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The LEM (LAP2, emerin, MAN1) domain is a globular module of approximately 40 amino acids, which is mostly found in the nucleoplasmic portions of metazoan inner nuclear membrane proteins. The LEM domain has been shown to mediate binding to BAF (barrier-to-autointegration factor) and BAF-DNA complexes. BAF dimers bind to double-stranded DNA non.
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Mammalian LEM-domain proteins (LEMs) are encoded by seven genes, including LAP2, EMD, LEMD1, LEMD2, LEMD3, ANKLE1, and ANKLE2. Though some LEMs were involved in various tumor progression, the expression and prognostic values of LEMs in prostate adenocarcinoma (PRAD) have yet to be analyzed. Herein, we investigated the expression, survival data, and immune infiltration levels of LEMs in PRAD.
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Functional redundancy is perhaps expected between LEM-D proteins in the same group, but not between LEM-D proteins in different groups due to their limited homology outside of the LEM-D. However functional overlap between group I and group II LEM-D proteins was first described in worms [ 44 , 45 ] and later found in other organisms [ 43.
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Emerin is a Conserved LEM-Domain Protein. The LEM-domain is a ~40-residue helix-loop-helix fold conserved both in eukaryotes and in prokaryotic DNA/RNA-binding proteins. 10 With one exception (Lap2 proteins have a second LEM-domain that binds DNA), 10 eukaryotic LEM-domains have one known function: they directly bind a conserved chromatin protein named barrier-to-autointegration factor (BAF.
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cl02649: LEM Superfamily. LEM (Lap2/Emerin/Man1) domain found in emerin, lamina-associated polypeptide 2 (LAP2), inner nuclear membrane protein Man1 and similar proteins. The family corresponds to a group of inner nuclear membrane proteins containing LEM domain. Emerin occurs in four phosphorylated forms and plays a role in cell cycle-dependent.
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The default LEM Agent configuration collects events from Windows System, application and Security logs. To generate a LEM Event, restart a Windows service that no impact on other applications. Generally, 'Print Spooler' service shown below is a great candidate for this test. In the LEM Web console, click on the MONITOR view.
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View/Edit Mouse. LEM domain-containing protein 3 (LEMD3), also known as MAN1, is an integral protein in the inner nuclear membrane (INM) of the nuclear envelope. It is encoded by the LEMD3 gene [5] and was first identified after it was isolated from the serum of a patient with a collagen vascular disease. [6]
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The LAP2-emerin-MAN1-domain (LEM-D) protein family has prominent roles within the nuclear lamina. The defining feature of this family is the ∼40 amino acid domain that binds Barrier-to-Autointegration Factor (BAF or BANF1), a metazoan histone-binding and sequence-independent DNA-binding protein [6, 7]. The LEM-D shares sequence similarity.
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LEM-domain proteins are involved in diverse cellular processes including replication and cell cycle control, chromatin organization and nuclear assembly, the regulation of gene expression and signaling pathways, as well as retroviral infection. Genetic analyses in different model organisms reveal new insights into the various functions of LEM.
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The LEM‐domain was initially described as a conserved globular module of approximately 40 amino acids. The three‐dimensional structure of this motif was determined in 2001 by Cai et al. and Laguri et al., who demonstrated that the LEM‐domain as well as the LEM‐like domain is composed of two parallel α‐helices that are connected by a.
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We focused this study of rigidity-driven cellular sensitization to TGFβ on LEM domain-containing protein 3 (LEMD3). LEMD3 is an integral inner nuclear membrane protein and a compelling target for two reasons: 1) it is a known inhibitor of TGFβ signaling; 2) it is biophysically connected to the cell's cytoskeleton, which is remodeled in an ECM stiffness-dependent fashion.
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