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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 ) that bind to two different epitopes on the scorpion toxins.
6 ovides a functional link between DDH and ICK scorpion toxins.
7 ists that can prevent or reverse toxicity of 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 nel alone and in complex with a lethal alpha-scorpion toxin, AaH2, by electron microscopy, both at 3.
13   Highlighting the polypharmacology of alpha-scorpion toxins, AaH2 also targets an unanticipated rece
14                          An insect-selective scorpion toxin (AaIT5) was purified from the venom of th
15 ght into the voltage sensor-trapping mode of scorpion toxin action, define the position of the voltag
16 ge dependence of activation and enhance beta-scorpion toxin action.
17              However, in the presence of the scorpion toxin agitoxin II a total loss of (15)NH(4)(+)
18          The structurally well-characterized scorpion toxin Agitoxin2 inhibits ion permeation through
19  alpha/beta-scaffold characteristic of other scorpion toxins, although very likely forming an uncommo
20 ids of the IVS3-S4 loop participate in alpha-scorpion toxin and sea anemone toxin binding to overlapp
21 av1.8 has amino acid variants that bind bark scorpion toxins and inhibit Na(+) currents, blocking act
22                                        alpha-Scorpion toxins and sea anemone toxins bind to a common
23                                         Both scorpion toxins are putative mimics of the II-III loop p
24 -go-go (hEAG), as well as application of the scorpion toxin BeKm-1, we identified that the S5-pore li
25                                         beta-Scorpion toxins bind specifically to neurotoxin receptor
26                                    The alpha-scorpions toxins bind to the resting state of Na(+) chan
27 egment contribute to the difference in alpha-scorpion toxin binding affinity between cardiac and neur
28 idues in the IIS4 segment do not affect beta-scorpion toxin binding but alter voltage dependence of a
29                                        alpha-Scorpion toxin binding to wild type and E1613R had simil
30  IVS3 to Arg or His blocked measurable alpha-scorpion toxin binding, but did not affect the level of
31 d in tsA-201 cells and tested for 125I-alpha-scorpion toxin binding.
32            Kinetic analysis showed that beta-scorpion toxin binds to the resting state, and subsequen
33 s to determine the X-ray structure of native scorpion toxin BmBKTx1; direct methods were used for pha
34 ximately 40% in the presence of 100 nM alpha-scorpion toxin, but no allosteric enhancement was observ
35 nnel sequence had reduced affinity for alpha-scorpion toxin characteristic of cardiac Na+ channels.
36 cially at the carboxyl termini, with another scorpion toxin, charybdotoxin (ChTX), which blocks both
37                                          The scorpion toxin, Charybdotoxin (CTX), blocks homotetramer
38      Here, the binding modes of two selected scorpion toxins, charybdotoxin (ChTx) and OSK1, to human
39      The potent and Na(V) 1.6 selective beta-scorpion toxin Cn2 was used to assess the effect of Na(V
40                                     The beta-scorpion toxin, Cn2, is selective for Na(V) 1.6 in dorsa
41 ed to the refolding of denatured and reduced scorpion toxin Cn5.
42               Molecular determinants of beta-scorpion toxin (CssIV) binding and action on rat brain s
43 usly improved a natural amino-acid form of a scorpion toxin-derived CD4-mimetic peptide and in parall
44 hat similarity in the mechanism of action of scorpion toxins does not always follow from an overall s
45 helix rather than the beta sheets with which scorpion toxins form their interaction surface.
46                              Ts3 is an alpha scorpion toxin from the venom of the Brazilian scorpion
47 related members of the alpha-KTX15 family of scorpion toxins have been shown to block the A-type K+ c
48                                         beta-Scorpion toxins, including toxin IV from Centruroides su
49                      The effects of beta4 on scorpion toxin inhibition kinetics are explained by the
50  analysis of sodium channel chimeras, a beta-scorpion toxin is shown here to negatively shift voltage
51                        Dissociation of alpha-scorpion toxin is substantially accelerated at all poten
52 N-terminal loop preceding the alpha-helix in scorpion toxins is one of the determinative domains in t
53  to the N-terminal alpha-helix of BmBKTx1, a scorpion toxin isolated from the venom of the Asian scor
54 re that resembles that of the Cs alpha/alpha scorpion toxins kappa-hefutoxin, kappa-KTx1.3, and Om-to
55                     We have identified a new scorpion toxin (kurtoxin) that binds to the alpha 1G T-t
56 microbial proteins within the superfamily of scorpion toxin-like proteins.
57 ly 2-fold increased sensitivity to the alpha-scorpion toxin LqhalphaIT.
58 tions at which it is specific for Kv1.3, the scorpion toxin margatoxin blocks most of the olfactory b
59      We recently reported the isolation of a scorpion toxin named U1-liotoxin-Lw1a (U1-LITX-Lw1a) tha
60 fine a three-point interaction site for beta-scorpion toxins on Na(V) channels.
61 upporting the two-binding-site hypothesis of scorpion toxins on RyRs.
62 used significant effects on binding of alpha-scorpion toxin or sea anemone toxin.
63 re not observed between ATX and either alpha-scorpion toxin or the pyrethroid deltamethrin.
64  of Lys-27, a residue highly conserved among scorpion toxins, points deep into the pore with its posi
65 channels and is thought to interact with the scorpion toxin residue, Lys27.
66                      We and others have used scorpion toxin scaffolds to display and examine CD4 epit
67  designed using the alpha-KTx scaffold of 31 scorpion toxin sequences known or predicted to bind to p
68  conserved disulfide bridges with respect to scorpion toxin structure and function.
69  in mice by intraplantar injection in OD1, a scorpion toxin that potentiates hNaV1.7.
70                             Chlorotoxin is a scorpion toxin that specifically binds to the surface of
71 n, we identified sequence resembling that in scorpion toxins that inhibit K(+) channels.
72 The ability of three structurally homologous scorpion toxins to block voltage-dependent K+ currents i
73                   Binding of alpha- and beta-scorpion toxins to two distinct, pseudo-symmetrically or
74                         Like the other alpha-scorpion toxins to which it is related, kurtoxin also in
75 g two amino acid substitutions into the beta scorpion toxin Ts1, we have chemically synthesized a nov
76 g toxins were synthesized as acceptors: beta-scorpion toxin (Ts1)-Bodipy, KIIIA-Bodipy, and GIIIA-Bod
77 scherichia coli and utilization of a labeled scorpion toxin was elaborated and applied to follow Kv1.
78              Here, we describe a peptidergic scorpion toxin (WaTx) that activates TRPA1 by penetratin
79 tes, iberiotoxin and charybdotoxin, peptidyl scorpion toxins, were both equally effective blockers of
80 ) channels are the molecular targets of beta-scorpion toxins, which shift the voltage dependence of a