ReviewNucleus (Austin, Tex.)
Lamin B receptor: multi-tasking at the nuclear envelope.
Review in Nucleus (Austin, Tex.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
82 citing papers in PubMed, 165 citations in OpenAlex.
- Repair and misrepair of telomeric DNA in dynamic interactions with PML nuclear bodies and lamin B1 in doxorubicin-treated cancer cells.Nucleus (Austin, Tex.) · 2026Article
- Antagonistic contributions of A-type and B-type lamins to LBR localization and dynamics.Nucleus (Austin, Tex.) · 2026Article
- A homozygous lamin B receptor variant resulting in Pelger-Huët anomaly without skeletal dysplasia.Nucleus (Austin, Tex.) · 2026Article
- Review
- B-type lamins maintain transcriptional homeostasis by spatially controlling chromatin-speckle proximity.Nucleic acids research · 2026Article
- Envelope-Limited Chromatin Sheets (ELCS) Formation in The Nuclear Envelope of HL-60/S4 Cells.bioRxiv : the preprint server for biology · 2026Article
- Antagonistic contributions of A-type and B-type lamins to LBR localization and dynamics.bioRxiv : the preprint server for biology · 2026Article
- Setting Up to Divide: Nuclear Mechanotransduction in the Regulation of Mitosis.Results and problems in cell differentiation · 2026Review
- Mitotic dynamics of the nuclear lamina in the backstage of chromosome separation.Communications biology · 2025Review
- New Roles of bZIP-Containing Membrane-Bound Transcription Factors in Chromatin Tethering and Karyoptosis.International journal of molecular sciences · 2025Review
- Review
- Coordinated control of genome-nuclear lamina interactions by topoisomerase 2B and lamin B receptor.Nucleic acids research · 2025Article
- MyoD1 localization at the nuclear periphery is mediated by association of WFS1 with active enhancers.Nature communications · 2025Article
- The Role of Lamins in Genome Organisation: A Modelling Perspective.Sub-cellular biochemistry · 2025Review
- Chromatin phase separation and nuclear shape fluctuations are correlated in a polymer model of the nucleus.Nucleus (Austin, Tex.) · 2024Article
- Lamin chromatin binding is modulated by interactions of different LAP2α domains with lamins and chromatin.iScience · 2024Article
- An integrated structural model of the DNA damage-responsive H3K4me3 binding WDR76:SPIN1 complex with the nucleosome.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Heterogeneous flexibility can contribute to chromatin segregation in the cell nucleus.Physical review. E · 2024Article
- Article
22 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lamin B receptor (LBR) is an integral membrane protein of the interphase nuclear envelope (NE). The N-terminal end resides in the nucleoplasm, binding to lamin B and heterochromatin, with the interactions disrupted during mitosis. The C-terminal end resides within the inner nuclear membrane, retreating with the ER away from condensing chromosomes during mitotic NE breakdown. Some of these properties are interpretable in terms of our current structural knowledge of LBR, but many of the structural features remain unknown. LBR apparently has an evolutionary history which brought together at least two ancient conserved structural domains (i.e., Tudor and sterol reductase). This convergence may have occurred with the emergence of the chordates and echinoderms. It is not clear what survival values have maintained LBR structure during evolution. But it seems likely that roles in post-mitotic nuclear reformation, interphase NE growth and compartmentalization of nuclear architecture might have provided some evolutionary advantage to preservation of the LBR gene.
Indexed as
Identifiers
What 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.