General Information of This Target
Target ID
BTDT00141
Target Name
Sodium channel protein type 9 subunit alpha (SCN9A)
Target Bioclass
Transporter and channel
Uniprot ID
Q15858
3D Structure
Download
2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
SCN9A
Gene ID
6335
Synonym
NENA; Neuroendocrine sodium channel; Peripheral sodium channel 1; Sodium channel protein type IX subunit alpha; Voltage-gated sodium channel subunit alpha Nav1.7
Sequence
MAMLPPPGPQSFVHFTKQSLALIEQRIAERKSKEPKEEKKDDDEEAPKPSSDLEAGKQLP
FIYGDIPPGMVSEPLEDLDPYYADKKTFIVLNKGKTIFRFNATPALYMLSPFSPLRRISI
KILVHSLFSMLIMCTILTNCIFMTMNNPPDWTKNVEYTFTGIYTFESLVKILARGFCVGE
FTFLRDPWNWLDFVVIVFAYLTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQ
SVKKLSDVMILTVFCLSVFALIGLQLFMGNLKHKCFRNSLENNETLESIMNTLESEEDFR
KYFYYLEGSKDALLCGFSTDSGQCPEGYTCVKIGRNPDYGYTSFDTFSWAFLALFRLMTQ
DYWENLYQQTLRAAGKTYMIFFVVVIFLGSFYLINLILAVVAMAYEEQNQANIEEAKQKE
LEFQQMLDRLKKEQEEAEAIAAAAAEYTSIRRSRIMGLSESSSETSKLSSKSAKERRNRR
KKKNQKKLSSGEEKGDAEKLSKSESEDSIRRKSFHLGVEGHRRAHEKRLSTPNQSPLSIR
GSLFSARRSSRTSLFSFKGRGRDIGSETEFADDEHSIFGDNESRRGSLFVPHRPQERRSS
NISQASRSPPMLPVNGKMHSAVDCNGVVSLVDGRSALMLPNGQLLPEVIIDKATSDDSGT
TNQIHKKRRCSSYLLSEDMLNDPNLRQRAMSRASILTNTVEELEESRQKCPPWWYRFAHK
FLIWNCSPYWIKFKKCIYFIVMDPFVDLAITICIVLNTLFMAMEHHPMTEEFKNVLAIGN
LVFTGIFAAEMVLKLIAMDPYEYFQVGWNIFDSLIVTLSLVELFLADVEGLSVLRSFRLL
RVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKIN
DDCTLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVYMMVMVIGNLVVL
NLFLALLLSSFSSDNLTAIEEDPDANNLQIAVTRIKKGINYVKQTLREFILKAFSKKPKI
SREIRQAEDLNTKKENYISNHTLAEMSKGHNFLKEKDKISGFGSSVDKHLMEDSDGQSFI
HNPSLTVTVPIAPGESDLENMNAEELSSDSDSEYSKVRLNRSSSSECSTVDNPLPGEGEE
AEAEPMNSDEPEACFTDGCVWRFSCCQVNIESGKGKIWWNIRKTCYKIVEHSWFESFIVL
MILLSSGALAFEDIYIERKKTIKIILEYADKIFTYIFILEMLLKWIAYGYKTYFTNAWCW
LDFLIVDVSLVTLVANTLGYSDLGPIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPS
IMNVLLVCLIFWLIFSIMGVNLFAGKFYECINTTDGSRFPASQVPNRSECFALMNVSQNV
RWKNLKVNFDNVGLGYLSLLQVATFKGWTIIMYAAVDSVNVDKQPKYEYSLYMYIYFVVF
IIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRP
GNKIQGCIFDLVTNQAFDISIMVLICLNMVTMMVEKEGQSQHMTEVLYWINVVFIILFTG
ECVLKLISLRHYYFTVGWNIFDFVVVIISIVGMFLADLIETYFVSPTLFRVIRLARIGRI
LRLVKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEDGINDMFN
FETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPKKVHPGSSVEGDCGNPSVGIFYF
VSYIIISFLVVVNMYIAVILENFSVATEESTEPLSEDDFEMFYEVWEKFDPDATQFIEFS
KLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDSLR
SQMEERFMSANPSKVSYEPITTTLKRKQEDVSATVIQRAYRRYRLRQNVKNISSIYIKDG
DRDDDLLNKKDMAFDNVNENSSPEKTDATSSTTSPPSYDSVTKPDKEKYEQDRTEKEDKG
KDSKESKK

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Family
the sodium channel (TC 1.A.1.10) family
Function
Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain.

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Taxonomy ID
9606
TCDB ID
1.A.1.10.5
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Primates
Family: Hominidae
Genus: Homo
Species: Homo sapiens
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Kappa-actitoxin-Avd4a Effective concentration 50
3 nM
[1- 5]
 Toxin Info    Delta/kappa-actitoxin-Avd4a Effective concentration 50
3 nM
[4- 10]
 Toxin Info    Alpha-mammal toxin AaH2 Effective concentration 50
6.8 nM
[11- 20]
 Toxin Info    Alpha-mammal toxin AnCra1 Effective concentration 50
136.7 nM
[21]
 Toxin Info    Nemertide alpha-2 Effective concentration 50
1.2967 μM
[22], [23]
 Toxin Info    Delta-conotoxin PVIA Effective concentration 50
1.9 μM
[24], [25], [26], [27]
 Toxin Info    O- MrVIA IC50
5.5 ± 0.9 mM
[28]
 Toxin Info    AM-8145-6 IC50
0.2 nM
[29]
 Toxin Info    AM-8145-9 IC50
0.2 nM
[29]
 Toxin Info    Pn3a-D8N IC50
0.2 nM
[30]
 Toxin Info    AM-8145-22 IC50
0.26 nM
[29]
 Toxin Info    AM-2752 IC50
0.3 nM
[29]
 Toxin Info    AM-5695 IC50
0.3 nM
[29]
 Toxin Info    AM-8145-33 IC50
0.3 nM
[29]
 Toxin Info    AM-8145-7 IC50
0.3 nM
[29]
 Toxin Info    Pn3a-D1K IC50
0.3 nM
[30]
 Toxin Info    Pn3a-D8K IC50
0.3 nM
[30]
 Toxin Info    AM-8145 IC50
0.5 nM
[29]
 Toxin Info    AM-8145-37 IC50
0.5 nM
[29]
 Toxin Info    AM-8145-4 IC50
0.5 nM
[29]
 Toxin Info    AM-8145-14 IC50
0.6 nM
[29]
 Toxin Info    AM-8145-8 IC50
0.6 nM
[29]
 Toxin Info    JZTx-V IC50
0.6 nM
[29]
 Toxin Info    E1A,E4A,Y33W IC50
0.6 ± 0.1 nM
[31]
 Toxin Info    AM0422 IC50
0.8 nM
[29]
 Toxin Info    AM-6120 IC50
0.8 nM
[29]
 Toxin Info    HwTx-IV (E1G,E4G,K18A) IC50
0.8 ± 1.1 nM
[31]
 Toxin Info    HwTx-IV (E4K,R26A,Y33W) IC50
0.9 ± 1.1 nM
[31]
 Toxin Info    AM-1647 IC50
1 nM
[29]
 Toxin Info    AM-8145-32 IC50
1 nM
[29]
 Toxin Info    AM-8145-34 IC50
1 nM
[29]
 Toxin Info    Pn3a-E10K IC50
1 nM
[30]
 Toxin Info    Pn3a-K24R IC50
1 nM
[30]
 Toxin Info    AM-8145-1 IC50
1.1 nM
[29]
 Toxin Info    AM-8145-30 IC50
1.1 nM
[29]
 Toxin Info    AM-8145-31 IC50
1.1 nM
[29]
 Toxin Info    AM-8145-13 IC50
1.3 nM
[29]
 Toxin Info    AM-8145-38 IC50
1.3 nM
[29]
 Toxin Info    AM-8145-5 IC50
1.6 nM
[29]
 Toxin Info    E1A,E4A,des (S19,S20),Y33W IC50
1.6 ± 0.3 nM
[31]
 Toxin Info    HwTx-IV (E4G) IC50
1.6 ± 1.1 nM
[31]
 Toxin Info    AM-8145-2 IC50
1.7 nM
[29]
 Toxin Info    E1G,E4G,des (S19,S20),Y33W IC50
1.7 ± 0.4 nM
[31]
 Toxin Info    [R26A]gHwTx-IV IC50
1.7 ± 0.5 nM
[32]
 Toxin Info    GPTX1 (Phe5 Met) IC50
2 nM
[33]
 Toxin Info    Pn3a-E13K IC50
2 nM
[30]
 Toxin Info    HwTx-IV (E1G,E4G) IC50
2.0 ± 1.1 nM
[31]
