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Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway ( By similarity ). By similarity.
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FIGURE 1. Mechanically stressed cells and LIM domain proteins. (a) Schematic of a layer of epithelial cells on top of an extracellular matrix (ECM). (b) Simple schematic of a LIM domain: Two zinc finger motifs. The magenta circles represent the well-conserved residues (typically cysteine or histidine) that chelate the zinc molecules.
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LIM domain is a unique double-zinc finger motif found in a variety of proteins such as homeodomain transcription factors, kinases, and adaptors. The LIM-containing proteins are involved in diverse biological processes including cytoskeleton organization, cell lineage specification and organ development. Dysfunctions of LIM domains induce pathological effects including muscle detachment.
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PDLIM7 (PDZ And LIM Domain 7) is a Protein Coding gene. Diseases associated with PDLIM7 include Lymphoepithelioma-Like Carcinoma and Hodgkin's Granuloma . Among its related pathways are Nervous system development and GDNF-Family Ligands and Receptor Interactions . An important paralog of this gene is PDLIM5.
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INTRODUCTION. NAFLD is the most common chronic liver disease and a risk factor for multiple metabolic disorders, such as obesity, type 2 diabetes, hyperlipidemia, and hypertension. 1 NAFL and NASH 2 are 2 representative types of NAFLD, the latter of which eventually leads to end-stage liver conditions, such as cirrhosis and HCC. However, lifestyle changes and weight loss are the only.
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The cytokine transforming growth factor β (TGF-β) is induced on tissue injury and regulates tissue remodeling and wound healing, but dysregulated signaling results in excess ECM deposition and fibrosis. The LIM (Lin11, Isl-1 & Mec-3) domain protein LIM domain only 7 (LMO7) is a TGF-β1 target gene in hepatoma cells, but its role in vascular.
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KEGG Orthology (KO) [BR:hsa00001] 09140 Cellular Processes 09144 Cellular community - eukaryotes 04520 Adherens junction 4008 (LMO7) 09180 Brite Hierarchies
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Background and aims: Hyperlipidemia has been extensively recognized as a high-risk factor for non-alcoholic steatohepatitis (NASH); however, clinical susceptibility to NASH is highly heterogeneous. The key controller(s) of NASH susceptibility in patients with hyperlipidemia have not yet been elucidated. Here, we aimed to reveal the key regulators of NASH in patients with hyperlipidemia and to.
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FIGURE 3: Hepatocyte-specific LIM domain only 7 (LMO7) deficiency exacerbates HFD-induced NASH in mice. (A) Western blot analysis of LMO7 expression in the liver tissues of Flox mice and LMO7-CKO mice (n = 3 per group). (B) Body weight ratios of Flox mice and Lmo7 -CKO mice fed an NCD or HFD diet for 24 weeks (n = 10 per group).
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The LIM domain, which is defined by a conserved cysteine-rich sequence, is a modular protein-binding interface that is found in numerous eukaryotic proteins. The LIM sequence specifies a double.
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1. Introduction. Zyxin family comprises of LIM-domain containing proteins that play crucial roles in mediating cellular signalling, tumorigenesis and developmental pathways, and have, therefore, been implicated in human disease [1,2,3,4,5].For example, Zyxin family proteins have been reported to be involved in various cancers including prostate, colorectal, lung, liver and melanoma [6,7,8,9].
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The protein encoded by this gene is representative of a family of proteins composed of conserved PDZ and LIM domains. LIM domains are proposed to function in protein-protein recognition in a variety of contexts including gene transcription and development and in cytoskeletal interaction. The LIM domains of this protein bind to protein kinases, whereas the PDZ domain binds to actin filaments.
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X-linked Emery-Dreifuss muscular dystrophy (X-EDMD) is inherited through mutations in emerin, a nuclear membrane protein. Emerin has proposed roles in nuclear architecture and gene regulation, but direct molecular links to disease were unknown. We report that Lim-domain only 7 (Lmo7) binds emerin di.
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The LIM domain was first identified in the developmentally regulated transcription factors L in-1, I sl-1, and M ec-3. The approximately 60 amino acid long domain has been identified in over 300 proteins from organisms ranging from yeast to human. The LIM domain is a zinc-binding, cysteine-rich motif consisting of two tandemly repeated zinc.
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LIM domain s are protein structural domains, composed of two contiguous zinc fingers, separated by a two- amino acid residue hydrophobic linker. [1] The domain name is an acronym of the three genes in which it was first identified (LIN-11, Isl-1 and MEC-3). [2] LIM is a protein interaction domain that is involved in binding to many structurally.