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Inhibition of the UFD-1-NPL-4 complex triggers an aberrant immune response in .
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The UFD-1 (ubiquitin fusion degradation 1)-NPL-4 (nuclear protein localization homolog 4) heterodimer is involved in extracting ubiquitinated proteins from several plasma membrane locations, including the endoplasmic reticulum. This heterodimer complex helps in the degradation of ubiquitinated proteins via the proteasome with the help of the AAA+ATPase CDC-48. While the ubiquitin-proteasome system is known to have important roles in maintaining innate immune responses, the role of the UFD-1-NPL-4 complex in regulating immunity remains elusive.
View Article and Find Full Text PDFTargeting USP21 to inhibit abdominal aortic aneurysm progression by suppressing the phenotypic transition of vascular smooth muscle cells.
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Department of Emergency Medicine, Qilu Hospital of Shandong University, Jinan 250012, China; Shandong Provincial Clinical Research Center for Emergency and Critical Care Medicine, Institute of Emergency and Critical Care Medicine of Shandong University, Chest Pain Center, Qilu Hospital of Shandong U
Abdominal aortic aneurysm (AAA) is a life-threatening condition lacking effective treatment. We investigate the role of the deubiquitinating enzyme USP21 in AAA development. Proteomic analysis reveals significant upregulation of USP21 in murine and human abdominal aortic tissues.
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Abdominal aortic aneurysm (AAA) is a potentially life-threatening vascular condition that currently lacks effective pharmacological treatment. The disease is strongly associated with chronic inflammation, where immune cells like macrophages play a crucial role. Efferocytosis, the process by which apoptotic cells are cleared, is involved in regulating inflammation.
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