Results 41 to 50 of about 53,083 (269)

Promoter hypermethylation as a mechanism for Lamin A/C silencing in a subset of neuroblastoma cells. [PDF]

PLoS ONE, 2017
Nuclear lamins support the nuclear envelope and provide anchorage sites for chromatin. They are involved in DNA synthesis, transcription, and replication.
Ines Rauschert, Fabian Aldunate, Jens Preussner, Miguel Arocena-Sutz, Vanina Peraza, Mario Looso, Juan C Benech, Ruben Agrelo   +7 more
doaj   +1 more source

Chromatin and lamin A determine two different mechanical response regimes of the cell nucleus

Molecular Biology of the Cell, 2017
Micromanipulation force measurements of single isolated nuclei at physiological strains and strain rates reveal two distinct cell nuclear mechanical regimes differentially governed by chromatin and lamin A.
Andrew D. Stephens, E. Banigan, S. Adam, R. Goldman, J. Marko   +4 more
semanticscholar   +1 more source

Dysfunctional polycomb transcriptional repression contributes to Lamin A/C dependent muscular dystrophy.

Journal of Clinical Investigation, 2020
Lamin A is a component of the inner nuclear membrane that, together with epigenetic factors, organizes the genome in higher order structures required for transcriptional control.
Andrea Bianchi, C. Mozzetta, Gloria Pegoli, F. Lucini, Sara Valsoni, V. Rosti, C. Petrini, A. Cortesi, Francesco Gregoretti, Laura Antonelli, Gennaro Oliva, Marco De Bardi, R. Rizzi, B. Bodega, Diego Pasini, F. Ferrari, C. Bearzi, C. Lanzuolo   +17 more
semanticscholar   +1 more source

Reduced expression of lamin A/C correlates with poor histological differentiation and prognosis in primary gastric carcinoma

Journal of Experimental & Clinical Cancer Research, 2009
Background Lamin A/C is very important in DNA replication, RNA dependent transcription and nuclear stabilization. Reduced or absent lamin A/C expression has been found to be a common feature of a variety of different cancers.
Xu Dazhi, Weng Desheng, Wu Lirong, Wu Zhengrong, Geng Jian, Zhao Fei   +5 more
doaj   +1 more source

Repo-Man/protein phosphatase 1 SUMOylation mediates binding to lamin A and serine 22 dephosphorylation

Open Biology, 2022
Lamin A phosphorylation/de-phosphorylation is an important process during cells division as it allows for nuclear envelope (NE) disassembly at mitotic entry and its re-assembly during mitotic exit.
Florentin Huguet, Ezgi Gokhan, Helen A. Foster, Hasnat A. Amin, Paola Vagnarelli   +4 more
doaj   +1 more source

Crucial Role of Lamin A/C in the Migration and Differentiation of MSCs in Bone

Cells, 2020
Lamin A/C, intermediate filament proteins from the nuclear lamina encoded by the LMNA gene, play a central role in mediating the mechanosignaling of cytoskeletal forces into nucleus.
Natividad Alcorta-Sevillano, Iratxe Macías, C. I. Rodríguez, A. Infante   +3 more
semanticscholar   +1 more source

Filament assembly of the C. elegans lamin in the absence of helix 1A

Nucleus, 2022
Lamins are the major constituent of the nuclear lamina, a protein meshwork underlying the inner nuclear membrane. Nuclear lamins are type V intermediate filaments that assemble into ~3.5 nm thick filaments.
Rebecca de Leeuw, Rafael Kronenberg-Tenga, Matthias Eibauer, Ohad Medalia   +3 more
doaj   +1 more source

Influences of lamin A levels on induction of pluripotent stem cells

Biology Open, 2012
Summary Lamin A is an inner nuclear membrane protein that maintains nuclear structure integrity, is involved in transcription, DNA damage response and genomic stability, and also links to cell differentiation, senescence, premature aging and associated ...
Bingfeng Zuo, Jiao Yang, Fang Wang, Lei Wang, Yu Yin, Jiameng Dan, Na Liu, Lin Liu   +7 more
doaj   +1 more source

Heterozygous lamin B1 and lamin B2 variants cause primary microcephaly and define a novel laminopathy

Genetics in Medicine, 2020
Lamins are the major component of nuclear lamina, maintaining structural integrity of the nucleus. Lamin A/C variants are well established to cause a spectrum of disorders ranging from myopathies to progeria, termed laminopathies.
D. Parry, Carol-Anne Martin, P. Greene, J. Marsh, J. C. P. E. L. M. F. J. M. C. R. H. M. J. G. C. C. E. Ambrose Arumugam Baple Bleda Boardman-Pretty Boiss, J. Ambrose, P. Arumugam, E. Baple, M. Bleda, F. Boardman-Pretty, J. Boissiere, C. Boustred, H. Brittain, M. Caulfield, G. Chan, C. Craig, L. Daugherty, A. de Burca, A. Devereau, G. Elgar, R. Foulger, T. Fowler, P. Furió-Tarí, A. Giess, J. Hackett, D. Halai, A. Hamblin, S. Henderson, J. Holman, T. Hubbard, K. Ibáñez, R. Jackson, L. J. Jones, D. Kasperaviciute, M. Kayikci, A. Kousathanas, L. Lahnstein, K. Lawson, S. Leigh, I. Leong, F. J. Lopez, F. Maleady-Crowe, J. Mason, E. McDonagh, L. Moutsianas, M. Mueller, N. Murugaesu, A. Need, C. Odhams, A. Orioli, C. Patch, D. Perez-Gil, M. Pereira, D. Polychronopoulos, J. Pullinger, T. Rahim, A. Rendon, P. Riesgo-Ferreiro, T. Rogers, M. Ryten, K. Savage, K. Sawant, R. Scott, A. Siddiq, A. Sieghart, D. Smedley, K. Smith, S. Smith, A. Sosinsky, W. Spooner, H. E. Stevens, A. Stuckey, R. Sultana, M. Tanguy, E. Thomas, S. Thompson, C. Tregidgo, A. Tucci, E. Walsh, S. Watters, M. Welland, E. Williams, K. Witkowska, S. Wood, M. Zarowiecki, Moira Blyth, H. Cox, D. Donnelly, L. Greenhalgh, S. Greville-Heygate, V. Harrison, K. Lachlan, C. McKenna, A. Quigley, Gillian Rea, L. Robertson, M. Suri, A. Jackson   +97 more
semanticscholar   +1 more source

The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.

PLoS ONE, 2012
Lamins' functions are regulated by phosphorylation at specific sites but our understanding of the role of such modifications is practically limited to the function of cdc 2 (cdk1) kinase sites in depolymerization of the nuclear lamina during mitosis.
Magdalena Zaremba-Czogalla, Katarzyna Piekarowicz, Katarzyna Wachowicz, Katarzyna Kozioł, Magda Dubińska-Magiera, Ryszard Rzepecki   +5 more
doaj   +1 more source