The inhibitory ankyrin and activator Rel proteins
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2015, Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular BiologyCitation Excerpt :They are one of the most common protein–protein interaction motifs (Lambert et al., 1990). Many studies discover that a wide variety of ankyrin repeats proteins function directly or indirectly in signal transduction, transcriptional regulation, and developmental regulation by protein–protein interaction (Batchelor et al., 1998; Baumgartner et al., 1998; Bork, 1993; Li et al., 2009; Michaely and Bennett, 1992; Nolan and Baltimore, 1992). The ankyrin repeats of Fem-1 are highly conserved among diverse organisms and the repeats number ranges from 7 to 9.
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2011, International Journal of Biochemistry and Cell BiologyCitation Excerpt :It is also recognized that T cell immunity fails to develop adequately in cancer patients and that impaired T cell function is one of the hallmarks of many cancers (Miescher et al., 1986; Loeffler et al., 1992; Ling et al., 1998). NF-κB is crucial for the development and the activation of T cell immunity, such that defective NF-κB can lead to impaired T cell function in cancers (Sen and Baltimore, 1986; Ullman et al., 1990; Nolan and Baltimore, 1992; Ghosh et al., 1994; Correa et al., 1997; Kim et al., 1999; Buggins et al., 2001; Thornton et al., 2004). Pertinent to RCC, both tumor-infiltrating lymphocytes and peripheral blood T cells of RCC patients exhibit impaired activation of NF-κB (Li et al., 1994; Kim et al., 1999; Uzzo et al., 1999b; Thornton et al., 2004).
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2003, Biochemical PharmacologyCitation Excerpt :NF-κB dimers are rendered transcriptionally inactive within the cytoplasm of the cell by the IκB inhibitors [7,8]. IκB proteins contain 5 to 7 ankyrin repeats consisting of 33 amino acids [9]. These repeats function as protein–protein interaction domains that are required for binding of IκB to NF-κB dimers.
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