|1.||Lawrence, Gary W: 3 articles (01/2015 - 09/2012)|
|2.||Klink, Vincent P: 2 articles (01/2015 - 09/2012)|
|3.||Wang, Jiafu: 2 articles (02/2014 - 12/2012)|
|4.||Meng, Jianghui: 2 articles (02/2014 - 12/2012)|
|5.||Dolly, J Oliver: 2 articles (12/2012 - 02/2012)|
|6.||Jiménez, Antonio J: 2 articles (12/2009 - 07/2006)|
|7.||Bátiz, Luis Federico: 2 articles (12/2009 - 07/2006)|
|8.||Pérez-Fígares, José Manuel: 2 articles (12/2009 - 07/2006)|
|9.||Páez, Patricia: 2 articles (12/2009 - 07/2006)|
|10.||Fountoulakis, M: 2 articles (05/2001 - 01/2001)|
07/01/2006 - "The investigation was designed to study: (i) the clinical evolution of hyh mice; (ii) factors other than the alpha-SNAP mutation that may influence the expression of hydrocephalus; (iii) the neuropathological features underlying the different forms of clinical evolution. "
12/01/2009 - "The hyh (hydrocephalus with hop gait) mouse carries a missense mutation in Napa gene that results in a point mutation (M105I) in alpha-SNAP protein. "
02/10/2004 - "The gene for soluble N-ethylmaleimide sensitive factor attachment protein alpha is mutated in hydrocephaly with hop gait (hyh) mice."
02/01/2009 - "Finally, the hydrocephalus with hop gait (hyh) mouse, which harbors a mutation in Napa [encoding N-ethylmaleimide-sensitive factor attachment protein alpha (alpha-SNAP)], also develops a progressive denudation of the neuroepithelium, leading to periventricular nodule formation. "
07/01/2006 - "The hyh mouse carrying a point mutation in the gene encoding for soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein alpha (alpha-SNAP) develops inherited hydrocephalus. "
|2.||Weight Loss (Weight Reduction)
08/01/2007 - "The study aimed to examine if dysmetabolic subjects (MetS+) have lower adiponectin gene expression and lower circulating adiponectin levels than non-dysmetabolic obese subjects (MetS-) at baseline, if adiponectin expression and adiponectin concentration rise more in the dysmetabolic group during weight loss, and if v-SNARE Vti1a (vesicle transport soluble NSF attachment protein receptor vps10p tail interacting 1a) expression increases during the weight loss, as a mechanism for increased adiponectin secretion. "
02/16/2001 - "To examine the molecular mechanisms of the membrane remodeling that accompanies bacterial invasion, soluble NSF attachment protein receptor (SNARE)-mediated membrane traffic was studied in cultured cells during infection by Salmonella typhimurium. "
01/01/2015 - "Experiments show the membrane fusion genes α soluble NSF attachment protein (α-SNAP) and syntaxin 31 (Gm-SYP38) contribute to the ability of Glycine max to defend itself from infection by the plant parasitic nematode Heterodera glycines. "
01/01/2013 - "As vesicle trafficking and fusion in planta are facilitated by a superfamily of proteins known as SNAREs (soluble N-ethylmaleimide-sensitive-factor attachment protein receptors), we screened ER-localized SNARES or SNARE-like proteins for their possible involvement in TuMV infection. "
01/01/2008 - "Furthermore, infection with wt RABV resulted in down-regulation of SNAREs such as alpha-SNAP, TRIM9, syntaxin, and pallidin, all of which are involved in docking and fusion of synaptic vesicles to and with the presynaptic membrane. "
04/01/2000 - "The presence of homologues of genes encoding proteins involved in steroid biogenesis (e.g., hydroxysteroid dehydrogenase), antioxidant functions (e.g., glutathione peroxidase), vesicle trafficking (e.g., two alpha-type soluble NSF attachment proteins), and other, unknown conserved cellular processes (e.g., Hal3 domain protein and GSN1/SUR4) suggests that significant modification of host cell function occurs upon viral infection. "
01/01/2011 - "Botulinum neurotoxin (BoNT), a Category A biodefense agent, delivers a protease to motor neuron cytosol that cleaves one or more soluble NSF attachment protein receptors (SNARE) proteins involved in neurotransmission to cause a flaccid paralysis. "
12/01/2011 - "Botulinum neurotoxins (BoNT) act via a four-step mechanism, viz., binding and internalization to neuronal cells, translocation of the catalytic domain into the cytosol and finally cleavage of one of the three soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) causing blockage of neurotransmitter release leading to flaccid paralysis. "
01/01/2010 - "After binding to the peripheral neurons, the central domain of BoNT helps the LC translocate into cytosol where its proteolytic action on SNARE (soluble NSF attachment protein receptor) proteins blocks exocytosis of acetyl choline leading to muscle paralysis and eventual death. "
12/01/2012 - "Botulinum neurotoxin (BoNT) A or E and tetanus toxin (TeTx) bind to motor-nerve endings and undergo distinct trafficking; their light-chain (LC) proteases cleave soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) peripherally or centrally and cause flaccid or spastic paralysis, respectively. "
|5.||Down Syndrome (Down's Syndrome)
01/01/2001 - "NSE, chapsyn 110 and beta SNAP were comparable in the control fetus panel and in Down Syndrome fetuses. "
05/01/2001 - "Synaptosomal proteins, beta-soluble N-ethylmaleimide-sensitive factor attachment protein (beta-SNAP), gamma-SNAP and synaptotagmin I in brain of patients with Down syndrome and Alzheimer's disease."
|1.||SNARE Proteins (SNAREs)
|3.||Proteins (Proteins, Gene)
|4.||Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
|5.||N-Ethylmaleimide-Sensitive Proteins (N-Ethylmaleimide-Sensitive Fusion Protein)
|6.||Qa-SNARE Proteins (Syntaxin)
|8.||R-SNARE Proteins (Vesicle-Associated Membrane Protein)
|10.||Endosomal Sorting Complexes Required for Transport