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N. T. Moldogazieva
Researcher at I.M. Sechenov First Moscow State Medical University
Publications - 30
Citations - 941
N. T. Moldogazieva is an academic researcher from I.M. Sechenov First Moscow State Medical University. The author has contributed to research in topics: Alpha-fetoprotein & Oxidative stress. The author has an hindex of 9, co-authored 27 publications receiving 536 citations. Previous affiliations of N. T. Moldogazieva include Russian National Research Medical University.
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[Relationship between structure and function of alpha-fetoprotein: conformational status and biological activity].
TL;DR: This review summarizes data on structure and function of AFP with emphasis on human AFP, which is intensively investigated and describes and analyses data obtained, mainly, during the last few years on study of conformational states of alpha-fetoprotein and relationship between conformational changes of AFP and its biological activity.
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Competitive affinity chromatography of human alpha fetoprotein on immobilized diethylstilbestrol
TL;DR: The competitive variant of the affinity chromatography on immobilized diets makes it possible to raise human AFP preparation purity and yield by decreasing the competition between AFP, and not binding free steroid hormones, ad albumin for immobilized diethylstilbestrol.
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Conformational dynamics of human α-fetoprotein-derived heptapeptide LDSYQCT analogs
N. T. Moldogazieva,Alexander A Terentiev,A. N. Kazimirsky,M. Yu. Antonov,Konstantin V. Shaitan +4 more
TL;DR: Conformational dynamics of a biologically active fragment of α-fetoprotein, the heptapeptide LDSYQCT, and its analogs obtained by site-directed substitutions of amino acid residues were studied.
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Pregnancy-Specific β1-Glycoproteins: Combined Biomarker Roles, Structure/Function Relationships and Implications for Drug Design
TL;DR: PSG-derived peptides may be used as a rationale to design novel drugs that mimic SLiMs involved in protein-protein interactions to inhibit domain-motif binding and to block cell signaling, and/or exert immunomodulatory, anti-inflammatory and proangiogenic effects.
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Human EGF-derived direct and reverse short linear motifs: conformational dynamics insight into the receptor-binding residues.
N. T. Moldogazieva,Konstantin V. Shaitan,Mikhail Yu. Antonov,Innokenty M. Mokhosoev,O. V. Levtsova,Alexander A Terentiev +5 more
TL;DR: The 22-member linear modules composed of direct and reverse AFP14–20-like heptapeptide motifs linked by CxxGY/FxGx consensus motif within epidermal growth factor (EGF), growth factors of EGF family and numerous regulatory proteins containing EGF-like modules are revealed.