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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Crystallin, beta B1

betaB1-crystallin, CRYBB1
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008] (from NCBI)
Papers on betaB1-crystallin
Clinical and molecular analysis of children with central pulverulent cataract from the Arabian Peninsula.
Alkuraya et al., Riyadh, Saudi Arabia. In Br J Ophthalmol, 2012
Sequencing of this gene revealed a homozygous c.171del mutation (p.N58Tfs*107) with a shared haplotype in all 16 children.
The benefits of being β-crystallin heteromers: βB1-crystallin protects βA3-crystallin against aggregation during co-refolding.
Yan et al., Beijing, China. In Biochemistry, 2012
The formation of beta-crystallin heteromers not only stabilizes the unstable acidic beta-crystallin but also protects them against aggregation during refolding from the stress-denatured states.
Truncation, cross-linking and interaction of crystallins and intermediate filament proteins in the aging human lens.
Aquilina et al., Wollongong, Australia. In Biochim Biophys Acta, 2011
The presence of significant amounts of small peptides derived from gammaS- and betaB1-crystallins in the water-insoluble fraction of the lens indicates that these interact tightly with cytoskeletal or membrane components.
Novel beta-crystallin gene mutations in Chinese families with nuclear cataracts.
Zhu et al., Beijing, China. In Arch Ophthalmol, 2011
Analyses of 20 Chinese families with hereditary nuclear congenital cataract revealed 3 novel mutations. Two of these mutations (V146M and I21N) affected betaB2-crystallin (CRYBB2). One mutation (R233H) was detected in betaB1-crystallin (CRYBB1).
A novel mutation in CRYBB1 associated with congenital cataract-microcornea syndrome: the p.Ser129Arg mutation destabilizes the βB1/βA3-crystallin heteromer but not the βB1-crystallin homomer.
Zhu et al., Beijing, China. In Hum Mutat, 2011
study identified a novel heterozygous p.Ser129Arg mutation in CRYBB1 in a congenital cataract-microcornea syndrome family of Chinese origin
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