M
Maria Micha-Screttas
Researcher at Princeton University
Publications - 63
Citations - 1236
Maria Micha-Screttas is an academic researcher from Princeton University. The author has contributed to research in topics: Metalation & Alkyl. The author has an hindex of 16, co-authored 62 publications receiving 1175 citations.
Papers
More filters
Journal ArticleDOI
A comparative study on structure–function relations of mixed-linkage (1→3), (1→4) linear β-d-glucans
TL;DR: In this article, the effects of fine structure and molecular size on the rheological properties of six mixed-linkage (1→3), ( 1→4)-β-d -glucans (β-glucan) in the solution and gel state were studied.
Journal ArticleDOI
Hydrolithiation of .alpha.-olefins by a regiospecific two-step process. Transformation of alkyl phenyl sulfides to alkyllithium reagents
Journal ArticleDOI
Markownikoff two-step hydrolithiation of .alpha.-olefins. Transformation of secondary and tertiary alkyl phenyl sulfides to the relevant alkyllithium reagents
Journal ArticleDOI
Dendrimers as biopharmaceuticals: synthesis and properties.
Carolina Villalonga-Barber,Maria Micha-Screttas,Barry R. Steele,Aristidis Georgopoulos,Costas Demetzos +4 more
TL;DR: The way in which the size, chemical constitution and physicochemical properties of dendrimers used for drug delivery may affect pharmacodynamic and pharmacokinetic parameters which are important considerations for drug bioavailability is illustrated.
Journal ArticleDOI
Engineered chimeric enzymes as tools for drug discovery: generating reliable bacterial screens for the detection, discovery, and assessment of estrogen receptor modulators.
Georgios Skretas,Aggeliki K. Meligova,Carolina Villalonga-Barber,Dimitra J. Mitsiou,Michael N. Alexis,Maria Micha-Screttas,B. R. Steele,Constantinos G. Screttas,David W. Wood +8 more
TL;DR: Strong evidence is presented here that the ability of the sensor to detect ligand binding and recognize pharmacologically critical properties arises from allosteric communication between the artificially combined protein domains, where different ligand-induced conformational changes in the receptor are transmitted to the catalytic domain and translated to distinct levels of enzyme efficiency.