A point mutation in a Shaker K+ channel changes its charybdotoxin binding site from low to high affinity.
about
Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K + channelRevisiting the role of Ca2+ in Shaker K+ channel gating.Reduced voltage sensitivity in a K+-channel voltage sensor by electric field remodeling.Mechanism of charybdotoxin block of a voltage-gated K+ channel.Slow inactivation in voltage gated potassium channels is insensitive to the binding of pore occluding peptide toxins.kappa-Conotoxin PVIIA is a peptide inhibiting the shaker K+ channel.Electrostatic distance geometry in a K+ channel vestibule.Proton probing of the charybdotoxin binding site of Shaker K+ channels.Helical structure and packing orientation of the S2 segment in the Shaker K+ channelA marine snail neurotoxin shares with scorpion toxins a convergent mechanism of blockade on the pore of voltage-gated K channels.Conformational changes in the C terminus of Shaker K+ channel bound to the rat Kvbeta2-subunitStabilization of the conductive conformation of a voltage-gated K+ (Kv) channel: the lid mechanismElectrophysiological characterization of Ts6 and Ts7, K⁺ channel toxins isolated through an improved Tityus serrulatus venom purification procedure.Mechanisms of activation of voltage-gated potassium channels.Nano-positioning system for structural analysis of functional homomeric proteins in multiple conformationsA variable residue in the pore of Kv1 channels is critical for the high affinity of blockers from sea anemones and scorpions.Generating a high affinity scorpion toxin receptor in KcsA-Kv1.3 chimeric potassium channels.Fast single-channel measurements resolve the blocking effect of Cs+ on the K+ channel.State-dependent inhibition of cystic fibrosis transmembrane conductance regulator chloride channels by a novel peptide toxin.Domain structure and conformational changes in rat KV2.1 ion channel.
P2860
Q24299971-29AF04CC-DC58-4B18-8F9C-AE3FB0E10FA9Q27678292-BD92DCDA-40D9-4111-8589-5B4A0C7F9C36Q28363697-F0322EE6-47B5-4933-9F79-B0EF6D6E83E8Q33739991-EABEB06B-4164-4F79-8588-C115857244AFQ34019855-D10BC883-CC10-4AE1-A934-C5312D0875DBQ34350663-CAFF23C2-D064-49B9-B80E-A19A94CBC8B4Q34450995-A2B9ACF6-D22A-4534-91BE-640F99F71E89Q35792758-0DBC0866-EE4B-4CDC-938C-9F26E6C89D1FQ36411951-ECE8B977-0C91-4611-A0BA-25CC61BB432FQ36420402-19310DF9-B66B-4119-8507-BEBFDC0F0D42Q36436819-E8FE87C1-B192-465A-B0E9-36A0D0A54D1FQ36689497-470A6A33-A9D7-4B6B-9322-DF6FA321EF44Q36910099-C289917B-C033-4B2A-9B77-C82D7D59D89AQ37670021-A29829AD-D9C3-4E95-8D9B-A764B96B9853Q38307149-9D001F0B-B4DB-4509-82DA-D0DA57BE69F7Q40011208-71E523DB-87D8-4AF9-AB64-745B98FCDDAEQ40423398-B06C8084-DD0E-4FB4-87CE-399CDB9F1B19Q40763711-32B8846D-EFCC-42C6-9CEB-31AFFA5019D9Q42544823-BD9715B4-2319-4DE5-A9A0-C052F6F111B9Q42635175-88BEA18F-0DAD-4AF9-BB79-B178E1E4CF61Q42685144-AAEC3A9F-0492-481C-A696-A34344B436EA
P2860
A point mutation in a Shaker K+ channel changes its charybdotoxin binding site from low to high affinity.
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
A point mutation in a Shaker K ...... ite from low to high affinity.
@ast
A point mutation in a Shaker K ...... ite from low to high affinity.
@en
A point mutation in a Shaker K ...... ite from low to high affinity.
@nl
type
label
A point mutation in a Shaker K ...... ite from low to high affinity.
@ast
A point mutation in a Shaker K ...... ite from low to high affinity.
@en
A point mutation in a Shaker K ...... ite from low to high affinity.
@nl
prefLabel
A point mutation in a Shaker K ...... ite from low to high affinity.
@ast
A point mutation in a Shaker K ...... ite from low to high affinity.
@en
A point mutation in a Shaker K ...... ite from low to high affinity.
@nl
P2860
P1433
P1476
A point mutation in a Shaker K ...... site from low to high affinity
@en
P2093
P2860
P356
10.1016/S0006-3495(92)81760-5
P407
P577
1992-04-01T00:00:00Z