spacer gif spacer gif spacer gif spacer gif spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Summary Freely available
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hennekes, H.
Right arrow Articles by Nigg, E. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hennekes, H.
Right arrow Articles by Nigg, E. A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?
Aebi, U., Cohn, J., Buhle, L. and Gerace, L (1986). The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323, 560-564.[Medline]

Bailer, S. M., Eppenberger, H. M., Griffiths, G. and Nigg, E. A (1991). Characterization of a 54-kDa protein of the inner nuclear membrane: evidence for cell cycle dependent interaction with the nuclear lamina. J. Cell Biol 114, 389-400.[Abstract/Free Full Text]

Beck, L. A., Hosick, T. J. and Sinensky, M (1990). Isoprenylation is required for the processing of the lamin A precursor. J. Cell Biol 110, 1489-1499.[Abstract/Free Full Text]

Benavente, R. and Krohne, G (1986). Involvement of nuclear lamins in postmitotic reorganization of chromatin as demonstrated by microinjection of lamin antibodies. J. Cell Biol 103, 1847-1854.[Abstract/Free Full Text]

Black, S. D (1992). Development of hydrophobicity parameters for prenylated proteins. Biochem. Biophys. Res. Commun 186, 1437-1442.[Medline]

Bossie, C. A. and Sanders, M. M (1993). A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate filament protein. J. Cell Sci 104, 1263-1272.[Abstract]

Bridger, J. M., Kill, I. R., O'Farrell, M. O. and Hutchison, C. J (1993). Internal lamin structures within G1 nuclei of human dermal fibroblasts. J. Cell Sci 104, 297-306.[Abstract]

Burke, B. and Gerace, L (1986). A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell 44, 639-652.[Medline]

Butrynski, J. E., Jones, T. L. Z., Backlund, P. S. Jr and Spiegel, A. M (1992). Differential isoprenylation of carboxy-terminal mutants of an inhibitory G-protein-subunit: neither farnesylation nor geranylgeranylation is sufficient for membrane attachment. Biochemistry 31, 8030-8035.[Medline]

Casey, P. J., Solski, P. A., Der, C. J. and Buss, J. E (1989). p21rasis modified by a farnesyl isoprenoid. Proc. Nat. Acad. Sci. USA 26, 8323-8327.

Casey, P. J (1992). Biochemistry of protein prenylation. J. Lipid Res 33, 1731-1740.[Medline]

Chavrier, P., Gorvel, J. P., Stelzer, E., Simons, K., Gruenberg, J. and Zerial, M (1991). Hypervariable C-terminal domain of rab proteins acts as a targeting signal. Nature 353, 769-772.[Medline]

Chen, C. and Okayama, H (1987). High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol 7, 2745-2752.[Abstract/Free Full Text]

Clarke, S (1992). Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu. Rev. Biochem 61, 355-386.[Medline]

Cox, A. D. and Der, C. J (1992). Protein prenylation: more than just glue?. Curr. Opin. Cell Biol 4, 1008-1016.[Medline]

Cox, A. D., Hisaka, M. M., Buss, J. E. and Der, C. J (1992). Specific isoprenoid modification is required for function of normal, but not oncogenic, ras protein. Mol. Cell. Biol 12, 2606-2615.[Abstract/Free Full Text]

Dabauvalle, M.-C., Loos, K., Merkert, H. and Scheer, U (1991). Spontaneous assembly of pore complex-containing membranes (\324Annulate Lamellae') in Xenopus egg extract in the absence of chromatin. J. Cell Biol 112, 1073-1082.[Abstract/Free Full Text]

Dagenais, A., Bibor Hardy, V., Laliberte, J.-F., Royal, A. and Simard, R (1985). Detection in BHK cells of a precursor form for lamin A. Exp. Cell Res 161, 269-276.[Medline]

Evan, G. I., Lewis, G. K., Ramsay, G. and Bishop, J. M (1985). Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol 5, 3610-3616.[Abstract/Free Full Text]

