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The protein kinase Akt/PKB regulates both prelamin A degradation and Lmna gene expression.

Bertacchini J, Beretti F, Cenni V, Guida M, Gibellini F, Mediani L, Marin O, Maraldi NM, de Pol A, Lattanzi G, Cocco L, Marmiroli S.

FASEB J. 2013 Jun;27(6):2145-55. doi: 10.1096/fj.12-218214. Epub 2013 Feb 21.


Lamin A Ser404 is a nuclear target of Akt phosphorylation in C2C12 cells.

Cenni V, Bertacchini J, Beretti F, Lattanzi G, Bavelloni A, Riccio M, Ruzzene M, Marin O, Arrigoni G, Parnaik V, Wehnert M, Maraldi NM, de Pol A, Cocco L, Marmiroli S.

J Proteome Res. 2008 Nov;7(11):4727-35. doi: 10.1021/pr800262g. Epub 2008 Sep 23.


Prelamin A-mediated nuclear envelope dynamics in normal and laminopathic cells.

Lattanzi G.

Biochem Soc Trans. 2011 Dec;39(6):1698-704. doi: 10.1042/BST20110657. Review.


The truncated prelamin A in Hutchinson-Gilford progeria syndrome alters segregation of A-type and B-type lamin homopolymers.

Delbarre E, Tramier M, Coppey-Moisan M, Gaillard C, Courvalin JC, Buendia B.

Hum Mol Genet. 2006 Apr 1;15(7):1113-22. Epub 2006 Feb 15.


Prelamin A and lamin A appear to be dispensable in the nuclear lamina.

Fong LG, Ng JK, Lammerding J, Vickers TA, Meta M, Coté N, Gavino B, Qiao X, Chang SY, Young SR, Yang SH, Stewart CL, Lee RT, Bennett CF, Bergo MO, Young SG.

J Clin Invest. 2006 Mar;116(3):743-52.


Emerin-prelamin A interplay in human fibroblasts.

Capanni C, Del Coco R, Mattioli E, Camozzi D, Columbaro M, Schena E, Merlini L, Squarzoni S, Maraldi NM, Lattanzi G.

Biol Cell. 2009 Sep;101(9):541-54. doi: 10.1042/BC20080175.


Lamin A precursor induces barrier-to-autointegration factor nuclear localization.

Capanni C, Cenni V, Haraguchi T, Squarzoni S, Schüchner S, Ogris E, Novelli G, Maraldi N, Lattanzi G.

Cell Cycle. 2010 Jul 1;9(13):2600-10. doi: 10.4161/cc.9.13.12080.


Lipodystrophy-linked LMNA p.R482W mutation induces clinical early atherosclerosis and in vitro endothelial dysfunction.

Bidault G, Garcia M, Vantyghem MC, Ducluzeau PH, Morichon R, Thiyagarajah K, Moritz S, Capeau J, Vigouroux C, Béréziat V.

Arterioscler Thromb Vasc Biol. 2013 Sep;33(9):2162-71. doi: 10.1161/ATVBAHA.113.301933. Epub 2013 Jul 11.


Human lipodystrophies linked to mutations in A-type lamins and to HIV protease inhibitor therapy are both associated with prelamin A accumulation, oxidative stress and premature cellular senescence.

Caron M, Auclair M, Donadille B, Béréziat V, Guerci B, Laville M, Narbonne H, Bodemer C, Lascols O, Capeau J, Vigouroux C.

Cell Death Differ. 2007 Oct;14(10):1759-67. Epub 2007 Jul 6.


Phosphorylation on protein kinase C sites inhibits nuclear import of lamin B2.

Hennekes H, Peter M, Weber K, Nigg EA.

J Cell Biol. 1993 Mar;120(6):1293-304.


Phosphorylation of lamins determine their structural properties and signaling functions.

Torvaldson E, Kochin V, Eriksson JE.

Nucleus. 2015;6(3):166-71. doi: 10.1080/19491034.2015.1017167. Epub 2015 Mar 20.


Organization and modulation of nuclear lamina structure.

Gerace L, Comeau C, Benson M.

J Cell Sci Suppl. 1984;1:137-60.


p34cdc2 acts as a lamin kinase in fission yeast.

Enoch T, Peter M, Nurse P, Nigg EA.

J Cell Biol. 1991 Mar;112(5):797-807.


Direct synthesis of lamin A, bypassing prelamin a processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice.

Coffinier C, Jung HJ, Li Z, Nobumori C, Yun UJ, Farber EA, Davies BS, Weinstein MM, Yang SH, Lammerding J, Farahani JN, Bentolila LA, Fong LG, Young SG.

J Biol Chem. 2010 Jul 2;285(27):20818-26. doi: 10.1074/jbc.M110.128835. Epub 2010 May 3.


Investigating the purpose of prelamin A processing.

Davies BS, Coffinier C, Yang SH, Barnes RH 2nd, Jung HJ, Young SG, Fong LG.

Nucleus. 2011 Jan-Feb;2(1):4-9. doi: 10.1093/hmg/ddq158. Review.


Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice.

Fong LG, Ng JK, Meta M, Coté N, Yang SH, Stewart CL, Sullivan T, Burghardt A, Majumdar S, Reue K, Bergo MO, Young SG.

Proc Natl Acad Sci U S A. 2004 Dec 28;101(52):18111-6. Epub 2004 Dec 17.


LMNA-linked lipodystrophies: from altered fat distribution to cellular alterations.

Bidault G, Vatier C, Capeau J, Vigouroux C, Béréziat V.

Biochem Soc Trans. 2011 Dec;39(6):1752-7. doi: 10.1042/BST20110675. Review.


Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina.

Lutz RJ, Trujillo MA, Denham KS, Wenger L, Sinensky M.

Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):3000-4. Erratum in: Proc Natl Acad Sci U S A 1992 Jun 15;89(12):5699.


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