 Toxin Info    Mu-theraphotoxin-Tp1a IC50
2.1 nM
[34]
 Toxin Info    AM-8145-36 IC50
2.5 nM
[29]
 Toxin Info    E1A,E4A IC50
2.8 ± 1.3 nM
[31]
 Toxin Info    AM-8145-3 IC50
3 nM
[29]
 Toxin Info    AM-8145-25 IC50
3.1 nM
[29]
 Toxin Info    m3-HwTx-IV IC50
3.3 ± 1.1 nM
[32]
 Toxin Info    HwTx-IV (E4K,R26Q) IC50
3.6 ± 1.1 nM
[31]
 Toxin Info    PTx2-3258 IC50
3.8 nM
[35]
 Toxin Info    Pn3a IC50
4 nM
[30]
 Toxin Info    Pn3a-D8G IC50
4 nM
[30]
 Toxin Info    GPTX1 (Phe5 Leu) IC50
5 nM
[33]
 Toxin Info    PTx2-3128 IC50
5 nM
[36]
 Toxin Info    rHwTx-IV (S25A) IC50
5.1 ± 0.2 nM
[31]
 Toxin Info    Mu/omega-theraphotoxin-Pmu1a IC50
5.5 - 7 nM
[37]
 Toxin Info    AM-8145-35 IC50
5.7 nM
[29]
 Toxin Info    rHwTx-IV (D14A) IC50
5.9 ± 0.01 nM
[31]
 Toxin Info    E1A IC50
6 ± 1 nM
[31]
 Toxin Info    rHwTx-IV (P11A) IC50
6.0 ± 0.1 nM
[31]
 Toxin Info    rHwTx-IV (L22A) IC50
6.1 ± 0.01 nM
[31]
 Toxin Info    rHwTx-IV (Y33A) IC50
6.1 ± 0.03 nM
[31]
 Toxin Info    rHwTx-IV (I35A) IC50
6.2 ± 0.06 nM
[31]
 Toxin Info    rHwTx-IV (F6A) IC50
6.3 ± 0.04 nM
[31]
 Toxin Info    rHwTx-IV (G36A) IC50
6.4 ± 0.02 nM
[31]
 Toxin Info    HwTx-IV (K18A) IC50
6.4 ± 1.1 nM
[31]
 Toxin Info    rHwTx-IV (L3A) IC50
6.6 ± 0.1 nM
[31]
 Toxin Info    rHwTx-IV (K27A) IC50
6.7 ± 0.03 nM
[31]
 Toxin Info    AM-8145-19 IC50
6.8 nM
[29]
 Toxin Info    rHwTx-IV (K7A) IC50
6.8 ± 0.08 nM
[31]
 Toxin Info    PTx2-3127 IC50
6.9 nM
[36]
 Toxin Info    rHwTx-IV (R26A) IC50
6.9 ± 0.04 nM
[31]
 Toxin Info    rHwTx-IV (K21A) IC50
6.9 ± 0.06 nM
[31]
 Toxin Info    rHwTx-IV (V23A) IC50
6.9 ± 0.07 nM
[31]
 Toxin Info    HwTx-IV (E1G) IC50
6.9 ± 1.1 nM
[31]
 Toxin Info    rHwTx-IV (S19A) IC50
7.0 ± 0.05 nM
[31]
 Toxin Info    rHwTx-IV (N13A) IC50
7.0 ± 0.1 nM
[31]
 Toxin Info    rHwTx-IV (K37A) IC50
7.0 ± 0.10 nM
[31]
 Toxin Info    rHwTx-IV (S12A) IC50
7.0 ± 0.13 nM
[31]
 Toxin Info    rHwTx-IV (N10A) IC50
7.0 ± 0.14 nM
[31]
 Toxin Info    rHwTx-IV (Q34A) IC50
7.1 ± 0.03 nM
[31]
 Toxin Info    rHwTx-IV (I5A) IC50
7.1 ± 0.08 nM
[31]
 Toxin Info    rHwTx-IV (S20A) IC50
7.2 ± 0.08 nM
[31]
 Toxin Info    rHwTx-IV (T28A) IC50
7.2 ± 0.13 nM
[31]
 Toxin Info    rHwTx-IV (K18A) IC50
7.3 ± 0.04 nM
[31]
 Toxin Info    rHwTx-IV (R29A) IC50
7.3 ± 0.04 nM
[31]
 Toxin Info    rHwTx-IV (Q15A) IC50
7.3 ± 0.13 nM
[31]
 Toxin Info    gHwTx-IV IC50
7.6 ± 1.5 nM
[32]
 Toxin Info    [R29A]gHwTx-IV IC50
7.7 ± 2.6 nM
[32]
 Toxin Info    PTx2-3361 IC50
8.6 nM
[35]
 Toxin Info    AM-8145-26 IC50
8.9 nM
[29]
 Toxin Info    GPTX1 (Phe5 Gly) IC50
9 nM
[33]
 Toxin Info    GPTX1 (Phe5 Ile) IC50
9 nM
[33]
 Toxin Info    des (S19,S20) IC50
9 ± 2 nM
[31]
 Toxin Info    Huwentoxin-IV IC50
9.6 - 33 nM
[31- 52]
 Toxin Info    HwTx-IV (E4K,CterCOOH) IC50
11.9 ± 1.1 nM
[31]
 Toxin Info    Pn3a-E13A IC50
12 nM
[30]
 Toxin Info    AM-8145-18 IC50
12.6 nM
[29]
 Toxin Info    HwTx-IV (E4K) IC50
14.2 ± 1.2 nM
[31]
 Toxin Info    HwTx-IV (E4G,CterCOOH) IC50
14.9 ± 1.1 nM
[31]
 Toxin Info    AM-8145-23 IC50
15 nM
[29]
 Toxin Info    Beta-theraphotoxin-Cd1a IC50
16 nM
[53]
 Toxin Info    AM-6122 IC50
16.4 nM
[29]
 Toxin Info    HWTX-IV IC50
17 nM
[31]
 Toxin Info    [R26A]gHwTx-IV IC50
18.7 ± 4.3 nM
[32]
 Toxin Info    AM-8145-27 IC50
19 nM
[29]
 Toxin Info    GPTX1 (Phe5 Val) IC50
19 nM
[33]
 Toxin Info    AM-8145-29 IC50
19.6 nM
[29]
 Toxin Info    PTx2-2 IC50
20 ± 2 nM
[54]
 Toxin Info    PTx2-3260 IC50
20.8 nM
[35]
 Toxin Info    AM-8145-11 IC50
22 nM
[29]
 Toxin Info    AM-8145-12 IC50
22 nM
[29]
 Toxin Info    HwTx-IV (Y33W) IC50
22.2 ± 1.2 nM
[31]
 Toxin Info    AM-8145-28 IC50
24 nM
[29]
 Toxin Info    Pn3a-K22R IC50
24 nM
[30]
 Toxin Info    Mu-scoloptoxin(03)-Ssm2a IC50
25.4 nM
[33- 56]
 Toxin Info    E4A IC50
26 ± 9 nM
[31]
 Toxin Info    GPTX1 (Phe5Ala) IC50
27 nM
[57]
 Toxin Info    PTx2-3 IC50
27 ± 8 nM
[54]
 Toxin Info    HwTx-IV (K36,CterCOOH) IC50
29.0 ± 1.2 nM
[31]
 Toxin Info    PTx2-17 IC50
30 ± 8 nM
[54]
 Toxin Info    PTx2-3066 IC50
30.8 nM
[35]
 Toxin Info    mHwTx-IV IC50
30.8 ± 5.2 nM
[31]
 Toxin Info    AM-8145-20 IC50
32 nM
[29]
 Toxin Info    PTx2-1 IC50
32 ± 16 nM
[54]
 Toxin Info    PTx2-3259 IC50
41.8 nM
[36]
 Toxin Info    PTx2-5 IC50
42 ± 5 nM
[54]
 Toxin Info    PTx2-4 IC50
43 ± 10 nM
[54]
 Toxin Info    ProTX-11 IC50
44 ± 7 nM
[54]
 Toxin Info    PhlTx1-D7A IC50
47.0 ± 40.9 nM
[58]
 Toxin Info    PTx2-3067 IC50
48.3 nM
[36]
 Toxin Info    GPTX1 (Ile10His) IC50
50 nM
[57]
 Toxin Info    GPTX1 (Ile10Ser) IC50
50 nM
[57]
 Toxin Info    PTx2-3064 IC50
52.6 nM
[35]
 Toxin Info    Mu-theraphotoxin-Os1a IC50
52.7 - 129.5 nM
[59]
 Toxin Info    P[G5]K IC50
58 nM
[60]
 Toxin Info    P[G6]K IC50
61 nM
[60]
 Toxin Info    PTx2-6 IC50
63 ± 7 nM
[54]
 Toxin Info    PTx2-18 IC50
64 ± 12 nM
[54]
 Toxin Info    AM-8145-10 IC50
71 nM
[29]
 Toxin Info    PTx2-3065 IC50
73.9 nM
[35]
 Toxin Info    PTx2-7 IC50
74 ± 5 nM
[54]
 Toxin Info    PTx2-19 IC50
76 ± 23 nM
[54]
 Toxin Info    Pn3a-K24A IC50
84 nM
[30]
 Toxin Info    PTx2-20 IC50
84 ± 16 nM
[54]
 Toxin Info    GPTX1 (Pro19Ala) IC50
90 nM
[61]
 Toxin Info    GPTX1 (Ile10Glu) IC50
90 nM
[57]
 Toxin Info    GPTX1 (Ile10Met) IC50
90 nM
[57]
 Toxin Info    PTx2-8 IC50
91 ± 11 nM
[54]
 Toxin Info    PTx2-21 IC50
91 ± 24 nM
[54]
 Toxin Info    P[G7]K IC50
94 nM
[60]
 Toxin Info    PTx2-9 IC50
97 ± 17 nM
[54]
 Toxin Info    PTx2-10 IC50
99 ± 11 nM
[54]
