| Name | Neuraminidase |
|---|---|
| Synonyms | Acetylneuraminyl hydrolase; Exo alpha sialidase; G9 sialidase; Lysosomal sialidase; N acetyl alpha neuraminidase 1; NANH; NEU; NEU 1… |
| Name | benzalkonium chloride |
|---|---|
| CAS | quaternary ammonium compounds, alkylbenzyldimethyl, chlorides |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 7536161 | Emadi-Khiav B, Mousli M, Bronner C, Landry Y: Human and rat cutaneous mast cells: involvement of a G protein in the response to peptidergic stimuli. Eur J Pharmacol. 1995 Jan 5;272(1):97-102. The hydrolysis of residues by neuraminidase and the inhibition of G proteins by benzalkonium chloride or pertussis toxin significantly inhibited the secretory response of cutaneous mast cells to neuropeptide Y-(18-36) and mastoparan. |
81(1,1,1,1) | Details |
| 7173980 | Coleman JW: Neuraminidase- and benzalkonium chloride-dependent inhibition of basic peptide-induced rat mast cell secretion. Immunol Lett. 1982 Oct;5(4):197-201. |
32(0,1,1,2) | Details |
| 7533476 | Estevez MD, Vieytes MR, Botana LM: Study of the activation mechanism of adriamycin on rat mast cells. . Agents Actions. 1994 Oct;42(3-4):86-91. release induced by compound 48/80, was markedly inhibited by pertussis toxin, cholera toxin, benzalkonium chloride and neuraminidase. |
31(0,1,1,1) | Details |
| 1373170 | Mousli M, Hugli TE, Landry Y, Bronner C: A mechanism of action for anaphylatoxin C3a stimulation of mast cells. . J Immunol. 1992 Apr 15;148(8):2456-61. was released in a nonlytic manner and the mast cell stimulation by both natural and synthetic factors was sensitive to pertussis toxin, neuraminidase, benzalkonium chloride, and to an excess of |
6(0,0,1,1) | Details |
| 9606019 | Chahdi A, Daeffler L, Bueb JL, Gies JP, Landry Y: The M2 muscarinic receptor antagonist methoctramine activates mast cells via pertussis toxin-sensitive G proteins. Naunyn Schmiedebergs Arch Pharmacol. 1998 Apr;357(4):357-62. Benzalkonium chloride, a selective inhibitor of secretion induced by basic secretagogues, inhibited the secretory response to methoctramine. [p-Glu5, D-Trp7,9,l0]-SPs5-11 (GPAnt-2), a well-characterized antagonist of G proteins, blocked the methoctramine-induced release when the antagonist was allowed to reach its intracellular target by streptolysin O-permeabilization. The response to methoctramine was prevented by the hydrolysis of residues of the cell surface by neuraminidase. |
1(0,0,0,1) | Details |
| 10431764 | Daeffler L, Nadra K, Eichwald V, Ohresser S, Landry Y: Effect of NMDA receptor ligands on mast cell release, a reappraisal. Naunyn Schmiedebergs Arch Pharmacol. 1999 Jun;359(6):512-8. Both - and arcaine-induced effects were independent upon extracellular and were largely inhibited by treatment of mast cells with pertussis toxin or benzalkonium chloride. The response to and arcaine was prevented by the hydrolysis of residues of the cell surface by neuraminidase, and was restored by permeabilization of the plasma membrane with streptolysine-O, indicating that polyamines act intracellularly. |
1(0,0,0,1) | Details |
| 10771034 | Mori K, Maru C, Takasuna K, Furuhama K: Mechanism of release induced by levofloxacin, a fluoroquinolone antibacterial agent. Eur J Pharmacol. 2000 Apr 7;394(1):51-5. Unlike that with the ionophore A23187, secretion due to levofloxacin or compound 48/80 was prevented by pretreatment with either pertussis toxin or benzalkonium chloride, a selective inhibitor of G proteins of G (i) subtypes. Moreover, the release elicited by levofloxacin or compound 48/80 was suppressed by hydrolysis of residues on the cell surface brought about by neuraminidase. |
1(0,0,0,1) | Details |
| 4102573 | Oxford JS, Potter CW, McLaren C, Hardy W: Inactivation of influenza and other viruses by a mixture of virucidal compounds. Appl Microbiol. 1971 Apr;21(4):606-10. A mixture of benzalkonium chloride, Triton X100, and (Resiguard F) had a marked virucidal effect on lipid-containing deoxyribonucleic and ribonucleic acid viruses, such as vaccinia virus, herpesvirus, and influenza virus. Electron microscopy showed that influenza particles became aggregated in the presence of Resiguard F and that the outer fringe of hemagglutinin and neuraminidase spikes seen in control virus preparations became indistinct. |
1(0,0,0,1) | Details |