Target Information

General Information of This Target
Target ID
BTDT00079
Target Name
Sodium channel protein type 4 subunit alpha (SCN4A)
Target Bioclass
Transporter and channel
Uniprot ID
P35499
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
SCN4A
Gene ID
6329
Synonym
SkM1; Sodium channel protein skeletal muscle subunit alpha; Sodium channel protein type IV subunit alpha; Voltage-gated sodium channel subunit alpha Nav1.4
Sequence
MARPSLCTLVPLGPECLRPFTRESLAAIEQRAVEEEARLQRNKQMEIEEPERKPRSDLEA
GKNLPMIYGDPPPEVIGIPLEDLDPYYSNKKTFIVLNKGKAIFRFSATPALYLLSPFSVV
RRGAIKVLIHALFSMFIMITILTNCVFMTMSDPPPWSKNVEYTFTGIYTFESLIKILARG
FCVDDFTFLRDPWNWLDFSVIMMAYLTEFVDLGNISALRTFRVLRALKTITVIPGLKTIV
GALIQSVKKLSDVMILTVFCLSVFALVGLQLFMGNLRQKCVRWPPPFNDTNTTWYSNDTW
YGNDTWYGNEMWYGNDSWYANDTWNSHASWATNDTFDWDAYISDEGNFYFLEGSNDALLC
GNSSDAGHCPEGYECIKTGRNPNYGYTSYDTFSWAFLALFRLMTQDYWENLFQLTLRAAG
KTYMIFFVVIIFLGSFYLINLILAVVAMAYAEQNEATLAEDKEKEEEFQQMLEKFKKHQE
ELEKAKAAQALEGGEADGDPAHGKDCNGSLDTSQGEKGAPRQSSSGDSGISDAMEELEEA
HQKCPPWWYKCAHKVLIWNCCAPWLKFKNIIHLIVMDPFVDLGITICIVLNTLFMAMEHY
PMTEHFDNVLTVGNLVFTGIFTAEMVLKLIAMDPYEYFQQGWNIFDSIIVTLSLVELGLA
NVQGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQ
LFGKSYKECVCKIALDCNLPRWHMHDFFHSFLIVFRILCGEWIETMWDCMEVAGQAMCLT
VFLMVMVIGNLVVLNLFLALLLSSFSADSLAASDEDGEMNNLQIAIGRIKLGIGFAKAFL
LGLLHGKILSPKDIMLSLGEADGAGEAGEAGETAPEDEKKEPPEEDLKKDNHILNHMGLA
DGPPSSLELDHLNFINNPYLTIQVPIASEESDLEMPTEEETDTFSEPEDSKKPPQPLYDG
NSSVCSTADYKPPEEDPEEQAEENPEGEQPEECFTEACVQRWPCLYVDISQGRGKKWWTL
RRACFKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRRVIRTILEYADKVFTYIFIMEM
LLKWVAYGFKVYFTNAWCWLDFLIVDVSIISLVANWLGYSELGPIKSLRTLRALRPLRAL
SRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYYCINTTTSERFDI
SEVNNKSECESLMHTGQVRWLNVKVNYDNVGLGYLSLLQVATFKGWMDIMYAAVDSREKE
EQPQYEVNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGKDIFMTEEQKKYY
NAMKKLGSKKPQKPIPRPQNKIQGMVYDLVTKQAFDITIMILICLNMVTMMVETDNQSQL
KVDILYNINMIFIIIFTGECVLKMLALRQYYFTVGWNIFDFVVVILSIVGLALSDLIQKY
FVSPTLFRVIRLARIGRVLRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFG
MSNFAYVKKESGIDDMFNFETFGNSIICLFEITTSAGWDGLLNPILNSGPPDCDPNLENP
GTSVKGDCGNPSIGICFFCSYIIISFLIVVNMYIAIILENFNVATEESSEPLGEDDFEMF
YETWEKFDPDATQFIAYSRLSDFVDTLQEPLRIAKPNKIKLITLDLPMVPGDKIHCLDIL
FALTKEVLGDSGEMDALKQTMEEKFMAANPSKVSYEPITTTLKRKHEEVCAIKIQRAYRR
HLLQRSMKQASYMYRHSHDGSGDDAPEKEGLLANTMSKMYGHENGNSSSPSPEEKGEAGD
AGPTMGLMPISPSDTAWPPAPPPGQTVRPGVKESLV

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Family
the sodium channel (TC 1.A.1.10) family
Function
Pore-forming subunit of a voltage-gated sodium channel complex through which Na(+) ions pass in accordance with their electrochemical gradient. Alternates between resting, activated and inactivated states. Required for normal muscle fiber excitability, normal muscle contraction and relaxation cycles, and constant muscle strength in the presence of fluctuating K(+) levels.

