The nuclear lamina comes of age
- Y. Gruenbaum, A. Margalit, R. Goldman, D. Shumaker, K. Wilson
- BiologyNature reviews. Molecular cell biology
- 2005
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.
Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson–Gilford progeria syndrome
- R. Goldman, D. Shumaker, F. Collins
- BiologyProceedings of the National Academy of Sciences…
- 7 June 2004
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.
Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin.
- T. Dechat, Katrin Pfleghaar, R. Goldman
- BiologyGenes & Development
- 1 April 2008
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.
Vimentin induces changes in cell shape, motility, and adhesion during the epithelial to mesenchymal transition
- M. Mendez, S. Kojima, R. Goldman
- BiologyThe FASEB Journal
- 1 June 2010
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 this…
Mutant nuclear lamin A leads to progressive alterations of epigenetic control in premature aging.
- D. Shumaker, T. Dechat, R. Goldman
- BiologyProceedings of the National Academy of Sciences…
- 6 June 2006
The epigenetic changes described most likely represent molecular mechanisms responsible for the rapid progression of premature aging in HGPS patients.
Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia
- M. Schoumacher, R. Goldman, D. Louvard, D. Vignjevic
- BiologyJournal of Cell Biology
- 3 May 2010
Microtubules and intermediate filaments cooperate with actin and other components of filopodia during invadopodia maturation.
Nuclear Lamins a and B1: Different Pathways of Assembly during Nuclear Envelope Formation in Living Cells
- R. Moir, M. Yoon, S. Khuon, R. Goldman
- Biology
- 11 December 2000
In later stages of G1, FRAP analyses suggest that both green fluorescent protein lamins A and B1 form higher order polymers throughout interphase nuclei.
Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments
- J. Eriksson, T. He, R. Goldman
- Biology, ChemistryJournal of Cell Science
- 22 February 2004
The results suggest that elevated phosphorylation regulates IF assembly in vivo by changing the equilibrium constant of subunit exchange towards a higher off-rate.
The A- and B-type nuclear lamin networks: microdomains involved in chromatin organization and transcription.
- T. Shimi, Katrin Pfleghaar, R. Goldman
- BiologyGenes & Development
- 15 December 2008
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.
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