 Toxin Info    GPTX1 (Asp1Ala) IC50
100 nM
[33]
 Toxin Info    GPTX1 (Ile10Thr) IC50
100 nM
[57]
 Toxin Info    GPTX1 (Ile10Val) IC50
100 nM
[57]
 Toxin Info    PTx2-22 IC50
109 ± 8 nM
[54]
 Toxin Info    GPTX1 (Ile10Phe) IC50
110 nM
[57]
 Toxin Info    Mu-theraphotoxin-Hd1a IC50
111 nM
[62]
 Toxin Info    HwTx-IV (R26A) IC50
111.7 ± 1.2 nM
[31]
 Toxin Info    P[G8]K IC50
112 nM
[60]
 Toxin Info    PTx2-11 IC50
113 ± 10 nM
[54]
 Toxin Info    HwTx-IV (T28W) IC50
114.1 ± 1.2 nM
[31]
 Toxin Info    GPTX1 (Asp12Ala) IC50
120 nM
[63]
 Toxin Info    GPTX1 (Arg18Ala) IC50
130 nM
[64]
 Toxin Info    GPTX1 (Ile10Leu) IC50
140 nM
[57]
 Toxin Info    GPTX1 (Ile10Tyr) IC50
140 nM
[57]
 Toxin Info    HwTx-IV (R26Q) IC50
141.4 ± 1.1 nM
[31]
 Toxin Info    P[G4]K IC50
148 nM
[60]
 Toxin Info    [G2]KIIIA IC50
154 nM
[60]
 Toxin Info    PTx2-3063 IC50
154 nM
[35]
 Toxin Info    [G4]KIIIA IC50
169 nM
[60]
 Toxin Info    GPTX1 (Pro11Ala) IC50
170 nM
[65]
 Toxin Info    GPTX1 (Val33Ala) IC50
170 nM
[66]
 Toxin Info    PhlTx1-A1Z IC50
171.5 ± 51.0 nM
[58]
 Toxin Info    HwTx-IV (CterCOOH) IC50
176.3 ± 1.1 nM
[31]
 Toxin Info    PhlTx1-S8A IC50
179.5 ± 118.4 nM
[58]
 Toxin Info    AM-8145-21 IC50
182 nM
[29]
 Toxin Info    PTx2-12 IC50
183 ± 34 nM
[54]
 Toxin Info    PTx2-2955 IC50
185 nM
[35]
 Toxin Info    [G3]KIIIA IC50
190 nM
[60]
 Toxin Info    GPTX1 (Asn13Ala) IC50
190 nM
[63]
 Toxin Info    GPTX1 (Leu21Ala) IC50
190 nM
[67]
 Toxin Info    GPTX1 (Ile10 2-Pal) IC50
190 nM
[57]
 Toxin Info    GPTX1 (Ile10Ala) IC50
210 nM
[65]
 Toxin Info    PTx2-13 IC50
218 ± 12 nM
[54]
 Toxin Info    GPTX1 (Ile10Asp) IC50
220 nM
[57]
 Toxin Info    PTx2-14 IC50
225 ± 32 nM
[54]
 Toxin Info    GPTX1 (Lys15Ala) IC50
230 nM
[64]
 Toxin Info    PTx2-15 IC50
232 ± 22 nM
[54]
 Toxin Info    [G5]PaurTx3 IC50
239 nM
[60]
 Toxin Info    PTx2-23 IC50
240 ± 49 nM
[54]
 Toxin Info    PhlTx1-K12A IC50
252.5 ± 13.6 nM
[58]
 Toxin Info    PTx2-16 IC50
253 ± 45 nM
[54]
 Toxin Info    Mu-theraphotoxin-Pspp1 IC50
254.3 ± 147.6 nM
[58]
 Toxin Info    GPTX1 (Thr26Ala) IC50
260 nM
[68]
 Toxin Info    GPTX1 (Gly4Ala) IC50
270 nM
[69]
 Toxin Info    GPTX1 (Ile10 4-CO2-F) IC50
280 nM
[57]
 Toxin Info    PaurTx3 IC50
290 nM
[60]
 Toxin Info    GPTX1 (Arg25Ala) IC50
330 nM
[70]
 Toxin Info    GPTX1 (Ile10Asn) IC50
330 nM
[57]
 Toxin Info    Mu-theraphotoxin-Phlo2a IC50
333 nM
[71]
 Toxin Info    P[G3]K IC50
342 nM
[60]
 Toxin Info    Delta-theraphotoxin-Cg1a 2 IC50
348 nM
[72- 78]
 Toxin Info    Delta-theraphotoxin-Cg1a 3 IC50
348 nM
[72- 78]
 Toxin Info    Delta-theraphotoxin-Cg1a 1 IC50
348 nM
[73- 79]
 Toxin Info    PaurTX3[LPATGG] IC50
359 nM
[60]
 Toxin Info    Mu-theraphotoxin-Phlo1b IC50
360 nM
[71]
 Toxin Info    KIIIA IC50
363 nM
[60]
 Toxin Info    [G5]KIIIA IC50
369 nM
[60]
 Toxin Info    GPTX1 (N-Term. Ala) IC50
370 nM
[33]
 Toxin Info    GPTX1 (Val22Ala) IC50
380 nM
[67]
 Toxin Info    [G6]KIIIA IC50
390 nM
[60]
 Toxin Info    GPTX1 (C-Term. -Ala) IC50
410 nM
[80]
 Toxin Info    GPTX1 (Leu3Ala) IC50
430 nM
[69]
 Toxin Info    GPTX1 (Met6Ala) IC50
430 nM
[81]
 Toxin Info    Voltage sensor toxin 3 IC50
430 nM
[82]
 Toxin Info    Voltage sensor toxin 3 IC50
430 nM
[83]
 Toxin Info    Mu-theraphotoxin-Phlo1a IC50
459 nM
[71]
 Toxin Info    GPTX1 (Lys28Ala) IC50
470 nM
[84]
 Toxin Info    GPTX1 (Ser24Ala) IC50
470 nM
[70]
 Toxin Info    AM-8145-16 IC50
471 nM
[29]
 Toxin Info    GPTX1 (Lys8Ala) IC50
500 nM
[85]
 Toxin Info    AM-8145-17 IC50
540 nM
[29]
 Toxin Info    Mu-theraphotoxin-Cg1a IC50
610 nM
[72- 87]
 Toxin Info    GPTX1 (Phe5Ala) IC50
630 nM
[81]
 Toxin Info    P[G2]K IC50
682 nM
[60]
 Toxin Info    GPTX1 (Asn20Ala) IC50
690 nM
[61]
 Toxin Info    GPTX1 (Ile10His) IC50
700 nM
[57]
 Toxin Info    PhlTx1-K15A IC50
706.4 ± 87.8 nM
[58]
 Toxin Info    GPTX1 (Tyr32Ala) IC50
800 nM
[88]
 Toxin Info    K[G5]PaurTx3 IC50
813 nM
[60]
 Toxin Info    AM-8145-15 IC50
825 nM
[29]
 Toxin Info    [G7]KIIIA IC50
860 nM
[60]
 Toxin Info    [G8]KIIIA IC50
920 nM
[60]
 Toxin Info    GPTX1 (Arg7-Ala) IC50
940 nM
[85]
 Toxin Info    GPTX1 (His27Ala) IC50
970 nM
[68]
 Toxin Info    PhlTx1-K25A IC50
> 10 μM
[58]
 Toxin Info    PhlTx1-W24A IC50
> 10 μM
[58]
 Toxin Info    PhlTx1-Y26A IC50
> 10 μM
[58]
 Toxin Info    AM-8145-24 IC50
>1 μM
[29]
 Toxin Info    Pn3a-D12T IC50
>1 μM
[30]
 Toxin Info    Pn3a-D14K IC50
>1 μM
[30]
 Toxin Info    Pn3a-K22A IC50
>1 μM
[30]
 Toxin Info    Pn3a-K24D IC50
>1 μM
[30]
 Toxin Info    Pn3a-W30A IC50
>1 μM
[30]
 Toxin Info    Pn3a-Y27A IC50
>1 μM
[30]
 Toxin Info    Hhn2b (G7W,N24S,W29A) IC50
>10 μM
[89]
 Toxin Info    Hhn2b (K4L) IC50
>10 μM
[89]
 Toxin Info    Hhn2b (V32W) IC50
>10 μM
[89]
 Toxin Info    HNTX-I IC50
>10 μM
[90]
 Toxin Info    HNTXI (E1G) IC50
>10 μM
[90]
 Toxin Info    HNTX-III (Gly4delete) IC50
>10 μM
[91]
 Toxin Info    HNTX-III (His26Lys) IC50
>10 μM
[91]
 Toxin Info    HNTX-III (Leu33Glu) IC50
>10 μM
[91]
 Toxin Info    HNTX-III (Leu33Lys) IC50
>10 μM
[91]
 Toxin Info    HNTX-III (Lys30Arg) IC50
>10 μM
[91]
 Toxin Info    HNTXI (L32W) IC50
>10 μM
[90]
 Toxin Info    Ca2a-T4 IC50
>100 μM
[92]
 Toxin Info    Ca2a-T5 IC50
>100 μM
[92]
 Toxin Info    Ca2a-T6 IC50
>100 μM
[92]
 Toxin Info    Ca2a-T7 IC50
>100 μM
[92]
 Toxin Info    Ca2a-T8 IC50
>100 μM
[92]
 Toxin Info    GPTX1 (Lys31Trp) IC50
>4.9 μM
[57]
 Toxin Info    GPTX1 (Met6Arg) IC50
