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1  affinity Kv1 channel antagonist, 125I-alpha-dendrotoxin.
2 s identical to a previously identified delta-dendrotoxin.
3 bolished by blocking Kv1 channels with alpha-dendrotoxin.
4 endent of firing, and is eliminated by alpha-dendrotoxin (0.1 microM), implicating slow inactivation
5                                              Dendrotoxin (1-300 nM; inhibits Kv1.1 and Kv1.2 channels
6  (10 muM) and margatoxin (10 muM) but not by dendrotoxin (100 nM), indicating that it arose from augm
7 ol/L, respectively, and insensitive to alpha-dendrotoxin (100 to 500 nmol/L), charybdotoxin (100 to 5
8 oimmunoprecipitation of radioiodinated alpha-dendrotoxin ((125)I-alphaDTX)-labelled VGKC complexes fr
9 haracteristic firing patterns, we used alpha-dendrotoxin (alpha-DTX) to eliminate the contribution of
10              In voltage clamp studies, alpha-dendrotoxin (alpha-DTX), a toxin with high specificity f
11 presence of 2 nM externally superfused alpha-dendrotoxin (alpha-DTX), or 50 nM superfused beta-BuTX,
12                                    The alpha-dendrotoxin (alpha-DTX)-sensitive current activated more
13                                    The alpha-dendrotoxin (alpha-DTX)-sensitive D-type K(+) current (I
14 e neurons expressed the transcripts of alpha-dendrotoxin (alpha-DTX)-sensitive, I(D) channel-forming
15 -aminopyridine (4-AP) and 0.5-1 microM alpha-dendrotoxin (alpha-DTX)] played a prominent role in sett
16 the functional interaction surfaces of delta-dendrotoxin and its voltage-gated potassium channel rece
17 (30 microM) and the selective peptide toxins dendrotoxin and mast cell degranulating peptide.
18 ndent potassium channel that is sensitive to dendrotoxin and mast cell degranulating peptide.
19 nt due to structural differences between the dendrotoxins and BPTI at the anti-protease loop; this ex
20 rative model building studies, involving the dendrotoxins and the proteinases, reveal that the key in
21 igh release probability, an insensitivity to dendrotoxin, and a lack of depolarization-induced presyn
22  is insensitive to tetraethylammonium, alpha-dendrotoxin, and E-4031.
23 tially by tetraethylammonium, charybdotoxin, dendrotoxin, and kaliotoxin.
24    Major secondary structural regions of the dendrotoxins are stable without much fluctuation during
25 onformation and protein folding of the three dendrotoxins are very similar to the published crystal s
26 nces of the three disulfides (in each of the dendrotoxins) are different from each other.
27 pyridine (4-AP, at micromolar levels), alpha-dendrotoxin at nanomolar levels, or blood-depressing sub
28                               That the delta-dendrotoxin binding site exists on separate K+ channel c
29 ory effects of these analogs on 125I-labeled dendrotoxin binding to rat brain membranes showed that r
30 annels and their ability to displace [(125)I]dendrotoxin binding to rat brain synaptosomal membranes.
31 nits and increase the number of cell surface dendrotoxin-binding sites when coexpressed with Kv1.2.
32                              We propose that dendrotoxin binds near the pore entryway but does not ac
33 d substitutions in ROMK1 indicate that delta-dendrotoxin binds to the pore region of ROMK1 even thoug
34                         To verify that delta-dendrotoxin blocks ROMK1 channels, a cDNA encoding the t
35             By contrast, inhibition by alpha-dendrotoxin did occur.
36 ent by low doses of 4-aminopyridine or alpha-dendrotoxin dramatically slows the falling phase of acti
37                                              Dendrotoxin (DTX) homologues are powerful blockers of K+
38 (from Kv1.1-1.6) determine susceptibility to dendrotoxin (DTX) homologues.
39 shold dynamics in layer 2-3 PNs, using alpha-dendrotoxin (DTX) or 4-aminopyridine (4-AP) to block the
40                               When bathed in dendrotoxin (DTX), most cells switched to tonic firing,
41              Three-dimensional structures of Dendrotoxin (DtX), Toxin-I (DpI), and Toxin-K (DpK) were
42 apezoid body (MNTB) revealed a low-threshold dendrotoxin (DTX)-sensitive current (ILT) and a high-thr
43 st with only minor differences, while larger dendrotoxin (DTX)-sensitive potassium currents were foun
44 e (4-AP) but not tetraethylammonium (TEA) or dendrotoxin (DTX).
45 ar to those of IKL, including sensitivity to dendrotoxin (DTX).
46 nel blockers 4-aminopyridine (4-AP) or alpha-dendrotoxin (DTX).
