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

Normal-mode-analysis-guided investigation of crucial intersubunit contacts in the cAMP-dependent gating in HCN channels.

Biophysical journal - 3 Jul 2012

Marni Farzana, Wu Shengjun, Shah Gaurav M, Xu Xin-ping, Hackett Amber R, Xie Changan, Shrestha Sabisha, Liu Lin, Liu Qinglian, Zhou Lei

Abstract excerpt

Protein structures define a complex network of atomic interactions in three dimensions. Direct visualization of the structure and analysis of the interaction potential energy are not straightforward approaches to pinpoint the atomic contacts that are crucial for protein function. We used the tetrameric hyperpolarization-activated cAMP-regulated (HCN) channel as a model system to study the intersubunit contacts in...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cyclic AMP

Share to Ion Channels

Share to Molecular Sequence Data

Share to Mutation

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 22828328
DOI: 10.1016/j.bpj.2012.05.030
PMCID: PMC3388215

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Normal-mode-analysis-guided investigation of crucial intersubunit contacts in the cAMP-dependent gating in HCN channels.PMID 22828328Read ↗

Structural basis for gating inhibition by the cytoplasmic domain in HCN1 channelsSemantic proximity Read ↗

Toward decrypting the allosteric mechanism of the ryanodine receptor based on coarse-grained structural and dynamic modeling.Semantic proximity Read ↗

Computational analysis of long-range allosteric communications in CFTRSemantic proximity Read ↗

Structural Basis for Hyperpolarization-dependent Opening of the Human HCN1 ChannelSemantic proximity Read ↗

HCN Channel C-Terminal Region Speeds Activation Rates Independently of Autoinhibition.Semantic proximity Read ↗

Structural basis of a Kv7.1 potassium channel gating module: studies of the intracellular c-terminal domain in complex with calmodulin.Semantic proximity Read ↗

An Allosteric Model for Electromechanical Coupling in Cardiac CNBD ChannelsSemantic proximity Read ↗

The projection analysis of NMR chemical shifts reveals extended EPAC autoinhibition determinants.Semantic proximity Read ↗

Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel.Semantic proximity Read ↗

Structural and energetic analysis of activation by a cyclic nucleotide binding domain.Semantic proximity Read ↗

Functional organization and conformational dynamics of the nicotinic receptor: a plausible structural interpretation of myasthenic mutations.Semantic proximity Read ↗

Subunit-specific conductance of single HCN pacemaker channels at femtosiemens resolutionSemantic proximity Read ↗

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