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Taxonomy ID
9606
TCDB ID
1.A.1.10.4
        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    U-actitoxin-Oulsp2 Inhibition rate . [1]
 Toxin Info    U1-theraphotoxin-Ap1a Inhibition rate . [2]
 Toxin Info    Beta-toxin Tf1a Inhibition rate
53 %
 [3]
 Toxin Info    PTx2-17 IC50
>17 nM
 [4]
 Toxin Info    PTx2-19 IC50
>17 nM
 [4]
 Toxin Info    Mu-conotoxin SxIIIC IC50
15.11 nM
 [5]
 Toxin Info    Mu/omega-theraphotoxin-Pmu1a IC50
62.9 nM
 [6]
 Toxin Info    O- MrVIA IC50
81 ± 16 nM
 [7]
 Toxin Info    ProTX-11 IC50
93 ± 17 nM
 [4]
 Toxin Info    Mu-theraphotoxin-Pn3a IC50
144 nM
 [8- 13]
 Toxin Info    GPTX1 (Phe5 Leu) IC50
900 nM
 [14]
 Toxin Info    GPTX1 (Phe5 Met) IC50
900 nM
 [14]
 Toxin Info    Mu-elapitoxin-Na1a IC50
>10 μM
 [15]
 Toxin Info    PTx2-10 IC50
>17 μM
 [4]
 Toxin Info    PTx2-11 IC50
>17 μM
 [4]
 Toxin Info    PTx2-12 IC50
>17 μM
 [4]
 Toxin Info    PTx2-13 IC50
>17 μM
 [4]
 Toxin Info    PTx2-14 IC50
>17 μM
 [4]
 Toxin Info    PTx2-15 IC50
>17 μM
 [4]
 Toxin Info    PTx2-16 IC50
>17 μM
 [4]
 Toxin Info    PTx2-18 IC50
>17 μM
 [4]
 Toxin Info    PTx2-20 IC50
>17 μM
 [4]
 Toxin Info    PTx2-21 IC50
>17 μM
 [4]
 Toxin Info    PTx2-22 IC50
>17 μM
 [4]
 Toxin Info    PTx2-23 IC50
>17 μM
 [4]
 Toxin Info    PTx2-5 IC50
>17 μM
 [4]
 Toxin Info    PTx2-6 IC50
>17 μM
 [4]
 Toxin Info    PTx2-8 IC50
>17 μM
 [4]
 Toxin Info    PTx2-9 IC50
>17 μM
 [4]
 Toxin Info    GPTX1 (N-Term. Glu) IC50
>2.2 μM
 [16]
 Toxin Info    GPTX1 (Leu3Ala) IC50
>3.0 μM
 [17]
 Toxin Info    GPTX1 (Pro19Lys) IC50
>3.4 μM
 [16]
 Toxin Info    GPTX1 (Gly4Arg) IC50
>3.7 μM
 [16]
 Toxin Info    GPTX1 (Lys8Ala) IC50
>3.9 μM
 [18]
 Toxin Info    GPTX1 (Arg7-Lys) IC50
>4.0 μM
 [16]
 Toxin Info    GPTX1 (Asn13Arg) IC50
>4.1 μM
 [16]
 Toxin Info    GPTX1 (Trp29Ala) IC50
>4.5 μM
 [19]
 Toxin Info    GPTX1 (Arg7-Ala) IC50
>4.6 μM
 [18]
 Toxin Info    GPTX1 (C-Term. -Lys) IC50
>4.6 μM
 [16]
 Toxin Info    GPTX1 (Tyr32Trp) IC50
>4.7 μM
 [16]
 Toxin Info    GPTX1 (Arg18Glu) IC50
>4.8 μM
 [16]
 Toxin Info    GPTX1 (N-Term. Ala) IC50
>4.8 μM
 [20]
 Toxin Info    GPTX1 (His27Lys) IC50
>4.9 μM
 [16]
 Toxin Info    GPTX1 (Lys28Ala) IC50
>4.9 μM
 [19]
 Toxin Info    GPTX1 (Arg25Ala) IC50
>5 μM
 [21]
 Toxin Info    GPTX1 (Arg25Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Arg7-Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Asn20Ala) IC50
>5 μM
 [22]
 Toxin Info    GPTX1 (Asn20Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (C-Term. -Arg) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Gly4Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Gly4Lys) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (His27Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Leu3Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Lys15Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Lys28Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Lys31Ala) IC50
>5 μM
 [23]