Farnsworth, C. C., Wolda, S. L., Gelb, M. H. and Glomset, J. A (1989). Human lamin B contains a farnesylated cysteine residue. J. Biol. Chem 264, 20422-20429.[Abstract/Free Full Text]

Fisher, D. Z., Chaudhary, N. and Blobel, G (1986). cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Nat. Acad. Sci. USA 83, 6450-6454.[Abstract/Free Full Text]

Foisner, R. and Gerace, L (1993). Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73, 1267-1279.[Medline]

Gallant, P. and Nigg, E. A (1992). Cyclin B2 undergoes cell cycle-dependent nuclear translocation and, when expressed as a non-destructible mutant, causes mitotic arrest in HeLa cells. J. Cell Biol 117, 213-224.[Abstract/Free Full Text]

Gerace, L. and Blobel, G (1980). The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19, 277-287.[Medline]

Gerace, L. and Burke, B (1988). Functional organization of the nuclear envelope. Annu. Rev. Cell Biol 4, 335-374.

Gieffers, C. and Krohne, G (1991). In vitro reconstitution of recombinant lamin A and a lamin A mutant lacking the carboxy-terminal tail. Eur. J. Cell Biol 55, 191-199.[Medline]

Glass, J. R. and Gerace, L (1990). Lamins A and B bind and assemble at the surface of mitotic chromosomes. J. Cell Biol 111, 1047-1057.[Abstract/Free Full Text]

Glomset, J. A., Gelb, M. H. and Farnsworth, C. C (1990). Prenyl proteins in eukaryotic cells: a new type of membrane anchor. Trends Biochem. Sci 15, 139-142.[Medline]

Goldman, A. E., Moir, R. D., Montag-Lowy, M., Stewart, M. and Goldman, R. D (1992). Pathway of incorporation of microinjected lamin A into the nuclear envelope. J. Cell Biol 119, 725-735.[Abstract/Free Full Text]

Goud, B (1992). Small GTP-binding proteins as compartmental markers. Semin. Cell Biol 3, 301-307.[Medline]

Hancock, J. F., Magee, A. I., Childs, J. E. and Marshall, C. J (1989). All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 57, 1167-1177.[Medline]

Hancock, J. F., Paterson, H. and Marshall, C. J (1990). A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21rasto the plasma membrane. Cell 63, 133-139.[Medline]

Hancock, J. F., Cadwallader, K., Paterson, H. and Marshall, C. J (1991). A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. EMBO J 10, 4033-4039.[Medline]

Heitlinger, E., Peter, M., H\212ner, M., Lustig, A., Aebi, U. and Nigg, E. A (1991). Expression of chicken lamin B2 in Escherichia coli: characterization of its structure, assembly, and molecular interactions. J. Cell Biol 113, 485-495.[Abstract/Free Full Text]

Heitlinger, E., Peter, M., Lustig, A., Villiger, W., Nigg, E. A. and Aebi, U (1992). The role of the head and tail domain in lamin structure and assembly: analysis of bacterially expressed chicken lamin A and truncated B2 lamins. J. Struct. Biol 108, 74-91.[Medline]

H\232ger, T. H., Zatloukal, K., Waizenegger, I. and Krohne, G (1990). Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin. Chromosoma 99, 379-390.[Medline]

H\232ger, T. H., Krohne, G. and Kleinschmidt, J. A (1991). Interaction of Xenopus lamins A and LII with chromatin in vitro mediated by a sequence element in the carboxyterminal domain. Exp. Cell Res 197, 280-289.[Medline]

Holtz, D., Tanaka, R. A., Hartwig, J. and McKeon, F (1989). The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope. Cell 59, 969-977.[Medline]

Horton, H., McMorrow, I. and Burke, B (1992). Independent expression and assembly properties of heterologous lamins A and C in murine embryonal carcinomas. Eur. J. Cell Biol 57, 172-183.[Medline]

Inglese, J., Koch, W. J., Caron, M. G. and Leftkowitz, R. J (1992). Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases. Nature 359, 147-150.[Medline]

Kalderon, D., Roberts, B. L., Richardson, W. D. and Smith, A. E (1984). A short amino acid sequence able to specify nuclear location. Cell 39, 499-509.[Medline]