>4.9 μM
[57]
 Toxin Info    GPTX1 (Tyr32Lys) IC50
>4.9 μM
[57]
 Toxin Info    GPTX1 (His27Glu) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Lys31Ala) IC50
>5 μM
[88]
 Toxin Info    GPTX1 (Lys31Glu) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Met6Lys) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Phe34Glu) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Phe34Lys) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Phe5Glu) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Ser24Glu) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Trp29Ala) IC50
>5 μM
[84]
 Toxin Info    GPTX1 (Trp29Arg) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Trp29Glu) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Trp29Lys) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Tyr32Glu) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Ile10Asn) IC50
>5 μM
[57]
 Toxin Info    GPTX1 (Ile10Asp) IC50
>5 μM
[57]
 Toxin Info    Ca2a-U1S IC50
>50 μM
[92]
 Toxin Info    K0G1-P18K-A21L-V IC50
0.007 ± 0.001 μM
[91]
 Toxin Info    P18K-A21L-V IC50
0.013 ± 0.002 μM
[91]
 Toxin Info    K0G1-N19L-A21L-V IC50
0.017 ± 0.005 μM
[91]
 Toxin Info    K0L1-P18K-A21L-L IC50
0.022 ± 0.003 μM
[91]
 Toxin Info    K0G1-A21L-V IC50
0.027 ± 0.007 μM
[91]
 Toxin Info    GPTX1 (Leu3Arg) IC50
0.03 ± 0 μM
[57]
 Toxin Info    GPTX1 (Met6Trp) IC50
0.03 ± 0.02 μM
[57]
 Toxin Info    HNTXI (E1G,N23S,D26H,L32W) IC50
0.036 ± 0.007 μM
[90]
 Toxin Info    GPTX1 (Thr26Arg) IC50
0.04 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Thr26Lys) IC50
0.04 ± 0.01 μM
[57]
 Toxin Info    K0G1-P18K-A21V IC50
0.040 ± 0.006 μM
[91]
 Toxin Info    A21L-V IC50
0.047 ± 0.016 μM
[91]
 Toxin Info    K0K1-N19L-A21L-L IC50
0.048 ± 0.022 μM
[91]
 Toxin Info    GPTX1 (Gly4Trp) IC50
0.05 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Val33Trp) IC50
0.05 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (C-Term. -Trp) IC50
0.05 ± 0.02 μM
[57]
 Toxin Info    GPTX1 (Thr26Trp) IC50
0.05 ± 0.02 μM
[57]
 Toxin Info    GPTX1 (Val33Lys) IC50
0.05 ± 0.02 μM
[57]
 Toxin Info    HNTX-III (Pro18Lys) IC50
0.050 ± 0.002 μM
[91]
 Toxin Info    GPTX1 (Asp12Trp) IC50
0.06 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Val22Arg) IC50
0.06 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Val22Trp) IC50
0.06 ± 0.03 μM
[57]
 Toxin Info    GPTX1 (Asp1Trp) IC50
0.07 ± 0.02 μM
[57]
 Toxin Info    GPTX1 (Pro19Arg) IC50
0.07 ± 0.02 μM
[57]
 Toxin Info    GPTX1 (Asn20Trp) IC50
0.07 ± 0.03 μM
[57]
 Toxin Info    HNTXI (N23S,D26H,L32W) IC50
0.071 ± 0.005 μM
[90]
 Toxin Info    HNTX-III (Tyr32Trp) IC50
0.075 ± 0.016 μM
[91]
 Toxin Info    HNTXI (N23S,D26H) IC50
0.079 ± 0.004 μM
[90]
 Toxin Info    GPTX1 (Pro11Trp) IC50
0.08 ± 0 μM
[57]
 Toxin Info    GPTX1 (Asn13Trp) IC50
0.08 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Val33Arg) IC50
0.08 ± 0.01 μM
[57]
 Toxin Info    HNTX-III (Lys0Gly1) IC50
0.086 ± 0.012 μM
[91]
 Toxin Info    K0G1-P18K-A21L-L IC50
0.087 ± 0.017 μM
[91]
 Toxin Info    GPTX-1 IC50
0.09 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Tyr32Trp) IC50
0.09 ± 0.02 μM
[57]
 Toxin Info    GPTX1 (Lys28Arg) IC50
0.09 ± 0.03 μM
[57]
 Toxin Info    GPTX1 (Ile10Glu) IC50
0.09 ± 0.06 μM
[57]
 Toxin Info    HNTX-III (Asn19Leu) IC50
0.092 ± 0.046 μM
[91]
 Toxin Info    HNTX-III (Ala21Val) IC50
0.099 ± 0.019 μM
[91]
 Toxin Info    GPTX1 (Asp12Arg) IC50
0.11 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Asp1Arg) IC50
0.11 ± 0.03 μM
[57]
 Toxin Info    GPTX1 (Leu21Trp) IC50
0.11 ± 0.03 μM
[57]
 Toxin Info    K0K1-P18K-A21L-L IC50
0.112 ± 0.027 μM
[91]
 Toxin Info    GPTX1 (Asp12Lys) IC50
0.12 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Pro19Lys) IC50
0.12 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (N-Term. Lys) IC50
0.12 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Leu3Lys) IC50
0.12 ± 0.05 μM
[57]
 Toxin Info    K0G1-N19L-A21L-L IC50
0.121 ± 0.010 μM
[91]
 Toxin Info    HNTX-III (Pro11Lys) IC50
0.127 ± 0.026 μM
[91]
 Toxin Info    GPTX1 (Ile10Trp) IC50
0.13 ± 0 μM
[57]
 Toxin Info    GPTX1 (C-Term. -Arg) IC50
0.13 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Lys8Arg) IC50
0.13 ± 0.05 μM
[57]
 Toxin Info    HNTX-III (Ala21Leu) IC50
0.133 ± 0.010 μM
[91]
 Toxin Info    GPTX1 (Asn13Arg) IC50
0.14 ± 0.03 μM
[57]
 Toxin Info    HNTX-III (Lys0Leu1) IC50
0.145 ± 0.049 μM
[91]
 Toxin Info    GPTX1 (Asp1Lys) IC50
0.15 ± 0.02 μM
[57]
 Toxin Info    HNTX-III (Gly1Lys) IC50
0.150 ± 0.024 μM
[91]
 Toxin Info    HNTX-III (Gly6Trp) IC50
0.167 ± 0.017 μM
[91]
 Toxin Info    GPTX1 (Asn20Arg) IC50
0.17 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (N-Term. Arg) IC50
0.17 ± 0.06 μM
[57]
 Toxin Info    GPTX1 (Ile10Arg) IC50
0.17 ± 0.11 μM
[57]
 Toxin Info    HNTXI (E1G,N23S,D26H) IC50
0.179 ± 0.024 μM
[90]
 Toxin Info    GPTX1 (Arg18Trp) IC50
0.18 ± 0.04 μM
[57]
 Toxin Info    GPTX1 (N-Term. Trp) IC50
0.20 ± 0.06 μM
[57]
 Toxin Info    GPTX1 (Phe5Trp) IC50
0.20 ± 0.08 μM
[57]
 Toxin Info    GPTX1 (Val22Lys) IC50
0.20 ± 0.12 μM
[57]
 Toxin Info    GPTX1 (Asn13Lys) IC50
0.21 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Gly4Lys) IC50
0.21 ± 0.04 μM
[57]
 Toxin Info    HNTX-III IC50
0.211 ± 0.049 μM
[91]
 Toxin Info    HNTX-III (Leu33Phe) IC50
0.215 ± 0.029 μM
[91]
 Toxin Info    GPTX1 (Arg18Glu) IC50
