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
Open accessAbstract
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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“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]
Experimental — accuracy not yet measuredIn the citing paper
“The nuclear surface of the nuclear envelope is lined by structural proteins, which contributes to the size, shape, and stability o the nucleus (41).”
From Senolytic Combination of Dasatinib and Quercetin Alleviates Intestinal Senescence and Inflammation and Modulates the Gut Microbiome in Aged Mice (2021) · cites this paper as [41]
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Cites
INTERMEDIATE FILAMENTS: Structure, Dynamics, Function and Disease
Fuchs, E. V., & Weber, K. (1994) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.63.070194.002021 · Cited by 1,427
Coupling of the nucleus and cytoplasm: Role of the LINC complex
Crisp, M., Liu, Q., Roux, K. J., Rattner, J. B., Shanahan, C. M., Burke, B. E., Stahl, P. D., & Hodzic, D. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200509124 · Cited by 1,379
Loss of a-Type Lamin Expression Compromises Nuclear Envelope Integrity Leading to Muscular Dystrophy
Sullivan, T. L., Escalante‐Alcalde, D., Bhatt, H., Anver, M. R., Bhat, N. R., Nagashima, K., Stewart, C. L., & Burke, B. E. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.5.913 · Cited by 1,224
The nuclear lamina is a meshwork of intermediate-type filaments
Aebi, U., Cohn, J., Buhle, L., & Gerace, L. (1986) · Nature · doi:10.1038/323560a0 · Cited by 982
The nuclear envelope lamina is reversibly depolymerized during mitosis
Gerace, L., & Blobel, G. (1980) · Cell · doi:10.1016/0092-8674(80)90409-2 · Cited by 962
Differences in the Localization and Morphology of Chromosomes in the Human Nucleus
Croft, J. A., Bridger, J. M., Boyle, S., Perry, P., Teague, P., & Bickmore, W. A. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.6.1119 · Cited by 933
Self-citationThe nuclear lamina comes of age
Gruenbaum, Y., Margalit, A., Goldman, R. D., Shumaker, D. K., & Wilson, K. L. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1550 · Cited by 836
McKeon, F., Kirschner, M. W., & Caput, D. (1986) · Nature · doi:10.1038/319463a0 · Cited by 827
Nuclear Lamins: Their Structure, Assembly, and Interactions
Stuurman, N., Heins, S., & Aebi, U. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1998.3987 · Cited by 726
Fisher, D. Z., Chaudhary, N., & Blobel, G. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.17.6450 · Cited by 721
Cited by
Sorted by citations
Lamin B1 loss is a senescence-associated biomarker
Freund, A., Laberge, R.-M., Demaria, M., & Campisi, J. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-10-0884 · Cited by 1,046
Saccon, T. D., Nagpal, R., Yadav, H., Cavalcante, M. B., Nunes, A. D. D. C., Schneider, A., Gesing, A., Hughes, B., Yousefzadeh, M., Tchkonia, T., et al. (2021) · The Journals of Gerontology: Series A · doi:10.1093/gerona/glab002 · Cited by 247
Mehta, I. S., Amira, M., Harvey, A., & Bridger, J. M. (2010) · Genome biology · doi:10.1186/gb-2010-11-1-r5 · Cited by 193
Self-citationDenais, C., & Lammerding, J. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4899-8032-8_20 · Cited by 189
The ATM signaling network in development and disease
Stracker, T. H., Roig, I., Knobel, P. A., & Marjanović, M. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00037 · Cited by 192
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
- bronze
- doi.org
- 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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