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

Quaternary structure of human small heat shock protein HSPB6 (Hsp20) in crowded media modeled by trimethylamine N-oxide (TMAO): Effect of protein phosphorylation.

Biochimie - 1 Jan 2015

Sluchanko Nikolai N, Chebotareva Natalia A, Gusev Nikolai B

Abstract excerpt

Effect of trimethylamine N-oxide (TMAO), well-known osmolyte, widely used to imitate crowded intracellular conditions, on the quaternary structure of recombinant human small heat shock protein HspB6 (Hsp20) was analyzed by means of size-exclusion chromatography, chemical crosslinking and analytical ultracentrifugation. Consistent with previous reports, in the absence of TMAO unphosphorylated, pseudophosphorylated...

Read the complete abstract on PubMed

Topics

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

Share to Heat-Shock Proteins
Share to HSP27 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrophobic and Hydrophilic Interactions

Share to Methylamines

Share to Molecular Chaperones

Share to Mutation

Share to Phosphorylation

Share to Protein Structure, Quaternary

Source

Identifiers

PMID: 25446653
DOI: 10.1016/j.biochi.2014.11.001

Genes

HSPB6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Quaternary structure of human small heat shock protein HSPB6 (Hsp20) in crowded media modeled by trimethylamine N-oxide (TMAO): Effect of protein phosphorylation.PMID 25446653Read ↗

Physico-chemical properties of two point mutants of small heat shock protein HspB6 (Hsp20) with abrogated cardioprotection.Semantic proximity Read ↗

Some properties of human small heat shock protein Hsp20 (HspB6).Semantic proximity Read ↗

Replacement of Arg in the conserved N-terminal RLFDQxFG motif affects physico-chemical properties and chaperone-like activity of human small heat shock protein HspB8 (Hsp22).Semantic proximity Read ↗

Study of HSPB6: Insights into the Properties of the Multifunctional Protective AgentSemantic proximity Read ↗

Characterization of Mutants of Human Small Heat Shock Protein HspB1 Carrying Replacements in the N-Terminal Domain and Associated with Hereditary Motor Neuron Diseases.Semantic proximity Read ↗

Forcing thermodynamically unfolded proteins to fold.Semantic proximity Read ↗

Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases.Semantic proximity Read ↗

Anisosmotic Modulation of Mutant Huntingtin Aggregation vis-a-vis HSP70 Induction─Implications for Aging, Hypo-Hydration, and Neurodegeneration.Semantic proximity Read ↗

Dissecting the Functional Role of the N-Terminal Domain of the Human Small Heat Shock Protein HSPB6Semantic proximity Read ↗

Chemical chaperones assist intracellular folding to buffer mutational variations.Semantic proximity Read ↗

Natural osmolytes remodel the aggregation pathway of mutant huntingtin exon 1.Semantic proximity Read ↗

Analysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1).Semantic proximity Read ↗

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