ATP-dependent interaction of the cytosolic domains of the inwardly rectifying K+ channel Kir6.2 revealed by fluorescence resonance energy transfer (Q35121325)

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scholarly article

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English	ATP-dependent interaction of the cytosolic domains of the inwardly rectifying K+ channel Kir6.2 revealed by fluorescence resonance energy transfer	scholarly article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

ATP-dependent interaction of the cytosolic domains of the inwardly rectifying K+ channel Kir6.2 revealed by fluorescence resonance energy transfer (English)

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Jonathan D Lippiat

object named as

Jonathan D Lippiat

2

0 references

4

object named as

Guy A Rutter

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Frances Ashcroft

3

object named as

Frances M Ashcroft

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

author name string

Takashi Tsuboi

1

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Europe PubMed Central

PubMed publication ID

6 August 2017

language of work or name

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publication date

17 December 2003

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Europe PubMed Central

PubMed publication ID

6 August 2017

Proceedings of the National Academy of Sciences of the United States of America

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Europe PubMed Central

PubMed publication ID

6 August 2017

101

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Europe PubMed Central

PubMed publication ID

6 August 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

76-81

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

Molecular mechanism for ATP-dependent closure of the K+ channel Kir6.2

1 reference

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Crystal structure of the potassium channel KirBac1.1 in the closed state

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Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution

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Interaction of the cytosolic domains of the Kir6.2 subunit of the K(ATP) channel is modulated by sulfonylureas

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The I182 region of k(ir)6.2 is closely associated with ligand binding in K(ATP) channel inhibition by ATP

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Diverse roles of K(ATP) channels learned from Kir6.2 genetically engineered mice

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Mapping of the physical interaction between the intracellular domains of an inwardly rectifying potassium channel, Kir6.2

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ATP-sensitive K+ channels and insulin secretion: their role in health and disease.

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ATP inhibition of KATP channels: control of nucleotide sensitivity by the N-terminal domain of the Kir6.2 subunit

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The green fluorescent protein

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Molecular analysis of ATP-sensitive K channel gating and implications for channel inhibition by ATP.

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The sulphonylurea receptor SUR1 regulates ATP-sensitive mouse Kir6.2 K+ channels linked to the green fluorescent protein in human embryonic kidney cells (HEK 293).

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Molecular determinants of KATP channel inhibition by ATP.

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MgATP activates the beta cell KATP channel by interaction with its SUR1 subunit.

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Octameric stoichiometry of the KATP channel complex

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Truncation of Kir6.2 produces ATP-sensitive K+ channels in the absence of the sulphonylurea receptor

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ATP-sensitive potassium channels: an overview.

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Glucose induces closure of single potassium channels in isolated rat pancreatic beta-cells

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Gating of inward rectifier K+ channels by proton-mediated interactions of N- and C-terminal domains.

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Direct photoaffinity labeling of Kir6.2 by [gamma-(32)P]ATP-[gamma]4-azidoanilide.

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The role of lysine 185 in the kir6.2 subunit of the ATP-sensitive channel in channel inhibition by ATP.

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Involvement of the N-terminus of Kir6.2 in the inhibition of the KATP channel by ATP.

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Identifiers

10.1073/PNAS.0306347101

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Europe PubMed Central

PubMed publication ID

6 August 2017

2004PNAS..101...76T

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PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 August 2017

ResearchGate publication ID

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