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Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson–Gilford progeria syndrome
It is shown by light and electron microscopy that HGPS is associated with significant changes in nuclear shape, including lobulation of the nuclear envelope, thickening of thenuclear lamina, loss of peripheral heterochromatin, and clustering of nuclear pores. Expand
The nuclear lamina comes of age
These complexes provide new insights into cell architecture, as a foundation for the understanding of the molecular mechanisms that underlie the human laminopathies — clinical disorders that range from Emery–Dreifuss muscular dystrophy to the accelerated ageing seen in Hutchinson–Gilford progeria syndrome. Expand
Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin.
An up-to-date overview of the functions of nuclear lamins is provided, emphasizing their roles in epigenetics, chromatin organization, DNA replication, transcription, and DNA repair. Expand
Vimentin induces changes in cell shape, motility, and adhesion during the epithelial to mesenchymal transition
Vimentin is used widely as a marker of the epithelial to mesenchymal transitions (EMTs) that take place during embryogenesis and metastasis, yet the functional implications of the expression of thisExpand
Mutant nuclear lamin A leads to progressive alterations of epigenetic control in premature aging.
The epigenetic changes described most likely represent molecular mechanisms responsible for the rapid progression of premature aging in HGPS patients. Expand
Nuclear Lamins a and B1: Different Pathways of Assembly during Nuclear Envelope Formation in Living Cells
In later stages of G1, FRAP analyses suggest that both green fluorescent protein lamins A and B1 form higher order polymers throughout interphase nuclei. Expand
Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
Microtubules and intermediate filaments cooperate with actin and other components of filopodia during invadopodia maturation.
The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription.
It is proposed that different lamins are organized into separate, but interacting, microdomains and that LB1 is essential for their organization and the organization and regulation of chromatin are influenced by interconnections between these laminmicrodomains. Expand
Nuclear lamins: building blocks of nuclear architecture.
Experimental and genetic evidence suggest that nuclear lamins are involved in a number of other functions including nuclear envelope assembly, DNA synthesis, transcription, and apoptosis, and speculate about possible mechanisms through which mutations in lamins give rise to disease. Expand
Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments
The results suggest that elevated phosphorylation regulates IF assembly in vivo by changing the equilibrium constant of subunit exchange towards a higher off-rate. Expand