Engineered interaction between SUR1 and Kir6.2 that enhances ATP sensitivity in KATP channels.
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The Nucleotide-Binding Sites of SUR1: A Mechanistic ModelSulfonylurea receptors regulate the channel pore in ATP-sensitive potassium channels via an intersubunit salt bridgeEngineered Kir6.2 mutations that correct the trafficking defect of K(ATP) channels caused by specific SUR1 mutationsStructurally distinct ligands rescue biogenesis defects of the KATP channel complex via a converging mechanism.KATP Channels in the Cardiovascular System.Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipidsCryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating.Anti-diabetic drug binding site in a mammalian KATP channel revealed by Cryo-EM.Probing Subunits Interactions in KATP Channels Using Photo-Crosslinking via Genetically Encoded p-Azido-L-phenylalanine.Molecular structure of human KATP in complex with ATP and ADP.Cryo-electron microscopy structures and progress toward a dynamic understanding of KATP channels.
P2860
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P2860
Engineered interaction between SUR1 and Kir6.2 that enhances ATP sensitivity in KATP channels.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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2012年论文
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name
Engineered interaction between ...... sensitivity in KATP channels.
@ast
Engineered interaction between ...... sensitivity in KATP channels.
@en
type
label
Engineered interaction between ...... sensitivity in KATP channels.
@ast
Engineered interaction between ...... sensitivity in KATP channels.
@en
prefLabel
Engineered interaction between ...... sensitivity in KATP channels.
@ast
Engineered interaction between ...... sensitivity in KATP channels.
@en
P2093
P2860
P356
P1476
Engineered interaction between ...... sensitivity in KATP channels.
@en
P2093
Emily B Pratt
Joel W Gay
Show-Ling Shyng
P2860
P304
P356
10.1085/JGP.201210803
P577
2012-07-16T00:00:00Z