gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

N-ethylmaleimide-sensitive factor

NSF, N-ethylmaleimide-sensitive factor, N-ethylmaleimide-sensitive fusion protein
binds AMPA receptor GluR2 subunit and acts to disrupt GluR2-PICK1 interactions; may play a role in AMPA receptor trafficking and stabilization [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: CAN, SNAP-25, V1a, Synaptobrevin, ACID
Papers using NSF antibodies
Termination of spiral waves during cardiac fibrillation via shock-induced phase resetting
Bodenschatz Eberhard et al., In Nature, 2004
... 01EZ0905/6; by the Kavli Institute for Theoretical Physics through NSFPHY05-51164; by the Pittsburgh Supercomputing Center (NSF TeraGrid); by the Pittsburgh NMR Center for Biomedical Research (NIH P41-EB001977) by ...
A novel role for p120 catenin in E-cadherin function.
Chen Peter, In PLoS ONE, 2001
... anti-cleaved PARP, active caspase-3, active caspase-7 and GAPDH pAbs (Cell Signaling); anti-E-cadherin, β-catenin, GM-130 and NSF mAbs (BD Biosciences, San Jose, CA); anti-ERGIC53 ...
Papers on NSF
Interactions between N-Ethylmaleimide-Sensitive Factor and GluA2 contribute to effects of glucocorticoid hormones on AMPA receptor function in the rodent hippocampus.
Krugers et al., Amsterdam, Netherlands. In Hippocampus, Feb 2016
Peptides which specifically block the interaction between N-Ethylmaleimide-Sensitive Factor (NSF) and the AMPAR-subunit GluA2 prevented the increase in synaptic transmission and surface expression of AMPARs known to occur after corticosterone application to hippocampal neurons.
The mammalian homologue of yeast AFG1 ATPase (Lactation elevated 1) mediates degradation of nuclear-encoded complex IV subunits.
Stiburek et al., Praha, Czech Republic. In Biochem J, Feb 2016
LACE1 is the human homologue of yeast mitochondrial Afg1 ATPase, a member of SEC18-NSF, PAS1, CDC48-VCP, TBP family.
The Atg17-Atg31-Atg29 Complex Coordinates with Atg11 to Recruit the Vam7 SNARE and Mediate Autophagosome-Vacuole Fusion.
Klionsky et al., Ann Arbor, United States. In Curr Biol, Feb 2016
Atg17 and Atg11 interact with the vacuolar SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) Vam7 independently of each other.
Assessment of urinary inhibitor or promoter activity in uric acid nephrolithiasis.
Maalouf et al., Dallas, United States. In J Urol, Jan 2016
PURPOSE: To assess the presence of a reduced inhibitor activity or an increased promoter activity in urine of idiopathic uric acid stone formers (IUASF) compared to non-stone formers (NSF) independent of urinary pH.
Structure and function of longin SNAREs.
Tareste et al., Paris, France. In J Cell Sci, Jan 2016
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins constitute the core membrane fusion machinery of intracellular transport and intercellular communication.
LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate.
Greggio et al., Padova, Italy. In Mol Neurodegener, Dec 2015
We have previously observed that LRRK2 interacts with NSF, a hexameric AAA+ ATPase that couples ATP hydrolysis to the disassembling of SNARE proteins allowing them to enter another fusion cycle during synaptic exocytosis.
Three steps forward, two steps back: mechanistic insights into the assembly and disassembly of the SNARE complex.
Munson et al., Worcester, United States. In Curr Opin Chem Biol, Dec 2015
These techniques were also key in elucidating mechanistic details into how the SNARE complex is disassembled, including details of the energetics required for ATP-dependent α-SNAP/NSF-mediated SNARE complex disassembly, and the structural changes that accompany ATP hydrolysis by the disassembly machinery.
Recent Advances in Deciphering the Structure and Molecular Mechanism of the AAA+ ATPase N-Ethylmaleimide-Sensitive Factor (NSF).
Brunger et al., Stanford, United States. In J Mol Biol, Dec 2015
UNASSIGNED: N-ethylmaleimide-sensitive factor (NSF), first discovered in 1988, is a key factor for eukaryotic trafficking, including protein and hormone secretion and neurotransmitter release.