Kinsella, B. T., Erdman, R. A. and Maltese, W. A (1991). Posttranslational modification of Ha-ras p21 by farnesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid. Proc. Nat. Acad. Sci. USA 88, 8934-8938.[Abstract/Free Full Text]

Kitten, G. T. and Nigg, E. A (1991). The CaaX motif is required for isoprenylation, carboxyl methylation and nuclear membrane association of lamin B2. J. Cell Biol 113, 13-23.[Abstract/Free Full Text]

Krek, W. and Nigg, E. A (1989). Structure and developmental expression of the chicken CDC2 kinase. EMBO J 8, 3071-3078.[Medline]

Krek, W. and Nigg, E. A (1991). Mutations of p34cdc2phosphorylation sites induce premature mitotic events in HeLa cells: evidence for a double block to p34cdc2kinase activation in vertebrates. EMBO J 10, 3331-3341.[Medline]

Krohne, G. and Benavente, R (1986). The nuclear lamins. A multigene family of proteins in evolution and differentiation. Exp. Cell Res 162, 1-10.[Medline]

Krohne, G., Wolin, S. L., McKeon, F. D., Franke, W. W. and Kirschner, M. W (1987). Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily. EMBO J 6, 3801-3808.[Medline]

Krohne, G., Waizenegger, I. and H\232ger, T. H (1989). The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope. J. Cell Biol 109, 2003-2011.[Abstract/Free Full Text]

Laliberte, J.-F., Dagenais, A., Filion, M., Bibor-Hardy, V., Simard, R. and Royal, A (1984). Identification of distinct messenger RNAs for nuclear lamin C and a putative precursor of nuclear lamin A. J. Cell Biol 98, 980-985.[Abstract/Free Full Text]

Lebel, S., Lampron, C., Royal, A. and Raymond, Y (1987). Lamins A and C appear during retinoic acid-induced differentiation of mouse embryonal carcinoma cells. J. Cell Biol 105, 1099-1104.[Abstract/Free Full Text]

Lehner, C. F., Furstenberger, G., Eppenberger, H. M. and Nigg, E. A (1986). Biogenesis of the nuclear lamina: In vivo synthesis and processing of nuclear protein precursors. Proc. Nat. Acad. Sci. USA 83, 2096-2099.[Abstract/Free Full Text]

Lehner, C. F., Stick, R., Eppenberger, H. M. and Nigg, E. A (1987). Differential expression of nuclear lamin proteins during chicken development. J. Cell Biol 105, 577-587.[Abstract/Free Full Text]

Loewinger, L. and McKeon, F (1988). Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm. EMBO J 7, 2301-2309.[Medline]

Lourim, D. and Lin, J. J.-C (1989). Expression of nuclear lamin A and muscle-specific proteins in differentiating muscle cells in ovo and in vitro. J. Cell Biol 109, 495-504.[Abstract/Free Full Text]

Luderus, M., Graaf, A., Mattia, E., Blaauwen, J., Grande, M., de Jong, L. and Driel, R (1992). Binding of matrix attachment regions to lamin B1. Cell 70, 949-959.[Medline]

Lutz, R. J., Trujillo, M. A., Denham, K. S., Wenger, L. and Sinensky, M (1992). Nucleoplasmic localization of prelamin A: implications for prenylation-dependent lamin A assembly into the nuclear lamina. Proc. Nat. Acad. Sci. USA 89, 3000-3004.[Abstract/Free Full Text]

Maltese, W. A (1990). Posttranslational modification of proteins by isoprenoids in mammalian cells. FASEB J 4, 3319-3328.[Abstract]

Marshall, C. J (1993). Protein prenylation: a mediator of protein-protein interactions. Science 259, 1865-1866.[Free Full Text]

McKeon, F. D., Kirschner, M. W. and Caput, D (1986). Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319, 463-468.[Medline]

McKeon, F. D (1991). Nuclear lamin proteins: domains required for nuclear targeting, assembly, and cell-cycle regulated dynamics. Curr. Opin. Cell Biol 3, 82-86.[Medline]