0.22 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Asp1Glu) IC50
0.22 ± 0.05 μM
[57]
 Toxin Info    GPTX1 (Pro11Glu) IC50
0.22 ± 0.12 μM
[57]
 Toxin Info    GPTX1 (Lys15Arg) IC50
0.22 ± 0.14 μM
[57]
 Toxin Info    HNTX-III (Pro18Trp) IC50
0.225 ± 0.027 μM
[91]
 Toxin Info    GPTX1 (Ile10Lys) IC50
0.23 ± 0.01 μM
[57]
 Toxin Info    GPTX1 (Gly4Arg) IC50
0.23 ± 0.06 μM
[57]
 Toxin Info    HNTX-III (Pro18Leu) IC50
0.255 ± 0.078 μM
[91]
 Toxin Info    GPTX1 (N-Term. Glu) IC50
0.27 ± 0.03 μM
[57]
 Toxin Info    GPTX1 (Phe34Trp) IC50
0.27 ± 0.04 μM
[57]
 Toxin Info    GPTX1 (Asn13Glu) IC50
0.28 ± 0.03 μM
[57]
 Toxin Info    GPTX1 (Asp12Glu) IC50
0.28 ± 0.05 μM
[57]
 Toxin Info    HNTX-III (Gly1Phe) IC50
0.282 ± 0.056 μM
[91]
 Toxin Info    GPTX1 (His27Trp) IC50
0.32 ± 0 μM
[57]
 Toxin Info    GPTX1 (Lys28Glu) IC50
0.34 ± 0.08 μM
[57]
 Toxin Info    GPTX1 (Arg18Lys) IC50
0.36 ± 0.09 μM
[57]
 Toxin Info    GPTX1 (Arg25Lys) IC50
0.38 ± 0.23 μM
[57]
 Toxin Info    HNTX-III (Asn19Lys) IC50
0.431 ± 0.058 μM
[91]
 Toxin Info    HNTXI (N23S) IC50
0.435 ± 0.072 μM
[90]
 Toxin Info    Hhn2b (G7W,N24S) IC50
0.44 ± 0.04 μM
[89]
 Toxin Info    GPTX1 (His27Arg) IC50
0.45 ± 0.06 μM
[57]
 Toxin Info    HNTX-III (Phe0Gly1) IC50
0.475 ± 0.091 μM
[91]
 Toxin Info    HNTX-III (Ala0Gly1) IC50
0.486 ± 0.073 μM
[91]
 Toxin Info    Ca2a IC50
0.487 μM
[92]
 Toxin Info    HNTX-III (Tyr20Trp) IC50
0.495 ± 0.039 μM
[91]
 Toxin Info    HNTX-III (21Val) IC50
0.512 ± 0.078 μM
[91]
 Toxin Info    K0G1-P18K-A21V-V IC50
0.526 ± 0.048 μM
[91]
 Toxin Info    GPTX1 (Arg7-Lys) IC50
0.54 ± 0.06 μM
[57]
 Toxin Info    GPTX1 (Val33Glu) IC50
0.56 ± 0.08 μM
[57]
 Toxin Info    HNTX-III (Lys27Gln) IC50
0.568 ± 0.042 μM
[91]
 Toxin Info    GPTX1 (Lys15Glu) IC50
0.59 ± 0 μM
[57]
 Toxin Info    GPTX1 (C-Term. -Lys) IC50
0.59 ± 0.04 μM
[57]
 Toxin Info    GPTX1 (Asn20Lys) IC50
0.63 ± 0.16 μM
[57]
 Toxin Info    HNTX-III (Lys25Arg) IC50
0.647 ± 0.046 μM
[91]
 Toxin Info    HNTXI (E1G,R25K,D26H,L32W) IC50
0.669 ± 0.070 μM
[90]
 Toxin Info    GPTX1 (Leu3Glu) IC50
0.67 ± 0.04 μM
[57]
 Toxin Info    GPTX1 (Thr26Glu) IC50
0.69 ± 0.06 μM
[57]
 Toxin Info    GPTX1 (Arg25Glu) IC50
0.72 ± 0.04 μM
[57]
 Toxin Info    HNTXI (E1G,R25K,D26H) IC50
0.766 ± 0.029 μM
[90]
 Toxin Info    HNTX-III (Gly4Gln) IC50
0.815 ± 0.031 μM
[91]
 Toxin Info    GPTX1 (Arg7-Glu) IC50
0.86 ± 0.34 μM
[57]
 Toxin Info    HNTX-III (Pro11Glu) IC50
0.927 ± 0.076 μM
[91]
 Toxin Info    GPTX1 (Lys31Arg) IC50
0.95 ± 0.08 μM
[57]
 Toxin Info    O-MrVIB IC50
1 μM
[93]
 Toxin Info    GPTX1 (Ile10Tyr) IC50
1 μM
[57]
 Toxin Info    Pn3a-Y4A IC50
1 μM
[30]
 Toxin Info    Hhn2b (G7W,N24S,W29F) IC50
1.0 ± 0.2 μM
[89]
 Toxin Info    GPTX1 (Tyr32Arg) IC50
1.03 ± 0.24 μM
[57]
 Toxin Info    GPTX1 (Ile10Phe) IC50
1.1 μM
[57]
 Toxin Info    GPTX1 (Ile10Thr) IC50
1.1 μM
[57]
 Toxin Info    GPTX1 (Phe34Ala) IC50
1.2 μM
[66]
 Toxin Info    HNTX-III (Phe5Trp) IC50
1.227 ± 0.167 μM
[91]
 Toxin Info    HNTX-III (S24N) IC50
1.28 μM
[94]
 Toxin Info    GPTX1 (Ile10Val) IC50
1.4 μM
[57]
 Toxin Info    GPTX1 (Asn20Glu) IC50
1.40 ± 0 μM
[57]
 Toxin Info    GPTX1 (Val22Glu) IC50
1.40 ± 0.57 μM
[57]
 Toxin Info    HNTXI (D26H) IC50
1.498 ± 0.093 μM
[90]
 Toxin Info    GPTX1 (His27Lys) IC50
1.5 ± 0.28 μM
[57]
 Toxin Info    HNTX-III (Thr10Glu) IC50
1.657 ± 0.037 μM
[91]
 Toxin Info    GPTX1 (Lys8Glu) IC50
1.70 ± 0.57 μM
[57]
 Toxin Info    GPTX1 (Gly4Glu) IC50
1.75 ± 0.21 μM
[57]
 Toxin Info    HNTX-III (Gly12Glu) IC50
1.891 ± 0.142 μM
[91]
 Toxin Info    GPTX1 (Ile10Ser) IC50
2 μM
[57]
 Toxin Info    A23V PoTx IC50
2.01 ± 0.102 μM
[95]
 Toxin Info    HNTX-III (Phe5Leu) IC50
2.041 ± 0.015 μM
[91]
 Toxin Info    PTx2-3126 IC50
2.3 μM
[36]
 Toxin Info    GPTX1 (Phe34Arg) IC50
2.35 ± 0.64 μM
[57]
 Toxin Info    GPTX1 (Ile10Leu) IC50
2.5 μM
[57]
 Toxin Info    Hhn2b (G7W) IC50
2.7 ± 0.4 μM
[89]
 Toxin Info    GPTX1 (Ile10 2-Pal) IC50
2.9 μM
[57]
 Toxin Info    HNTX-III (Y20H,S24N) IC50
2.99 μM
[94]
 Toxin Info    HNTX-III (Tyr32Leu) IC50
3.076 ± 0.054 μM
[91]
 Toxin Info    GPTX1 (Ile10Met) IC50
3.1 μM
[57]
 Toxin Info    Beta-theraphotoxin-Cd1a IC50
3.34 μM
[53]
 Toxin Info    GPTX1 (Met6Glu) IC50
3.50 ± 0.71 μM
[57]
 Toxin Info    GPTX1 (Phe5Arg) IC50
3.60 ± 0.28 μM
[57]
 Toxin Info    PoTx IC50
3.98 ± 0.352 μM
[95]
 Toxin Info    GPTX1 (Ile10 4-CO2-F) IC50
4 μM
[57]
 Toxin Info    Hhn2b (N24S) IC50
4 ± 0.5 μM
[89]
 Toxin Info    Ca2a-K27A IC50
4.073 ± 0.5669 μM
[92]
 Toxin Info    GPTX1 (C-Term. -Glu) IC50
4.45 ± 0.64 μM
[57]
 Toxin Info    GPTX1 (Ile10Glu) IC50
4.5 μM
[57]
 Toxin Info    HwTx-IV (K32N) IC50
5.752.0 ± 0.0016 μM
[31]
 Toxin Info    HNTX-III (His26Leu) IC50
5.781 ± 0.117 μM
[91]
 Toxin Info    HNTX-III (H26D) IC50
7.58 μM
[94]
 Toxin Info    HNTX-III (His26Asp) IC50
7.58 ± 0.020 μM
[91]
 Toxin Info    A23E PoTx IC50
7.78 ± 0.912 μM
[95]
 Toxin Info    Hhn2b (G7W,N24A) IC50
8.6 ± 1.7 μM
[89]
 Toxin Info    Ca2a-T13 IC50
8.89 μM
[92]
 Toxin Info    HNTX-III (Y20H) IC50
9.56 μM
[94]
 Toxin Info    Ca2a-T1 IC50
14.71 μM
[92]
 Toxin Info    Ca2a-T2 IC50
16.49 μM
[92]
 Toxin Info    Ca2a-T3 IC50
39.59 μM
[92]
 Toxin Info    Ca2a-T11 IC50
49.18 μM
[92]
 Toxin Info    Ca2a-T10 IC50
53.55 μM
[92]
 Toxin Info    Ca2a-T9 IC50
67.31 μM
[92]
 Toxin Info    Ca2a-K18A IC50
683.3 ± 130.5 μM
[92]
 Toxin Info    rHwTx-IV (W30Y) pIC50
5.7 ± 0.08 .
