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

Protein interaction patterns in different cellular environments are revealed by in-cell NMR.

Scientific reports - 24 Sept 2015

Barbieri Letizia, Luchinat Enrico, Banci Lucia

Abstract excerpt

In-cell NMR allows obtaining atomic-level information on biological macromolecules in their physiological environment. Soluble proteins may interact with the cellular environment in different ways: either specifically, with their functional partners, or non-specifically, with other cellular components. Such behaviour often causes the disappearance of the NMR signals. Here we show that by introducing mutations on...

Read the complete abstract on PubMed

Topics

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

Share to Carrier Proteins
Share to HEK293 Cells
Share to Intracellular Space

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnetic Resonance Spectroscopy

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Profilins

Share to Protein Interaction Mapping

Share to Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 26399546
DOI: 10.1038/srep14456
PMCID: PMC4585868

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

Protein interaction patterns in different cellular environments are revealed by in-cell NMR.PMID 26399546Read ↗

In-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and Maturation.Semantic proximity Read ↗

Correlating the structure and activity of <i>Y. pestis</i> Ail in a bacterial cell envelopeSemantic proximity Read ↗

Visualizing Proteins in Human Cells at Near‐Physiological Concentrations with Sensitive 19 F NMR Chemical TagsSemantic proximity Read ↗

Self-Assembly of Human Profilin-1 Detected by Carr-Purcell-Meiboom-Gill Nuclear Magnetic Resonance (CPMG NMR) Spectroscopy.Semantic proximity Read ↗

NMR spectroscopy captures the essential role of dynamics in regulating biomolecular function.Semantic proximity Read ↗

Monitoring DNA-Ligand Interactions in Living Human Cells Using High-Resolution NMR SpectroscopySemantic proximity Read ↗

Visualizing Molecules of Functional <i>Human</i> ProfilinSemantic proximity Read ↗

NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.Semantic proximity Read ↗

Real-time pure shift ¹⁵N HSQC of proteins: a real improvement in resolution and sensitivity.Semantic proximity Read ↗

A new carbamidemethyl-linked lanthanoid chelating tag for PCS NMR spectroscopy of proteins in living HeLa cells.Semantic proximity Read ↗

Guided reconstitution of membrane protein fragments.Semantic proximity Read ↗

Intracellular environment can change protein conformational dynamics in cells through weak interactions.Semantic proximity Read ↗

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