Results 211 to 220 of about 25,530 (255)
Alterations in bone malformation in the absence of the endosomal SNAREs Vti1a and Vti1b. [PDF]
PLoS OneSchmücker S +6 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
SNARE Proteins in Synaptic Vesicle Fusion
2023Neurotransmitters are stored in small membrane-bound vesicles at synapses; a subset of synaptic vesicles is docked at release sites. Fusion of docked vesicles with the plasma membrane releases neurotransmitters. Membrane fusion at synapses, as well as all trafficking steps of the secretory pathway, is mediated by SNARE proteins.
Mark T, Palfreyman +2 more
openaire +2 more sources
Characteristics of SNARE proteins are defined by distinctive properties of SNARE motifs
Biochimica et Biophysica Acta (BBA) - General Subjects, 2020Syntaxin-1A and Sso1 are syntaxin family SNARE proteins engaged in synaptic vesicle fusion and yeast exocytosis. The syntaxin-1A SNARE motif can form a fusogenic SNARE complex with Sso1 partners. However, a chimera in which the SNARE motif in syntaxin-1A is introduced into Sso1 was not functional in yeast because the chimera is retained in the ER ...
Kankai, Shao +5 more
openaire +2 more sources
SNARE Protein Structure and Function
Annual Review of Cell and Developmental Biology, 2003▪ Abstract The SNARE superfamily has become, since its discovery approximately a decade ago, the most intensively studied element of the protein machinery involved in intracellular trafficking. Intracellular membrane fusion in eukaryotes requires SNARE (soluble N-ethylmaleimide-sensitive-factor attachment protein receptor) proteins that form ...
Daniel, Ungar, Frederick M, Hughson
openaire +2 more sources
Are Neuronal SNARE Proteins Ca2+ Sensors?
Journal of Molecular Biology, 2005The neuronal SNARE complex formed by synaptobrevin, syntaxin and SNAP-25 plays a central role in Ca2+-triggered neurotransmitter release. The SNARE complex contains several potential Ca2+-binding sites on the surface, suggesting that the SNAREs may be involved directly in Ca2+-binding during release.
Xiaocheng, Chen +3 more
openaire +2 more sources
SNARE Proteins as Signaling Elements
2013SNAREs (N-ethylmaleimide-sensitive factor adaptor protein receptors) are small polypeptides (∼200–400 amino acid) which are characterized by a particular domain, the SNARE motif that can form a coiled-coil structure via hetero-oligomeric interactions. These protein interactions are highly stable leading to the formation of the so-called SNARE complex ...
Ul Rehman R., Di Sansebastiano G. P.
openaire +2 more sources
SNARE protein analog‐mediated membrane fusion
Journal of Peptide Science, 2015Fusion of lipid membranes to form a single bilayer is an essential process for life and provides important biological functions including neurotransmitter release. Membrane fusion proteins facilitate approximation of interacting membranes to overcome the energy barrier.
Pawan, Kumar +2 more
openaire +2 more sources
Structure and function of SNARE and SNARE-interacting proteins
Quarterly Reviews of Biophysics, 2005This review focuses on the so-called SNARE (soluble N-ethyl maleimide sensitive factor attachment protein receptor) proteins that are involved in exocytosis at the pre-synpatic plasma membrane. SNAREs play a role in docking and fusion of synaptic vesicles to the active zone, as well as in the Ca2+-triggering step itself, most likely in combination with
openaire +2 more sources
Milk Secretion: The Role of SNARE Proteins
Journal of Mammary Gland Biology and Neoplasia, 2013During lactation, polarized mammary epithelial secretory cells (MESCs) secrete huge quantities of the nutrient molecules that make up milk, i.e. proteins, fat globules and soluble components such as lactose and minerals. Some of these nutrients are only produced by the MESCs themselves, while others are to a great extent transferred from the blood ...
Sandrine, Truchet +2 more
openaire +2 more sources