Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

By Vladimir N Uversky, Christopher J. Oldfield, A. Keith Dunker. 2005

826 citations recorded by the source corpus.

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In Molecular Biology

Citations in the corpus

SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, background): “These dynamic protein structures can be experimentally observed as their backbone angles vary over time due to their innate ﬂexibility [1].”
Prediction of Protein Binding Regions in Disordered Proteins (2009, background): “Disordered segments are often involved for complex signaling and regulatory processes [20] such as cell cycle control, gene regulation or signal transduction in the intracellular region of transmembrane proteins [83].”
Flexible nets (2005, background): “That is, such proteins could have completely different geometries in the rigidiﬁed structures that are induced upon binding to different partners [48].”
Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes (2006, background): “Recent reviews [18–20] discuss the importance of intrinsic disorder for protein–protein interactions that involve binding to multiple partners.”
A decade and a half of protein intrinsic disorder: Biology still waits for physics (2013, background): “This suggests that disorder, with its ability to be implemented in various signaling, recognition, and regulation pathways and networks, is important for the maintenance of life in eukaryotic and especially muticellular eukaryotic organisms.(4,45,78,134) Also, the finding that alternatively spliced ”
Intrinsic disorder in transcription factors. (2006, background): “As order, molten globule, premolten globule, and random coil conformation possess defined structural differences, they could be characterized by the following experimental approaches and applications [for recent review see Uversky et al 2005]:”
Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell (2019, background): “Several studies have reported lists of Gene Ontology functional classes 69 that are enriched in IDPs, including but not limited to: cell regulation, transcription, translation, 70 signaling, and alternative splicing [22-29].”
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “Furthermore, preservation of intrinsic disorder within dynamic signaling complexes provides disorder carriers with the capability to be engaged in entropic chain activities, which rely entirely on an extended randomcoil conformation of a polypeptide that is able to carry out its function while stayi”
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners (2008, background): “the disordered regions are the identification sites of the protein to be regulated [148] – and (2) ordered proteins play the active role – i.”
Natively unstructured regions in proteins identified from contact predictions (2007, neutral): “al., 2006; Namba, 2001; Romero, et al., 2004; Tompa, 2005; Uversky, et al., 2000; Uversky, et al., 2005; Wright and Dyson, 1999).”
Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life (2014, background): “Many IDRs contain specific identification regions, which they use to participate in various regulation, recognition, signaling and control pathways [11, 12].”
Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life (2012, background): “…and regulation, and there are complex and well-developed regulation networks in eukaryotic and especially in multicellular organisms that evidently rely on the ability of IDPs to perform a variety of necessary functions (Dunker et al., 2005; Uversky & Dunker, 2010; Uversky et al., 2005).”
Inferring Stabilizing Mutations from Protein Phylogenies: Application to Influenza Hemagglutinin (2009, background): “This assumption is imperfect, since some proteins are natively unfolded [33], only kinetically stable [34], or specifically selected for marginal stability in order to aid in regulation [35].”