scispace - formally typeset
U

Ursula Rothlisberger

Researcher at École Polytechnique Fédérale de Lausanne

Publications -  338
Citations -  24706

Ursula Rothlisberger is an academic researcher from École Polytechnique Fédérale de Lausanne. The author has contributed to research in topics: Density functional theory & Excited state. The author has an hindex of 68, co-authored 322 publications receiving 20418 citations. Previous affiliations of Ursula Rothlisberger include Curtin University & University of Milan.

Papers
More filters
Journal ArticleDOI

Acid-Induced Degradation of Phosphorescent Dopants for OLEDs and Its Application to the Synthesis of Tris-heteroleptic Iridium(III) Bis-cyclometalated Complexes

TL;DR: This work reproduced the loss of picolinate and acetylacetonate ancillary ligands in solution by the addition of Brønsted or Lewis acids and advantageously used this degradation reaction for the efficient synthesis of tris-heteroleptic cyclometalated iridium(III) complexes.
Journal ArticleDOI

Influence of Hydrogen-Bonding Substituents on the Cytotoxicity of RAPTA Compounds

TL;DR: The reactivity of the functionalized RAPTA compounds with a 14-mer oligonucleotide (established by mass spectrometry) has been rationalized by DFT calculations, which indicate that environmental factors are important.
Journal ArticleDOI

Molecular Engineering of a Fluorene Donor for Dye-Sensitized Solar Cells

TL;DR: In this paper, the electronic and steric properties of a fluorene donor are engineered to meet all the requirements of D-pi-A. sensitized solar cells, including the ability to control the electron-transfer processes that ensure efficient dye-regeneration and prevent undesired electron recombination.
Journal ArticleDOI

Drug resistance in HIV‐1 protease: Flexibility‐assisted mechanism of compensatory mutations

TL;DR: The authors' calculations indicate that the dynamical fluctuations of the mutated enzyme differ from those in the wild type, and it is anticipated that this “flexibility‐assisted” mechanism might be effective in the vast majority of compensatory mutations, which do not change the electrostatic properties of the enzyme.