[96]
 Toxin Info    rHwTx-IV (K18F) pIC50
6.5 ± 0.03 .
[96]
 Toxin Info    rHwTx-IV (D14P) pIC50
6.6 ± 0.03 .
[96]
 Toxin Info    rHwTx-IV (R26G) pIC50
6.6 ± 0.06 .
[96]
 Toxin Info    rHwTx-IV (N13G) pIC50
6.8 ± 0.07 .
[96]
 Toxin Info    rHwTx-IV (R26K) pIC50
6.8 ± 0.22 .
[96]
 Toxin Info    rHwTx-IV (W30K) pIC50
6.9 ± 0.12 .
[96]
 Toxin Info    rHwTx-IV (G36I) pIC50
7.0 ± 0.07 .
[96]
 Toxin Info    rHwTx-IV pIC50
7.0 ± 0.14 .
[96]
 Toxin Info    rHwTx-IV (K27W) pIC50
7.2 ± 0.06 .
[96]
 Toxin Info    rHwTx-IV (Y33T) pIC50
7.2 ± 0.07 .
[96]
 Toxin Info    rHwTx-IV (S19Q) pIC50
7.4 ± 0.22 .
[96]
 Toxin Info    rHwTx-IV (Q34L) pIC50
7.5 ± 0.04 .
[96]
 Toxin Info    rHwTx-IV (S20N) pIC50
7.5 ± 0.05 .
[96]
 Toxin Info    rHwTx-IV (Q34S) pIC50
7.5 ± 0.07 .
[96]
 Toxin Info    rHwTx-IV (S19P) pIC50
7.5 ± 0.09 .
[96]
 Toxin Info    rHwTx-IV (E4Q) pIC50
7.5 ± 0.10 .
[96]
 Toxin Info    rHwTx-IV (E4N) pIC50
7.6 ± 0.03 .
[96]
 Toxin Info    rHwTx-IV (E1N) pIC50
7.6 ± 0.1 .
[96]
 Toxin Info    rHwTx-IV (A8R) pIC50
7.7 ± 0.02 .
[96]
 Toxin Info    rHwTx-IV (K37R) pIC50
7.7 ± 0.03 .
[96]
 Toxin Info    rHwTx-IV (S19N) pIC50
7.7 ± 0.04 .
[96]
 Toxin Info    rHwTx-IV (S25I) pIC50
7.7 ± 0.07 .
[96]
 Toxin Info    rHwTx-IV (Q34F) pIC50
7.7 ± 0.18 .
[96]
 Toxin Info    rHwTx-IV (E4R) pIC50
7.9 ± 0.06 .
[96]
 Toxin Info    rHwTx-IV (K21R) pIC50
7.9 ± 0.13 .
[96]
References
Ref 1 Comprehensive EST analysis of the symbiotic sea anemone, Anemonia viridis. BMC Genomics. 2009 Jul 23;10:333. doi: 10.1186/1471-2164-10-333.
Ref 2 A Low Molecular Weight Protein from the Sea Anemone Anemonia viridis with an Anti-Angiogenic Activity. Mar Drugs. 2018 Apr 19;16(4):134. doi: 10.3390/md16040134.
Ref 3 The mining of toxin-like polypeptides from EST database by single residue distribution analysis. BMC Genomics. 2011 Jan 31;12:88. doi: 10.1186/1471-2164-12-88.
Ref 4 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 5 Evidence of accelerated evolution and ectodermal-specific expression of presumptive BDS toxin cDNAs from Anemonia viridis. Mar Drugs. 2013 Oct 30;11(11):4213-31. doi: 10.3390/md11114213.
Ref 6 Sea anemone peptides with a specific blocking activity against the fast inactivating potassium channel Kv3.4. J Biol Chem. 1998 Mar 20;273(12):6744-9. doi: 10.1074/jbc.273.12.6744.
Ref 7 Modulation of Kv3 subfamily potassium currents by the sea anemone toxin BDS: significance for CNS and biophysical studies. J Neurosci. 2005 Sep 21;25(38):8735-45. doi: 10.1523/JNEUROSCI.2119-05.2005.
Ref 8 Modulation of neuronal sodium channels by the sea anemone peptide BDS-I. J Neurophysiol. 2012 Jun;107(11):3155-67. doi: 10.1152/jn.00785.2011. Epub 2012 Mar 21.
Ref 9 A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structure. Biochemistry. 1989 Mar 7;28(5):2178-87. doi: 10.1021/bi00431a032.
Ref 10 Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry. 1989 Mar 7;28(5):2188-98. doi: 10.1021/bi00431a033.
Ref 11 Precursors of Androctonus australis scorpion neurotoxins. Structures of precursors, processing outcomes, and expression of a functional recombinant toxin II. J Biol Chem. 1989 Nov 15;264(32):19259-65.
Ref 12 The amino-acid sequence of neurotoxin II of Androctonus australis Hector. Eur J Biochem. 1972 Jul 24;28(3):381-8. doi: 10.1111/j.1432-1033.1972.tb01924.x.
Ref 13 Disulfide bonds of toxin II of the scorpion Androctonus australis Hector. Eur J Biochem. 1974 Sep 16;47(3):483-9. doi: 10.1111/j.1432-1033.1974.tb03716.x.
Ref 14 Characterization of Amm VIII from Androctonus mauretanicus mauretanicus: a new scorpion toxin that discriminates between neuronal and skeletal sodium channels. Biochem J. 2003 Nov 1;375(Pt 3):551-60. doi: 10.1042/BJ20030688.
Ref 15 Expression of the standard scorpion alpha-toxin AaH II and AaH II mutants leading to the identification of some key bioactive elements. Biochim Biophys Acta. 2005 May 25;1723(1-3):91-9. doi: 10.1016/j.bbagen.2005.01.008. Epub 2005 Jan 29.
Ref 16 The scorpion toxin Amm VIII induces pain hypersensitivity through gain-of-function of TTX-sensitive Na? channels. Pain. 2013 Aug;154(8):1204-15. doi: 10.1016/j.pain.2013.03.037. Epub 2013 Apr 6.
Ref 17 Orthorhombic crystals and three-dimensional structure of the potent toxin II from the scorpion Androctonus australis Hector. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7443-7. doi: 10.1073/pnas.85.20.7443.
Ref 18 Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution. J Mol Biol. 1994 Apr 22;238(1):88-103. doi: 10.1006/jmbi.1994.1270.
Ref 19 Ab initio structure determination and refinement of a scorpion protein toxin. Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):551-7. doi: 10.1107/S0907444997005386.
Ref 20 Molecular basis of the high insecticidal potency of scorpion alpha-toxins. J Biol Chem. 2004 Jul 23;279(30):31679-86. doi: 10.1074/jbc.M402048200. Epub 2004 May 8.
Ref 21 Expression and purification of recombinant alpha-toxin AnCra1 from the scorpion Androctonus crassicauda and its functional characterization on mammalian sodium channels. Mol Biol Rep. 2021 Sep;48(9):6303-6312. doi: 10.1007/s11033-021-06624-2. Epub 2021 Aug 11.
Ref 22 Peptide ion channel toxins from the bootlace worm, the longest animal on Earth. Sci Rep. 2018 Mar 22;8(1):4596. doi: 10.1038/s41598-018-22305-w.
Ref 23 Functional Characterization of the Nemertide Family of Peptide Toxins. J Nat Prod. 2021 Aug 27;84(8):2121-2128. doi: 10.1021/acs.jnatprod.1c00104. Epub 2021 Aug 16.
Ref 24 Purification, characterization, synthesis, and cloning of the lockjaw peptide from Conus purpurascens venom. Biochemistry. 1995 Apr 18;34(15):4913-8. doi: 10.1021/bi00015a002.
Ref 25 Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 1996 May 9;381(6578):148-51. doi: 10.1038/381148a0.
Ref 26 Distinction among neuronal subtypes of voltage-activated sodium channels by mu-conotoxin PIIIA. J Neurosci. 2000 Jan 1;20(1):76-80. doi: 10.1523/JNEUROSCI.20-01-00076.2000.
Ref 27 Delta-conotoxin structure/function through a cladistic analysis. Biochemistry. 2001 Nov 6;40(44):13201-8. doi: 10.1021/bi010683a.
Ref 28 Isolation, characterization and total regioselective synthesis of the novel O-conotoxin MfVIA from Conus magnificus that targets voltage-gated sodium channels. Biochem Pharmacol. 2012 Aug 15;84(4):540-8. doi: 10.1016/j.bcp.2012.05.008. Epub 2012 May 16.
