F
Fatemeh Madani
Researcher at Stockholm University
Publications - 18
Citations - 1443
Fatemeh Madani is an academic researcher from Stockholm University. The author has contributed to research in topics: Cell-penetrating peptide & Endosome. The author has an hindex of 10, co-authored 15 publications receiving 1272 citations. Previous affiliations of Fatemeh Madani include Karolinska University Hospital & Karolinska Institutet.
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Journal ArticleDOI
Mechanisms of Cellular Uptake of Cell-Penetrating Peptides
TL;DR: A review focused on uptake mechanisms used by CPPs for membrane translocation and certain experimental factors that affect the mechanism(s) are given.
Journal ArticleDOI
Cytosolic antibody delivery by lipid-sensitive endosomolytic peptide
Misao Akishiba,Toshihide Takeuchi,Yoshimasa Kawaguchi,Kentarou Sakamoto,Hao-Hsin Yu,Ikuhiko Nakase,Ikuhiko Nakase,Tomoka Takatani-Nakase,Fatemeh Madani,Astrid Gräslund,Shiroh Futaki +10 more
TL;DR: This work reports an approach to deliver proteins, which include antibodies, into cells by using endosomolytic peptides derived from the cationic and membrane-lytic spider venom peptide M-lycotoxin and demonstrates the L17E-mediated cytosolic delivery of exosome-encapsulated proteins.
Journal ArticleDOI
Elucidating cell-penetrating peptide mechanisms of action for membrane interaction, cellular uptake, and translocation utilizing the hydrophobic counter-anion pyrenebutyrate.
Peter Guterstam,Fatemeh Madani,Hisaaki Hirose,Toshihide Takeuchi,Shiroh Futaki,Samir El Andaloussi,Astrid Gräslund,Ülo Langel +7 more
TL;DR: The pathway for cellular uptake of oligo arginine is dominated by direct membrane translocation, whereas the pathway for oligoarginine-mediated oligonucleotide translocation isdominated by endocytosis.
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Hairpin structure of a biarsenical–tetracysteine motif determined by NMR spectroscopy
TL;DR: The structure of a 12 amino acid peptide FLNCCPGCCMEP bound to the fluorophore ReAsH based on resorufin shows that the backbone structure of the peptide is fairly well defined, with a hairpinlike turn, similar to a type-II beta-turn, formed by the central CPGC segment.
Journal ArticleDOI
Modeling the endosomal escape of cell-penetrating peptides using a transmembrane pH gradient
Fatemeh Madani,Rania Abdo,Staffan Lindberg,Hisaaki Hirose,Shiroh Futaki,Ülo Langel,Astrid Gräslund +6 more
TL;DR: The results show that the light-induced pH gradient induced by BR facilitates vesicle membrane translocation, particularly for the intermediately hydrophobic CPPs, and much less for hydrophilic C PPs.