ライフサイエンスコーパス: bee venom

1 vespid venom, but not in those treated with bee venom.

2 ultiple species and is the major allergen in bee venom.

3 is dispensable for the allergic response to bee venom.

4 tudied after adding glutamate and sPLA2 from bee venom.

5 s of Mycobacterium chelonae infections after bee venom acupuncture.

6 ic skin and soft tissue infections following bee venom acupuncture.

7 B cells specific for the major bee venom allergen phospholipase A2 (PLA) were isolated

8 B cells specific for the major bee venom allergen PLA isolated from nonallergic beekeep

9 depot effect, prolonging the availability of bee venom allergens at the site of administration.

10 increased by adding rSSMA of other important bee venom allergens.

11 and/or Ves v 1, and 78.3% of single-positive bee venom-allergic patients had sIgE to Api m 1.

12 n secreted phospholipase A(2) (sPLA(2), from bee venom and bovine pancreas) and a transition-state an

13 Although very different from the bee venom and mammalian hyaluronidase sequences, the E.

14 ients and controls, sIgE to rSSMA Api m 1 of bee venom and to Ves v 1 and Ves v 5 of wasp venom were

15 d from beekeepers who displayed tolerance to bee venom antigens and allergic patients before and afte

16 The bee venom antimicrobial peptide, melittin, besides showi

17 Molecular dynamics simulations of bee venom apamin, and an analogue having an Asn to Ala s

18 Sensitivity of bee venom Api m 1 could be increased by adding rSSMA of

19 Honey bee venom (BV) allergies are very common; however, the l

20 he ImmunoCAP system for routine diagnosis of bee venom (BV) allergy.

21 Here, we investigated the putative role of bee venom (Bv) in human FOXP3-expressing Treg homeostasi

22 The secreted phospholipase A(2) from bee venom (bvPLA(2)) contains a membrane binding surface

23 finding was explained by demonstrating that bee venom-derived phospholipase A2 (PLA2) activates T ce

24 IgG4-switched memory B cells expanded after bee venom exposure.

25 (TPN), a 21 amino acid peptide isolated from bee venom, has been reported to inhibit Kir1.1 and Kir3.

26 ied distinct sensitization profiles in honey bee venom (HBV) allergy, some of which were dominated by

27 rted (beta/alpha)8 barrel resembling that of bee venom hyaluronidase, and a novel, EGF-like domain, c

28 ially inhibited sPLA2 OS2 but not sPLA2 from bee venom-induced arachidonic acid release.

29 Whereas activation of the inflammasome by bee venom induces a caspase-1-dependent inflammatory res

30 protein toxin originally isolated from honey bee venom, inhibits only certain eukaryotic inward-recti

31 in (TPN), a small protein derived from honey bee venom, inhibits the GIRK1/4 and ROMK1 channels with

32 Here we show that bee venom is detected by the NOD-like receptor family, p

33 Melittin, the major component of the bee venom, is an amphipathic, cationic peptide with a wi

34 ally evolved gain-of-function variant of the bee venom lytic peptide melittin identified in a high-th

35 o occurs if cells are reacted in medium with bee venom melittin, which penetrates cells and forms mem

36 Among the different sPLA(2)s tested, bee venom, Naja naja, and porcine and human pancreatic P

37 cial catalysis by phospholipase A2 (PLA2) of bee venom on zwitterionic vesicles of 1-palmitoyl-2-oleo

38 es of the cecropin A and residues 2-9 of the bee venom peptide mellitin.

39 ry conductance values and sensitivity to the bee venom peptide toxin, apamin.

40 ere synthesized encompassing portions of the bee venom peptide, apamin, and the sequence KWLAESVRAGK

41 c example of membrane-induced folding is the bee-venom peptide melittin that is largely unstructured

42 Kinetic characterization of bee venom phospholipase A(2) activity at bile salt+phosp

43 activity of the synthetic analogues against bee venom phospholipase A(2) suggests that cacospongiono

44 ATX generates LPA from CHO cells primed with bee venom phospholipase A(2), and ATX-mediated LPA produ

45 ing phosphatidylcholine (PC), using snake or bee venom phospholipase A(2).

46 Interfacial catalytic constants for bee venom phospholipase A2 (bvPLA2) have been obtained f

47 The basis for tight binding of bee venom phospholipase A2 (bvPLA2) to anionic versus zw

48 pheles stephensi mosquitoes that express the bee venom phospholipase A2 (PLA2) gene from the gut-spec

49 pecific suppressor T cell (Ts) hybridoma and bee venom phospholipase A2 (PLA2)-specific Ts hybridoma

50 ipoprotein were active, LDL was treated with bee venom phospholipase A2 (PLA2).

51 oxalate) has been developed to determine how bee venom phospholipase A2 sits on the membrane.

52 activity of the synthetic analogues against bee venom phospholipase A2 suggests that the cacospongio

53 In bee venom phospholipase A2, histidine-34 probably functi

54 onphospholipid as a novel substrate of honey bee venom phospholipase A2.

55 and with a structurally divergent group III bee venom PLA(2) (bvPLA(2)).

56 We found that bee venom PLA2 induced a T helper type 2 (Th2) cell-type

57 Here we examined how bee venom PLA2 is sensed by the innate immune system and

58 nd enzymatic activity of membrane-associated bee venom PLA2, covering a pressure range up to 2 kbar.

59 ns to three membrane peptides: melittin from bee venom, the transmembrane domain of the M2 protein fr

60 A (from moth) with residues 2-9 of melittin (bee venom)], three fluorescence signals report oxidative

61 f allergen-specific B cells before and after bee venom tolerance induction.

62 Pretreatment with the bee venom toxin apamin enhanced this response.

63 Melittin, the main component of dry bee venom, was used as a model amphipathic alpha-helical

64 Here, by modifying a toxin from the honey bee venom, we have successfully engineered an inhibitor

65 melittin, the active molecule of apitoxin or bee venom, were investigated on human red blood cells (R