 Toxin Info    GPTX1 (Lys31Arg) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Lys31Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Lys31Trp) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Lys8Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Met6Arg) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Met6Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Met6Lys) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Phe34Ala) IC50
>5 μM
 [24]
 Toxin Info    GPTX1 (Phe34Arg) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Phe34Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Phe34Lys) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Phe34Trp) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Phe5Arg) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Phe5Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Pro11Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Ser24Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Thr26Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Trp29Arg) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Trp29Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Trp29Lys) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Tyr32Ala) IC50
>5 μM
 [23]
 Toxin Info    GPTX1 (Tyr32Arg) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Tyr32Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Tyr32Lys) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Val22Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Val33Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (C-Term. -Glu) IC50
>5 μM
 [25]
 Toxin Info    GPTX1 (C-Term. -Glu) IC50
>5 μM
 [16]
 Toxin Info    GPTX1 (Met6Trp) IC50
0.2 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Asp12Trp) IC50
0.4 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Val33Trp) IC50
0.5 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Asp12Arg) IC50
0.6 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Gly4Trp) IC50
0.6 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Thr26Arg) IC50
0.6 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Asp12Lys) IC50
0.7 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Asn20Trp) IC50
0.7 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Thr26Lys) IC50
0.7 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Thr26Trp) IC50
0.7 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Val22Arg) IC50
0.7 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Asp12Ala) IC50
0.9 ± 0.1 μM
 [26]
 Toxin Info    GPTX1 (Ile10Arg) IC50
0.9 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Leu3Arg) IC50
0.9 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Val33Lys) IC50
1.2 ± 0.2 μM
 [16]
 Toxin Info    PTx2-2 IC50
1.242 ± 0. 257 μM
 [4]
 Toxin Info    GPTX1 (Asn20Arg) IC50
1.4 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Pro19Arg) IC50
1.4 ± 0.424 μM
 [16]
 Toxin Info    GPTX1 (Asp1Lys) IC50
1.5 ± 0 μM
 [16]
 Toxin Info    GPTX1 (Asp1Arg) IC50
1.5 ± 0 1 μM
 [16]
 Toxin Info    GPTX1 (Pro11Trp) IC50
1.5 ± 0.3 μM
 [16]
 Toxin Info    GPTX1 (Pro19Ala) IC50
1.5 ± 0.3 μM
 [22]
 Toxin Info    GPTX1 (Val33Arg) IC50
1.5 ± 0.8 μM
 [16]
 Toxin Info    PTx2-1 IC50
1.765 ± 0.611 μM
 [4]
 Toxin Info    GPTX1 (Lys8Arg) IC50
1.8 ± 0 μM
 [16]
 Toxin Info    GPTX1 (Asp1Ala) IC50
1.8 ± 0.1 μM
 [20]
 Toxin Info    GPTX1 (Leu3Lys) IC50
