Use of venom peptides to probe ion channel structure and function.
about
Molecular pathophysiology and pharmacology of the voltage-sensing module of neuronal ion channelsObstructing toxin pathways by targeted pore blockageFrom foe to friend: using animal toxins to investigate ion channel functionNew Tricks of an Old Pattern: STRUCTURAL VERSATILITY OF SCORPION TOXINS WITH COMMON CYSTEINE SPACINGChaperone-mediated native folding of a β-scorpion toxin in the periplasm of Escherichia coliA Tarantula-Venom Peptide Antagonizes the TRPA1 Nociceptor Ion Channel by Binding to the S1–S4 Gating DomainSample limited characterization of a novel disulfide-rich venom peptide toxin from terebrid marine snail Terebra variegataChemical synthesis, 3D structure, and ASIC binding site of the toxin mambalgin-2Latarcins: versatile spider venom peptidesASIC and ENaC type sodium channels: conformational states and the structures of the ion selectivity filtersToxin diversity revealed by a transcriptomic study of Ornithoctonus huwena.Membrane-tethered ligands: tools for cell-autonomous pharmacological manipulation of biological circuits.Molecular dynamics study of binding of µ-conotoxin GIIIA to the voltage-gated sodium channel Na(v)1.4.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Systematic study of binding of μ-conotoxins to the sodium channel NaV1.4.Native pyroglutamation of huwentoxin-IV: a post-translational modification that increases the trapping ability to the sodium channel.Emerging trends in precision fabrication of microapertures to support suspended lipid membranes for sensors, sequencing, and beyond.MmTX1 and MmTX2 from coral snake venom potently modulate GABAA receptor activity.Production of Recombinant Alpha Neurotoxin of Scorpion Venom Mesobuthus eupeus and Analysis of its Immunogenicity.Androcin, a novel type of cysteine-rich venom peptide from Androctonus bicolor, induces akinesia and anxiety-like symptoms in mice.Molecular Diversity and Gene Evolution of the Venom Arsenal of Terebridae Predatory Marine Snails.Binding modes of μ-conotoxin to the bacterial sodium channel (NaVAb)Mechanism of Ion Permeation in Mammalian Voltage-Gated Sodium Channels.New Kunitz-Type HCRG Polypeptides from the Sea Anemone Heteractis crispaVenom On-a-Chip: A Fast and Efficient Method for Comparative Venomics.Differential evolution and neofunctionalization of snake venom metalloprotease domainsFluorescent protein-scorpion toxin chimera is a convenient molecular tool for studies of potassium channelsDesign and Synthesis of Analogues of Marine Natural Product Galaxamide, an N-methylated Cyclic Pentapeptide, as Potential Anti-Tumor Agent in Vitro.Ion channel engineering: perspectives and strategies.Modifications of natural peptides for nanoparticle and drug design.A multi-protease, multi-dissociation, bottom-up-to-top-down proteomic view of the Loxosceles intermedia venom.Molecular Simulations of Disulfide-Rich Venom Peptides with Ion Channels and Membranes.Cardiotoxin-I: an unexpectedly potent insulinotropic agent.Identification and characterization of toxins in the venom gland of the Chinese bird spider, Haplopelma hainanum, by transcriptomic analysis.Activation of band 3 mediates group A Streptococcus streptolysin S-based beta-haemolysis.Why do we study animal toxins?A computational design approach for virtual screening of peptide interactions across K(+) channel families.Orthogonal separation and identification of long-chain peptides from scorpion Buthus martensi Karsch venom by using two-dimensional mixed-mode reversed phase-reversed phase chromatography coupled to tandem mass spectrometry.Natural product modulators of human sensations and mood: molecular mechanisms and therapeutic potential.Using voltage-sensor toxins and their molecular targets to investigate NaV 1.8 gating.
