ライフサイエンスコーパス: scorpion toxin

1 r dynamics simulations of a small protein (a scorpion toxin).

2 IIS3-S4 reduce the binding affinity of beta-scorpion toxin.

3 between the voltage sensors and a pore-bound scorpion toxin.

4 e detectable only after activation with beta scorpion toxin.

5 ovides a functional link between DDH and ICK scorpion toxins.

6 ists that can prevent or reverse toxicity of scorpion toxins.

7 ) that bind to two different epitopes on the scorpion toxins.

8 rged amphiphiles as well as a number of beta-scorpion toxins.

9 red structure of Kv1.3 based on mapping with scorpion toxins.

10 ht on the structure/function relationship of scorpion toxins.

11 ctural features characteristic of long-chain scorpion toxins: a two and a half-turn alpha-helix, a th

12 An insect-selective scorpion toxin (AaIT5) was purified from the venom of th

13 ght into the voltage sensor-trapping mode of scorpion toxin action, define the position of the voltag

14 ge dependence of activation and enhance beta-scorpion toxin action.

15 The structurally well-characterized scorpion toxin Agitoxin2 inhibits ion permeation through

16 alpha/beta-scaffold characteristic of other scorpion toxins, although very likely forming an uncommo

17 ids of the IVS3-S4 loop participate in alpha-scorpion toxin and sea anemone toxin binding to overlapp

18 av1.8 has amino acid variants that bind bark scorpion toxins and inhibit Na(+) currents, blocking act

19 alpha-Scorpion toxins and sea anemone toxins bind to a common

20 Both scorpion toxins are putative mimics of the II-III loop p

21 -go-go (hEAG), as well as application of the scorpion toxin BeKm-1, we identified that the S5-pore li

22 beta-Scorpion toxins bind specifically to neurotoxin receptor

23 The alpha-scorpions toxins bind to the resting state of Na(+) chan

24 egment contribute to the difference in alpha-scorpion toxin binding affinity between cardiac and neur

25 idues in the IIS4 segment do not affect beta-scorpion toxin binding but alter voltage dependence of a

26 alpha-Scorpion toxin binding to wild type and E1613R had simil

27 IVS3 to Arg or His blocked measurable alpha-scorpion toxin binding, but did not affect the level of

28 d in tsA-201 cells and tested for 125I-alpha-scorpion toxin binding.

29 Kinetic analysis showed that beta-scorpion toxin binds to the resting state, and subsequen

30 s to determine the X-ray structure of native scorpion toxin BmBKTx1; direct methods were used for pha

31 ximately 40% in the presence of 100 nM alpha-scorpion toxin, but no allosteric enhancement was observ

32 nnel sequence had reduced affinity for alpha-scorpion toxin characteristic of cardiac Na+ channels.

33 cially at the carboxyl termini, with another scorpion toxin, charybdotoxin (ChTX), which blocks both

34 The scorpion toxin, Charybdotoxin (CTX), blocks homotetramer

35 Here, the binding modes of two selected scorpion toxins, charybdotoxin (ChTx) and OSK1, to human

36 ed to the refolding of denatured and reduced scorpion toxin Cn5.

37 Molecular determinants of beta-scorpion toxin (CssIV) binding and action on rat brain s

38 usly improved a natural amino-acid form of a scorpion toxin-derived CD4-mimetic peptide and in parall

39 hat similarity in the mechanism of action of scorpion toxins does not always follow from an overall s

40 helix rather than the beta sheets with which scorpion toxins form their interaction surface.

41 Ts3 is an alpha scorpion toxin from the venom of the Brazilian scorpion

42 related members of the alpha-KTX15 family of scorpion toxins have been shown to block the A-type K+ c

43 beta-Scorpion toxins, including toxin IV from Centruroides su

44 analysis of sodium channel chimeras, a beta-scorpion toxin is shown here to negatively shift voltage

45 Dissociation of alpha-scorpion toxin is substantially accelerated at all poten

46 N-terminal loop preceding the alpha-helix in scorpion toxins is one of the determinative domains in t

47 to the N-terminal alpha-helix of BmBKTx1, a scorpion toxin isolated from the venom of the Asian scor

48 re that resembles that of the Cs alpha/alpha scorpion toxins kappa-hefutoxin, kappa-KTx1.3, and Om-to

49 We have identified a new scorpion toxin (kurtoxin) that binds to the alpha 1G T-t

50 microbial proteins within the superfamily of scorpion toxin-like proteins.

51 ly 2-fold increased sensitivity to the alpha-scorpion toxin LqhalphaIT.

52 tions at which it is specific for Kv1.3, the scorpion toxin margatoxin blocks most of the olfactory b

53 We recently reported the isolation of a scorpion toxin named U1-liotoxin-Lw1a (U1-LITX-Lw1a) tha

54 fine a three-point interaction site for beta-scorpion toxins on Na(V) channels.

55 upporting the two-binding-site hypothesis of scorpion toxins on RyRs.

56 used significant effects on binding of alpha-scorpion toxin or sea anemone toxin.

57 re not observed between ATX and either alpha-scorpion toxin or the pyrethroid deltamethrin.

58 of Lys-27, a residue highly conserved among scorpion toxins, points deep into the pore with its posi

59 channels and is thought to interact with the scorpion toxin residue, Lys27.

60 We and others have used scorpion toxin scaffolds to display and examine CD4 epit

61 designed using the alpha-KTx scaffold of 31 scorpion toxin sequences known or predicted to bind to p

62 conserved disulfide bridges with respect to scorpion toxin structure and function.

63 in mice by intraplantar injection in OD1, a scorpion toxin that potentiates hNaV1.7.

64 Chlorotoxin is a scorpion toxin that specifically binds to the surface of

65 n, we identified sequence resembling that in scorpion toxins that inhibit K(+) channels.

66 The ability of three structurally homologous scorpion toxins to block voltage-dependent K+ currents i

67 Binding of alpha- and beta-scorpion toxins to two distinct, pseudo-symmetrically or

68 Like the other alpha-scorpion toxins to which it is related, kurtoxin also in

69 g two amino acid substitutions into the beta scorpion toxin Ts1, we have chemically synthesized a nov

70 g toxins were synthesized as acceptors: beta-scorpion toxin (Ts1)-Bodipy, KIIIA-Bodipy, and GIIIA-Bod

71 scherichia coli and utilization of a labeled scorpion toxin was elaborated and applied to follow Kv1.

72 tes, iberiotoxin and charybdotoxin, peptidyl scorpion toxins, were both equally effective blockers of

73 ) channels are the molecular targets of beta-scorpion toxins, which shift the voltage dependence of a