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Keywords: lamin
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Articles
Biochem Soc Trans (2018) 46 (1): 37–42.
Published: 01 December 2017
...Howard J. Worman Mutations in the lamin A/C gene ( LMNA ) encoding intermediate filament proteins associated with the inner nuclear membrane cause diseases known as laminopathies. Most LMNA mutations cause dilated cardiomyopathy with variable skeletal muscular dystrophy. Cell signaling...
Articles
Biochem Soc Trans (2017) 45 (6): 1333–1344.
Published: 17 November 2017
... © 2017 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2017 cancer karyoplasmic ratio lamin NET nuclear size A larger nuclear size accompanied by a reduced heterochromatin interaction with the nuclear periphery might also enable faster...
Articles
Biochem Soc Trans (2017) 45 (6): 1279–1293.
Published: 10 November 2017
... mutation in exon 11 of the LMNA gene (c.1824C>T, p.G608G), resulting in the increased usage of a cryptic splice site and production of a truncated unprocessed lamin A protein named progerin. Since the genetic cause for HGPS was published in 2003, numerous potential treatment options have rapidly emerged...
Articles
Biochem Soc Trans (2011) 39 (6): 1715–1718.
Published: 21 November 2011
...Christopher J. Hutchison Progeroid laminopathies are characterized by the abnormal processing of lamin A, the appearance of misshapen nuclei, and the accumulation and persistence of DNA damage. In the present article, I consider the contribution of defective DNA damage pathways to the pathology...
Articles
Biochem Soc Trans (2011) 39 (6): 1729–1734.
Published: 21 November 2011
... to the nucleus. Nesprins and SUN proteins, located at the nuclear envelope, form the LINC (linker of nucleoskeleton and cytoskeleton) complex that connects the nucleus to the cytoskeleton; underlying nuclear lamins contribute to anchoring LINC complex components at the nuclear envelope. Disruption of the LINC...
Articles
Biochem Soc Trans (2010) 38 (1): 297–300.
Published: 19 January 2010
...Clare R. Foster; Stefan A. Przyborski; Robert G. Wilson; Christopher J. Hutchison Lamins are multifunctional proteins that are often aberrantly expressed or localized in tumours. Here, we endeavour to assess their uses as cancer biomarkers: to diagnose tumours, analyse cancer characteristics...
Articles
Biochem Soc Trans (2010) 38 (1): 257–262.
Published: 19 January 2010
...Juergen Scharner; Viola F. Gnocchi; Juliet A. Ellis; Peter S. Zammit A-type laminopathies are a group of diseases resulting from mutations in the intermediate filament proteins lamin A and C (both encoded by the LMNA gene), but for which the pathogenic mechanisms are little understood. In some...
Articles
Biochem Soc Trans (2010) 38 (1): 301–306.
Published: 19 January 2010
...Mirta Boban; Juliane Braun; Roland Foisner Nuclear intermediate filaments formed by A- and B-type lamins are central components of the nucleoskeleton and are required for the architecture and integrity of the nucleus. There is growing evidence that lamins are also involved in regulatory pathways...
Articles
Biochem Soc Trans (2010) 38 (1): 253–256.
Published: 19 January 2010
... encoding lamins and associated proteins have been shown to cause a diverse range of human diseases often called laminopathies or nuclear envelopathies. Most of these diseases have tissue-selective phenotypes, suggesting that the nuclear envelope must function in cell-type- and developmental-stage-specific...
Articles
Biochem Soc Trans (2008) 36 (6): 1378–1383.
Published: 19 November 2008
... community. It is a permanent network of core filaments underlying thicker fibres which is proposed to be a platform for numerous important nuclear activities such as transcription and DNA repair. Interestingly, A- and B-type lamin proteins and emerin are components of this nuclear structure; however...
Articles
Biochem Soc Trans (2008) 36 (6): 1350–1353.
Published: 19 November 2008
...Naomi D. Willis; Robert G. Wilson; Christopher J. Hutchison Abnormalities in the expression, distribution and structural organization of A-type lamins are most commonly associated with a spectrum of inherited disorders which predominantly affect mesenchymal lineages, collectively known...
Articles
Biochem Soc Trans (2008) 36 (6): 1344–1349.
Published: 19 November 2008
... and EMD , responsible for EDMD (Emery–Dreifuss muscular dystrophy). LMNA encodes A-type lamins, whereas EMD encodes emerin, both located in the nuclear envelope. Mutation or loss of A-type lamins or emerin in the terminally differentiated myonuclei of muscle fibres results in muscle damage. Importantly...
Articles
Biochem Soc Trans (2008) 36 (6): 1335–1338.
Published: 19 November 2008
...Susan C. Brown; Richard J. Piercy; Francesco Muntoni; Caroline A. Sewry EDMD (Emery–Dreifuss muscular dystrophy) is caused by mutations in either the gene encoding for lamin A/C ( LMNA ) located at 1q21.2–q21.3 or emerin ( EMD ) located at Xq28. Autosomal dominant EDMD caused by LMNA mutations...
Articles
Biochem Soc Trans (2008) 36 (6): 1339–1343.
Published: 19 November 2008
...Martin W. Goldberg; Jindriska Fiserova; Irm Huttenlauch; Reimer Stick Lamins are intermediate filament proteins that form a network lining the inner nuclear membrane. They provide mechanical strength to the nuclear envelope, but also appear to have many other functions as reflected in the array...
Articles
Biochem Soc Trans (2005) 33 (5): 1073–1077.
Published: 26 October 2005
... of unknown function or AGPAT2 encoding an enzyme involved in triacylglycerol synthesis. The Dunnigan syndrome [FPLD2 (familial partial lipodystrophy of the Dunnigan type)] is due to mutations in LMNA encoding the lamin A/C, belonging to the complex group of laminopathies that could comprise muscular...