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

Membrane-binding mechanism of a peripheral membrane protein through microsecond molecular dynamics simulations.

Journal of molecular biology - 9 Nov 2012

Rogaski Brent, Klauda Jeffery B

Abstract excerpt

A homologue oxysterol binding protein of yeast (Osh4) peripherally binds to organelle and plasma membranes and promotes lipid transport and membrane contact. Extensive molecular dynamics simulations of Osh4 are used to characterize the structure and mechanism of protein attachment to various mode...

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 Lipids
Share to Membrane Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Binding

Source

Identifiers

PMID: 22925581
DOI: 10.1016/j.jmb.2012.08.015

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-22925581-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Membrane-binding mechanism of a peripheral membrane protein through microsecond molecular dynamics simulations.PMID 22925581Read ↗

Lipid-regulated sterol transfer between closely apposed membranes by oxysterol-binding protein homologues.Semantic proximity Read ↗

Dynamics and energetics of the mammalian phosphatidylinositol transfer protein phospholipid exchange cycle.Semantic proximity Read ↗

Probing the dynamic regulation of peripheral membrane proteins using hydrogen deuterium exchange-MS (HDX-MS).Semantic proximity Read ↗

In silico modeling human VPS13 proteins associated with donor and target membranes suggests lipid transfer mechanisms.Semantic proximity Read ↗

A new targeting motif for endoplasmic reticulum surface proteinsSemantic proximity Read ↗

Using Hydrogen-Deuterium Exchange Mass Spectrometry to Examine Protein-Membrane Interactions.Semantic proximity Read ↗

Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II.Semantic proximity Read ↗

Flexible and Extended Linker Domains Support Efficient Targeting of Heh2 to the Inner Nuclear Membrane.Semantic proximity Read ↗

<i>In silico</i> modelling human VPS13 proteins associated with donor and target membranes suggests lipid transfer mechanismsSemantic proximity Read ↗

Unraveling membrane properties at the organelle-level with LipidDynSemantic proximity Read ↗

Resurrection of a functional phosphatidylinositol transfer protein from a pseudo-Sec14 scaffold by directed evolution.Semantic proximity Read ↗

A hot-spot motif characterizes the interface between a designed ankyrin-repeat protein and its target ligand.Semantic proximity Read ↗

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