2 contains 3, E4/2 and E3/3 each contain 2, E4/3 contains 1, and E4/4 contains 0. The number of cysteine residues per mole (CysR/mole) provides a numerical, biochemical scale in lieu of the genotype-based categories.4 fragment can promote intracellular accumulation of amyloid peptide beta 42 Journal of Neurochemistry (2010, April) Dafnis I, Stratikos E, Tzinia AK, Tsilibary EC, Zannis VI, & Chroni A