SNARE-Ware: The Role of SNARE-Domain Proteins in Plant Biology [PDF]
Annual Review of Cell and Developmental Biology, 2007 In yeast and animal cells, members of the superfamily of N-ethylmaleimide-sensitive factor adaptor protein receptor (SNARE)-domain-containing proteins are key players in vesicle-associated membrane fusion events during transport processes between individual compartments of the endomembrane system, including exocytosis and endocytosis.
Lipka, V., Kwon, C., Panstruga, R.
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Syntaxin 16 and syntaxin 5 are required for efficient retrograde transport of several exogenous and endogenous cargo proteins [PDF]
, 2007 Retrograde transport allows proteins and lipids to leave the endocytic pathway to reach other intracellular compartments, such as trans-Golgi network (TGN)/Golgi membranes, the endoplasmic reticulum and, in some instances, the cytosol. Here, we have used
Amessou, Mohamed +7 more
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Cell Reports, 2013 Rapid endocytosis, which takes only a few seconds, is widely observed in secretory cells. Although it is more efficient in recycling vesicles than in slow clathrin-mediated endocytosis, its underlying mechanism, thought to be clathrin independent, is ...
Jianhua Xu +7 more
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LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate [PDF]
, 2016 Background Lrrk2, a gene linked to Parkinson\u2019s disease, encodes a large scaffolding protein with kinase and GTPase activities implicated in vesicle and cytoskeletal-related processes.
Arrigoni, Giorgio +15 more
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Snake and spider toxins induce a rapid recovery of function of botulinum neurotoxin paralysed neuromuscular junction [PDF]
, 2015 Botulinum neurotoxins (BoNTs) and some animal neurotoxins (-Bungarotoxin, -Btx, from elapid snakes and -Latrotoxin, -Ltx, from black widow spiders) are pre-synaptic neurotoxins that paralyse motor axon terminals with similar clinical outcomes in patients.
Duregotti, Elisa +6 more
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Synaptic proteins promote calcium-triggered fast transition from point contact to full fusion. [PDF]
, 2012 The molecular underpinnings of synaptic vesicle fusion for fast neurotransmitter release are still unclear. Here, we used a single vesicle-vesicle system with reconstituted SNARE and synaptotagmin-1 proteoliposomes to decipher the temporal sequence of ...
Brunger, Axel T +13 more
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VAMP721 conformations unmask an extended motif for K+ channel binding and gating control [PDF]
, 2016 Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins play a major role in membrane fusion and contribute to cell expansion, signaling, and polar growth in plants.
Blatt, Mike R. +4 more
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SNARE proteins mediate lipid bilayer fusion [PDF]
Proceedings of the National Academy of Sciences, 1999 Lipid bilayers compartmentalize eukaryotic cells into distinct organelles. This compartmentalization allows for specialization of diverse cellular processes, from DNA polymerization to zymogen proteolysis. While the specific complement of proteins present in each organelle defines its function, there is a dynamic flux between these organelles.
J B, Bock, R H, Scheller
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The mesoscale organization of syntaxin 1A and SNAP25 is determined by SNARE–SNARE interactions
eLife, 2021 SNARE proteins have been described as the effectors of fusion events in the secretory pathway more than two decades ago. The strong interactions between SNARE domains are clearly important in membrane fusion, but it is unclear whether they are involved ...
Jasmin Mertins +5 more
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A KNN Model Based on Manhattan Distance to Identify the SNARE Proteins
IEEE Access, 2020 SNARE proteins, known as membrane fusion proteins, play a primary role to mediate vesicle fusion. Loss of function of the SNARE protein can lead to a variety of diseases. A method to accurately identify the SNARE protein is important and necessary.
Xing Gao, Guilin Li
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