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Coding Regions of Intrinsic Disorder Accommodate Parallel Functions

Trends in Biochemical Sciences, 2016
Numerous DNA- and RNA-level functions are embedded in protein-coding regions, which constrains their structure, function, and evolution. Accumulating evidence suggests that such additional, overlapping functions occur preferentially in the coding sequences of intrinsically disordered proteins/regions (IDPs/IDRs), especially in those that are newly ...
Tompa, Peter, PANCSA, Rita
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Analyzing the Sequences of Intrinsically Disordered Regions with CIDER and localCIDER

2020
Intrinsically disordered proteins and protein regions are ubiquitous across eukaryotic proteomes where they play a range of functional roles. Unlike folded proteins, IDRs lack a well-defined native state but exist in heterogeneous ensembles of conformations.
Garrett M, Ginell, Alex S, Holehouse
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Introduction to intrinsically disordered proteins and regions

2019
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are fascinating dynamic conformational ensembles that are observed under physiological conditions. They facilitate a wide variety of biological processes via mechanisms that are distinct from their structured counterparts.
Oldfield, Christopher J.   +3 more
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Prediction of the Disordered Regions of Intrinsically Disordered Proteins Based on the Molecular Functions

Protein & Peptide Letters, 2020
Background: Intrinsically disordered proteins lack a well-defined three dimensional structure under physiological conditions while possessing the essential biological functions. They take part in various physiological processes such as signal transduction, transcription and posttranslational modifications and etc.
WeiXia, Xie, Yong E, Feng
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Acetylation of intrinsically disordered regions regulates phase separation

Nature Chemical Biology, 2018
Liquid-liquid phase separation (LLPS) of proteins containing intrinsically disordered regions (IDRs) has been proposed as a mechanism underlying the formation of membrane-less organelles. Tight regulation of IDR behavior is essential to ensure that LLPS only takes place when necessary.
Makoto Saito   +7 more
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Interleukin-11: A Multifunctional Cytokine with Intrinsically Disordered Regions

Cell Biochemistry and Biophysics, 2016
Cytokine interleukin-11 (IL-11) is a multifunctional protein with diverse roles in the normal cell signaling and in various pathologies. The structure of IL-11 is characterized by a four-helix bundle motif comprising two pairs of antiparallel α-helices arranged in an up-up-down-down configuration.
Eugene A. Permyakov   +2 more
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Computational Methods to Predict Intrinsically Disordered Regions and Functional Regions in Them

2023
Intrinsically disordered regions (IDRs) are protein regions that do not adopt fixed tertiary structures. Since these regions lack ordered three-dimensional structures, they should be excluded from the target portions of homology modeling. IDRs can be predicted from the amino acid sequences, because their amino acid compositions are different from that ...
Hiroto, Anbo   +2 more
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Engineering intrinsically disordered regions for guiding genome navigation

Molecular Cell
Intrinsically disordered regions (IDRs) navigate transcription factors (TFs) to their binding sites in genomes, raising the question of how IDR sequences can encode for specific genome recognition. To define the principles of IDR-directed binding, we designed de novo IDRs and tested their activity in directing selective binding across the budding yeast
Jing, Liu   +4 more
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Controlling entropy to tune the functions of intrinsically disordered regions

Current Opinion in Structural Biology, 2014
Intrinsically disordered regions (IDRs) are fundamental units of protein function and regulation. Despite their inability to form a unique stable tertiary structure in isolation, many IDRs adopt a defined conformation upon binding and achieve their function through their interactions with other biomolecules.
Tilman, Flock   +3 more
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PREDICTION OF BOUNDARIES BETWEEN INTRINSICALLY ORDERED AND DISORDERED PROTEIN REGIONS

Biocomputing 2003, 2002
Using proteins with both disordered and ordered regions collected through literature searches and database scanning, we assembled a set of 24-residue long segments centered on their order/disorder boundaries as well as a larger set of non-boundary segments consisting of either order or disorder.
Predrag Radivojac   +3 more
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