A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly.
Hughson et al., Princeton, United States. In Science, Oct 2015
Fusion of intracellular transport vesicles requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18-family (SM) proteins.
ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes.
Zhong et al., Stanford, United States. In Nature, May 2015
Here we report that ATG14 (also known as beclin-1-associated autophagy-related key regulator (Barkor) or ATG14L), an essential autophagy-specific regulator of the class III phosphatidylinositol 3-kinase complex, promotes membrane tethering of protein-free liposomes, and enhances hemifusion and full fusion of proteoliposomes reconstituted with the target (t)-SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) syntaxin 17 (STX17) and SNAP29, and the vesicle (v)-SNARE VAMP8 (vesicle-associated membrane protein 8).
Spring-loaded unraveling of a single SNARE complex by NSF in one round of ATP turnover.
Yoon et al., Taejŏn, South Korea. In Science, Apr 2015
During intracellular membrane trafficking, N-ethylmaleimide-sensitive factor (NSF) and alpha-soluble NSF attachment protein (α-SNAP) disassemble the soluble NSF attachment protein receptor (SNARE) complex for recycling of the SNARE proteins.
Mechanistic insights into the recycling machine of the SNARE complex.
Brunger et al., Stanford, United States. In Nature, Mar 2015
The ATPase NSF (N-ethylmaleimide sensitive factor), together with SNAPs (soluble NSF attachment protein), disassembles the SNARE complex into its protein components, making individual SNAREs available for subsequent rounds of fusion.
Formation of Tubulovesicular Carriers from Endosomes and Their Fusion to the trans-Golgi Network.
Bonifacino et al., Spain. In Int Rev Cell Mol Biol, 2014
Specific tethering factors and SNARE (SNAP (Soluble NSF Attachment Protein) Receptor) complexes are then required for the docking and fusion with the acceptor membrane.
The Synaptic Vesicle Release Machinery.
Xu et al., Dallas, United States. In Annu Rev Biophys, 2014
The SNAREs Syntaxin-1, Synaptobrevin, and SNAP-25 play a central role in membrane fusion, forming SNARE complexes that bridge the vesicle and plasma membranes and that are disassembled by NSF-SNAPs.
The Get1/2 transmembrane complex is an endoplasmic-reticulum membrane protein insertase.
Denic et al., Cambridge, United States. In Nature, 2014
Hundreds of tail-anchored proteins, including soluble N-ethylmaleimide-sensitive factor attachment receptors (SNAREs) involved in vesicle fusion, are inserted post-translationally into the endoplasmic reticulum membrane by a dedicated protein-targeting pathway.
Candidate pathway association study in cocaine dependence: the control of neurotransmitter release.
Ribasés et al., Barcelona, Spain. In World J Biol Psychiatry, 2012
Single and multiple-marker analyses revealed a strong association between cocaine dependence and the NSF gene.
Potential cellular functions of N-ethylmaleimide sensitive factor in the photoreceptor.
Craft et al., Los Angeles, United States. In Adv Exp Med Biol, 2011
Arr1 and NSF interaction are necessary for both maintenance and modulation of normal photoreceptor synaptic regulation and NSF-RP2 interaction may play an important role in membrane protein trafficking in the photoreceptor.
Activity-dependent interactions of NSF and SNAP at living synapses.
Ordway et al., Penn Hills, United States. In Mol Cell Neurosci, 2011
Data show that NSF and SNAP exhibit activity-dependent binding to each other within living presynaptic terminals as well as distinctive interactions and mobilities.
Thioredoxin increases exocytosis by denitrosylating N-ethylmaleimide-sensitive factor.
Lowenstein et al., Rochester, United States. In J Biol Chem, 2011
Knockdown of TRX1 increases the level of S-nitrosylated NSF, prolongs the inhibition of exocytosis, and suppresses leukocyte
Both pre- and postsynaptic activity of Nsf prevents degeneration of hair-cell synapses.
Nicolson et al., Portland, United States. In Plos One, 2010
results establish a role for Nsf in the maintenance of synaptic contacts between hair cells and afferent neurons, mediated in part via the secretion of trophic signaling factors
share on facebooktweetadd +1mail to friends