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pubmed-article:16105755pubmed:abstractTextNUP98 is fused to a variety of partner genes, including abdominal B-like HOX, in human myeloid and T-cell malignancies via chromosomal translocation involving 11p15. NUP98 encodes a 98-kd nucleoporin that is a component of the nuclear pore complex and functions in nucleocytoplasmic transport, with its N-terminal GLFG repeats used as a docking site for karyopherins. Disruption of NUP98 may affect the nuclear pore function, and the abnormal expression and altered function of fusion partners may also be critical for leukemia development. Recent studies using mouse models expressing NUP98-HOX have confirmed its leukemogenic potential, and cooperative genes for NUP98-HOXA9 in leukemogenesis have been identified in these studies.Thus, the NUP98 chimera is a unique molecule that provides valuable information regarding nuclear pore function and the role of the homeobox protein in leukemogenesis/carcinogenesis.lld:pubmed
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pubmed-article:16105755pubmed:articleTitleNUP98 fusion in human leukemia: dysregulation of the nuclear pore and homeodomain proteins.lld:pubmed
pubmed-article:16105755pubmed:affiliationDepartment of Carcinogenesis, The Cancer Institute, Japanese Foundation for Cancer Research, Tokyo, Japan. takuro-ind@umin.ac.jplld:pubmed
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