Results 31 to 40 of about 3,841,423 (288)
Nature Communications, 2021 The SARS-CoV-2 nucleocapsid (N) protein binds the viral RNA genome and contains two ordered domains flanked by three intrinsically-disordered regions. Here, the authors show that RNA binding induces liquid-liquid phase separation of N, which is driven by
Shan Lu +8 more
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The N-terminal intrinsically disordered domain of mgm101p is localized to the mitochondrial nucleoid. [PDF]
, 2013 The mitochondrial genome maintenance gene, MGM101, is essential for yeasts that depend on mitochondrial DNA replication. Previously, in Saccharomyces cerevisiae, it has been found that the carboxy-terminal two-thirds of Mgm101p has a functional core ...
George Desmond Clark-Walker (281878) +12 more
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Protein intrinsic disorder in plants
Frontiers in Plant Science, 2013 To some extent contradicting the classical paradigm of the relationship between protein 3D structure and function, now it is clear that large portions of the proteomes, especially in higher organisms, lack a fixed structure and still perform very important functions.
Pazos, Florencio +3 more
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Order, Disorder, and Everything in Between
Molecules, 2016 In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs)
Shelly DeForte, Vladimir N. Uversky
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Prediction of protein-protein interaction sites in intrinsically disordered proteins
Frontiers in Molecular Biosciences, 2022 Intrinsically disordered proteins (IDPs) participate in many biological processes by interacting with other proteins, including the regulation of transcription, translation, and the cell cycle.
Ranran Chen +10 more
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INTRINSIC PROTEIN DISORDER AND PROTEIN-PROTEIN INTERACTIONS [PDF]
Biocomputing 2012, 2011 Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity ...
Wei-Lun Hsu +7 more
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Expanded Interactome of the Intrinsically Disordered Protein Dss1
Cell Reports, 2018 Summary: Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes.
Signe M. Schenstrøm +7 more
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Intrinsically Disordered Proteins in Neurodegeneration [PDF]
Biophysical Journal, 2016 Intrinsically disordered proteins (IDPs) have gained wide recognition due to their versatile roles in cell physiology and pathology. A large repertoire of IDPs has been implicated in numerous diseases, making them potential targets for therapeutic intervention.
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Conformational Recognition of an Intrinsically Disordered Protein [PDF]
Biophysical Journal, 2014 There is a growing interest in understanding the properties of intrinsically disordered proteins (IDPs); however, the characterization of these states remains an open challenge. IDPs appear to have functional roles that diverge from those of folded proteins and revolve around their ability to act as hubs for protein-protein interactions.
Krieger J. M. +7 more
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D2P2: database of disordered protein predictions [PDF]
, 2013 We present the Database of Disordered Protein Prediction (D2P2), available at http://d2p2.pro (including website source code). A battery of disorder predictors and their variants, VL-XT, VSL2b, PrDOS, PV2, Espritz and IUPred, were run on all protein ...
Oates, Matt E. +3 more
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