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The nuclear membrane, also known as the nuclear envelope or nucleolemma, is a double-layered structure composed of phospholipid bilayers that encloses the nucleus in eukaryotic cells. It functions as a selective barrier, separating the genetic material in the nucleus from the cytoplasm, thereby protecting the DNA and controlling the exchange of molecules such as proteins and RNA through nuclear pores. The nuclear membrane consists of two distinct membranes (inner and outer) that connect at multiple nuclear pore complexes, which regulate the flow of macromolecules between the nucleus and cytoplasm. The inner membrane is supported by the nuclear lamina, a network of proteins (mainly lamins) involved in structural support, chromatin organization, and gene expression regulation. Mutations in nuclear membrane components can lead to diseases such as laminopathies, highlighting its importance in cellular stability and disease. This entry is problematic or too generic to be a correct 'target' as it is a structure, not a single molecule or actionable target. The nuclear membrane is not a drug target (receptor, enzyme, transporter, etc.), but a subcellular organelle structure made up of multiple component proteins and complexes; the entry as a whole is not a therapeutic target but its components might be. Disease relevance exists mainly in the context of genetic defects affecting its structural proteins (like lamins), but 'nuclear membrane' itself is not generally cited as a direct disease target or biomarker. No drugs, mechanisms, or biomarkers directly target the nuclear membrane as a whole—drug targeting or biomarker relevance would be defined at the level of its component proteins (such as nuclear pore proteins or lamins), not the membrane as a collective structure. If a 'target' is required, specifying a member protein (e.g., Lamin A/C, nuclear pore complex protein) is necessary to retrieve structured, druggable, or biomarkers information.
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