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

The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.

Cell stress & chaperones - 1 Sept 2018

Jovcevski Blagojce, Andrew Aquilina J, Benesch Justin L P, Ecroyd Heath

Abstract excerpt

αB-Crystallin (HSPB5) is a small heat-shock protein that is composed of dimers that then assemble into a polydisperse ensemble of oligomers. Oligomerisation is mediated by heterologous interactions between the C-terminal tail of one dimer and the core "α-crystallin" domain of another and stabilised by interactions made by the N-terminal region. Comparatively little is known about the latter contribution, but...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Crystallin B Chain
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Domains

Share to Protein Multimerization

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 29520626
DOI: 10.1007/s12192-018-0889-y
PMCID: PMC6111084

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

The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.PMID 29520626Read ↗

Deletion of Specific Conserved Motifs from the N-Terminal Domain of αB-Crystallin Results in the Activation of Chaperone Functions.Semantic proximity Read ↗

The p.K90N mutation in human HSPB5 highlights the critical role of lysine 90 in chaperone function and structural integrity.Semantic proximity Read ↗

The role of the conserved COOH-terminal triad in alphaA-crystallin aggregation and functionality.Semantic proximity Read ↗

Structural and functional studies of D109A human αB-crystallin contributing to the development of cataract and cardiomyopathy diseasesSemantic proximity Read ↗

Investigating the role of double mutations R12C/P20R, and R12C/R69C on structure, chaperone-like activity, and amyloidogenic properties of human αB-crystallin.Semantic proximity Read ↗

The interaction between alphaA- and alphaB-crystallin is sequence-specific.Semantic proximity Read ↗

Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation.Semantic proximity Read ↗

Structural and Functional Consequences of Age-Related Isomerization in α-CrystallinsSemantic proximity Read ↗

Structural and functional defects caused by point mutations in the alpha-crystallin domain of a bacterial alpha-heat shock protein.Semantic proximity Read ↗

Engineering of a Polydisperse Small Heat-Shock Protein Reveals Conserved Motifs of Oligomer PlasticitySemantic proximity Read ↗

The Double-Edged Sword of αB-Crystallin Chaperone Activity: Insights from P39L Mutant at N-terminal regionSemantic proximity Read ↗

Unveiling the structural and functional consequences of the p.D109G pathogenic mutation in human αB-Crystallin responsible for restrictive cardiomyopathy and skeletal myopathy.Semantic proximity Read ↗

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