Ref 29 Discovery of Tarantula Venom-Derived Na(V)1.7-Inhibitory JzTx-V Peptide 5-Br-Trp24 Analogue AM-6120 with Systemic Block of Histamine-Induced Pruritis. J Med Chem. 2018 Nov 8;61(21):9500-9512. doi: 10.1021/acs.jmedchem.8b00736. Epub 2018 Oct 22.
Ref 30 Mapping the Molecular Surface of the Analgesic Na(V)1.7-Selective Peptide Pn3a Reveals Residues Essential for Membrane and Channel Interactions. ACS Pharmacol Transl Sci. 2020 Feb 19;3(3):535-546. doi: 10.1021/acsptsci.0c00002. eCollection 2020 Jun 12.
Ref 31 Potency optimization of Huwentoxin-IV on hNav1.7: a neurotoxin TTX-S sodium-channel antagonist from the venom of the Chinese bird-eating spider Selenocosmia huwena. Peptides. 2013 Jun;44:40-6. doi: 10.1016/j.peptides.2013.03.011. Epub 2013 Mar 19.
Ref 32 Manipulation of a spider peptide toxin alters its affinity for lipid bilayers and potency and selectivity for voltage-gated sodium channel subtype 1.7. J Biol Chem. 2020 Apr 10;295(15):5067-5080. doi: 10.1074/jbc.RA119.012281. Epub 2020 Mar 5.
Ref 33 Engineering potent and selective analogues of GpTx-1, a tarantula venom peptide antagonist of the Na(V)1.7 sodium channel. J Med Chem. 2015 Mar 12;58(5):2299-314. doi: 10.1021/jm501765v. Epub 2015 Feb 19.
Ref 34 Identification and Characterization of ProTx-III [-TRTX-Tp1a], a New Voltage-Gated Sodium Channel Inhibitor from Venom of the Tarantula Thrixopelma pruriens. Mol Pharmacol. 2015 Aug;88(2):291-303. doi: 10.1124/mol.115.098178. Epub 2015 May 15.
Ref 35 The alchemy of culture: intoxicants in society. BMJ. 1998 Nov 28;317(7171):1532B. doi: 10.1136/bmj.317.7171.1532b.
Ref 36 Computational design of peptides to target Na(V)1.7 channel with high potency and selectivity for the treatment of pain. Elife. 2022 Dec 28;11:e81727. doi: 10.7554/eLife.81727.
Ref 37 Pmu1a, a novel spider toxin with dual inhibitory activity at pain targets hNa(V) 1.7 and hCa(V) 3 voltage-gated channels. FEBS J. 2023 Jul;290(14):3688-3702. doi: 10.1111/febs.16773. Epub 2023 Mar 23.
Ref 38 cDNA sequence analysis of seven peptide toxins from the spider Selenocosmia huwena. Toxicon. 2003 Dec;42(7):715-23. doi: 10.1016/j.toxicon.2003.08.007.
Ref 39 Molecular diversification based on analysis of expressed sequence tags from the venom glands of the Chinese bird spider Ornithoctonus huwena. Toxicon. 2008 Jun 15;51(8):1479-89. doi: 10.1016/j.toxicon.2008.03.024. Epub 2008 Mar 27.
Ref 40 Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena. J Biol Chem. 2002 Dec 6;277(49):47564-71. doi: 10.1074/jbc.M204063200. Epub 2002 Sep 11.
Ref 41 Native pyroglutamation of huwentoxin-IV: a post-translational modification that increases the trapping ability to the sodium channel. PLoS One. 2013 Jun 24;8(6):e65984. doi: 10.1371/journal.pone.0065984. Print 2013.
Ref 42 Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding to receptor site 4 and trapping the domain ii voltage sensor in the closed configuration. J Biol Chem. 2008 Oct 3;283(40):27300-13. doi: 10.1074/jbc.M708447200. Epub 2008 Jul 14.
Ref 43 Synthesis and characterization of huwentoxin-IV, a neurotoxin inhibiting central neuronal sodium channels. Toxicon. 2008 Feb;51(2):230-9. doi: 10.1016/j.toxicon.2007.09.008. Epub 2007 Sep 29.
Ref 44 The tarantula toxins ProTx-II and huwentoxin-IV differentially interact with human Nav1.7 voltage sensors to inhibit channel activation and inactivation. Mol Pharmacol. 2010 Dec;78(6):1124-34. doi: 10.1124/mol.110.066332. Epub 2010 Sep 20.
Ref 45 Common molecular determinants of tarantula huwentoxin-IV inhibition of Na+ channel voltage sensors in domains II and IV. J Biol Chem. 2011 Aug 5;286(31):27301-10. doi: 10.1074/jbc.M111.246876. Epub 2011 Jun 9.
Ref 46 Gating modifier toxins isolated from spider venom: Modulation of voltage-gated sodium channels and the role of lipid membranes. J Biol Chem. 2018 Jun 8;293(23):9041-9052. doi: 10.1074/jbc.RA118.002553. Epub 2018 Apr 27.
Ref 47 Screening, large-scale production and structure-based classification of cystine-dense peptides. Nat Struct Mol Biol. 2018 Mar;25(3):270-278. doi: 10.1038/s41594-018-0033-9. Epub 2018 Feb 26.
Ref 48 Chemical Synthesis, Proper Folding, Na(v) Channel Selectivity Profile and Analgesic Properties of the Spider Peptide Phlotoxin 1. Toxins (Basel). 2019 Jun 21;11(6):367. doi: 10.3390/toxins11060367.
Ref 49 Analysis of the structural and molecular basis of voltage-sensitive sodium channel inhibition by the spider toxin huwentoxin-IV (-TRTX-Hh2a). J Biol Chem. 2013 Aug 2;288(31):22707-20. doi: 10.1074/jbc.M113.461392. Epub 2013 Jun 12.
Ref 50 Spider peptide toxin HwTx-IV engineered to bind to lipid membranes has an increased inhibitory potency at human voltage-gated sodium channel hNa(V)1.7. Biochim Biophys Acta Biomembr. 2017 May;1859(5):835-844. doi: 10.1016/j.bbamem.2017.01.020. Epub 2017 Jan 20.
Ref 51 The structure, dynamics and selectivity profile of a NaV1.7 potency-optimised huwentoxin-IV variant. PLoS One. 2017 Mar 16;12(3):e0173551. doi: 10.1371/journal.pone.0173551. eCollection 2017.
Ref 52 Structures of human Na(v)1.7 channel in complex with auxiliary subunits and animal toxins. Science. 2019 Mar 22;363(6433):1303-1308. doi: 10.1126/science.aaw2493. Epub 2019 Feb 14.
Ref 53 Discovery and mode of action of a novel analgesic -toxin from the African spider Ceratogyrus darlingi. PLoS One. 2017 Sep 7;12(9):e0182848. doi: 10.1371/journal.pone.0182848. eCollection 2017.
Ref 54 Development of ProTx-II Analogues as Highly Selective Peptide Blockers of Na(v)1.7 for the Treatment of Pain. J Med Chem. 2022 Jan 13;65(1):485-496. doi: 10.1021/acs.jmedchem.1c01570. Epub 2021 Dec 21.
Ref 55 Discovery of a selective NaV1.7 inhibitor from centipede venom with analgesic efficacy exceeding morphine in rodent pain models. Proc Natl Acad Sci U S A. 2013 Oct 22;110(43):17534-9. doi: 10.1073/pnas.1306285110. Epub 2013 Sep 30.
Ref 56 Weaponization of a Hormone: Convergent Recruitment of Hyperglycemic Hormone into the Venom of Arthropod Predators. Structure. 2015 Jul 7;23(7):1283-92. doi: 10.1016/j.str.2015.05.003. Epub 2015 Jun 11.
Ref 57 Single Residue Substitutions That Confer Voltage-Gated Sodium Ion Channel Subtype Selectivity in the NaV1.7 Inhibitory Peptide GpTx-1. J Med Chem. 2016 Mar 24;59(6):2704-17. doi: 10.1021/acs.jmedchem.5b01947. Epub 2016 Mar 10.
Ref 58 Evaluation of the Spider (Phlogiellus genus) Phlotoxin 1 and Synthetic Variants as Antinociceptive Drug Candidates. Toxins (Basel). 2019 Aug 22;11(9):484. doi: 10.3390/toxins11090484.
Ref 59 From identification to functional characterization of cyriotoxin-1a, an antinociceptive toxin from the spider Cyriopagopus schioedtei. Br J Pharmacol. 2019 May;176(9):1298-1314. doi: 10.1111/bph.14628. Epub 2019 Apr 9.
Ref 60 Enzymatic Ligation of a Pore Blocker Toxin and a Gating Modifier Toxin: Creating Double-Knotted Peptides with Improved Sodium Channel Na(V)1.7 Inhibition. Bioconjug Chem. 2020 Jan 15;31(1):64-73. doi: 10.1021/acs.bioconjchem.9b00744. Epub 2019 Dec 16.
Ref 61 Application of ultra-performance liquid chromatography coupled with quadrupole time-of-flight mass spectrometry to identify curcumin metabolites produced by human intestinal bacteria. J Chromatogr B Analyt Technol Biomed Life Sci. 2015 Mar 15;985:38-47. doi: 10.1016/j.jchromb.2015.01.014. Epub 2015 Jan 24.
