The interplay between structure and function in intrinsically unstructured proteins

By Peter Tompa. FEBS Letters, 2005

716 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/484883479bf716d5bf061a4d46441a76f77691e6

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Citations in the corpus

A decade and a half of protein intrinsic disorder: Biology still waits for physics (2013, background): “factors, which could promote changes in cellular localization of IDPs or protect them from the degradation machinery.(13,70,138,223,224) Overall, this study clearly showed that the chaos seemingly introduced into the protein world by the discovery of IDPs is under the tight control.”
Prediction of Protein Binding Regions in Disordered Proteins (2009, background): “Recent characterization of IUPs based on their functions shows that disorder can help these proteins to fulfill their functions in various ways [8,9].”
Insights into Late Embryogenesis Abundant (LEA) Proteins in Plants: From Structure to the Functions (2014, background): “Performance of more than one function, “moonlightening”, is not uncommon among proteins and it is more likely to evolve in unfolded, rather than in folded proteins [78].”
Intrinsic disorder here, there, and everywhere, and nowhere to escape from it (2017, background): “However, some IDPs/ IDPRs maintain their functional disorder under conditions of macromolecular crowding and even in living cells, indicating that the physiological state of many proteins relies on the absence of ordered structure [15–19], that some functions simply cannot be done by ordered protein”
A comprehensive assessment of long intrinsic protein disorder from the DisProt database (2018, background): “We may distinguish flavors of disorder by distinct amino acid composition (Vucetic et al. , 2003), backbone flexibility (Cilia et al. , 2013; Martin et al. , 2010), evolutionary conservation (Bellay et al. , 2011), function (Peng et al. , 2015; Tompa, 2005; Xue et al. , 2012) and length.”
Natively Unstructured Loops Differ from Other Loops (2007, background): “Several detailed studies have specifically identified unstructured regions in hub proteins that are involved in signaling [3,5,6,60–62].”
Keap1 Recruits Neh2 through Binding to ETGE and DLG Motifs: Characterization of the Two-Site Molecular Recognition Model (2006, background): “5 ppm) (58), a feature typical of intrinsically disordered polypeptides (10, 55).”
The Enigmatic LEA Proteins and Other Hydrophilins1[W] (2008, neutral): “2; McCubbin et al., 1985; Eom et al., 1996; Lisse et al., 1996; Russouw et al., 1997; Ismail et al., 1999b; Wolkers et al., 2001; Soulages et al., 2002, 2003; Goyal et al., 2003; Shih et al., 2004; Dyson and Wright, 2005; Tompa, 2005; Mouillon et al., 2006; Kovacs et al., 2008).”
Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins (2010, background): “In the case of many proteins, like entropic chains, the function directly originates from their permanent disordered state [22].”
DisProt 7.0: a major update of the database of disordered proteins (2016, neutral): “…shown that in certain cases their function arises directly from the disordered state (entropic chains), whereas in many other cases their function em-anates from molecular recognition accompanied by induced folding to specific binding partners, such as another protein, RNA or DNA molecule (9,10).”