1.9 ± 0.4 μM
 [16]
 Toxin Info    GPTX1 (Ser24Ala) IC50
1.9 ± 0.6 μM
 [21]
 Toxin Info    GPTX1 (Phe5 Ile) IC50
2 μM
 [14]
 Toxin Info    GPTX1 (Val22Lys) IC50
2.0 ± 0.4 μM
 [16]
 Toxin Info    GPTX1 (Asn13Trp) IC50
2.0 ± 0.7 μM
 [16]
 Toxin Info    GPTX1 (Asp12Glu) IC50
2.3 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Phe5Trp) IC50
2.3 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Lys15Arg) IC50
2.3 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Asn13Lys) IC50
2.4 ± 0 μM
 [16]
 Toxin Info    GPTX1 (N-Term. Lys) IC50
2.4 ± 0.3 μM
 [16]
 Toxin Info    GPTX1 (Leu21Trp) IC50
2.5 ± 0.4 μM
 [16]
 Toxin Info    GPTX1 (N-Term. Arg) IC50
2.6 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (His27Arg) IC50
2.6 ± 0.3 μM
 [16]
 Toxin Info    GPTX1 (Ile10Lys) IC50
2.6 ± 0.6 μM
 [16]
 Toxin Info    GPTX1 (His27Trp) IC50
2.6 ± 1.2 μM
 [16]
 Toxin Info    GPTX1 (Asp1Trp) IC50
2.6 ± 1.3 μM
 [16]
 Toxin Info    GPTX1 (Asn13Ala) IC50
2.7 ± 0.2 μM
 [26]
 Toxin Info    GPTX1 (C-Term. -Trp) IC50
2.7 ± 0.8 μM
 [16]
 Toxin Info    GPTX1 (Lys28Arg) IC50
2.8 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Ile10Ala) IC50
3.0 ± 0.1 μM
 [27]
 Toxin Info    GPTX1 (Pro11Ala) IC50
3.0 ± 0.5 μM
 [27]
 Toxin Info    GPTX1 (Arg18Ala) IC50
3.0 ± 0.6 μM
 [28]
 Toxin Info    GPTX1 (Leu21Ala) IC50
3.0 ± 0.7 μM
 [29]
 Toxin Info    GPTX1 (Thr26Ala) IC50
3.2 ± 0.1 μM
 [30]
 Toxin Info    GPTX1 (Gly4Ala) IC50
3.2 ± 0.4 μM
 [17]
 Toxin Info    GPTX1 (Val22Trp) IC50
3.4 ± 1.0 μM
 [16]
 Toxin Info    GPTX1 (Asp1Glu) IC50
3.5 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Asn20Lys) IC50
3.7 ± 0.3 μM
 [16]
 Toxin Info    GPTX1 (Val22Ala) IC50
3.7 ± 0.3 μM
 [29]
 Toxin Info    GPTX1 (Arg18Trp) IC50
3.7 ± 0.4 μM
 [16]
 Toxin Info    GPTX1 (Arg18Lys) IC50
3.8 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Met6Ala) IC50
3.8 ± 0.5 μM
 [31]
 Toxin Info    GPTX1 (Arg25Lys) IC50
3.9 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (N-Term. Trp) IC50
3.9 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Phe5 Val) IC50
4.1 μM
 [14]
 Toxin Info    GPTX1 (His27Ala) IC50
4.1 ± 0.4 μM
 [30]
 Toxin Info    PTx2-3 IC50
4.136 ± 0. 674 μM
 [4]
 Toxin Info    GPTX1 (Ile10Trp) IC50
4.4 ± 0.1 μM
 [16]
 Toxin Info    GPTX1 (Asn13Glu) IC50
4.4 ± 0.3 μM
 [16]
 Toxin Info    GPTX1 (Ile10Glu) IC50
4.5 ± 0.2 μM
 [16]
 Toxin Info    GPTX1 (Val33Ala) IC50
4.5 ± 0.5 μM
 [24]
 Toxin Info    GPTX1 (Lys15Ala) IC50
4.7 ± 0.3 μM
 [28]
 Toxin Info    PTx2-4 IC50
4.774 ± 0.227 μM
 [4]
 Toxin Info    U18-theraphotoxin-Cg1a IC50
5.42 μM
 [32], [33], [34]
 Toxin Info    Mu-theraphotoxin-Os1a IC50
7.7 μM
 [35]
 Toxin Info    GPTX1 (Phe5Ala) IC50
8.5 μM
 [14]
 Toxin Info    PTx2-3258 IC50
8.877 μM
 [36]
 Toxin Info    GPTX1 (Phe5 Gly) IC50
11 μM
 [14]
 Toxin Info    PTx2-3127 IC50
11.53 μM
 [37]
 Toxin Info    PTx2-7 IC50
15.210 ± 1.138 μM
 [4]
 Toxin Info    GPTX1 (Phe5Ala) IC50
45 ± 3 μM
 [31]
References
Ref 1 Synthesis, folding, structure and activity of a predicted peptide from the sea anemone Oulactis sp. with an ShKT fold. Toxicon. 2018 Aug;150:50-59. doi: 10.1016/j.toxicon.2018.05.006. Epub 2018 May 19.