Ref 62 Seven novel modulators of the analgesic target NaV 1.7 uncovered using a high-throughput venom-based discovery approach. Br J Pharmacol. 2015 May;172(10):2445-58. doi: 10.1111/bph.13081. Epub 2015 Mar 4.
Ref 63 Evaluation of Diverse Community Asthma Interventions: Balancing Health Outcomes with Developing Community Capacity for Evidence-Based Program Measurement. Popul Health Manag. 2015 Oct;18(5):342-50. doi: 10.1089/pop.2014.0144. Epub 2015 Feb 6.
Ref 64 Changes to collagen structure during leather processing. J Agric Food Chem. 2015 Mar 11;63(9):2499-505. doi: 10.1021/jf506357j. Epub 2015 Feb 25.
Ref 65 Quantitative analysis of thiolated ligand exchange on gold nanoparticles monitored by 1H NMR spectroscopy. Anal Chem. 2015 Mar 3;87(5):2771-8. doi: 10.1021/ac504081k. Epub 2015 Feb 6.
Ref 66 Utilization of blood cultures in Danish hospitals: a population-based descriptive analysis. Clin Microbiol Infect. 2015 Apr;21(4):344.e13-21. doi: 10.1016/j.cmi.2014.11.018. Epub 2014 Nov 23.
Ref 67 High-performance liquid chromatography method for ferric iron chelators using a post-column reaction with Calcein Blue. J Chromatogr B Analyt Technol Biomed Life Sci. 2015 Mar 15;985:48-53. doi: 10.1016/j.jchromb.2015.01.027. Epub 2015 Jan 24.
Ref 68 Mango polyphenols and its protective effects on diseases associated to oxidative stress. Curr Pharm Biotechnol. 2015;16(3):272-80. doi: 10.2174/138920101603150202143532.
Ref 69 Video comment on Geoffroy Vanbiervliet et al., pages 871-877. Endoscopy. 2014 Oct;46(10):v4. doi: 10.1055/s-0034-1391663. Epub 2015 Feb 6.
Ref 70 Therapies targeting oxidative stress for human diseases: where are we now?. Curr Pharm Biotechnol. 2015;16(3):195. doi: 10.2174/156802661503150202123740.
Ref 71 Three Peptide Modulators of the Human Voltage-Gated Sodium Channel 1.7, an Important Analgesic Target, from the Venom of an Australian Tarantula. Toxins (Basel). 2015 Jun 30;7(7):2494-513. doi: 10.3390/toxins7072494.
Ref 72 Molecular diversity and evolution of cystine knot toxins of the tarantula Chilobrachys jingzhao. Cell Mol Life Sci. 2008 Aug;65(15):2431-44. doi: 10.1007/s00018-008-8135-x.
Ref 73 Proteomic and peptidomic analysis of the venom from Chinese tarantula Chilobrachys jingzhao. Proteomics. 2007 Jun;7(11):1892-907. doi: 10.1002/pmic.200600785.
Ref 74 Effects and mechanism of Chinese tarantula toxins on the Kv2.1 potassium channels. Biochem Biophys Res Commun. 2007 Jan 19;352(3):799-804. doi: 10.1016/j.bbrc.2006.11.086. Epub 2006 Nov 27.
Ref 75 Characterization of the excitatory mechanism induced by Jingzhaotoxin-I inhibiting sodium channel inactivation. Toxicon. 2007 Sep 15;50(4):507-17. doi: 10.1016/j.toxicon.2007.04.018. Epub 2007 May 3.
Ref 76 Molecular determinants for the tarantula toxin jingzhaotoxin-I interacting with potassium channel Kv2.1. Toxicon. 2013 Mar 1;63:129-36. doi: 10.1016/j.toxicon.2012.12.001. Epub 2012 Dec 13.
Ref 77 Molecular determinant for the tarantula toxin Jingzhaotoxin-I slowing the fast inactivation of voltage-gated sodium channels. Toxicon. 2016 Mar 1;111:13-21. doi: 10.1016/j.toxicon.2015.12.009. Epub 2015 Dec 23.
Ref 78 Sequence-specific assignment of 1H-NMR resonance and determination of the secondary structure of Jingzhaotoxin-I. Acta Biochim Biophys Sin (Shanghai). 2005 Aug;37(8):567-72. doi: 10.1111/j.1745-7270.2005.00078.x.
Ref 79 Jingzhaotoxin-I, a novel spider neurotoxin preferentially inhibiting cardiac sodium channel inactivation. J Biol Chem. 2005 Apr 1;280(13):12069-76. doi: 10.1074/jbc.M411651200. Epub 2004 Nov 17.
Ref 80 Subcutaneously administered antibiotics: a national survey of current practice from the French Infectious Diseases (SPILF) and Geriatric Medicine (SFGG) society networks. Clin Microbiol Infect. 2015 Apr;21(4):370.e1-3. doi: 10.1016/j.cmi.2014.11.017. Epub 2014 Nov 23.
Ref 81 The anti-cancer potency and mechanism of a novel tumor-activated fused toxin, DLM. Toxins (Basel). 2015 Feb 4;7(2):423-38. doi: 10.3390/toxins7020423.
Ref 82 Two tarantula venom peptides as potent and differential Na(V) channels blockers. Toxicon. 2014 Jan;77:58-67. doi: 10.1016/j.toxicon.2013.10.029. Epub 2013 Nov 7.
Ref 83 Localization of the voltage-sensor toxin receptor on KvAP. Biochemistry. 2004 Aug 10;43(31):10071-9. doi: 10.1021/bi049463y.
Ref 84 In situ cobalt-cobalt oxide/N-doped carbon hybrids as superior bifunctional electrocatalysts for hydrogen and oxygen evolution. J Am Chem Soc. 2015 Feb 25;137(7):2688-94. doi: 10.1021/ja5127165. Epub 2015 Feb 17.
Ref 85 Metabolomics of the bio-degradation process of aflatoxin B1 by actinomycetes at an initial pH of 6.0. Toxins (Basel). 2015 Feb 4;7(2):439-56. doi: 10.3390/toxins7020439.
Ref 86 Expression and characterization of jingzhaotoxin-34, a novel neurotoxin from the venom of the tarantula Chilobrachys jingzhao. Peptides. 2009 Jun;30(6):1042-8. doi: 10.1016/j.peptides.2009.02.018. Epub 2009 Mar 13.
Ref 87 Selective Closed-State Nav1.7 Blocker JZTX-34 Exhibits Analgesic Effects against Pain. Toxins (Basel). 2018 Feb 2;10(2):64. doi: 10.3390/toxins10020064.
Ref 88 Blood culture series benefit may be limited to selected clinical conditions: time to reassess. Clin Microbiol Infect. 2015 Apr;21(4):332-6. doi: 10.1016/j.cmi.2014.11.019. Epub 2014 Nov 27.
Ref 89 Rational Engineering Defines a Molecular Switch That Is Essential for Activity of Spider-Venom Peptides against the Analgesics Target NaV1.7. Mol Pharmacol. 2015 Dec;88(6):1002-10. doi: 10.1124/mol.115.100784. Epub 2015 Oct 1.
Ref 90 Engineering Gain-of-Function Analogues of the Spider Venom Peptide HNTX-I, A Potent Blocker of the hNa(V)1.7 Sodium Channel. Toxins (Basel). 2018 Sep 4;10(9):358. doi: 10.3390/toxins10090358.
Ref 91 Engineering of highly potent and selective HNTX-III mutant against hNa(v)1.7 sodium channel for treatment of pain. J Biol Chem. 2021 Jan-Jun;296:100326. doi: 10.1016/j.jbc.2021.100326. Epub 2021 Jan 23.
Ref 92 General mechanism of spider toxin family I acting on sodium channel Nav1.7. Zool Res. 2022 Sep 18;43(5):886-896. doi: 10.24272/j.issn.2095-8137.2022.185.
Ref 93 muO-conotoxin MrVIB selectively blocks Nav1.8 sensory neuron specific sodium channels and chronic pain behavior without motor deficits. Proc Natl Acad Sci U S A. 2006 Nov 7;103(45):17030-5. doi: 10.1073/pnas.0601819103. Epub 2006 Oct 31.
Ref 94 Natural mutations change the affinity of -theraphotoxin-Hhn2a to voltage-gated sodium channels. Toxicon. 2015 Jan;93:24-30. doi: 10.1016/j.toxicon.2014.11.220. Epub 2014 Nov 6.
Ref 95 A reexamination of poneratoxin from the venom of the bullet ant Paraponera clavata. Peptides. 2017 Dec;98:51-62. doi: 10.1016/j.peptides.2016.05.012. Epub 2016 Jun 3.
Ref 96 Comprehensive engineering of the tarantula venom peptide huwentoxin-IV to inhibit the human voltage-gated sodium channel hNa(v)1.7. J Biol Chem. 2020 Jan 31;295(5):1315-1327. doi: 10.1074/jbc.RA119.011318. Epub 2019 Dec 23.
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