Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Molecular Dynamics Simulations of KirBac1.1 Mutants Reveal Global Gating Changes of Kir Channels.

Journal of chemical information and modeling - 27 Apr 2015

Linder Tobias, Wang Shizhen, Zangerl-Plessl Eva-Maria, Nichols Colin G, Stary-Weinzinger Anna

Abstract excerpt

Prokaryotic inwardly rectifying (KirBac) potassium channels are homologous to mammalian Kir channels. Their activity is controlled by dynamical conformational changes that regulate ion flow through a central pore. Understanding the dynamical rearrangements of Kir channels during gating requires high-resolution structure information from channels crystallized in different conformations and insight into the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Hydrogen Bonding
Share to Ion Channel Gating

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipid Metabolism

Share to Molecular Dynamics Simulation

Share to Mutant Proteins

Share to Potassium Channels, Inwardly Rectifying

Share to Rotation

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 25794351
DOI: 10.1021/acs.jcim.5b00010
PMCID: PMC4415035

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular Dynamics Simulations of KirBac1.1 Mutants Reveal Global Gating Changes of Kir Channels.PMID 25794351Read ↗

Integrative Study of the Structural and Dynamical Properties of a KirBac3.1 Mutant: Functional Implication of a Highly Conserved Tryptophan in the Transmembrane Domain.Semantic proximity Read ↗

Conformational changes at cytoplasmic intersubunit interactions control Kir channel gating.Semantic proximity Read ↗

Atomistic basis of opening and conduction in mammalian inward rectifier potassium (Kir2.2) channels.Semantic proximity Read ↗

Structural rearrangements underlying ligand-gating in Kir channels.Semantic proximity Read ↗

Structural Basis for Differences in Dynamics Induced by Leu Versus Ile Residues in the CD Loop of Kir Channels.Semantic proximity Read ↗

State-dependent network connectivity determines gating in a K+ channel.Semantic proximity Read ↗

KirBac1.1: it's an inward rectifying potassium channel.Semantic proximity Read ↗

The Molecular Mechanism of Opening the Helix Bundle Crossing (HBC) Gate of a Kir Channel.Semantic proximity Read ↗

The Kir channel immunoglobulin domain is essential for Kir1.1 (ROMK) thermodynamic stability, trafficking and gating.Semantic proximity Read ↗

Structures of closed and open states of a voltage-gated sodium channel.Semantic proximity Read ↗

The differential impacts of equivalent gating-charge mutations in voltage-gated sodium channels.Semantic proximity Read ↗

Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.