Ref 2 Characterization of a novel peptide toxin from Acanthoscurria paulensis spider venom: a distinct cysteine assignment to the HWTX-II family. Biochemistry. 2013 Apr 9;52(14):2440-52. doi: 10.1021/bi4000035. Epub 2013 Mar 29.
Ref 3 Subtype Specificity of -Toxin Tf1a from Tityus fasciolatus in Voltage Gated Sodium Channels. Toxins (Basel). 2018 Aug 22;10(9):339. doi: 10.3390/toxins10090339.
Ref 4 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 5 Discovery, Pharmacological Characterisation and NMR Structure of the Novel -Conotoxin SxIIIC, a Potent and Irreversible Na(V) Channel Inhibitor. Biomedicines. 2020 Oct 2;8(10):391. doi: 10.3390/biomedicines8100391.
Ref 6 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 7 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 8 Pharmacological characterisation of the highly Na(V)1.7 selective spider venom peptide Pn3a. Sci Rep. 2017 Jan 20;7:40883. doi: 10.1038/srep40883.
Ref 9 Corrigendum: Pharmacological characterisation of the highly Na(V)1.7 selective spider venom peptide Pn3a. Sci Rep. 2017 May 26;7:46816. doi: 10.1038/srep46816.
Ref 10 Antiallodynic effects of the selective NaV1.7 inhibitor Pn3a in a mouse model of acute postsurgical pain: evidence for analgesic synergy with opioids and baclofen. Pain. 2019 Aug;160(8):1766-1780. doi: 10.1097/j.pain.0000000000001567.
Ref 11 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 12 Spider Venom Peptide Pn3a Inhibition of Primary Afferent High Voltage-Activated Calcium Channels. Front Pharmacol. 2021 Jan 28;11:633679. doi: 10.3389/fphar.2020.633679. eCollection 2020.
Ref 13 -Theraphotoxin Pn3a inhibition of Ca(V)3.3 channels reveals a novel isoform-selective drug binding site. Elife. 2022 Jul 20;11:e74040. doi: 10.7554/eLife.74040.
Ref 14 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 15 Naja atra venom peptide reduces pain by selectively blocking the voltage-gated sodium channel Nav1.8. J Biol Chem. 2019 May 3;294(18):7324-7334. doi: 10.1074/jbc.RA118.007370. Epub 2019 Feb 25.
Ref 16 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 17 Atypical presentation in adults in the largest community outbreak of leishmaniasis in Europe (Fuenlabrada, Spain). Clin Microbiol Infect. 2015 Mar;21(3):269-73. doi: 10.1016/j.cmi.2014.10.017. Epub 2014 Oct 29.
Ref 18 High prevalence of human herpesvirus type 8 infection in patients with pulmonary tuberculosis in Taiwan. Clin Microbiol Infect. 2015 Mar;21(3):266.e5-7. doi: 10.1016/j.cmi.2014.10.015. Epub 2014 Oct 29.
Ref 19 Dynamics of hepatitis B virus quasispecies heterogeneity in association with nucleos(t)ide analogue treatment determined by MALDI-TOF MS. Clin Microbiol Infect. 2015 Mar;21(3):288.e1-4. doi: 10.1016/j.cmi.2014.10.004. Epub 2014 Oct 29.
Ref 20 Rapidly growing mycobacteria in Singapore, 2006-2011. Clin Microbiol Infect. 2015 Mar;21(3):236-41. doi: 10.1016/j.cmi.2014.10.018. Epub 2014 Nov 4.
Ref 21 Factors associated with subsequent nontuberculous mycobacterial lung disease in patients with a single sputum isolate on initial examination. Clin Microbiol Infect. 2015 Mar;21(3):250.e1-7. doi: 10.1016/j.cmi.2014.08.025. Epub 2014 Oct 29.
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