Cited by 123Nuclear Structure and FunctionSkin and Cellular Biology ResearchGenomics and Chromatin Dynamics

The DOI matches its Crossref record; 69 of the 69 references it cites were found in a registry or an index.

The nuclear lamina. Both a structural framework and a platform for genome organization

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Abstract

The inner face of the nuclear envelope of metazoan cells is covered by a thin lamina consisting of a one-layered network of intermediate filaments interconnecting with a complex set of transmembrane proteins and chromatin associating factors. The constituent proteins, the lamins, have recently gained tremendous recognition, because mutations in the lamin A gene, LMNA, are the cause of a complex group of at least 10 different diseases in human, including the Hutchinson-Gilford progeria syndrome. The analysis of these disease entities has made it clear that besides cytoskeletal functions, the lamina has an important role in the "behaviour" of the genome and is, probably as a consequence of this function, intimately involved in cell fate decisions. Furthermore, these functions are related to the involvement of lamins in organizing the position and functional state of interphase chromosomes as well as to the occurrence of lamins and lamina-associated proteins within the nucleoplasm. However, the structural features of these lamins and the nature of the factors that assist them in genome organization present an exciting challenge to modern biochemistry and cell biology.

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Crossref · 10.1111/j.1742-4658.2007.05694.x

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  • Lamina-associated domains (LADs), typically located at the nuclear periphery, are enriched in repressive chromatin marks and correlate with low transcriptional activity.

    “Lamina-associated domains (LADs), typically located at the nuclear periphery, are enriched in repressive chromatin marks and correlate with low transcriptional activity [74,75].”

    From Origin and Evolution of Genes in Eukaryotes: Mechanisms, Dynamics, and Functional Implications (2025) · cites this paper as [74]

    In “Genome organization and the nuclear lamina” (page unavailable), the paper says that gene-poor chromosomes lie at the nuclear periphery, abutting the lamina. It does not identify lamina-associated domains or report their enrichment in repressive chromatin marks or a correlation with low transcriptional activity; it says the role of positioning in gene-expression control remains unclear. (LLM, conf=0.86)

    Experimental — accuracy not yet measured
  • The nuclear surface of the nuclear envelope is lined by structural proteins, which contributes to the size, shape, and stability of the nucleus.

    “The nuclear surface of the nuclear envelope is lined by structural proteins, which contributes to the size, shape, and stability o the nucleus (41).”

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Metadata

Authors
Bridger, J. M., Foeger, N., Kill, I. R., & Herrmann, H.
Affiliations
  • Brunel University of London (GB)
  • Vienna Biocenter (AT)
  • German Cancer Research Center (DE)
Venue
The FEBS Journal
Publisher
Wiley
Published
2007-02-28
Volume
274
Issue
6
Pages
1354-1361
ISSN
  • 1742-464X (ISSN-L)
  • 1742-4658
OpenAlex
W1482103235
Cited by
123
References
69
Citations by year
2026: 1 · 2025: 4 · 2024: 4 · 2023: 3 · 2022: 2 · 2021: 5 · 2020: 2 · 2019: 2 · 2018: 4 · 2017: 2 · 2016: 3 · 2015: 6 · 2014: 4 · 2013: 7 · 2012: 8
FWCI
1.36
Type
journal article
Language
en
Open access
Locations
  • FEBS Journal (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Deutsches Krebsforschungszentrum
  • European Commission
  • Austrian Science Fund
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
nuclear lamina, nuclear lamins, lamin A/C, Hutchinson-Gilford progeria syndrome, nuclear envelope, intermediate filaments, chromatin proteins, genome organization, interphase chromosomes, cell fate determination
MeSH terms
Protein Conformation, Proteins, Genome, Nuclear Lamina

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