ArticleMolecular vision2010
The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.
Article in Molecular vision, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- The Structural Order of Crystallin Proteins During Early Human Lens Development.Investigative ophthalmology & visual science · 2026Article
- Impact of Salinity Stress on Antioxidant Enzyme Activity, Histopathology, and Gene Expression in the Hepatopancreas of the Oriental River Prawn,Animals : an open access journal from MDPI · 2025Article
- Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins.The Biochemical journal · 2025Article
- Chaperone activity of human small heat shock protein-GST fusion proteins.Cell stress & chaperones · 2017Article
- The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.Cell stress & chaperones · 2017Article
- Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS.The Journal of biological chemistry · 2016Article
- The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.Nature structural & molecular biology · 2015Article
- Small heat-shock proteins: important players in regulating cellular proteostasis.Cellular and molecular life sciences : CMLS · 2015Review
- Article
- Changes in solvent accessibility of wild-type and deamidated βB2-crystallin following complex formation with αA-crystallin.Experimental eye research · 2012Article
- Single-molecule fluorescence-based approach reveals novel mechanistic insights into human small heat shock protein chaperone function.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeThe molecular chaperone αB-crystallin is found in high concentrations in the lens and is present in all major body tissues. Its structure and the mechanism by which it protects its target protein from aggregating and precipitating are not known.
methodsDynamic light scattering and X-ray solution scattering techniques were used to investigate structural features of the αB-crystallin oligomer when complexed with target proteins under mild stress conditions, i.e., reduction of α-lactalbumin at 37 °C and malate dehydrogenase when heated at 42 °C. In this investigation, the size, shape and particle distribution of the complexes were determined in real-time following the induction of stress.
resultsOverall, it is observed that the mass distribution, hydrodynamic radius, and spherical shape of the αB-crystallin oligomer do not alter significantly when it complexes with its target protein.
conclusionsThe data are consistent with the target protein being located in the outer protein shell of the αB-crystallin oligomer where it is readily accessible for possible refolding via the action of other molecular chaperones.
Indexed as
Identifiers
21152271PMC2998715W2099866231What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.