Results 71 to 80 of about 2,659 (169)

Laminopathies: what can humans learn from fruit flies

Cellular & Molecular Biology Letters, 2018
Lamin proteins are type V intermediate filament proteins (IFs) located inside the cell nucleus. They are evolutionarily conserved and have similar domain organization and properties to cytoplasmic IFs. Lamins provide a skeletal network for chromatin, the
Marta Pałka, Aleksandra Tomczak, Katarzyna Grabowska, Magdalena Machowska, Katarzyna Piekarowicz, Dorota Rzepecka, Ryszard Rzepecki   +6 more
doaj   +1 more source

Current Topics of Progressive Cardiac Conduction Disease

Journal of Arrhythmia, Volume 42, Issue 3, June 2026.
Many genes and the protein cause PCCD. Mutation of NaV1.5 or CX40 cause isolated PCCD, but mutation of lamin A/C, emerin, or desmin lead to cardiomyopathy, and PCCD. Mutation of transcription factor NCX2‐5, and Tbx5 associated with atrial septal defect and abnormal development of conduction system.
Naokata Sumitomo, Hitoshi Mori, Takashi Kumamoto, Taisuke Ishikawa, Akiko Seki, Naomasa Makita, Jean‐Jacques Schott, Arthur A. M. Wilde   +7 more
wiley   +1 more source

Targeted Regulation of Nuclear Lamins by Ubiquitin and Ubiquitin-Like Modifiers

Cells, 2020
Nuclear lamins (NLs) are essential components of the animal cell nucleus involved in the regulation of a plethora of molecular and cellular processes.
Michael Blank
doaj   +1 more source

Metabolic Profiling Reveals Organ‐Specific Molecular Pathologies and Aging‐Associated Biomarkers in Progeroid Laminopathy

Smart Medicine, Volume 5, Issue 3, June 2026.
This study integrates transcriptomic, lipidomic, and metabolomic profiling of the heart, lung, skin, and serum from Hutchinson–Gilford progeria syndrome (HGPS) mouse models and human progeroid laminopathy (PL) cohorts. Through multi‐organ analyses, we reveal organ‐specific aging signatures, and importantly, cross‐species serum metabolomics identify ...
Lidan Hu, Xiaoyang Zhao, Yingxian Zhang, Jingjing Wang, Guozhen Wang, Xiaoli Liu, Zhan Feng, Jiazhen Yin, Zhaoyang Peng, Langping Gao, Jianhua Mao, Ning Shen   +11 more
wiley   +1 more source

Nuclear envelope proteins and chromatin arrangement: a pathogenic mechanism for laminopathies

European Journal of Histochemistry, 2009
The involvement of the nuclear envelope in the modulation of chromatin organization is strongly suggested by the increasing number of human diseases due to mutations of nuclear envelope proteins.
NM Maraldi, G Lattanzi, C Capanni, M Columbaro, L Merlini, E Mattioli, P Sabatelli   +6 more
doaj   +1 more source

Dynamic expression of lamin B1 during adult neurogenesis in the vertebrate brain

Developmental Dynamics, Volume 255, Issue 2, Page 187-208, February 2026.
Abstract Background In mammals, specific brain regions such as the dentate gyrus (DG) of the hippocampus and the subventricular zone (SVZ) of the lateral ventricles harbor adult neural stem/progenitor cells (ANSPCs) that give rise to new neurons and contribute to structural and functional brain plasticity.
Diana Zhilina, Lizbeth A. Bolaños Castro, Juan Sebastian Eguiguren, Sara Zocher, Anne Karasinsky, Dimitri Widmer, Alexandre Espinós, Victor Borrell, Michael Brand, Kyoko Miura, Oliver Zierau, Maximina H. Yun, Tomohisa Toda   +12 more
wiley   +1 more source

The p.R249W Mutation in LMNA-Related Congenital Muscular Dystrophy Causes Nuclear Deformities and an Enrichment in Lamin A/C at the Ends of the Nucleus

Cells
LMNA-related congenital muscular dystrophy (L-CMD) is a rare genetic disorder that causes skeletal muscle weakening and wasting. Although L-CMD is caused by a variety of de novo point mutations in the LMNA gene, the p.R249W (Arg.249Trp.) pathogenic ...
Catherine Harvey, Zixuan Zhu, Iden Han, Kan Cao   +3 more
doaj   +1 more source

Disruption of Nuclear‐Cytoskeletal Linkage by Coil‐1a LMNA Mutations in Emery–Dreifuss Muscular Dystrophy

Journal of Cachexia, Sarcopenia and Muscle, Volume 17, Issue 1, February 2026.
ABSTRACT Background Emery–Dreifuss muscular dystrophy (EDMD) is a progressive genetic myopathy that mainly affects the muscles used for movement (skeletal muscles) and the heart (cardiac muscles). The disease is frequently associated with mutations in genes encoding nuclear envelope proteins, most notably LMNA, which encodes lamin A—a critical ...
So‐mi Kang, Ran Kim, Tae‐Gyun Woo, Soyoung Park, Yeongseon Ji, Ha Eun Kim, Yu Jin Jeong, Jeongmo Kim, Yeonhee Kim, Woochul Chang, Bae‐Hoon Kim, Bum‐Joon Park   +11 more
wiley   +1 more source

Informing Dose for Pediatric Rare Diseases—A Survey of Recent Orphan Drugs Approvals

Clinical and Translational Science, Volume 19, Issue 2, February 2026.
ABSTRACT Collectively, pediatric rare diseases affect millions of children worldwide. Yet, treatment options are limited. Dose selection presents unique challenges in pediatric rare disease drug development. Traditional dose‐finding approaches are impractical for these populations, and conventional pediatric dosing methods like exposure matching face ...
Elimika Pfuma Fletcher, Chloe Kim, Hannah Mei, Bilal AbuAsal, Sherbet Samuels, Rajanikanth Madabushi, Anuradha Ramamoorthy   +6 more
wiley   +1 more source

Identification of Genes and Pathways Regulated by Lamin A in Heart

Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2020
Background Mutations in the LMNA gene, encoding LMNA (lamin A/C), causes distinct disorders, including dilated cardiomyopathies, collectively referred to as laminopathies. The genes (coding and noncoding) and regulatory pathways controlled by LMNA in the
Jordi Coste Pradas, Gaelle Auguste, Scot J. Matkovich, Raffaella Lombardi, Suet Nee Chen, Tyrone Garnett, Kyle Chamberlain, Jalish Mahmud Riyad, Thomas Weber, Sanjay K. Singh, Matthew J. Robertson, Cristian Coarfa, Ali J. Marian, Priyatansh Gurha   +13 more
doaj   +1 more source