Meier, J., Campbell, K. H. S., Ford, C. C., Stick, R. and Hutchison, C. J (1991). The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs. J. Cell Sci 98, 271-279.[Abstract/Free Full Text]

Moores, S. L., Schaber, M. D., Mosser, S. D., Rands, E., O'Hara, M. B., Garsky, V. M., Marshall, M. S., Pompliano, D. L. and Gibbs, J. B (1991). Sequence dependence of protein isoprenylation. J. Biol. Chem 266, 14603-14610.[Abstract/Free Full Text]

Munro, S. and Pelham, H. R. B (1987). A C-terminal signal prevents secretion of luminal ER proteins. Cell 48, 899-907.[Medline]

Newport, J. W., Wilson, K. L. and Dunphy, W. G (1990). A lamin-independent pathway for nuclear envelope assembly. J. Cell Biol 111, 2247-2259.[Abstract/Free Full Text]

Nigg, E. A (1989). The nuclear envelope. Curr. Opin. Cell. Biol 1, 435-440.[Medline]

Nigg, E. A (1992). Assembly and cell cycle dynamics of the nuclear lamina. Semin. Cell Biol 3, 245-253.[Medline]

Nigg, E. A., Kitten, G. T. and Vorburger, K (1992). Targeting lamin proteins to the nuclear envelope: the role of Caax box modifications. Biochem. Soc. Trans 20, 500-504.[Medline]

Padan, R., Nainudel-Epszteyn, S., Goitein, R., Fainsod, A. and Gruenbaum, Y (1990). Isolation and characterization of the Drosophilia nuclear envelope otefin cDNA. J. Biol. Chem 265, 7808-7813.[Abstract/Free Full Text]

Paddy, M. R., Agard, D. A. and Sedat, J. W (1992). An extended view of nuclear lamin structure, function, and dynamics. Semin. Cell Biol 3, 255-266.[Medline]

Peter, M., Kitten, G. T., Lehner, C. F., Vorburger, K., Bailer, S. M., Maridor, G. and Nigg, E. A (1989). Cloning and sequencing of cDNA clones encoding chicken lamins A and B1 and comparison of the primary structures of vertebrate A-and B-type lamins. J. Mol. Biol 208, 393-404.[Medline]

Peter, M. and Nigg, E. A (1991). Ectopic expression of an A-type lamin does not interfere with differentiation of lamin A-negative embryonal carcinoma cells. J. Cell Sci 100, 589-598.[Abstract/Free Full Text]

Powell, L. and Burke, B (1990). Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: In vivo evidence for the interaction of p55 with the nuclear lamina. J. Cell Biol 111, 2225-2234.[Abstract/Free Full Text]

R\232ber, R.-A., Weber, K. and Osborn, M (1989). Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: a developmental study. Development 105, 365-378.[Abstract]

Schafer, W. R. and Rine, J (1992). Protein prenylation- genes, enzymes, targets, and functions. Annu. Rev. Genet 26, 209-.[Medline]

Schmidt-Zachmann, M. S. and Nigg, E. A (1993). Protein localization to the nucleolus: a search for targeting domains in nucleolin. J. Cell Sci 105, 799-806.[Abstract]

Seabra, M. C., Reiss, Y., Casey, P. J., Brown, M. S. and Goldstein, J. L (1991). Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit. Cell 65, 429-434.[Medline]

Senior, A. and Gerace, L (1988). Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina. J. Cell Biol 107, 2029-2036.[Abstract/Free Full Text]

Simos, G. and Georgatos, S. D (1992). The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins. EMBO J 11, 4027-4036.[Medline]

Stewart, C. and Burke, B (1987). Teratocarcinoma stem cells and early mouse embryos contain only a single major lamin polypeptide closely resembling lamin B. Cell 51, 383-392.[Medline]

Stick, R., Angres, B., Lehner, C. F. and Nigg, E. A (1988). The fates ofchicken nuclear lamin proteins during mitosis: Evidence for a reversible redistribution of lamin B2 between inner nuclear membrane and elements of the endoplasmic reticulum. J. Cell Biol 107, 397-406.[Abstract/Free Full Text]

