A
Astrid Gräslund
Researcher at Stockholm University
Publications - 295
Citations - 13965
Astrid Gräslund is an academic researcher from Stockholm University. The author has contributed to research in topics: Ribonucleotide reductase & Peptide. The author has an hindex of 63, co-authored 283 publications receiving 12744 citations. Previous affiliations of Astrid Gräslund include Umeå University.
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Cell Penetrating Peptides
Mattias Hällbrink,Margus Pooga,Madis Tallin Unive Metsis,Priit Kogerman,Andreas Valkna,Anne Meikas,Maria Lindgren,Astrid Gräslund,Göran Eriksson,Claes Göran Östensson,Metka V. Budihna,Matjaz Zorko,Anna Elmquist,Ursel Soomets,Pontus Lundberg,Peter Järver,Külliki Saar,Samir El-Andaloussi,Kalle Kilk,Ülo Langel +19 more
TL;DR: In this paper, a method for predicting or designing, detecting, and/or verifying a novel cell-penetrating peptide (CPP) was proposed and used for treating and preventing a medical condition.
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.
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A library of IR bands of nucleic acids in solution.
TL;DR: This review presents a compilation and discussion of infrared (IR) bands characteristic of nucleic acids in various conformations, aimed at highlighting specific features that are useful for following major changes in nucleic acid structures.
Journal ArticleDOI
Efficient Intracellular Delivery of Nucleic Acid Pharmaceuticals Using Cell-Penetrating Peptides
Ikuhiko Nakase,Hidetaka Akita,Kentaro Kogure,Astrid Gräslund,Ülo Langel,Hideyoshi Harashima,Shiroh Futaki +6 more
TL;DR: The R8-MEND showed high transfection efficiency comparable to that of adenovirus in non-dividing cells, and understanding the cellular uptake mechanisms of CPPs will further improve CPP-mediated NAP delivery.
Journal ArticleDOI
High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β-peptide
TL;DR: Fluorescence experiments show that zinc shares a common binding site with copper and that the metals have similar affinities for amyloid β‐peptide, and metal‐induced structure of the peptide counteracts aggregation at low metal ion concentrations.