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Critical Reviews™ in Eukaryotic Gene Expression

Published 6 issues per year

ISSN Print: 1045-4403

ISSN Online: 2162-6502

The Impact Factor measures the average number of citations received in a particular year by papers published in the journal during the two preceding years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) IF: 1.6 To calculate the five year Impact Factor, citations are counted in 2017 to the previous five years and divided by the source items published in the previous five years. 2017 Journal Citation Reports (Clarivate Analytics, 2018) 5-Year IF: 2.2 The Immediacy Index is the average number of times an article is cited in the year it is published. The journal Immediacy Index indicates how quickly articles in a journal are cited. Immediacy Index: 0.3 The Eigenfactor score, developed by Jevin West and Carl Bergstrom at the University of Washington, is a rating of the total importance of a scientific journal. Journals are rated according to the number of incoming citations, with citations from highly ranked journals weighted to make a larger contribution to the eigenfactor than those from poorly ranked journals. Eigenfactor: 0.00058 The Journal Citation Indicator (JCI) is a single measurement of the field-normalized citation impact of journals in the Web of Science Core Collection across disciplines. The key words here are that the metric is normalized and cross-disciplinary. JCI: 0.33 SJR: 0.345 SNIP: 0.46 CiteScore™:: 2.5 H-Index: 67

Indexed in

Involvement of Prelamin A in Laminopathies

Volume 17, Issue 4, 2007, pp. 317-334
DOI: 10.1615/CritRevEukarGeneExpr.v17.i4.50
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ABSTRACT

The precursor protein of the nuclear lamina constituent lamin A is a 74-kDa protein called prelamin A which undergoes subsequent steps of posttranslational modification at its C-terminal CaaX residue. The unexpected finding that accumulation of unprocessable prelamin A is the molecular basis of the most severe laminopathies so far identified, including Hutchinson—Gilford progeria and restrictive dermopathy, has opened new perspectives in the study of the pathogenic mechanisms causing all lamin A/C-linked disorders, as well as new interest in the analysis of molecular mechanisms regulating prelamin A processing. However, complete knowledge of the cellular pathways affected downstream of prelamin A accumulation is still lacking, but it could give new insights both in normal and pathogenic mechanisms regulated by lamins. In this article, we review the involvement of defects of prelamin A processing in the pathogenesis of a group of laminopathies. In particular, we discuss the possibility that mutations leading to accumulation of particular forms of prelamin A result in specific nuclear abnormalities and impairment of nuclear functions leading to cell senescence or altered metabolism.

CITED BY
  1. Camozzi Daria, D’Apice Maria Rosaria, Schena Elisa, Cenni Vittoria, Columbaro Marta, Capanni Cristina, Maraldi Nadir M., Squarzoni Stefano, Ortolani Michela, Novelli Giuseppe, Lattanzi Giovanna, Altered chromatin organization and SUN2 localization in mandibuloacral dysplasia are rescued by drug treatment, Histochemistry and Cell Biology, 138, 4, 2012. Crossref

  2. Maraldi Nadir M., Lattanzi Giovanna, Cenni Vittoria, Bavelloni Alberto, Marmiroli Sandra, Manzoli Francesco A., Laminopathies and A-type lamin-associated signalling pathways, Advances in Enzyme Regulation, 50, 1, 2010. Crossref

  3. Capanni Cristina, Squarzoni Stefano, Cenni Vittoria, D’Apice Maria Rosaria, Gambineri Alessandra, Novelli Giuseppe, Wehnert Manfred, Pasquali Renato, Maraldi Nadir M., Lattanzi Giovanna, Familial partial lipodystrophy, mandibuloacral dysplasia and restrictive dermopathy feature barrier-to-autointegration factor (BAF) nuclear redistribution, Cell Cycle, 11, 19, 2012. Crossref

  4. Zini Nicoletta, Avnet Sofia, Ghisu Sonia, Maraldi Nadir Mario, Squarzoni Stefano, Baldini Nicola, Lattanzi Giovanna, Effects of prelamin A processing inhibitors on the differentiation and activity of human osteoclasts, Journal of Cellular Biochemistry, 105, 1, 2008. Crossref