Stick, R (1992). The gene structure of Xenopus nuclear lamin A: a model for the evolution of A-type from B-type lamins by exon shuffling. Chromosoma 101, 566-574.[Medline]

Ulitzur, N., Harel, A., Feinstein, N. and Gruenbaum, Y (1992). Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract. J. Cell Biol 119, 17-25.[Abstract/Free Full Text]

Vorburger, K., Kitten, G. T. and Nigg, E. A (1989). Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif. EMBO J 8, 4007-4013.[Medline]

Vorburger, K., Lehner, C. F., Kitten, G., Eppenberger, H. M. and Nigg, E. A (1989). A second higher vertebrate B-type lamin: cDNA sequence determination and in vitro processing of chicken lamin B2. J. Mol. Biol 208, 405-415.[Medline]

Weber, K., Plessmann, U. and Traub, P (1989). Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina. FEBS Lett 257, 411-414.[Medline]

Wolin, S. L., Krohne, G. and Kirschner, M. W (1987). A new lamin in Xenopus somatic tissues displays strong homology to human lamin A. EMBO J 6, 3809-3818.[Medline]

Worman, H. J., Yuan, J., Blobel, G. and Georgatos, S. D (1988). A lamin B receptor in the nuclar envelope. Proc. Nat. Acad. Sci. USA 85, 8531-8534.[Abstract/Free Full Text]

Worman, H. J., Evans, C. D. and Blobel, G (1990). The lamin B receptor of the nuclear envelope inner membrane: A polytopic protein with eight potential transmembrane domains. J. Cell Biol 111, 1535-1542.[Abstract/Free Full Text]

Yuan, J., Simos, G., Blobel, G. and Georgatos, S. D (1991). Binding of lamin A to polynucleosomes. J. Biol. Chem 266, 9211-9215.[Abstract/Free Full Text]


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
Mol. Biol. CellHome page
J. Barrowman, C. Hamblet, C. M. George, and S. Michaelis
Analysis of Prelamin A Biogenesis Reveals the Nucleus to be a CaaX Processing Compartment
Mol. Biol. Cell, December 1, 2008; 19(12): 5398 - 5408.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
B. C. Capell, M. Olive, M. R. Erdos, K. Cao, D. A. Faddah, U. L. Tavarez, K. N. Conneely, X. Qu, H. San, S. K. Ganesh, et al.
A farnesyltransferase inhibitor prevents both the onset and late progression of cardiovascular disease in a progeria mouse model
PNAS, October 14, 2008; 105(41): 15902 - 15907.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. Coffinier, S. E. Hudon, R. Lee, E. A. Farber, C. Nobumori, J. H. Miner, D. A. Andres, H. P. Spielmann, C. A. Hrycyna, L. G. Fong, et al.
A Potent HIV Protease Inhibitor, Darunavir, Does Not Inhibit ZMPSTE24 or Lead to an Accumulation of Farnesyl-prelamin A in Cells
J. Biol. Chem., April 11, 2008; 283(15): 9797 - 9804.
[Abstract] [Full Text] [PDF]


Home page
GENES CELLSHome page
R. Ukekawa, K. Miki, M. Fujii, H. Hirano, and D. Ayusawa
Accumulation of multiple forms of lamin A with down-regulation of FACE-1 suppresses growth in senescent human cells
Genes Cells, March 1, 2007; 12(3): 397 - 406.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. G. Young, M. Meta, S. H. Yang, and L. G. Fong
Prelamin A Farnesylation and Progeroid Syndromes
J. Biol. Chem., December 29, 2006; 281(52): 39741 - 39745.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
A. E. Rusinol and M. S. Sinensky
Farnesylated lamins, progeroid syndromes and farnesyl transferase inhibitors.
J. Cell Sci., August 15, 2006; 119(Pt 16): 3265 - 3272.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
L. G. Fong, D. Frost, M. Meta, X. Qiao, S. H. Yang, C. Coffinier, and S. G. Young
A Protein Farnesyltransferase Inhibitor Ameliorates Disease in a Mouse Model of Progeria
Science, March 17, 2006; 311(5767): 1621 - 1623.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
A. D. Basso, P. Kirschmeier, and W. R. Bishop
Thematic review series: Lipid Posttranslational Modifications. Farnesyl transferase inhibitors
J. Lipid Res., January 1, 2006; 47(1): 15 - 31.
[Abstract] [Full Text] [PDF]


