Results 61 to 70 of about 13,129,737 (272)
, 2010 The extended Fes-CIP4 homology (EFC)/FCH-BAR (F-BAR) domain tubulates membranes. Overexpression of the pacsin2 EFC/F-BAR domain resulted in tubular localization inside cells and deformed liposomes into tubules in vitro.
Shimada, Atsushi +9 more
core +1 more source
Reconstructing enzyme evolution by protein engineering
FEBS Letters, EarlyView.Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler +2 more
wiley +1 more source
Structure‐forward targeting of claudins with synthetic binders
FEBS Letters, EarlyView.Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley +1 more source
Strong normalisation for applied lambda calculi [PDF]
Logical Methods in Computer Science, 2005 We consider the untyped lambda calculus with constructors and recursively defined constants. We construct a domain-theoretic model such that any term not denoting bottom is strongly normalising provided all its `stratified approximations' are.
Ulrich Berger
doaj +1 more source
Curved EFC/F-BAR-Domain Dimers Are Joined End to End into a Filament for Membrane Invagination in Endocytosis [PDF]
Cell, 2007 Pombe Cdc15 homology (PCH) proteins play an important role in a variety of actin-based processes, including clathrin-mediated endocytosis (CME). The defining feature of the PCH proteins is an evolutionarily conserved EFC/F-BAR domain for membrane association and tubulation.
Shimada, Atsushi +20 more
openaire +2 more sources
Conformation of F-BAR domain lattices looking up from the membrane towards the protein.
, 2013 Individual F-BAR domains are differentiated by color. Initial (A) and final (B) conformation of the F-BAR domain lattices on top of the membrane taken from one of the systems, simulations LATTICES, shown in Fig.
Hang Yu (278278) +1 more
core +1 more source
Translophagy—A potential link between autophagy impairment and translational errors
FEBS Letters, EarlyView.Neurodegenerative diseases are characterised by the accumulation of abnormal proteins and protein aggregates, but their origin often remains unknown. We propose that selective autophagy removes damaged protein‐making machinery, preventing errors during protein synthesis.
Mykola V. Korolchuk +11 more
wiley +1 more source
Energies, 2022 When an induction motor is running at stable speed and low slip, the fault signal of the induction motor’s broken bar faults are easily submerged by the power frequency (50 Hz) signal. Thus, it is difficult to extract fault characteristics. The left-side
Xinyue Liu +6 more
doaj +1 more source
"""Bend it"": Membrane sculpting by F-BAR domain lattices" [PDF]
, 2014 The image shows how a particular protein, named F-BAR domain, works in teams to bend flat cellular membrane into tubules. To generate organelles, eukaryotic cells sculpt their membranes into compartments, often employing proteins as chaperones,for ...
Yu, Hang
core
The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation
FEBS Letters, EarlyView.Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge +6 more
wiley +1 more source