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- W1550160333 endingPage "34" @default.
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- W1550160333 abstract "Many proteins (or protein regions) are intrinsically disordered. They lack unique 3D structures in their native, functional states under physiological conditions in vitro (Wright and Dyson, 1999; Uversky et al., 2000; Dunker et al., 2001, 2002a,b; Tompa, 2002, 2003; Uversky, 2002a,b, 2003; Minezaki et al., 2006). The major functions of such proteins and regions are signaling, recognition, and regulation activities (Wright and Dyson, 1999, 2009; Dunker et al., 2002a,b; 2005; 2008a,b; Dyson and Wright, 2005; Uversky et al., 2005; Radivojac et al., 2007; Dunker and Uversky, 2008; Oldfield et al., 2008; Tompa et al., 2009). Owing to these crucial functional roles, intrinsically disordered proteins (IDPs) are highly abundant in all species. According to computational predictions, typically 7–30% prokaryotic proteins contain long disordered regions of more than 30 consecutive residues, whereas in eukaryotes the amount of such proteins reaches 45–50% (Romero et al., 1997, 2001; Dunker et al., 2001; Ward et al., 2004; Oldfield et al., 2005a,b; Feng et al., 2006). Furthermore, almost 70% of proteins in the PDB (which is biased to structured proteins) have intrinsically disordered regions (IDRs), which are indicated by missing electron density (Obradovic et al., 2003). Numerous disordered proteins have been shown to be associated with cancer (Iakoucheva et al., 2002), cardiovascular disease (Cheng et al., 2006), amyloidoses (Uversky, 2008a), neurodegenerative diseases (Uversky, 2008b), diabetes, and other human diseases (Uversky et al., 2008), an" @default.
- W1550160333 created "2016-06-24" @default.
- W1550160333 creator A5011869206 @default.
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- W1550160333 creator A5077957543 @default.
- W1550160333 creator A5083199032 @default.
- W1550160333 creator A5091785779 @default.
- W1550160333 date "2011-10-24" @default.
- W1550160333 modified "2023-10-17" @default.
- W1550160333 title "Do Viral Proteins Possess Unique Features?" @default.
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