Home page
J. Lipid Res.Home page
S. G. Young, L. G. Fong, and S. Michaelis
Thematic Review Series: Lipid Posttranslational Modifications. Prelamin A, Zmpste24, misshapen cell nuclei, and progeria--new evidence suggesting that protein farnesylation could be important for disease pathogenesis
J. Lipid Res., December 1, 2005; 46(12): 2531 - 2558.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
M. W. Glynn and T. W. Glover
Incomplete processing of mutant lamin A in Hutchinson-Gilford progeria leads to nuclear abnormalities, which are reversed by farnesyltransferase inhibition
Hum. Mol. Genet., October 15, 2005; 14(20): 2959 - 2969.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
M. P. Mallampalli, G. Huyer, P. Bendale, M. H. Gelb, and S. Michaelis
Inhibiting farnesylation reverses the nuclear morphology defect in a HeLa cell model for Hutchinson-Gilford progeria syndrome
PNAS, October 4, 2005; 102(40): 14416 - 14421.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
J. I. Toth, S. H. Yang, X. Qiao, A. P. Beigneux, M. H. Gelb, C. L. Moulson, J. H. Miner, S. G. Young, and L. G. Fong
Blocking protein farnesyltransferase improves nuclear shape in fibroblasts from humans with progeroid syndromes
PNAS, September 6, 2005; 102(36): 12873 - 12878.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
B. C. Capell, M. R. Erdos, J. P. Madigan, J. J. Fiordalisi, R. Varga, K. N. Conneely, L. B. Gordon, C. J. Der, A. D. Cox, and F. S. Collins
Inhibiting farnesylation of progerin prevents the characteristic nuclear blebbing of Hutchinson-Gilford progeria syndrome
PNAS, September 6, 2005; 102(36): 12879 - 12884.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. H. Yang, M. O. Bergo, J. I. Toth, X. Qiao, Y. Hu, S. Sandoval, M. Meta, P. Bendale, M. H. Gelb, S. G. Young, et al.
Blocking protein farnesyltransferase improves nuclear blebbing in mouse fibroblasts with a targeted Hutchinson-Gilford progeria syndrome mutation
PNAS, July 19, 2005; 102(29): 10291 - 10296.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
C. Capanni, E. Mattioli, M. Columbaro, E. Lucarelli, V. K. Parnaik, G. Novelli, M. Wehnert, V. Cenni, N. M. Maraldi, S. Squarzoni, et al.
Altered pre-lamin A processing is a common mechanism leading to lipodystrophy
Hum. Mol. Genet., June 1, 2005; 14(11): 1489 - 1502.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
J. Gruber, T. Lampe, M. Osborn, and K. Weber
RNAi of FACE1 protease results in growth inhibition of human cells expressing lamin A: implications for Hutchinson-Gilford progeria syndrome
J. Cell Sci., February 15, 2005; 118(4): 689 - 696.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
L. G. Fong, J. K. Ng, M. Meta, N. Cote, S. H. Yang, C. L. Stewart, T. Sullivan, A. Burghardt, S. Majumdar, K. Reue, et al.
Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice
PNAS, December 28, 2004; 101(52): 18111 - 18116.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
T. Ralle, C. Grund, W. W. Franke, and R. Stick
Intranuclear membrane structure formations by CaaX-containing nuclear proteins
J. Cell Sci., December 1, 2004; 117(25): 6095 - 6104.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
R. Veluthakal, R. Amin, and A. Kowluru
Interleukin-1{beta} induces posttranslational carboxymethylation and alterations in subnuclear distribution of lamin B in insulin-secreting RINm5F cells
Am J Physiol Cell Physiol, October 1, 2004; 287(4): C1152 - C1162.
[Abstract] [Full Text] [PDF]


