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

Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants.

Physical chemistry chemical physics : PCCP - 21 Nov 2013

Prasanna Xavier, Praveen P J, Sengupta Durba

Abstract excerpt

The association of transmembrane helices is an important event in several biological processes, but the factors governing association, especially the non-specific environmental effects, have still not been elucidated. Here, we use coarse-grain molecular dynamics simulations to study the association of ErbB2 transmembrane helices and three "oncogenic mutants." Self-assembly simulations and the dimerization...

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 Dimerization
Share to Lipid Bilayers

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

Share to Molecular Dynamics Simulation

Share to Protein Structure, Secondary

Share to Receptor, ErbB-2

Share to Thermodynamics

Source

Identifiers

PMID: 24096861
DOI: 10.1039/c3cp52447g

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

Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants.PMID 24096861Read ↗

Lipid-mediated interactions tune the association of glycophorin A helix and its disruptive mutants in membranes.Semantic proximity Read ↗

Mapping the free energy landscape of K-Ras4B dimerizationSemantic proximity Read ↗

Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state.Semantic proximity Read ↗

Dynamical rearrangement of human epidermal growth factor receptor 2 upon antibody binding: effects on the dimerizationSemantic proximity Read ↗

Membrane insertion and dimerization of glycophorin-A mutations studied by free energy simulations.Semantic proximity Read ↗

Free Energy Landscape of Lipid Interactions with Regulatory Binding Sites on the Transmembrane Domain of the EGF Receptor.Semantic proximity Read ↗

Additive energetic contributions of multiple peptide positions determine the relative promiscuity of viral and human sequences for PDZ domain targetsSemantic proximity Read ↗

Identification of a region within the ErbB2/HER2 intracellular domain that is necessary for ligand-independent association.Semantic proximity Read ↗

On a mechanistic impact of transmembrane tetramerization in pathological activation of RTKsSemantic proximity Read ↗

Leukocyte integrin αLβ2 transmembrane association dynamics revealed by coarse-grained molecular dynamics simulations.Semantic proximity Read ↗

The effect of hydrophilic substitutions and anionic lipids upon the transverse positioning of the transmembrane helix of the ErbB2 (neu) protein incorporated into model membrane vesicles.Semantic proximity Read ↗

Detailed description of an alpha helix-->pi bulge transition detected by molecular dynamics simulations of the p185c-erbB2 V659G transmembrane domain.Semantic proximity Read ↗

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