Ask about this productRelated genes to: LDB3 Blocking Peptide
- Gene:
- LDB3 NIH gene
- Name:
- LIM domain binding 3
- Previous symbol:
- CMD1C
- Synonyms:
- PDLIM6, KIAA0613, ZASP
- Chromosome:
- 10q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-12-04
- Date modifiied:
- 2019-04-23
Related products to: LDB3 Blocking Peptide
Related articles to: LDB3 Blocking Peptide
- Myofibrillar myopathies (MFM) form a large group of clinically and genetically heterogeneous protein aggregate diseases. We investigated whether a novel quantitative MRI protocol can reveal new aspects of structural and biochemical muscle pathology in three classic MFM subtypes. - Source: PubMed
Mathy Claudius SGast Lena VHoltzhausen ChristianGerhalter TeresaStuprich ChristophTürk MatthiasHeiss RafaelMarty BenjaminLaun Frederik BWanschitz Julia VHametner SimonDörfler ArndUder MichaelBäuerle TobiasNagel Armin MSchröder Rolf - Mutations in the gene are implicated in myofibrillar myopathy and cardiomyopathy. Consider cardiac conduction defects and the muscle's sensitivity to some anaesthetics when providing anaesthesia in the perioperative period. We present the anaesthetic management of a 76-year-old man with genetically confirmed mutation who presented for prostate biopsy with a background of progressive distal myopathy, mild cardiac involvement, and normal activities of daily living (ADL), undergoing anaesthesia using total intravenous anaesthesia (TIVA) to avoid the use of volatile agents or neuromuscular blockers. In this patient with a history of -associated myopathy, the use of TIVA provided a safe and effective technique of anaesthesia, and reinforced the need for an individualised anaesthetic strategy in neuromuscular disease (NMD). - Source: PubMed
Publication date: 2026/02/03
Swami Shashikant ShankarCampbell MarkBasappakokati Deepika Rani - RBM20 regulates pre-mRNA splicing, and its mutations cause dilated cardiomyopathy by disrupting cardiac RNA splicing, particularly of the TTN gene. While RBM20 is known to affect TTN splicing in the heart, its role in skeletal muscle remains unclear. This study investigated the effects of an RBM20 variant using an Rbm20 I538T knock-in mouse model, performing pathological and RNA-seq analyses to assess its impact on skeletal muscle. - Source: PubMed
Publication date: 2026/03/04
Miura AyaYamamoto TakumaNishiguchi MinoriNishio Hajime - Alzheimer's disease (AD) brains have variable neuropathologic and biochemical changes. Capturing epigenetic factors associated with this variability can reveal novel biological insights into AD pathophysiology. Here, we conduct an epigenome-wide association study of DNA methylation in 472 AD brains with neuropathologic and biochemical brain protein levels core to AD pathogenesis. Using a novel regional methylation (rCpGm) approach, we identify 5478 significant associations, 99.7% of which associate with tau biochemical measures, and 93 concordant associations in external datasets. Transcriptome-methylome integration reveals enrichment in oligodendrocyte genes, including known AD risk gene BIN1, myelination genes MYRF, MBP and MAG previously implicated in AD, and novel genes like LDB3. Further characterization of these perturbations in independent AD and primary tauopathy datasets highlights consistent tau-related associations. In summary, we uncover the integrative epigenomic landscape of AD, demonstrate tau-related oligodendrocyte gene perturbations as a common potential pathomechanism across tauopathies and share findings via our Multiomic Atlas. - Source: PubMed
Publication date: 2026/03/03
Oatman Stephanie RReddy Joseph SAtashgaran AminWang XueMin YuhaoQuicksall ZacharyVanelderen FloorCarrasquillo Minerva MLiu Chia-ChenYamazaki YuNguyen Thuy THeckman MichaelZhao NaDeTure MichaelMurray Melissa EBu GuojunKanekiyo TakahisaDickson Dennis WAllen MarietErtekin-Taner Nilüfer - PGM1-congenital disorder of glycosylation (PGM1-CDG) is frequently associated with cardiomyopathy. Although galactose therapy corrects glycosylation defects, cardiac dysfunction typically persists, suggesting a glycosylation-independent mechanism. Recent evidence of mitochondrial abnormalities in PGM1-deficient human and murine heart, together with the association of PGM1 with the Z-disk protein LDB3 (ZASP/Cypher), suggests a critical role for PGM1 in cardiomyocyte structural and energetic homeostasis. We hypothesized that PGM1-related cardiomyopathy arises from a glycosylation-independent disruption of Z-disk-mitochondrial coupling driven by loss of PGM1-LDB3 interactions, resulting in mitochondrial energy failure and impaired contractile function. - Source: PubMed
Publication date: 2026/02/21
Radenkovic SilviaPreston GraemeBudhraja RohitMuffels IrenaLigezka AnnaStaff Nathan PHrstka RonBalakrishnan BijinaShah RameenVerberkmoes SanneShammas IbrahimBosnyak InezStiers Kyle MLai KentBeamer Lesa JPandey AkhileshMorava EvaKozicz Tamas