Home page
J. Med. Genet.Home page
K Fukuchi, T Katsuya, K Sugimoto, M Kuremura, H D Kim, L Li, and T Ogihara
LMNA mutation in a 45 year old Japanese subject with Hutchinson-Gilford progeria syndrome
J. Med. Genet., May 1, 2004; 41(5): e67 - e67.
[Full Text] [PDF]


Home page
JCBHome page
C. P. Maske, M. S. Hollinshead, N. C. Higbee, M. O. Bergo, S. G. Young, and D. J. Vaux
A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Rce1 and carboxymethylation
J. Cell Biol., September 29, 2003; 162(7): 1223 - 1232.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
C. Hutchison, M Alvarez-Reyes, and O. Vaughan
Lamins in disease: why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes?
J. Cell Sci., January 1, 2001; 114(1): 9 - 19.
[Abstract] [PDF]


Home page
JCBHome page
R. D. Moir, M. Yoon, S. Khuon, and R. D. Goldman
Nuclear Lamins a and B1: Different Pathways of Assembly during Nuclear Envelope Formation in Living Cells
J. Cell Biol., December 11, 2000; 151(6): 1155 - 1168.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
M. Izumi, O. A. Vaughan, C. J. Hutchison, and D. M. Gilbert
Head and/or CaaX Domain Deletions of Lamin Proteins Disrupt Preformed Lamin A and C But Not Lamin B Structure in Mammalian Cells
Mol. Biol. Cell, December 1, 2000; 11(12): 4323 - 4337.
[Abstract] [Full Text]


Home page
Mol. Biol. CellHome page
H. Hofemeister, K. Weber, and R. Stick
Association of Prenylated Proteins with the Plasma Membrane and the Inner Nuclear Membrane Is Mediated by the Same Membrane-targeting Motifs
Mol. Biol. Cell, September 1, 2000; 11(9): 3233 - 3246.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
R. M. Barton and H. J. Worman
Prenylated Prelamin A Interacts with Narf, a Novel Nuclear Protein
J. Biol. Chem., October 15, 1999; 274(42): 30008 - 30018.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
M. Goldberg, H. Lu, N. Stuurman, R. Ashery-Padan, A. M. Weiss, J. Yu, D. Bhattacharyya, P. A. Fisher, Y. Gruenbaum, and M. F. Wolfner
Interactions among Drosophila Nuclear Envelope Proteins Lamin, Otefin, and YA
Mol. Cell. Biol., July 1, 1998; 18(7): 4315 - 4323.
[Abstract] [Full Text]


Home page
J. Cell Sci.Home page
T. Mical and M. Monteiro
The role of sequences unique to nuclear intermediate filaments in the targeting and assembly of human lamin B: evidence for lack of interaction of lamin B with its putative receptor
J. Cell Sci., January 12, 1998; 111(23): 3471 - 3485.
[Abstract] [PDF]


Home page
Mol. Cell. Biol.Home page
J. Liu and M. F. Wolfner
Functional Dissection of YA, an Essential, Developmentally Regulated Nuclear Lamina Protein in Drosophila melanogaster
Mol. Cell. Biol., January 1, 1998; 18(1): 188 - 197.
[Abstract] [Full Text]


Home page
JCBHome page
B. Lenz-Bohme, J. Wismar, S. Fuchs, R. Reifegerste, E. Buchner, H. Betz, and B. Schmitt
Insertional Mutation of the Drosophila Nuclear Lamin Dm0 Gene Results in Defective Nuclear Envelopes, Clustering of Nuclear Pore Complexes, and Accumulation of Annulate Lamellae
J. Cell Biol., June 2, 1997; 137(5): 1001 - 1016.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
F. Kilic, M. B. Dalton, S. K. Burrell, J. P. Mayer, S. D. Patterson, and M. Sinensky
In Vitro Assay and Characterization of the Farnesylation-dependent Prelamin A Endoprotease
J. Biol. Chem., February 21, 1997; 272(8): 5298 - 5304.
[Abstract] [Full Text] [PDF]


