prelamin A

12/01/2013 - "Previous studies in cells from individuals with Hutchinson-Gilford progeria syndrome have shown that blocking of farnesylation of prelamin A ameliorates the nuclear shape abnormalities. "
03/31/2009 - "Different prelamin A forms accumulate in human fibroblasts: a study in experimental models and progeria."
01/01/2009 - "Different prelamin A forms accumulate in human fibroblasts: a study in experimental models and progeria."
10/01/2022 - "Status of treatment strategies for Hutchinson-Gilford progeria syndrome with a focus on prelamin: A posttranslational modification."
01/01/2022 - "Accumulation of the farnesylated prelamin A variant progerin, with an internal deletion including its processing site, causes Hutchinson-Gilford progeria syndrome. "

01/01/2022 - "In this context, it becomes more obvious how farnesylated prelamin A accumulation to toxic levels alters timing of DNA damage signaling and 53BP1 recruitment, thus contributing to cellular senescence and accelerated organismal aging as observed in progeroid laminopathies."
01/01/2019 - "Prelamin A accumulation has been found in all progeroid laminopathies and is obviously linked to cell and organism aging. "
01/01/2016 - "Finally, we show that specific laminopathy-associated mutations exhibit both positive and negative effects on prelamin A accumulation, indicating that these mutations affect prelamin A processing efficiency in different manners. "
01/01/2016 - "Prelamin A processing, accumulation and distribution in normal cells and laminopathy disorders."
01/01/2016 - "Since laminopathies mainly affect tissues of mesenchymal origin, we tested this hypothesis by generating an experimental model of laminopathy by inducing prelamin A accumulation in human mesenchymal stem cells (hMSCs). "

07/01/2015 - "The aim of this study is to use an experimental LMNA-lipodystrophy model based on human mesenchymal stem cell (hMSC)-derived adipocytes that accumulate prelamin A to gain deeper insights into the mechanisms governing these diseases. "
09/19/2008 - "These studies strongly support our hypothesis that HIV-PIs block prelamin A processing by directly affecting the enzymatic activity of ZMPSTE24, and in this way they may contribute to lipodystrophy in individuals undergoing HIV-PI treatment."
04/01/2012 - "The pathological mechanism by which prelamin A accumulation induces the lipodystrophy associated phenotypes remains unclear. "
11/01/2011 - "Similarly to humans, mice deficient in Zmpste24 accumulate prelamin A and display phenotypic features of accelerated aging, including lipodystrophy. "
04/11/2008 - "ZMPSTE24 deficiency in humans causes an accumulation of prelamin A and leads to lipodystrophy and other disease phenotypes. "

09/02/2016 - "LMNA missense mutations causing familial partial lipodystrophy do not lead to an accumulation of prelamin A."
04/01/2015 - "Our results suggest that there is a relationship between mutated prelamin-A accumulation and the severity of the phenotypes in homozygous familial partial lipodystrophy type 2 patients who harbor the LMNA T655fsX49 mutation. "
01/01/2009 - "Site-dependent differences in both prelamin A and adipogenic genes in subcutaneous adipose tissue of patients with type 2 familial partial lipodystrophy."
10/01/2010 - "Prelamin A accumulation establishes a link with other types of familial lipodystrophies, as familial partial lipodystrophy."
09/02/2016 - "A variety of missense mutations in LMNA (the gene for lamin C and prelamin A) cause familial partial lipodystrophy (FPLD), a disease associated with reduced adipose tissue, particularly in the limbs. "

10/08/2013 - "These studies may also improve our knowledge of the mechanisms leading to mitochondrial dysfunction during normal aging, since both progerin and prelamin A have been found to accumulate during normal aging."
07/01/2015 - "Prelamin A accumulating hMSC-derived adipocytes revealed increased lipolysis, mitochondrial dysfunction, and endoplasmic reticulum stress. "
10/08/2013 - "We also found mitochondrial dysfunction in fibroblasts from adult progeroid mice expressing progerin (Lmna(G609G/G609G) knock-in mice) or prelamin A (Zmpste24-null mice). "
11/01/2011 - "These results, together with the observation of an increased mitochondrial response to oxidative stress, support the relationship between defective prelamin A processing and mitochondrial dysfunction and highlight the relevance of oxidative damage in lipoatrophy and aging. "
07/01/2015 - "Prelamin A accumulation causes mitochondrial dysfunction, endoplasmic reticulum stress, and altered lipid metabolism resembling a premature aging phenotype."