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Showing 31-43 of 43 results for "840034P" within Papers
Antti H Rantamäki et al.
Scientific reports, 9(1), 18349-18349 (2019-12-05)
Understanding the toxicity of ionic liquids (ILs) is crucial in the search of greener chemicals. By comparing in vivo toxicity and in vitro interactions determined between compounds and biomimetic lipid membranes, more detailed toxicity vs. structure relation can be obtained.
Carina Drechsler et al.
Biophysical journal, 115(8), 1509-1517 (2018-09-30)
Lipid asymmetries between the outer and inner leaflet of the lipid bilayer exist in nearly all biological membranes. Although living cells spend great effort to adjust and maintain these asymmetries, little is known about the biophysical phenomena within asymmetric membranes
Guangtao Li et al.
Proceedings of the National Academy of Sciences of the United States of America, 113(49), 14025-14030 (2016-11-23)
Our understanding of membranes and membrane lipid function has lagged far behind that of nucleic acids and proteins, largely because it is difficult to manipulate cellular membrane lipid composition. To help solve this problem, we show that methyl-α-cyclodextrin (MαCD)-catalyzed lipid
Adsorption of O-phospho-L-serine and L-serine onto poorly crystalline apatite
Benaziz L, et al.
Journal of Colloid and Interface Science, 238(1), 48-53 (2001)
Phosphatidylserine and the human brain
Glade MJ and Smith K
Nutrition, 31(6), 781-786 (2015)
Karishma Bhasne et al.
The journal of physical chemistry. B, 124(5), 708-717 (2020-01-10)
α-Synuclein is an intrinsically disordered protein that adopts an α-helical structure upon binding to the negatively charged lipid membrane. Binding-induced conformational change of α-synuclein plays a crucial role in the regulation of synaptic plasticity. In this work, we utilized the
Vanessa T R Kiraly et al.
International journal of biological macromolecules, 146, 320-331 (2020-01-04)
The Hsp70 family of heat shock proteins plays a critical function in maintaining cellular homeostasis within various subcellular compartments. The human mitochondrial Hsp70 (HSPA9) has been associated with cellular death, senescence, cancer and neurodegenerative diseases, which is the rational for
Examination of the Interaction between a Membrane Active Peptide and Artificial Bilayers by Dual Polarisation Interferometry
Payne JAE, et al.
Bio-protocol, 7(1), e2087-e2087 (2017)
Dorotea Fracchiolla et al.
eLife, 5 (2016-11-24)
Selective autophagy is mediated by cargo receptors that link the cargo to the isolation membrane via interactions with Atg8 proteins. Atg8 proteins are localized to the membrane in an ubiquitin-like conjugation reaction, but how this conjugation is coupled to the
R J Perrin et al.
The Journal of biological chemistry, 275(44), 34393-34398 (2000-08-23)
alpha-Synuclein has been centrally implicated in neurodegenerative disease, and a normal function in developmental synaptic plasticity has been suggested by studies in songbirds. A variety of observations suggest the protein partitions between membrane and cytosol, a behavior apparently conferred by
Josef Melcr et al.
Journal of chemical theory and computation, 16(1), 738-748 (2019-11-26)
Phosphatidylserine (PS) lipids are important signaling molecules and the most common negatively charged lipids in eukaryotic membranes. The signaling can be often regulated by calcium, but its interactions with PS headgroups are not fully understood. Classical molecular dynamics (MD) simulations
Yousef Nademi et al.
Nanoscale, 12(2), 1032-1045 (2019-12-18)
Cell entry of polymeric nanoparticles (NPs) bearing polynucleotides is an important stage for successful gene delivery. In this work, we addressed the influence of cell membrane lipids on the integrity and configurational changes of NPs composed of short interfering ribonucleic
John M Harrington et al.
The Journal of biological chemistry, 289(36), 24811-24820 (2014-07-20)
Haptoglobin-related protein (Hpr) is a component of a minor subspecies of high density lipoproteins (HDL) that function in innate immunity. Here we show that assembly of Hpr into HDL is mediated by its retained N-terminal signal peptide, an unusual feature
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