Results 31 to 40 of about 156,443 (294)
Ubiquitin Interacting Motifs: Duality Between Structured and Disordered Motifs
Frontiers in Molecular Biosciences, 2021 Ubiquitin is a small protein at the heart of many cellular processes, and several different protein domains are known to recognize and bind ubiquitin. A common motif for interaction with ubiquitin is the Ubiquitin Interacting Motif (UIM), characterized ...
Matteo Lambrughi +10 more
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Frontiers in Genetics, 2020 Pathogen infection triggers extensive reprogramming of the plant transcriptome, including numerous genes the function of which is unknown. Due to their wide taxonomic distribution, genes encoding proteins with Domains of Unknown Function (DUFs) activated
Marie Didelon +4 more
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Intrinsically Disordered Energy Landscapes [PDF]
Scientific Reports, 2015 Abstract Analysis of an intrinsically disordered protein (IDP) reveals an underlying multifunnel structure for the energy landscape. We suggest that such ‘intrinsically disordered’ landscapes, with a number of very different competing low-energy structures, are likely to characterise IDPs and provide a useful way ...
Yassmine Chebaro +3 more
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WRKYs in Durum wheat: Intrinsic disorder and interactions [PDF]
Network Biology, 2022 The WRKY transcription factors are involved in a range of biological processes in plants, including the response to biotic and abiotic stresses and plant immunity.
Mouna Choura, Faical Brini
doaj
Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs
Biomolecules, 2021 ErbBs are receptor tyrosine kinases involved not only in development, but also in a wide variety of diseases, particularly cancer. Their extracellular, transmembrane, juxtamembrane, and kinase folded domains were described extensively over the past 20 ...
Louise Pinet +2 more
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Intrinsic Disorder and Functional Proteomics [PDF]
Biophysical Journal, 2007 The recent advances in the prediction of intrinsically disordered proteins and the use of protein disorder prediction in the fields of molecular biology and bioinformatics are reviewed here, especially with regard to protein function. First, a close look is taken at intrinsically disordered proteins and then at the methods used for their experimental ...
Radivojac, Predrag +5 more
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Buried and accessible surface area control intrinsic protein flexibility [PDF]
, 2013 Proteins experience a wide variety of conformational dynamics that can be crucial for facilitating their diverse functions. How is the intrinsic flexibility required for these motions encoded in their three-dimensional structures?
Marsh, Joseph A; id_orcid
core +1 more source
Inferring function using patterns of native disorder in proteins [PDF]
, 2007 Natively unstructured regions are a common feature of eukaryotic proteomes. Between 30% and 60% of proteins are predicted to contain long stretches of disordered residues, and not only have many of these regions been confirmed experimentally, but they ...
Swindells, MB +14 more
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Intrinsically disordered proteins: modes of binding with emphasis on disordered domains
Open Biology, 2021 Our notions of protein function have long been determined by the protein structure–function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly ...
Owen Michael Morris +2 more
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Concentrating on intrinsic disorder [PDF]
Nature Reviews Molecular Cell Biology, 2018 Many eukaryotic proteins, including key transcription regulators, contain intrinsically disordered regions (IDRs), which serve as flexible interaction platforms. The molecular understanding of IDR-based interactions is now emerging, providing new insights into how IDRs promote protein compartmentalization and/or phase separation and how these processes
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