Results 61 to 70 of about 1,084,218 (302)
Reciprocal control of viral infection and phosphoinositide dynamics
FEBS Letters, EarlyView.Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley +1 more source
Journal of Lipid Research, 2000 We have identified a G-to-A transition in exon 3 of the APOC3 gene resulting in a novel Ala23Thr apolipoprotein (apo) C-III variant, associated with apoC-III deficiency in three unrelated Yucatan Indians.
Haiqun Liu +9 more
doaj +1 more source
Frontiers in Physiology, 2022 Lipids modulate the function of many ion channels, possibly through direct lipid-protein interactions. The recent outpouring of ion channel structures by cryo-EM has revealed many lipid binding sites.
Wayland W. L. Cheng +2 more
doaj +1 more source
, 2006 Using integral equation theory of liquids to a binary mixed fluid lipid membrane, we study the membrane-mediated interactions between the macroions and the redistribution of neutral and charged lipids due to binding macroions.
Ma, Yu-qiang, Shi, Xia-qing
core +1 more source
The N-Terminus of Apolipoprotein A-V Adopts a Helix-Bundle Molecular Architecture [PDF]
, 2008 Previous studies of recombinant full-length human apolipoprotein A-V (apoA-V) provided evidence of the presence of two independently folded structural domains.
Beckstead, J. A. +6 more
core +3 more sources
FEBS Letters, EarlyView.Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho +3 more
wiley +1 more source
Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E
Journal of Lipid Research, 1999 The N-terminal domain of human apolipoprotein E3 (apoE3) adopts an elongated, globular four helix bundle conformation in the lipid-free state. Upon lipid binding, the protein is thought to undergo a significant conformational change that is essential for
Carl A. Fisher, Robert O. Ryan
doaj +1 more source
Frontiers in Plant Science, 2020 The heterooctameric vesicle-tethering complex exocyst is important for plant development, growth, and immunity. Multiple paralogs exist for most subunits of this complex; especially the membrane-interacting subunit EXO70 underwent extensive amplification
Tamara Pečenková +16 more
doaj +1 more source
STAR Protocols, 2022 Summary: Here, we present a protocol to construct artificial lipid droplets to study the binding affinity of lipid droplet-associated proteins. We provide procedures to construct adiposomes and prepare recombinant lipid droplet-associated proteins.
Zelun Zhi +5 more
doaj +1 more source
Endoplasmic Reticulum Export of GPI-Anchored Proteins [PDF]
, 2019 Protein export from the endoplasmic reticulum (ER) is an essential process in all eukaryotes driven by the cytosolic coat complex COPII, which forms vesicles at ER exit sites for transport of correctly assembled secretory cargo to the Golgi apparatus ...
López Martín, Sergio +3 more
core +1 more source