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Chemistry and Physics of Lipids|February 20, 2019
Nanodiscs bounded by styrene-maleic acid allow trans-cis isomerization of enclosed photoswitches of azobenzene labeled lipidsJ J Domínguez Pardo, C A van Walree, M R Egmond, et al.
Biochemistry|September 4, 1990
Tryptophan fluorescence study on the interaction of the signal peptide of the Escherichia coli outer membrane protein PhoE with model membranesJ A Killian, R C Keller, M Struyvé, et al.
Biochemistry|January 23, 1996
Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane alpha-helical peptides: importance of hydrophobic mismatch and proposed role of tryptophansJ A Killian, I Salemink, M R de Planque, et al.
Developmental Pharmacology and Therapeutics|January 1, 1989
Pharmacokinetics of alfentanil in newborn premature infants and older childrenP J Davis, A Killian, R L Stiller, et al.
BMC Genomics|February 15, 2018
FuSpot: a web-based tool for visual evaluation of fusion candidatesJackson A Killian, Taha M Topiwala, Alex R Pelletier, et al.
Biochimica Et Biophysica Acta|November 27, 1987
Solvent determined conformation of gramicidin affects the ability of the peptide to induce hexagonal HII phase formation in dioleoylphosphatidylcholine model membranesH Tournois, J A Killian, D W Urry, et al.
Biochemistry|July 2, 1998
Influence of lipid/peptide hydrophobic mismatch on the thickness of diacylphosphatidylcholine bilayers. A 2H NMR and ESR study using designed transmembrane alpha-helical peptides and gramicidin AM R de Planque, D V Greathouse, R E Koeppe, et al.
Biochemistry|March 15, 2000
Tryptophan-anchored transmembrane peptides promote formation of nonlamellar phases in phosphatidylethanolamine model membranes in a mismatch-dependent mannerP C van der Wel, T Pott, S Morein, et al.
Annals of Emergency Medicine|August 29, 2001
Soluble intercellular adhesion molecule-1 as a predictor of early adverse events in patients with chest pain compatible with myocardial ischemiaG S Hillis, C Terregino, P Taggart, et al.
Biochemistry|September 12, 1995
PhoE signal peptide inserts into micelles as a dynamic helix-break-helix structure, which is modulated by the environment. A two-dimensional 1H NMR studyV Chupin, J A Killian, J Breg, et al.
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