P2860
Q26800090-51198FD0-BE55-4773-AC7E-864ABD7E950AQ26827489-3EB6B24D-D10F-4C5F-BB0E-9D0550D7EDDFQ26864410-085C34DD-4ACA-475D-99F3-797455424CE1Q27676696-AB76E170-ABEB-45B2-B6B9-28F41523D5DEQ27679850-0DD61EE8-F919-4ABD-AFD1-95ED681A72EDQ27681733-F0EDD8B4-EFB3-494B-B557-4AB4BD85121EQ27683121-45ADDFD0-9528-4389-92EF-9CB3625547F3Q27687917-E97D9969-508D-4336-8BC8-F73F807A4D87Q28266394-34606D20-7A32-4538-9631-179DDC5C3773Q28278216-FA715E31-711A-411B-BC5C-125817CA14B6Q33784251-8E789480-CAC5-4C45-A62C-43D93A63B9B0Q33816544-8143B1C0-67C4-4948-8D25-EE3C61F2EB9FQ34061826-FCB81923-98CF-418B-AE92-CEE7973A9E44Q34312732-4EBA6D80-91F6-4C62-9D4D-8FCFB5F7B325Q34792648-53BB5DB1-F938-4652-A78B-61E16DE4C7A6Q34795674-6A6CAE06-AB2A-484A-91DC-1ABE33D575BFQ35009631-6D17CD95-79B0-4849-A273-384E9484FED3Q35134568-5DBC1607-BA00-491F-98AA-2104AEB5AA6CQ35144485-8567CC43-7D7B-48B6-B23C-02DE13B7A99BQ35163762-E80AC32B-D035-47D2-91F8-632CD2BFF301Q35646753-B8CEC69D-5FD9-4AE0-B596-977DC831E14AQ35743263-690A72A3-3FA4-40DD-97AA-6B691467073EQ35746284-203E7EE0-B5E1-4C69-A905-DD6E98D85204Q36226721-EC31F75B-4A70-4852-A9B3-72BC57E1AD6FQ36384225-AA45EE9A-9B63-45FD-9510-C59E81353A14Q36666341-9E1F4D71-11FD-4E66-A4CE-69FD09927319Q37271728-3EDEF334-EB7C-4729-AE35-0CDA87928BCEQ37290902-BF01738A-D98D-4A6E-BDA1-AC51A884B4F8Q38247898-D0C9F5BC-78EE-4A65-8A6A-6C52C263B359Q38369494-29498EFE-8477-441A-923C-3FB5C02641FDQ38374212-3DFD0D54-6159-41DF-BDEE-8E639C5BF845Q39164064-E991756E-34C4-4BE2-95D2-16CE7D76CED8Q39312845-23F5509F-BA7F-4885-AACC-2A0DA076B819Q40201040-3EEC0BF5-F4DA-46CB-97F4-B8E9AC55227EQ40559607-A4F166D3-F299-4723-91B8-2076DB01F78BQ42957096-F7054A39-ED28-4ADE-BAF9-0ECF58CCCAEBQ43155868-724313EE-A8D0-41E2-8D3F-7D1F723CDD48Q43970043-FA17A728-6781-4A63-88FB-CD84AA894FC4Q47652702-2BE3E699-9057-4EE2-9F7A-B89CB1A94D7BQ48203350-992BE49C-5272-4949-AC41-545D838689D9
P2860
Use of venom peptides to probe ion channel structure and function.
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Use of venom peptides to probe ion channel structure and function.
@ast
Use of venom peptides to probe ion channel structure and function.
@en
type
label
Use of venom peptides to probe ion channel structure and function.
@ast
Use of venom peptides to probe ion channel structure and function.
@en
prefLabel
Use of venom peptides to probe ion channel structure and function.
@ast
Use of venom peptides to probe ion channel structure and function.
@en
P2860
P356
P1476
Use of venom peptides to probe ion channel structure and function.
@en
P2860
P304
13315-13320
P356
10.1074/JBC.R109.076596
P407
P577
2010-02-26T00:00:00Z