scispace - formally typeset
A

Ana Estévez-Braun

Researcher at University of La Laguna

Publications -  135
Citations -  2649

Ana Estévez-Braun is an academic researcher from University of La Laguna. The author has contributed to research in topics: Maytenus & Knoevenagel condensation. The author has an hindex of 25, co-authored 127 publications receiving 2323 citations. Previous affiliations of Ana Estévez-Braun include University of Las Palmas de Gran Canaria & Hospital Universitario de Canarias.

Papers
More filters
Journal ArticleDOI

Recent Studies on Natural Products as Anticancer Agents

TL;DR: This review deals with new natural molecules liable to become anticancer drugs, as well as recent specific strategies for a selective treatment of cancer.
Journal ArticleDOI

Antiplasmodial Activity of Naphthoquinones Related to Lapachol and β‐Lapachone

TL;DR: In this paper, the in vitro antiplasmodial activity of 26 naphthoquinone derivatives related to the natural lapachol and beta-lapachone was tested.
Journal ArticleDOI

Synthesis and pharmacophore modeling of naphthoquinone derivatives with cytotoxic activity in human promyelocytic leukemia HL-60 cell line.

TL;DR: The computational models have facilitated the identification of structural elements of the ligands that are key for antitumoral properties and provide a valuable tool in designing new and more potent cytotoxic analogues.
Journal ArticleDOI

Inhibitory effects of lapachol derivatives on epstein-barr virus activation.

TL;DR: Ten of the naphthoquinone lapachol derivatives tested for their inhibitory effects on Epstein-Barr virus early antigen activation induced by 12-O-tetradecanoylphorbol-13-acetate are reported for the first time, their structures being thoroughly determined by spectroscopic methods.
Journal ArticleDOI

Design and synthesis of a novel series of pyranonaphthoquinones as topoisomerase II catalytic inhibitors.

TL;DR: A new set of pyranonaphthoquinones derivatives is designed and synthesized and it is found that six of them act as catalytic inhibitors of the enzyme in vitro, which strongly preclude the enzyme from decatenating or relaxing suitable substrates.