Results 91 to 100 of about 2,118,036 (319)
An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane
FEBS Letters, EarlyView.Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa +3 more
wiley +1 more source
Methods in MicroscopyCryo-electron microscopy (cryoEM) grid preparation is one of the bottlenecks in using cryoEM for macromolecular structure determination. Despite significant advancements in the development of blot-free instruments, their high cost limits their widespread
Valimehr Sepideh +4 more
doaj +1 more source
, 2016 Cell membranes separate the inside and outside of cells. Membrane proteins in the cell membrane control the traffic of molecules across the membrane and are therefore targets for a lot of drugs: about 50 % of all approved drugs target a membrane protein!
Scheidelaar, S. +2 more
core
The ubiquitin ligase RNF115 is required for the clearance of damaged lysosomes
FEBS Letters, EarlyView.Upon lysosomal rupture, an E3 ubiquitin ligase RNF115 translocates from the cytosol to the damaged lysosomal membrane. Moreover, RNF115 depletion impairs the clearance of damaged lysosomes, identifying it as a key regulator of lysosomal quality control.
Sae Nakanaga +3 more
wiley +1 more source
Membrane proteins in the outer mebrane of plastids and mitochondria [PDF]
, 2006 Channels of the plastid and mitochondrial outer membranes facilitate the turnover of molecules and ions via these membranes. Although channels have been studied many questions pertaining to the whole diversity of plastid and mitochondrial channels in ...
Ilkavets, Iryna
core
Novel single-molecule force spectroscopy approaches to characterize interactions of membrane proteins [PDF]
, 2012 : Atomic force microscopy (AFM) based single-molecule force spectroscopy (SMFS) is a biophysical tool used to investigate folding and unfolding of biological macromolecules, like membrane proteins. Unfolding of single membrane proteins can be recorded by
Zocher, Michael
core +1 more source
FEBS Letters, EarlyView.Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley +1 more source
Molecules and Cells: Various approaches employing cytokines and cytokine gene–modified tumor cells have been explored to induce antitumor responses, yet their widespread application has been limited due to efficacy concerns and adverse effects. In this study, interleukin-7
Hee-Su Shin +5 more
doaj +1 more source
Solute channels of the outer membrane: from bacteria to chloroplasts [PDF]
, 2007 Chloroplasts, unique organelles of plants, originated from endosymbiosis of an ancestor of today's cyanobacteria with a mitochondria-containing host cell. It is assumed that the outer envelope membrane, which delimits the chloroplast from the surrounding
Philippar, Katrin +2 more
core +1 more source
pH‐mediated activation of the lysosomal arginine sensor SLC38A9
FEBS Letters, EarlyView.Cells monitor nutrient levels via the lysosomal transporter SLC38A9 to activate the mechanistic target of rapamycin complex 1 (mTORC1). This study reveals that SLC38A9 function is regulated by pH. We identified histidine 544 as a critical pH sensor that undergoes conformational changes to control amino acid efflux from lysosomes; therefore, it ...
Xuelang Mu, Ampon Sae Her, Tamir Gonen
wiley +1 more source