Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Roberta A. Parente"'
Publikováno v:
Biochemistry. 33:6721-6731
A kinetic model for pore-mediated and perturbation-mediated flip-flop is presented and used to characterize the mechanism of peptide-induced phospholipid flip-flop in bilayers. The model assumes that certain peptides can bind to and aggregate within
Publikováno v:
Biochemistry. 29:8713-8719
The solution properties and bilayer association of two synthetic 30 amino acid peptides, GALA and LAGA, have been investigated at pH 5 and 7.5. These peptides have the same amino acid composition and differ only in the positioning of glutamic acid an
Publikováno v:
Biochemistry. 29:8720-8728
The synthetic, amphipathic peptide GALA undergoes a pH-dependent conformational change and induces leakage of contents from large unilamellar phosphatidylcholine vesicles when in a helical conformation. The kinetics of this process have been investig
Autor:
Theodore F. Taraschi, Sol M. Gruner, Andrew S. Janoff, Keir C. Neuman, Sharma R. Minchey, Walter Perkins, Richard B. Dause, Roberta A. Parente
Publikováno v:
Science. 273:330-332
The development of artificial surfactants for the treatment of respiratory distress syndrome (RDS) requires lipid systems that can spread rapidly from solution to the air-water interface. Because hydration-repulsion forces stabilize liposomal bilayer
Autor:
Elias Fattal, Jan Wilschut, Shlomo Nir, Roberta A. Parente, Francis C. SzokaJr., Jose L. Nieva
Publikováno v:
Trafficking of Intracellular Membranes: ISBN: 9783642795497
The understanding of the interrelationships among dynamics, structure, and function of membrane-interacting peptide segments has been intensely studied during the last decade.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f44745ab067c25d2928a603b5875b08
https://doi.org/10.1007/978-3-642-79547-3_6
https://doi.org/10.1007/978-3-642-79547-3_6
Autor:
Joëlle De Meutter, Erik Goormaghtigh, Francis C. Szoka, Roberta A. Parente, Véronique Cabiaux, Jean Marie Ruysschaert
Publikováno v:
European journal of biochemistry. 195(2)
GALA, a synthetic, amphipathic 30-amino-acid peptide, based upon a Glu-Ala-Leu-Ala motive, was designed to mimic the behavior of viral fusion proteins. GALA is a water-soluble peptide with an aperiodic conformation at neutral pH, and becomes an amphi
Autor:
Roberta A. Parente, Barry R. Lentz
Publikováno v:
Biochemistry. 23:2353-2362
Large unilamellar vesicles (LUV) have been prepared by three procedures from several synthetic and natural phosphatidylcholines. Reverse-phase evaporation vesicles (REV) and fusion vesicles were prepared by established procedures. A published procedu
Publikováno v:
Journal of Biological Chemistry. 263:4724-4730
A synthetic, amphipathic 30-amino acid peptide with the major repeat unit Glu-Ala-Leu-Ala (GALA) was designed to mimic the behavior of the fusogenic sequences of viral fusion proteins. GALA is a water-soluble peptide with an aperiodic conformation at
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 812:493-502
Differential scanning calorimetry and freeze-fracture electron microscopy have been used to characterize the phase behavior and morphology of two types of unilamellar vesicles composed of synthetic phosphatidylcholines. The first type displayed an av
Publikováno v:
Biochemistry. 26:2964-2972
A 30-residue amphipathic peptide was designed to interact with uncharged bilayers in a pH-dependent fashion. This was achieved by a pH-induced random coil-alpha-helical transition, exposing a hydrophobic face in the peptide. The repeat unit of the pe