The Journal of Steroid Biochemistry and Molecular Biology
Volume 56, Issues 1–6, January 1996, Pages 23-30
A component of the 26S proteasome binds an orphan member of the nuclear hormone receptor superfamily
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Cited by (21)
Potential role of LMP2 as an anti-oncogenic factor in human uterine leiomyosarcoma: Morphological significance of calponin h1
2012, FEBS LettersCitation Excerpt :The relative amounts of LMP2 and LMP7 vary significantly among tissues and cell lines in mice and humans [33], and LMP2 levels in proteasomes show greater variation among tissues than do those of LMP7 [33]. Proteasome subunits that are not incorporated into complexes are believed to individually mediate gene transcriptional activation together with other co-factors [34]. For instance, LMP2 is also reportedly required for estrogen receptor-mediated gene transcription as well as for estrogen-stimulated cell cycle progression [35].
Characterization and localization of Plasmodium falciparum homolog of prokaryotic ClpQ/HslV protease
2007, Molecular and Biochemical ParasitologyExpanding functional diversity of the coactivators
2005, Trends in Biochemical SciencesQuaternary structure of the ATPase complex of human 26s proteasomes determined by chemical cross-linking
2001, Archives of Biochemistry and Biophysics
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Present address: Hormone Research Center, Dept. of Biology, Chonnam National University, Kwangju, South Korea 500-757.
Copyright © 1996 Published by Elsevier Ltd.