K. Oglęcka

N-terminal peptides from unprocessed prion proteins enter cells by macropinocytosis.

Ű. Langel, Kamila Oglęcka, A. Gräslund, 2006, Biochemical and biophysical research communications.

Dual functions of the human antimicrobial peptide LL-37-target membrane perturbation and host cell cargo delivery.

B. Nordén, Kamila Oglęcka, A. Gräslund, 2010, Biochimica et biophysica acta.

Transient pearling and vesiculation of membrane tubes under osmotic gradients.

A. Parikh, R. Kraut, Kamila Oglęcka, 2013, Faraday discussions.

Weak Glycolipid Binding of a Microdomain-Tracer Peptide Correlates with Aggregation and Slow Diffusion on Cell Membranes

R. Kraut, T. Wohland, Kamila Oglęcka, 2012, PloS one.

Membrane binding of pH-sensitive influenza fusion peptides. positioning, configuration, and induced leakage in a lipid vesicle model.

Astrid Gräslund, Per Lincoln, B. Nordén, 2007, Biochemistry.

Membrane perturbation effects of peptides derived from the N-termini of unprocessed prion proteins.

A. Pramanik, Kamila Oglęcka, A. Gräslund, 2005, Biochimica et biophysica acta.

NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles.

E. Papadopoulos, H. Dyson, P. Wright, 2006, Biochemistry.

Relevance of the N-terminal NLS-like sequence of the prion protein for membrane perturbation effects.

Ű. Langel, Kamila Oglęcka, A. Gräslund, 2008, Biochimica et biophysica acta.