Random mutagenesis screening indicates the absence of a separate H+-sensor in the pH-sensitive Kir channels

Random mutagenesis screening indicates the absence of a separate H+-sensor in the pH-sensitive Kir channels

عرض إصدارات أخرى (2)

Several inwardly-rectifying (Kir) potassium channels (Kin l 1, Kir41 and Kir4 2) are characterised by their sensitivity to inhibition by intracellular H+ within the physiological range The mechanism by which these channels are regulated by intracellular pH has been the subject of intense scrutiny fo...

وصف كامل

التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	Paynter, J, Shang, L, Bollepalli, M, Baukrowitz, T, Tucker, S
التنسيق:	Journal article
اللغة:	English
منشور في:	LANDES BIOSCIENCE 2010

مواد مشابهة

Random mutagenesis screening indicates the absence of a separate H(+)-sensor in the pH-sensitive Kir channels.
حسب: Paynter, J, وآخرون
منشور في: (2010)

Random mutagenesis screening indicates the absence of a separate H(+)-sensor in the pH-sensitive Kir channels.
حسب: Paynter, J, وآخرون
منشور في: (2010)

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Structural and functional analysis of the putative pH sensor in the Kir1.1 (ROMK) potassium channel.
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H bonding at the helix-bundle crossing controls gating in Kir potassium channels.
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Differential pH sensitivity of Kir4.1 and Kir4.2 and their modulation by heteropolymerisation with Kir5.1
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Conformational rearrangements during PIP2 gating in Kir channels
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A Structural Model of a Kir Channel in the Open State Derived from Mutagenic Scanning of the Pore Gating Energetics
حسب: Bollepalli, M, وآخرون
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Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor.
حسب: Tucker, S, وآخرون
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Inward rectification in KATP channels: a pH switch in the pore.
حسب: Baukrowitz, T, وآخرون
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Genetic Inactivation of Kcnj16 Identifies Kir5.1 as an Important Determinant of Neuronal PCO2/pH Sensitivity
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pH dependence of the inwardly rectifying potassium channel, Kir5.1, and localization in renal tubular epithelia.
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Non-equivalent role of TM2 gating hinges in heteromeric Kir4.1/Kir5.1 potassium channels.
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State-dependent network connectivity determines gating in a K+ channel.
حسب: Bollepalli, M, وآخرون
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Identification of gain of function mutations in KirBac potassium channels by genetic complementation in K+ auxotrophic strains of E-coli and yeast.
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Intrinsic sensitivity of Kir1.1 (ROMK) to glibenclamide in the absence of SUR2B. Implications for the identity of the renal ATP-regulated secretory K+ channel.
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Functional complementation and genetic deletion studies of KirBac channels: Activatory mutations highlight gating-sensitive domains
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Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.
حسب: Paynter, J, وآخرون
منشور في: (2010)

The role of lysine 185 in the kir6.2 subunit of the ATP-sensitive channel in channel inhibition by ATP.
حسب: Reimann, F, وآخرون
منشور في: (1999)

Long chain CoA esters as competitive antagonists of phosphatidylinositol 4,5-bisphosphate activation in Kir channels.
حسب: Rapedius, M, وآخرون
منشور في: (2005)

Structural changes in the cytoplasmic pore of the Kir1.1 channel during pH<sub>i</sub>-gating probed by FRET
حسب: Shieh Ru-Chi, وآخرون
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Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.
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Evaluation of Root pH Change Through Gel Containing pH-sensitive Indicator Bromocresol Purple
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Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating.
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منشور في: (2012)

Correction Notice: Evaluation of Root pH Change Through Gel Containing pH-sensitive Indicator Bromocresol Purple
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منشور في: (2018-04-01)

Sensitivity of the plant vacuolar malate channel to pH, Ca2+ and anion-channel blockers.
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K2P and Kir K+ Channels in Physiological Bilayers
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pH sensitive adsorption of polypeptide/sodium dodecyl sulfate mixtures.
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How highly charged anionic lipids bind and regulate ion channels.
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