Home page
JCBHome page
P. Chen, S. K. Sapperstein, J. D. Choi, and S. Michaelis
Biogenesis of the Saccharomyces cerevisiae Mating Pheromone a-Factor
J. Cell Biol., January 27, 1997; 136(2): 251 - 269.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Ashery-Padan, A. M. Weiss, N. Feinstein, and Y. Gruenbaum
Distinct Regions Specify the Targeting of Otefin to the Nucleoplasmic Side of the Nuclear Envelope
J. Biol. Chem., January 24, 1997; 272(4): 2493 - 2499.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
K Shimada, M Harata, and S Mizuno
A nuclear matrix-associated high molecular mass nuclear antigen, HMNA, of chicken and marked decrease of its immunoreactivity during the progression of S phase
J. Cell Sci., January 12, 1997; 110(24): 3031 - 3041.
[Abstract] [PDF]


Home page
J. Cell Sci.Home page
G. Pugh, P. Coates, E. Lane, Y Raymond, and R. Quinlan
Distinct nuclear assembly pathways for lamins A and C lead to their increase during quiescence in Swiss 3T3 cells
J. Cell Sci., January 10, 1997; 110(19): 2483 - 2493.
[Abstract] [PDF]


Home page
J. Cell Sci.Home page
M Klapper, K Exner, A Kempf, C Gehrig, N Stuurman, P. Fisher, and G Krohne
Assembly of A- and B-type lamins studied in vivo with the baculovirus system
J. Cell Sci., January 10, 1997; 110(20): 2519 - 2532.
[Abstract] [PDF]


Home page
J. Cell Sci.Home page
D Lourim, A Kempf, and G Krohne
Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: increase of lamin LI protein synthesis during meiotic maturation
J. Cell Sci., January 7, 1996; 109(7): 1775 - 1785.
[Abstract] [PDF]


Home page
J. Biol. Chem.Home page
L. Martin, C. Crimaudo, and L. Gerace
cDNA Cloning and Characterization of Lamina-associated Polypeptide 1C (LAP1C), an Integral Protein of the Inner Nuclear Membrane
J. Biol. Chem., April 14, 1995; 270(15): 8822 - 8828.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
D Riemer, N Stuurman, M Berrios, C Hunter, P. Fisher, and K Weber
Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins
J. Cell Sci., January 10, 1995; 108(10): 3189 - 3198.
[Abstract] [PDF]


Home page
J. Cell Sci.Home page
N Stuurman, N Maus, and P. Fisher
Interphase phosphorylation of the Drosophila nuclear lamin: site-mapping using a monoclonal antibody
J. Cell Sci., January 9, 1995; 108(9): 3137 - 3144.
[Abstract] [PDF]


Home page
J. Cell Sci.Home page
P Hozak, A. Sasseville, Y Raymond, and P. Cook
Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
J. Cell Sci., January 2, 1995; 108(2): 635 - 644.
[Abstract] [PDF]


Home page
J. Cell Sci.Home page
A. Sasseville and Y Raymond
Lamin A precursor is localized to intranuclear foci
J. Cell Sci., January 1, 1995; 108(1): 273 - 285.
[Abstract] [PDF]


Home page
J. Cell Sci.Home page
R. Cary, M. Klymkowsky, R. Evans, A Domingo, J. Dent, and L. Backhus
Vimentin's tail interacts with actin-containing structures in vivo
J. Cell Sci., January 6, 1994; 107(6): 1609 - 1622.
[Abstract] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
M. Alsheimer, E. von Glasenapp, M. Schnolzer, H. Heid, and R. Benavente
Meiotic lamin C2: The unique amino-terminal hexapeptide GNAEGR is essential for nuclear envelope association
PNAS, November 21, 2000; 97(24): 13120 - 13125.
[Abstract] [Full Text] [PDF]


This Article
Right arrow Summary Freely available
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hennekes, H.
Right arrow Articles by Nigg, E. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hennekes, H.
Right arrow Articles by Nigg, E. A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?