  5. Rivas D., Li W., Akter R., Henderson J. E., Duque G., Accelerated Features of Age-Related Bone Loss in Zmpste24 Metalloproteinase-Deficient Mice, The Journals of Gerontology Series A: Biological Sciences and Medical Sciences, 64A, 10, 2009. Crossref

  6. Marmiroli Sandra, Bertacchini Jessika, Beretti Francesca, Cenni Vittoria, Guida Marianna, De Pol Anto, Maraldi Nadir M., Lattanzi Giovanna, A-type lamins and signaling: The PI 3-kinase/Akt pathway moves forward, Journal of Cellular Physiology, 220, 3, 2009. Crossref

  7. Maraldi Nadir M., Capanni Cristina, Cenni Vittoria, Fini Milena, Lattanzi Giovanna, Laminopathies and lamin-associated signaling pathways, Journal of Cellular Biochemistry, 112, 4, 2011. Crossref

  8. Maraldi Nadir M., Capanni Cristina, Del Coco Rosalba, Squarzoni Stefano, Columbaro Marta, Mattioli Elisabetta, Lattanzi Giovanna, Manzoli Francesco A., Muscular laminopathies: Role of prelamin A in early steps of muscle differentiation, Advances in Enzyme Regulation, 51, 1, 2011. Crossref

  9. Mattioli E, Columbaro M, Capanni C, Maraldi N M, Cenni V, Scotlandi K, Marino M T, Merlini L, Squarzoni S, Lattanzi G, Prelamin A-mediated recruitment of SUN1 to the nuclear envelope directs nuclear positioning in human muscle, Cell Death & Differentiation, 18, 8, 2011. Crossref

  10. Maraldi Nadir M., Capanni Cristina, Lattanzi Giovanna, Camozzi Daria, Facchini Andrea, Manzoli Francesco A., SREBP1 interaction with prelamin A forms: A pathogenic mechanism for lipodystrophic laminopathies, Advances in Enzyme Regulation, 48, 1, 2008. Crossref

  11. Casasola Andrea, Scalzo David, Nandakumar Vivek, Halow Jessica, Recillas-Targa Félix, Groudine Mark, Rincón-Arano Héctor, Prelamin A processing, accumulation and distribution in normal cells and laminopathy disorders, Nucleus, 7, 1, 2016. Crossref

  12. Celli Florian, Petitalot Ambre, Samson Camille, Theillet François-Xavier, Zinn-Justin Sophie, 1H, 13C and 15N backbone resonance assignment of the lamin C-terminal region specific to prelamin A, Biomolecular NMR Assignments, 12, 2, 2018. Crossref

  13. Maraldi Nadir M., Lattanzi Giovanna, Laminopathies, in Cytoskeleton and Human Disease, 2012. Crossref

  14. Lattanzi Giovanna, Prelamin A-mediated nuclear envelope dynamics in normal and laminopathic cells, Biochemical Society Transactions, 39, 6, 2011. Crossref

  15. Lattanzi Giovanna, Ortolani Michela, Columbaro Marta, Prencipe Sabino, Mattioli Elisabetta, Lanzarini Catia, Maraldi Nadir M., Cenni Vittoria, Garagnani Paolo, Salvioli Stefano, Storci Gianluca, Bonafè Massimiliano, Capanni Cristina, Franceschi Claudio, Centenarian lamins: rapamycin targets in longevity, Journal of Cell Science, 2013. Crossref

  16. Wu Jing, Guan Fei, Luo Wei, Yuan Zhi‐Wei, Chen Rong‐Qiong, Gou Xin, Shi Xin, Guo Hai‐Xiang, Fang Ke‐Wei, Retracted : Prelamin A overexpression promotes detrusor calcification/aging in urinary incontinence via prelamin A accumulation , Journal of Cellular Physiology, 234, 10, 2019. Crossref

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