Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.11.8 (FAST)
 758 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Three ipsilateral (MSR, PSR, IPSI SLOW) and two contralateral segmental reflexes (CON FAST, CON SLOW) were recorded from L4 or L5 ventral roots of the neonate rat spinal cord in vitro. MSR, PSR and CON FAST were evoked from lower threshold afferents; more intense stimulation evoked IPSI SLOW and CON SLOW. 2. Kainate/AMPA receptors were involved in mediation of MSR, PSR, CON FAST, IPSI SLOW and CON SLOW and NMDA receptors in mediation of CON FAST, IPSI SLOW and CON SLOW. 3. All five reflexes were depressed by 5-HT (IC50 1.2-7.9 microM; order of sensitivity, CON SLOW > CON FAST = IPSI SLOW > MSR = PSR); and by 5-CT (IC50 1.9-8.8 nM; order of sensitivity, MSR > IPSI SLOW = CON FAST = CON SLOW > PSR). alpha-Me-5-HT also depressed all five reflexes. 4. Dipropyl-5-CT selectively depressed MSR and CON SLOW (IC50 90-170 nM) but was less potent than 5-CT. 8-OH-DPAT selectively depressed MSR (IC50 1.1 microM), IPSI SLOW and CON SLOW (IC50 5.7-7.6 microM), while methylsergide depressed only MSR (IC50 26 nM). 5. Phenyl biguanide and m-chlorophenyl biguanide (5-HT3 receptor agonists) had no significant effects on any reflex. 6. It is concluded that a 5-HT1-like receptor mediates depression of the MSR. A different receptor or a mixed population of receptors, but not 5-HT3 receptors, mediate inhibition of PSR, CON FAST, IPSI SLOW and CON SLOW.
Gen Pharmacol 1992 Nov
PMID:FAST and SLOW ipsilateral and contralateral spinal reflexes in the neonate rat are modulated by 5-HT. 148 13

Aquareoviruses AqRVs have a close relationship with orthoreoviruses. However, they contain an additional genome segment, S11, which encodes nonstructural protein NS26. We previously showed that NS26 can enhance the fusogenic activity of the fusion-associated small transmembrane FAST protein NS16 from AqRV. In this study, a TLPK motif in NS26 was identified as being important for the enhancement. When the TLPK motif was deleted from NS26, the enhanced efficiency of the NS16-mediated cellcell fusion was significantly impaired. Further mutational analysis showed that the lysine K residue in the TLPK motif was critical for the enhancement. Additionally, deletion of the TLPK motif prevented NS26 from interacting with lysosomes. These findings suggested that the TLPK motif is important for NS26 to enhance the fusogenic activity of NS16, and NS26 may utilize the lysosome to benefit the fusion process.
J Gen Virol 2015 May
PMID:Identification of a functional motif in the AqRV NS26 protein required for enhancing the fusogenic activity of FAST protein NS16. 2560 27