47 hannel current was blocked by 1 microM alpha-dendrotoxin (DTX); we also observed two other DTX-sensit
48  critical for high-affinity binding of snake dendrotoxins (DTX).
49 cal recordings reveal that recombinant delta-dendrotoxin has a half-maximal inhibition constant (Kd)
50                                  Mamba snake dendrotoxins have been used extensively in biochemical a
51              Low-voltage-activated Kv1-type (dendrotoxin-I sensitive) K+ currents increased in amplit
52                                              Dendrotoxin-I, a relatively specific blocker of Kv1.1, b
53 neurons in their amplitude or sensitivity to dendrotoxin-I, a selective K+ channel antagonist.
54  generation threshold by the activation of a dendrotoxin-I-sensitive, voltage-gated K(+) conductance.
55 ntibodies were detected using a (125)I-alpha-dendrotoxin immunoprecipitation assay in 38% of group A
56                   These results suggest that dendrotoxins inhibit K+ channels by recognizing the stru
57                 We report the isolation of a dendrotoxin inhibitor of ROMK1, a channel belonging to t
58 ed the action of the Kv1.1-selective blocker dendrotoxin K (DTX-K).
59                                              Dendrotoxin K (DTXK) is a 57-residue protein from mamba
60  was attenuated by the Kv1.1 channel blocker dendrotoxin K, suggesting an axonal origin.
61 ing Kv1.1 and Kv1.2 containing channels with dendrotoxin-K (DTX-K) and tityustoxin-Kalpha (TsTX-Kalph
62 v1.1 demonstrated that the mamba snake toxin dendrotoxin-K (DTX-K) blocked the Kv1.1 outward current
63 ially inhibited by 10 nM margatoxin or 10 nM dendrotoxin-K and blocked by 5 mM TEA(+).
64 ndrotoxin, margatoxin, and agitoxin, but not dendrotoxin-K or XE991.
65 ication of the K(v)1.1 selective antagonist, Dendrotoxin-K, in several L-DRG subclasses (L1, L2, L3,
66 r 100 nM iberiotoxin but unaffected by 10 nM dendrotoxin-K.
67 roteins that are complexed with (125)I-alpha-dendrotoxin-labelled potassium channels in brain extract
68 ibodies by immunoprecipitation of 125I-alpha-dendrotoxin-labelled rabbit brain K+ channels.
69 tibodies that immunoprecipitate (125)I-alpha-dendrotoxin-labelled voltage-gated potassium channels ex
70                       First, the toxin alpha-Dendrotoxin, like Charybdotoxin, is seen to attach to th
71 cy were occluded by the K+ channel blockers, dendrotoxin, margatoxin, and agitoxin, but not dendrotox
72 contrast, inhibiting Kv1 channels with alpha-dendrotoxin or maurotoxin strongly increased firing rate
73  subthreshold current was resistant to alpha-dendrotoxin, paxilline, apamin, and tetraethylammonium b
74 lockers, including tetraethylammonium, alpha-dendrotoxin, phrixotoxin-2, and BDS-I, did not mimic or
75                                              Dendrotoxin proteins isolated from Mamba snake venom blo
76               Application of apamin or alpha-dendrotoxin revealed late spikes in older bushy cells, s
77 ivated more rapidly than IKs; and (iv) alpha-dendrotoxin selectively blocked IKf.
78 ownregulation of a low-threshold, sustained, dendrotoxin-sensitive (DTX) potassium current, I(DS).
79 -1, P<0.05), and no 100- to 200-nmol/L alpha-dendrotoxin-sensitive current was found (n=8).
80 y of the axonal Kv1.1 channels that underlie dendrotoxin-sensitive D-type potassium current.
81 eature of auditory neurons, is regulated via dendrotoxin-sensitive low-threshold voltage-activated (L
82 ogical demonstration of the involvement of a dendrotoxin-sensitive potassium current in presynaptic i
83                            The low-threshold dendrotoxin-sensitive sustained potassium current (IDS)
84      In the mammalian hippocampal formation, dendrotoxin-sensitive voltage-gated K(+) (Kv) channels m
85                         Sensitivity to alpha-dendrotoxin suggests that Kv1-containing potassium chann
86 ase loop; this explains the inability of the dendrotoxins to inhibit proteinases.
87 osing the proposed active site region of the dendrotoxins to the anionic sites of the K+ channel rece
88 ndritic recordings, and focal application of dendrotoxin together indicate that the channels mediatin
89                                        delta-Dendrotoxin uses a triangular patch formed by seven side
90 ce calcium-dependent K+ channels), and alpha-dendrotoxin (voltage-sensitive K+ channels).
91 rom the CHO/K(V)1.3 cells, except that alpha-dendrotoxin was more potent at blocking binding to rat b
92 esults constrain the possible orientation of dendrotoxin with respect to the K(+) channel structure.