ěyvind Halskau
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Vitellogenin recognizes cell damage through membrane binding and shields living cells from reactive oxygen species
H Havukainen, D MŘnch, A Baumann, S Zhong, ě Halskau, ...
Journal of Biological Chemistry 288 (39), 28369-28381, 2013
Adsorption behavior of acidic and basic proteins onto citrate-coated Au surfaces correlated to their native fold, stability, and pI
WR Glomm, ě Halskau, AMD Hanneseth, S Volden
The Journal of Physical Chemistry B 111 (51), 14329-14345, 2007
The membrane-bound conformation of α-lactalbumin studied by NMR-monitored 1H exchange
ě Halskau, N┼ Fr°ystein, A Muga, A Martınez
Journal of molecular biology 321 (1), 99-110, 2002
HAMLET interacts with lipid membranes and perturbs their structure and integrity
AK Mossberg, M Puchades, ě Halskau, A Baumann, I Lanekoff, Y Chao, ...
PloS one 5 (2), e9384, 2010
The interaction of peripheral proteins and membranes studied with α-lactalbumin and phospholipid bilayers of various compositions
AV Agas°ster, ě Halskau, E Fuglebakk, NA Fr°ystein, A Muga, ...
Journal of Biological Chemistry 278 (24), 21790-21797, 2003
Large-scale modulation of thermodynamic protein folding barriers linked to electrostatics
ě Halskau Jr, R Perez-Jimenez, B Ibarra-Molero, J Underhaug, V Mu˝oz, ...
Proceedings of the National Academy of Sciences 105 (25), 8625-8630, 2008
Amino acid contacts in proteins adapted to different temperatures: hydrophobic interactions and surface charges play a key role
G SŠlensminde, ě Halskau, I Jonassen
Extremophiles 13, 11-20, 2009
Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase, and negatively charged membranes
ě Halskau, M Ying, A Baumann, R Kleppe, D Rodriguez-Larrea, B Almňs, ...
Journal of Biological Chemistry 284 (47), 32758-32769, 2009
Linking new paradigms in protein chemistry to reversible membrane-protein interactions
O Halskau, A Muga, A MartÝnez
Current Protein and Peptide Science 10 (4), 339-359, 2009
Conformational flexibility of α-lactalbumin related to its membrane binding capacity
ě Halskau, J Underhaug, N┼ Fr°ystein, A MartÝnez
Journal of molecular biology 349 (5), 1072-1086, 2005
Same System− Different Results: The Importance of Protein-Introduction Protocols in Langmuir-Monolayer Studies of Lipid-Protein Interactions
WR Glomm, S Volden, ě Halskau Jr, MHG Ese
Analytical chemistry 81 (8), 3042-3050, 2009
HIV-1 p6—A structured to flexible multifunctional membrane-interacting protein
SMě Solbak, TR Reksten, F Hahn, V Wray, P Henklein, P Henklein, ...
Biochimica et Biophysica Acta (BBA)-Biomembranes 1828 (2), 816-823, 2013
Deconstructing honeybee vitellogenin: novel 40 kDa fragment assigned to its N terminus
H Havukainen, ě Halskau, L Skjaerven, B Smedal, GV Amdam
Journal of Experimental Biology 214 (4), 582-592, 2011
Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins
G SŠlensminde, ě Halskau, R Helland, NP Willassen, I Jonassen
Extremophiles 11, 585-596, 2007
α-Lactalbumin binding and membrane integrity—effect of charge and degree of unsaturation of glycerophospholipids
I R°dland, ě Halskau, A MartÝnez, H Holmsen
Biochimica et Biophysica Acta (BBA)-Biomembranes 1717 (1), 11-20, 2005
The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes
┼A Skjevik, M Mileni, A Baumann, ě Halskau, K Teigen, RC Stevens, ...
Journal of molecular biology 426 (1), 150-168, 2014
HAMLET forms annular oligomers when deposited with phospholipid monolayers
A Baumann, AU Gjerde, M Ying, C Svanborg, H Holmsen, WR Glomm, ...
Journal of molecular biology 418 (1-2), 90-102, 2012
A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation
H Havukainen, J Underhaug, F Wolschin, G Amdam, ě Halskau
Journal of Experimental Biology 215 (11), 1837-1846, 2012
Social pleiotropy and the molecular evolution of honey bee vitellogenin
H Havukainen, ě Halskau, GV Amdam
Molecular ecology 20 (24), 5111-5113, 2011
Tunable photophysical properties, conformation and function of nanosized protein–gold constructs
SM Lystvet, S Volden, G Singh, M Yasuda, ě Halskau, WR Glomm
RSC advances 3 (2), 482-495, 2013
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